HUMAN:HNRPU

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	HNRNPU (synonyms: HNRPU, SAFA, U21.1)
Protein Name(s)	Heterogeneous nuclear ribonucleoprotein U hnRNP U Scaffold attachment factor A SAF-A p120 pp120
External Links
UniProt	Q00839
EMBL	X65488 AF068846 BX323046 BC003367 BC003621 BC007950 BC024767 BC034925
CCDS	CCDS31081.1 CCDS41479.1
PIR	S22765
RefSeq	NP_004492.2 NP_114032.2 XP_016856604.1 XP_016856605.1 XP_016856606.1
UniGene	Hs.106212 Hs.411490 Hs.743421
PDB	1ZRJ
PDBsum	1ZRJ
ProteinModelPortal	Q00839
SMR	Q00839
BioGrid	109433
DIP	DIP-684N
IntAct	Q00839
MINT	MINT-1654412
STRING	9606.ENSP00000283179
iPTMnet	Q00839
PhosphoSitePlus	Q00839
SwissPalm	Q00839
BioMuta	HNRNPU
DMDM	254763463
EPD	Q00839
MaxQB	Q00839
PaxDb	Q00839
PeptideAtlas	Q00839
PRIDE	Q00839
DNASU	3192
Ensembl	ENST00000283179 ENST00000444376
GeneID	3192
KEGG	hsa:3192
UCSC	uc001iaz.2
CTD	3192
DisGeNET	3192
GeneCards	HNRNPU
HGNC	HGNC:5048
HPA	CAB011532 HPA041057 HPA058707
MIM	602869
neXtProt	NX_Q00839
OpenTargets	ENSG00000153187
PharmGKB	PA162391486
eggNOG	ENOG410IR1W ENOG410Y1WQ
GeneTree	ENSGT00390000020210
HOGENOM	HOG000253920
HOVERGEN	HBG061101
InParanoid	Q00839
KO	K12888
OMA	RQMADTG
OrthoDB	EOG091G041T
PhylomeDB	Q00839
TreeFam	TF317301
Reactome	[www.reactome.org/content/detail/R-HSA-72163 R-HSA-72163] [www.reactome.org/content/detail/R-HSA-72203 R-HSA-72203]
SIGNOR	Q00839
ChiTaRS	HNRNPU
EvolutionaryTrace	Q00839
GeneWiki	HNRPU
GenomeRNAi	3192
PRO	PR:Q00839
Proteomes	UP000005640
Bgee	ENSG00000153187
CleanEx	HS_HNRNPU
ExpressionAtlas	Q00839
Genevisible	Q00839
GO	GO:0071013 GO:0009986 GO:0070937 GO:0036464 GO:0031012 GO:0030529 GO:0016020 GO:0005654 GO:0005634 GO:0005524 GO:0001047 GO:0003677 GO:0035326 GO:0034046 GO:0043021 GO:0003723 GO:0070034 GO:0055013 GO:0071549 GO:0032922 GO:0070934 GO:0010467 GO:0000398 GO:0032211 GO:0001649 GO:2000373 GO:0010628 GO:0006396
Gene3D	1.10.720.30 3.40.50.300
InterPro	IPR001870 IPR013320 IPR026745 IPR027417 IPR003034 IPR003877
PANTHER	PTHR12381:SF63
Pfam	PF02037 PF00622
SMART	SM00513 SM00449
SUPFAM	SSF49899 SSF52540
PROSITE	PS50188 PS50800

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0005654	nucleoplasm	PMID:28221134^[1]	ECO:0000314			C		Human hnRNP U. Figure 3, immunofluorescence spectroscopy confirmed localization to the nucleoplasm.	complete CACAO 12414
involved_in	GO:1990845	adaptive thermogenesis	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q8VEK3	P		Seeded From UniProt	complete
involved_in	GO:0090336	positive regulation of brown fat cell differentiation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q8VEK3	P		Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:18082603^[2]	ECO:0000353	physical interaction evidence used in manual assertion	RNAcentral:URS00004416C5_9606	F		Seeded From UniProt	complete
involved_in	GO:0048255	mRNA stabilization	PMID:17174306^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0003730	mRNA 3'-UTR binding	PMID:17174306^[3]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:19617346^[4]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:1990904	ribonucleoprotein complex	PMID:19617346^[4]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003714	transcription corepressor activity	PMID:23811339^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:23811339^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003779	actin binding	PMID:15711563^[6]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:15711563^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	PMID:28221134^[1]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0071385	cellular response to glucocorticoid stimulus	PMID:9353307^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0000122	negative regulation of transcription by RNA polymerase II	PMID:9353307^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0016607	nuclear speck	PMID:9353307^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:9353307^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0000993	RNA polymerase II complex binding	PMID:10490622^[8]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0001097	TFIIH-class transcription factor complex binding	PMID:10490622^[8]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
colocalizes_with	GO:0090575	RNA polymerase II transcription factor complex	PMID:10490622^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0033673	negative regulation of kinase activity	PMID:10490622^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034244	negative regulation of transcription elongation from RNA polymerase II promoter	PMID:10490622^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0000381	regulation of alternative mRNA splicing, via spliceosome	PMID:22325991^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0017069	snRNA binding	PMID:22325991^[9]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0036002	pre-mRNA binding	PMID:22325991^[9]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:9204873^[10]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:9204873^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:9405365^[11]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:1990904	ribonucleoprotein complex	PMID:9405365^[11]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:1990837	sequence-specific double-stranded DNA binding	PMID:9405365^[11]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003682	chromatin binding	PMID:9405365^[11]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0000228	nuclear chromosome	PMID:11003645^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:11003645^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:1990837	sequence-specific double-stranded DNA binding	PMID:11003645^[12]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0031490	chromatin DNA binding	PMID:11003645^[12]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003727	single-stranded RNA binding	PMID:1628625^[13]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003697	single-stranded DNA binding	PMID:1628625^[13]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:28622508^[14]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:28622508^[14]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:28622508^[14]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003682	chromatin binding	PMID:28622508^[14]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:1902275	regulation of chromatin organization	PMID:28622508^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1902889	protein localization to spindle microtubule	PMID:21242313^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21242313^[15]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:1990498	mitotic spindle microtubule	PMID:21242313^[15]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0072686	mitotic spindle	PMID:21242313^[15]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0000776	kinetochore	PMID:21242313^[15]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:1990023	mitotic spindle midzone	PMID:21242313^[15]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1901673	regulation of mitotic spindle assembly	PMID:21242313^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:11909954^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003682	chromatin binding	PMID:11909954^[16]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:1990904	ribonucleoprotein complex	PMID:11909954^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:2000648	positive regulation of stem cell proliferation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q8VEK3	P		Seeded From UniProt	complete
involved_in	GO:1990280	RNA localization to chromatin	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q8VEK3	P		Seeded From UniProt	complete
involved_in	GO:0009048	dosage compensation by inactivation of X chromosome	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q8VEK3	P		Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:26244333^[17]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0016363	nuclear matrix	PMID:8174554^[18]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:8174554^[18]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0034046	poly(G) binding	PMID:8174554^[18]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0017130	poly(C) RNA binding	PMID:8174554^[18]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008143	poly(A) binding	PMID:8174554^[18]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003725	double-stranded RNA binding	PMID:8174554^[18]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003690	double-stranded DNA binding	PMID:8174554^[18]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003697	single-stranded DNA binding	PMID:8174554^[18]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:1902425	positive regulation of attachment of mitotic spindle microtubules to kinetochore	PMID:21242313^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007346	regulation of mitotic cell cycle	PMID:25986610^[19]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0030496	midbody	PMID:25986610^[19]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0072686	mitotic spindle	PMID:25986610^[19]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005813	centrosome	PMID:25986610^[19]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:1990841	promoter-specific chromatin binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q8VEK3	F		Seeded From UniProt	complete
enables	GO:0099122	RNA polymerase II C-terminal domain binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q8VEK3	F		Seeded From UniProt	complete
involved_in	GO:2000737	negative regulation of stem cell differentiation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q8VEK3	P		Seeded From UniProt	complete
involved_in	GO:1990830	cellular response to leukemia inhibitory factor	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q8VEK3	P		Seeded From UniProt	complete
involved_in	GO:2000737	negative regulation of stem cell differentiation	PMID:21235343^[20]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:2000373	positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q6IMY8	P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:19617346^[4]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0044877	protein-containing complex binding	PMID:19617346^[4]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0043021	ribonucleoprotein complex binding	PMID:19617346^[4]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003714	transcription corepressor activity	PMID:19617346^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0051457	maintenance of protein location in nucleus	PMID:19617346^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032211	negative regulation of telomere maintenance via telomerase	PMID:18082603^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0070034	telomerase RNA binding	PMID:18082603^[2]	ECO:0000353	physical interaction evidence used in manual assertion	RNAcentral:URS00004A7003_9606	F		Seeded From UniProt	complete
part_of	GO:0005697	telomerase holoenzyme complex	PMID:18082603^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0098577	inactive sex chromosome	PMID:14608463^[21]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0016363	nuclear matrix	PMID:14608463^[21]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:14608463^[21]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003697	single-stranded DNA binding	PMID:8068679^[22]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003690	double-stranded DNA binding	PMID:8068679^[22]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003727	single-stranded RNA binding	PMID:8068679^[22]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0009986	cell surface	PMID:7993898^[23]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0000978	RNA polymerase II proximal promoter sequence-specific DNA binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q8VEK3	F		Seeded From UniProt	complete
involved_in	GO:0032922	circadian regulation of gene expression	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q8VEK3	P		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q8VEK3	P		Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:19946888^[24]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0036464	cytoplasmic ribonucleoprotein granule	PMID:15121898^[25]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:16210410^[26]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000134)\|part_of:(CL:0000062)	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:22720776^[27]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0001649	osteoblast differentiation	PMID:16210410^[26]	ECO:0007005	high throughput direct assay evidence used in manual assertion		P	results_in_determination_of:(CL:0000134)	Seeded From UniProt	complete
part_of	GO:0071013	catalytic step 2 spliceosome	PMID:11991638^[28]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070937	CRD-mediated mRNA stability complex	PMID:19029303^[29]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0070934	CRD-mediated mRNA stabilization	PMID:19029303^[29]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:22681889^[30]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:22658674^[31]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:1990904	ribonucleoprotein complex	PMID:17289661^[32]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0000398	mRNA splicing, via spliceosome	PMID:11991638^[28]	ECO:0000305	curator inference used in manual assertion	GO:0071013	P		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0032839	dendrite cytoplasm	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0098963	C		Seeded From UniProt	complete
involved_in	GO:2000737	negative regulation of stem cell differentiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8VEK3 ensembl:ENSMUSP00000047571	P		Seeded From UniProt	complete
involved_in	GO:2000648	positive regulation of stem cell proliferation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8VEK3 ensembl:ENSMUSP00000047571	P		Seeded From UniProt	complete
involved_in	GO:1990845	adaptive thermogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8VEK3 ensembl:ENSMUSP00000047571	P		Seeded From UniProt	complete
enables	GO:1990841	promoter-specific chromatin binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8VEK3 ensembl:ENSMUSP00000047571	F		Seeded From UniProt	complete
involved_in	GO:1990830	cellular response to leukemia inhibitory factor	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8VEK3 ensembl:ENSMUSP00000047571	P		Seeded From UniProt	complete
involved_in	GO:1990280	RNA localization to chromatin	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8VEK3 ensembl:ENSMUSP00000047571	P		Seeded From UniProt	complete
enables	GO:0099122	RNA polymerase II C-terminal domain binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8VEK3 ensembl:ENSMUSP00000047571	F		Seeded From UniProt	complete
involved_in	GO:0098963	dendritic transport of messenger ribonucleoprotein complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8VEK3 ensembl:ENSMUSP00000047571	P		Seeded From UniProt	complete
part_of	GO:0098577	inactive sex chromosome	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8VEK3 ensembl:ENSMUSP00000047571	C		Seeded From UniProt	complete
involved_in	GO:0090336	positive regulation of brown fat cell differentiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8VEK3 ensembl:ENSMUSP00000047571	P		Seeded From UniProt	complete
involved_in	GO:0055013	cardiac muscle cell development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8VEK3 ensembl:ENSMUSP00000047571	P		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8VEK3 ensembl:ENSMUSP00000047571	P		Seeded From UniProt	complete
enables	GO:0043565	sequence-specific DNA binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8VEK3 ensembl:ENSMUSP00000047571	F		Seeded From UniProt	complete
involved_in	GO:0032922	circadian regulation of gene expression	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8VEK3 ensembl:ENSMUSP00000047571	P		Seeded From UniProt	complete
involved_in	GO:0009048	dosage compensation by inactivation of X chromosome	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8VEK3 ensembl:ENSMUSP00000047571	P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8VEK3 ensembl:ENSMUSP00000047571	C		Seeded From UniProt	complete
enables	GO:0003723	RNA binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8VEK3 ensembl:ENSMUSP00000047571	F		Seeded From UniProt	complete
enables	GO:0000978	RNA polymerase II proximal promoter sequence-specific DNA binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8VEK3 ensembl:ENSMUSP00000047571	F		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR026745	C		Seeded From UniProt	complete
involved_in	GO:0006396	RNA processing	PMID:1628625^[13]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:1628625^[13]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:1628625^[13]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0016070	RNA metabolic process	Reactome:R-HSA-8953854	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	Reactome:R-HSA-72160 Reactome:R-HSA-72143 Reactome:R-HSA-72139 Reactome:R-HSA-72130 Reactome:R-HSA-72127 Reactome:R-HSA-72124 Reactome:R-HSA-72107 Reactome:R-HSA-72103 Reactome:R-HSA-156661	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0000398	mRNA splicing, via spliceosome	Reactome:R-HSA-72163	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006325	chromatin organization	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0156	P		Seeded From UniProt	complete
involved_in	GO:0007275	multicellular organism development	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0217	P		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F		Seeded From UniProt	complete
part_of	GO:0000775	chromosome, centromeric region	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0137	C		Seeded From UniProt	complete
part_of	GO:0000776	kinetochore	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0995	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		Seeded From UniProt	complete
involved_in	GO:0007049	cell cycle	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0131	P		Seeded From UniProt	complete
involved_in	GO:0051301	cell division	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0132	P		Seeded From UniProt	complete
involved_in	GO:0006397	mRNA processing	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0507	P		Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
part_of	GO:0005681	spliceosomal complex	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0747	C		Seeded From UniProt	complete
involved_in	GO:0048511	rhythmic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0090	P		Seeded From UniProt	complete
involved_in	GO:0030154	cell differentiation	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0221	P		Seeded From UniProt	complete
enables	GO:0003723	RNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0694	F		Seeded From UniProt	complete
part_of	GO:0005694	chromosome	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0158 UniProtKB-SubCell:SL-0468	C		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0238	F		Seeded From UniProt	complete
part_of	GO:0005856	cytoskeleton	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0206	C		Seeded From UniProt	complete
involved_in	GO:0008380	RNA splicing	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0508	P		Seeded From UniProt	complete
part_of	GO:0016607	nuclear speck	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0186	C		Seeded From UniProt	complete
part_of	GO:0030496	midbody	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0469	C		Seeded From UniProt	complete
part_of	GO:0005819	spindle	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0251	C		Seeded From UniProt	complete
part_of	GO:0016363	nuclear matrix	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0181	C		Seeded From UniProt	complete
part_of	GO:0000777	condensed chromosome kinetochore	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0149	C		Seeded From UniProt	complete
part_of	GO:0005815	microtubule organizing center	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0048	C		Seeded From UniProt	complete
part_of	GO:0000922	spindle pole	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0448	C		Seeded From UniProt	complete
part_of	GO:0009986	cell surface	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0310	C		Seeded From UniProt	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Capitanio, JS et al. (2017) Human Nup98 regulates the localization and activity of DExH/D-box helicase DHX9. Elife 6 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 Fu, D & Collins, K (2007) Purification of human telomerase complexes identifies factors involved in telomerase biogenesis and telomere length regulation. Mol. Cell 28 773-85 PubMed GONUTS page
↑ ^3.0 ^3.1 Yugami, M et al. (2007) hnRNP-U enhances the expression of specific genes by stabilizing mRNA. FEBS Lett. 581 1-7 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 ^4.6 Ameyar-Zazoua, M et al. (2009) Physical and functional interaction between heterochromatin protein 1alpha and the RNA-binding protein heterogeneous nuclear ribonucleoprotein U. J. Biol. Chem. 284 27974-9 PubMed GONUTS page
↑ ^5.0 ^5.1 Bi, HS et al. (2013) H19 inhibits RNA polymerase II-mediated transcription by disrupting the hnRNP U-actin complex. Biochim. Biophys. Acta 1830 4899-906 PubMed GONUTS page
↑ ^6.0 ^6.1 Kukalev, A et al. (2005) Actin and hnRNP U cooperate for productive transcription by RNA polymerase II. Nat. Struct. Mol. Biol. 12 238-44 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 Eggert, M et al. (1997) The glucocorticoid receptor is associated with the RNA-binding nuclear matrix protein hnRNP U. J. Biol. Chem. 272 28471-8 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 ^8.3 ^8.4 Kim, MK & Nikodem, VM (1999) hnRNP U inhibits carboxy-terminal domain phosphorylation by TFIIH and represses RNA polymerase II elongation. Mol. Cell. Biol. 19 6833-44 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 Xiao, R et al. (2012) Nuclear matrix factor hnRNP U/SAF-A exerts a global control of alternative splicing by regulating U2 snRNP maturation. Mol. Cell 45 656-68 PubMed GONUTS page
↑ ^10.0 ^10.1 Göhring, F & Fackelmayer, FO (1997) The scaffold/matrix attachment region binding protein hnRNP-U (SAF-A) is directly bound to chromosomal DNA in vivo: a chemical cross-linking study. Biochemistry 36 8276-83 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 ^11.3 Göhring, F et al. (1997) The novel SAR-binding domain of scaffold attachment factor A (SAF-A) is a target in apoptotic nuclear breakdown. EMBO J. 16 7361-71 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 ^12.3 Kipp, M et al. (2000) SAF-Box, a conserved protein domain that specifically recognizes scaffold attachment region DNA. Mol. Cell. Biol. 20 7480-9 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 ^13.3 ^13.4 Kiledjian, M & Dreyfuss, G (1992) Primary structure and binding activity of the hnRNP U protein: binding RNA through RGG box. EMBO J. 11 2655-64 PubMed GONUTS page
↑ ^14.0 ^14.1 ^14.2 ^14.3 ^14.4 Nozawa, RS et al. (2017) SAF-A Regulates Interphase Chromosome Structure through Oligomerization with Chromatin-Associated RNAs. Cell 169 1214-1227.e18 PubMed GONUTS page
↑ ^15.0 ^15.1 ^15.2 ^15.3 ^15.4 ^15.5 ^15.6 ^15.7 Ma, N et al. (2011) The nuclear scaffold protein SAF-A is required for kinetochore-microtubule attachment and contributes to the targeting of Aurora-A to mitotic spindles. J. Cell. Sci. 124 394-404 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 Martens, JH et al. (2002) Scaffold/matrix attachment region elements interact with a p300-scaffold attachment factor A complex and are bound by acetylated nucleosomes. Mol. Cell. Biol. 22 2598-606 PubMed GONUTS page
↑ Yamada, N et al. (2015) Xist Exon 7 Contributes to the Stable Localization of Xist RNA on the Inactive X-Chromosome. PLoS Genet. 11 e1005430 PubMed GONUTS page
↑ ^18.0 ^18.1 ^18.2 ^18.3 ^18.4 ^18.5 ^18.6 ^18.7 Fackelmayer, FO et al. (1994) Nucleic-acid-binding properties of hnRNP-U/SAF-A, a nuclear-matrix protein which binds DNA and RNA in vivo and in vitro. Eur. J. Biochem. 221 749-57 PubMed GONUTS page
↑ ^19.0 ^19.1 ^19.2 ^19.3 Douglas, P et al. (2015) Phosphorylation of SAF-A/hnRNP-U Serine 59 by Polo-Like Kinase 1 Is Required for Mitosis. Mol. Cell. Biol. 35 2699-713 PubMed GONUTS page
↑ Vizlin-Hodzic, D et al. (2011) SAF-A has a role in transcriptional regulation of Oct4 in ES cells through promoter binding. Cell Reprogram 13 13-27 PubMed GONUTS page
↑ ^21.0 ^21.1 ^21.2 Helbig, R & Fackelmayer, FO (2003) Scaffold attachment factor A (SAF-A) is concentrated in inactive X chromosome territories through its RGG domain. Chromosoma 112 173-82 PubMed GONUTS page
↑ ^22.0 ^22.1 ^22.2 Fackelmayer, FO & Richter, A (1994) Purification of two isoforms of hnRNP-U and characterization of their nucleic acid binding activity. Biochemistry 33 10416-22 PubMed GONUTS page
↑ Jordan, P et al. (1994) Major cell surface-located protein substrates of an ecto-protein kinase are homologs of known nuclear proteins. Biochemistry 33 14696-706 PubMed GONUTS page
↑ Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page
↑ Villacé, P et al. (2004) The composition of Staufen-containing RNA granules from human cells indicates their role in the regulated transport and translation of messenger RNAs. Nucleic Acids Res. 32 2411-20 PubMed GONUTS page
↑ ^26.0 ^26.1 Foster, LJ et al. (2005) Differential expression profiling of membrane proteins by quantitative proteomics in a human mesenchymal stem cell line undergoing osteoblast differentiation. Stem Cells 23 1367-77 PubMed GONUTS page
↑ Todd, MA & Picketts, DJ (2012) PHF6 interacts with the nucleosome remodeling and deacetylation (NuRD) complex. J. Proteome Res. 11 4326-37 PubMed GONUTS page
↑ ^28.0 ^28.1 Jurica, MS et al. (2002) Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis. RNA 8 426-39 PubMed GONUTS page
↑ ^29.0 ^29.1 Weidensdorfer, D et al. (2009) Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs. RNA 15 104-15 PubMed GONUTS page
↑ Baltz, AG et al. (2012) The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Mol. Cell 46 674-90 PubMed GONUTS page
↑ Castello, A et al. (2012) Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 149 1393-406 PubMed GONUTS page
↑ Jønson, L et al. (2007) Molecular composition of IMP1 ribonucleoprotein granules. Mol. Cell Proteomics 6 798-811 PubMed GONUTS page

[PMID:28221134-1] 1.0 ^1.1 Capitanio, JS et al. (2017) Human Nup98 regulates the localization and activity of DExH/D-box helicase DHX9. Elife 6 PubMed GONUTS page

[PMID:18082603-2] 2.0 ^2.1 ^2.2 ^2.3 Fu, D & Collins, K (2007) Purification of human telomerase complexes identifies factors involved in telomerase biogenesis and telomere length regulation. Mol. Cell 28 773-85 PubMed GONUTS page

[PMID:17174306-3] 3.0 ^3.1 Yugami, M et al. (2007) hnRNP-U enhances the expression of specific genes by stabilizing mRNA. FEBS Lett. 581 1-7 PubMed GONUTS page

[PMID:19617346-4] 4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 ^4.6 Ameyar-Zazoua, M et al. (2009) Physical and functional interaction between heterochromatin protein 1alpha and the RNA-binding protein heterogeneous nuclear ribonucleoprotein U. J. Biol. Chem. 284 27974-9 PubMed GONUTS page

[PMID:23811339-5] 5.0 ^5.1 Bi, HS et al. (2013) H19 inhibits RNA polymerase II-mediated transcription by disrupting the hnRNP U-actin complex. Biochim. Biophys. Acta 1830 4899-906 PubMed GONUTS page

[PMID:15711563-6] 6.0 ^6.1 Kukalev, A et al. (2005) Actin and hnRNP U cooperate for productive transcription by RNA polymerase II. Nat. Struct. Mol. Biol. 12 238-44 PubMed GONUTS page

[PMID:9353307-7] 7.0 ^7.1 ^7.2 ^7.3 Eggert, M et al. (1997) The glucocorticoid receptor is associated with the RNA-binding nuclear matrix protein hnRNP U. J. Biol. Chem. 272 28471-8 PubMed GONUTS page

[PMID:10490622-8] 8.0 ^8.1 ^8.2 ^8.3 ^8.4 Kim, MK & Nikodem, VM (1999) hnRNP U inhibits carboxy-terminal domain phosphorylation by TFIIH and represses RNA polymerase II elongation. Mol. Cell. Biol. 19 6833-44 PubMed GONUTS page

[PMID:22325991-9] 9.0 ^9.1 ^9.2 Xiao, R et al. (2012) Nuclear matrix factor hnRNP U/SAF-A exerts a global control of alternative splicing by regulating U2 snRNP maturation. Mol. Cell 45 656-68 PubMed GONUTS page

[PMID:9204873-10] 10.0 ^10.1 Göhring, F & Fackelmayer, FO (1997) The scaffold/matrix attachment region binding protein hnRNP-U (SAF-A) is directly bound to chromosomal DNA in vivo: a chemical cross-linking study. Biochemistry 36 8276-83 PubMed GONUTS page

[PMID:9405365-11] 11.0 ^11.1 ^11.2 ^11.3 Göhring, F et al. (1997) The novel SAR-binding domain of scaffold attachment factor A (SAF-A) is a target in apoptotic nuclear breakdown. EMBO J. 16 7361-71 PubMed GONUTS page

[PMID:11003645-12] 12.0 ^12.1 ^12.2 ^12.3 Kipp, M et al. (2000) SAF-Box, a conserved protein domain that specifically recognizes scaffold attachment region DNA. Mol. Cell. Biol. 20 7480-9 PubMed GONUTS page

[PMID:1628625-13] 13.0 ^13.1 ^13.2 ^13.3 ^13.4 Kiledjian, M & Dreyfuss, G (1992) Primary structure and binding activity of the hnRNP U protein: binding RNA through RGG box. EMBO J. 11 2655-64 PubMed GONUTS page

[PMID:28622508-14] 14.0 ^14.1 ^14.2 ^14.3 ^14.4 Nozawa, RS et al. (2017) SAF-A Regulates Interphase Chromosome Structure through Oligomerization with Chromatin-Associated RNAs. Cell 169 1214-1227.e18 PubMed GONUTS page

[PMID:21242313-15] 15.0 ^15.1 ^15.2 ^15.3 ^15.4 ^15.5 ^15.6 ^15.7 Ma, N et al. (2011) The nuclear scaffold protein SAF-A is required for kinetochore-microtubule attachment and contributes to the targeting of Aurora-A to mitotic spindles. J. Cell. Sci. 124 394-404 PubMed GONUTS page

[PMID:11909954-16] 16.0 ^16.1 ^16.2 Martens, JH et al. (2002) Scaffold/matrix attachment region elements interact with a p300-scaffold attachment factor A complex and are bound by acetylated nucleosomes. Mol. Cell. Biol. 22 2598-606 PubMed GONUTS page

[PMID:26244333-17] Yamada, N et al. (2015) Xist Exon 7 Contributes to the Stable Localization of Xist RNA on the Inactive X-Chromosome. PLoS Genet. 11 e1005430 PubMed GONUTS page

[PMID:8174554-18] 18.0 ^18.1 ^18.2 ^18.3 ^18.4 ^18.5 ^18.6 ^18.7 Fackelmayer, FO et al. (1994) Nucleic-acid-binding properties of hnRNP-U/SAF-A, a nuclear-matrix protein which binds DNA and RNA in vivo and in vitro. Eur. J. Biochem. 221 749-57 PubMed GONUTS page

[PMID:25986610-19] 19.0 ^19.1 ^19.2 ^19.3 Douglas, P et al. (2015) Phosphorylation of SAF-A/hnRNP-U Serine 59 by Polo-Like Kinase 1 Is Required for Mitosis. Mol. Cell. Biol. 35 2699-713 PubMed GONUTS page

[PMID:21235343-20] Vizlin-Hodzic, D et al. (2011) SAF-A has a role in transcriptional regulation of Oct4 in ES cells through promoter binding. Cell Reprogram 13 13-27 PubMed GONUTS page

[PMID:14608463-21] 21.0 ^21.1 ^21.2 Helbig, R & Fackelmayer, FO (2003) Scaffold attachment factor A (SAF-A) is concentrated in inactive X chromosome territories through its RGG domain. Chromosoma 112 173-82 PubMed GONUTS page

[PMID:8068679-22] 22.0 ^22.1 ^22.2 Fackelmayer, FO & Richter, A (1994) Purification of two isoforms of hnRNP-U and characterization of their nucleic acid binding activity. Biochemistry 33 10416-22 PubMed GONUTS page

[PMID:7993898-23] Jordan, P et al. (1994) Major cell surface-located protein substrates of an ecto-protein kinase are homologs of known nuclear proteins. Biochemistry 33 14696-706 PubMed GONUTS page

[PMID:19946888-24] Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page

[PMID:15121898-25] Villacé, P et al. (2004) The composition of Staufen-containing RNA granules from human cells indicates their role in the regulated transport and translation of messenger RNAs. Nucleic Acids Res. 32 2411-20 PubMed GONUTS page

[PMID:16210410-26] 26.0 ^26.1 Foster, LJ et al. (2005) Differential expression profiling of membrane proteins by quantitative proteomics in a human mesenchymal stem cell line undergoing osteoblast differentiation. Stem Cells 23 1367-77 PubMed GONUTS page

[PMID:22720776-27] Todd, MA & Picketts, DJ (2012) PHF6 interacts with the nucleosome remodeling and deacetylation (NuRD) complex. J. Proteome Res. 11 4326-37 PubMed GONUTS page

[PMID:11991638-28] 28.0 ^28.1 Jurica, MS et al. (2002) Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis. RNA 8 426-39 PubMed GONUTS page

[PMID:19029303-29] 29.0 ^29.1 Weidensdorfer, D et al. (2009) Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs. RNA 15 104-15 PubMed GONUTS page

[PMID:22681889-30] Baltz, AG et al. (2012) The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Mol. Cell 46 674-90 PubMed GONUTS page

[PMID:22658674-31] Castello, A et al. (2012) Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 149 1393-406 PubMed GONUTS page

[PMID:17289661-32] Jønson, L et al. (2007) Molecular composition of IMP1 ribonucleoprotein granules. Mol. Cell Proteomics 6 798-811 PubMed GONUTS page

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HUMAN:HNRPU

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