HUMAN:LA

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	SSB
Protein Name(s)	Lupus La protein La autoantigen La ribonucleoprotein Sjoegren syndrome type B antigen SS-B
External Links
UniProt	P05455
EMBL	X13697 J04205 BT009862 AB451228 AC009967 CH471058 CH471058 BC001289 BC020818 M20328
CCDS	CCDS2237.1
PIR	A31888
RefSeq	NP_001281074.1 NP_003133.1
UniGene	Hs.632535
PDB	1OWX 1S79 1S7A 1YTY 1ZH5 2VOD 2VON 2VOO 2VOP
PDBsum	1OWX 1S79 1S7A 1YTY 1ZH5 2VOD 2VON 2VOO 2VOP
DisProt	DP00229
ProteinModelPortal	P05455
SMR	P05455
BioGrid	112619
DIP	DIP-29750N
IntAct	P05455
MINT	MINT-5002383
STRING	9606.ENSP00000260956
ChEMBL	CHEMBL2040701
PhosphoSite	P05455
DMDM	125985
MaxQB	P05455
PaxDb	P05455
PeptideAtlas	P05455
PRIDE	P05455
DNASU	6741
Ensembl	ENST00000260956 ENST00000409333
GeneID	6741
KEGG	hsa:6741
UCSC	uc002ufk.3
CTD	6741
GeneCards	GC02P170649
HGNC	HGNC:11316
HPA	CAB004643 HPA012385 HPA017287
MIM	109090
neXtProt	NX_P05455
PharmGKB	PA36140
eggNOG	COG5193
GeneTree	ENSGT00760000119379
HOGENOM	HOG000006947
HOVERGEN	HBG001407
InParanoid	P05455
KO	K11090
OMA	FHELFSG
PhylomeDB	P05455
TreeFam	TF314476
Reactome	REACT_22339 REACT_63
ChiTaRS	SSB
EvolutionaryTrace	P05455
GeneWiki	Sjogren_syndrome_antigen_B
GenomeRNAi	6741
NextBio	26296
PMAP-CutDB	P05455
PRO	PR:P05455
Proteomes	UP000005640
Bgee	P05455
CleanEx	HS_SSB
ExpressionAtlas	P05455
Genevestigator	P05455
GO	GO:0005634 GO:0030529 GO:0003729 GO:0000166 GO:0044822 GO:0000049 GO:0008334 GO:0006400
Gene3D	1.10.10.10 3.30.70.330
InterPro	IPR002344 IPR006630 IPR012677 IPR014886 IPR000504 IPR011991
Pfam	PF05383 PF00076 PF08777
PRINTS	PR00302
SMART	SM00715 SM00360
PROSITE	PS50961 PS50102

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0048255	mRNA stabilization	PMID:9154801^[1]	ECO:0000314			P	Figure 9. Effect of La protein on different mRNAs' half lives.	complete
enables	GO:0003723	RNA binding	PMID:3192525^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0071045	nuclear histone mRNA catabolic process	PMID:9154801^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:1990825	sequence-specific mRNA binding	PMID:9154801^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006409	tRNA export from nucleus	PMID:17308035^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0008033	tRNA processing	PMID:17308035^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:17308035^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:17308035^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0008266	poly(U) RNA binding	PMID:15004549^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008266	poly(U) RNA binding	PMID:16387655^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008266	poly(U) RNA binding	PMID:12842046^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
NOT\|enables	GO:0042803	protein homodimerization activity	PMID:12842046^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0001682	tRNA 5'-leader removal	PMID:10983981^[7]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P87058	P	Seeded From UniProt	complete
involved_in	GO:0042780	tRNA 3'-end processing	PMID:10983981^[7]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P87058	P	Seeded From UniProt	complete
enables	GO:0000049	tRNA binding	PMID:10983981^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0075522	IRES-dependent viral translational initiation	PMID:12384597^[8]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0000784	nuclear chromosome, telomeric region	PMID:19135898^[9]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:1903608	protein localization to cytoplasmic stress granule	PMID:24965446^[10]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:24965446^[10]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:22681889^[11]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:22658674^[12]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P32067 ensembl:ENSMUSP00000130313	C	Seeded From UniProt	complete
enables	GO:0003723	RNA binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P32067 ensembl:ENSMUSP00000130313	F	Seeded From UniProt	complete
enables	GO:0003676	nucleic acid binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000504 InterPro:IPR035979	F	Seeded From UniProt	complete
enables	GO:0003723	RNA binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002344 InterPro:IPR014886	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:IPR002344	C	Seeded From UniProt	complete
involved_in	GO:0006396	RNA processing	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002344	P	Seeded From UniProt	complete
part_of	GO:1990904	ribonucleoprotein complex	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002344	C	Seeded From UniProt	complete
part_of	GO:1990904	ribonucleoprotein complex	PMID:3192525^[2]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0008334	histone mRNA metabolic process	PMID:9154801^[1]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006400	tRNA modification	PMID:10983981^[7]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0003729	mRNA binding	PMID:9154801^[1]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0000049	tRNA binding	PMID:10983981^[7]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	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: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
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Notes

References

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

↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 McLaren, RS et al. (1997) Human La protein: a stabilizer of histone mRNA. Mol. Cell. Biol. 17 3028-36 PubMed GONUTS page
↑ ^2.0 ^2.1 Chambers, JC et al. (1988) Genomic structure and amino acid sequence domains of the human La autoantigen. J. Biol. Chem. 263 18043-51 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 Bayfield, MA et al. (2007) Conservation of a masked nuclear export activity of La proteins and its effects on tRNA maturation. Mol. Cell. Biol. 27 3303-12 PubMed GONUTS page
↑ Alfano, C et al. (2004) Structural analysis of cooperative RNA binding by the La motif and central RRM domain of human La protein. Nat. Struct. Mol. Biol. 11 323-9 PubMed GONUTS page
↑ Teplova, M et al. (2006) Structural basis for recognition and sequestration of UUU(OH) 3' temini of nascent RNA polymerase III transcripts by La, a rheumatic disease autoantigen. Mol. Cell 21 75-85 PubMed GONUTS page
↑ ^6.0 ^6.1 Jacks, A et al. (2003) Structure of the C-terminal domain of human La protein reveals a novel RNA recognition motif coupled to a helical nuclear retention element. Structure 11 833-43 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 ^7.4 Intine, RV et al. (2000) Control of transfer RNA maturation by phosphorylation of the human La antigen on serine 366. Mol. Cell 6 339-48 PubMed GONUTS page
↑ Ray, PS & Das, S (2002) La autoantigen is required for the internal ribosome entry site-mediated translation of Coxsackievirus B3 RNA. Nucleic Acids Res. 30 4500-8 PubMed GONUTS page
↑ Déjardin, J & Kingston, RE (2009) Purification of proteins associated with specific genomic Loci. Cell 136 175-86 PubMed GONUTS page
↑ ^10.0 ^10.1 Jefferson, M et al. (2014) Host factors that interact with the pestivirus N-terminal protease, Npro, are components of the ribonucleoprotein complex. J. Virol. 88 10340-53 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

[PMID:9154801-1] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 McLaren, RS et al. (1997) Human La protein: a stabilizer of histone mRNA. Mol. Cell. Biol. 17 3028-36 PubMed GONUTS page

[PMID:3192525-2] 2.0 ^2.1 Chambers, JC et al. (1988) Genomic structure and amino acid sequence domains of the human La autoantigen. J. Biol. Chem. 263 18043-51 PubMed GONUTS page

[PMID:17308035-3] 3.0 ^3.1 ^3.2 ^3.3 Bayfield, MA et al. (2007) Conservation of a masked nuclear export activity of La proteins and its effects on tRNA maturation. Mol. Cell. Biol. 27 3303-12 PubMed GONUTS page

[PMID:15004549-4] Alfano, C et al. (2004) Structural analysis of cooperative RNA binding by the La motif and central RRM domain of human La protein. Nat. Struct. Mol. Biol. 11 323-9 PubMed GONUTS page

[PMID:16387655-5] Teplova, M et al. (2006) Structural basis for recognition and sequestration of UUU(OH) 3' temini of nascent RNA polymerase III transcripts by La, a rheumatic disease autoantigen. Mol. Cell 21 75-85 PubMed GONUTS page

[PMID:12842046-6] 6.0 ^6.1 Jacks, A et al. (2003) Structure of the C-terminal domain of human La protein reveals a novel RNA recognition motif coupled to a helical nuclear retention element. Structure 11 833-43 PubMed GONUTS page

[PMID:10983981-7] 7.0 ^7.1 ^7.2 ^7.3 ^7.4 Intine, RV et al. (2000) Control of transfer RNA maturation by phosphorylation of the human La antigen on serine 366. Mol. Cell 6 339-48 PubMed GONUTS page

[PMID:12384597-8] Ray, PS & Das, S (2002) La autoantigen is required for the internal ribosome entry site-mediated translation of Coxsackievirus B3 RNA. Nucleic Acids Res. 30 4500-8 PubMed GONUTS page

[PMID:19135898-9] Déjardin, J & Kingston, RE (2009) Purification of proteins associated with specific genomic Loci. Cell 136 175-86 PubMed GONUTS page

[PMID:24965446-10] 10.0 ^10.1 Jefferson, M et al. (2014) Host factors that interact with the pestivirus N-terminal protease, Npro, are components of the ribonucleoprotein complex. J. Virol. 88 10340-53 PubMed GONUTS page

[PMID:22681889-11] 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:22658674-12] Castello, A et al. (2012) Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 149 1393-406 PubMed GONUTS page

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HUMAN:LA

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