HUMAN:VIME

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	VIM
Protein Name(s)	Vimentin
External Links
UniProt	P08670
EMBL	M14144 X56134 AF328728 Z19554 AK056766 AK097336 AK290643 CR407690 AK222507 AK222602 EF445046 EF445046 AL133415 CH471072 CH471072 BC000163 BC030573 BC066956 X16478 M18895 M18888 M18889 M18890 M18891 M18892 M18893 M18894 M25246
CCDS	CCDS7120.1
PIR	S13115
RefSeq	NP_003371.2 XP_006717563.1
UniGene	Hs.455493 Hs.691131
PDB	1GK4 1GK6 1GK7 3G1E 3KLT 3S4R 3SSU 3SWK 3TRT 3UF1 4MCY 4MCZ 4MD0 4MD5 4MDI 4MDJ
PDBsum	1GK4 1GK6 1GK7 3G1E 3KLT 3S4R 3SSU 3SWK 3TRT 3UF1 4MCY 4MCZ 4MD0 4MD5 4MDI 4MDJ
ProteinModelPortal	P08670
SMR	P08670
BioGrid	113272
DIP	DIP-32507N
IntAct	P08670
MINT	MINT-118802
PhosphoSite	P08670
DMDM	55977767
DOSAC-COBS-2DPAGE	P08670
OGP	P08670
REPRODUCTION-2DPAGE	IPI00418471 P08670
SWISS-2DPAGE	P08670
UCD-2DPAGE	P08670
MaxQB	P08670
PaxDb	P08670
PeptideAtlas	P08670
PRIDE	P08670
DNASU	7431
Ensembl	ENST00000224237 ENST00000544301
GeneID	7431
KEGG	hsa:7431
UCSC	uc001iou.2
CTD	7431
GeneCards	GC10P017270
H-InvDB	HIX0035657
HGNC	HGNC:12692
HPA	CAB000080 CAB058687 HPA001762
MIM	116300 193060
neXtProt	NX_P08670
Orphanet	98984
PharmGKB	PA37311
eggNOG	NOG146769
HOVERGEN	HBG013015
InParanoid	P08670
KO	K07606
OMA	INTEFKA
OrthoDB	EOG7FV3Q8
PhylomeDB	P08670
TreeFam	TF330122
Reactome	REACT_13541 REACT_16969
ChiTaRS	VIM
EvolutionaryTrace	P08670
GeneWiki	Vimentin
GenomeRNAi	7431
NextBio	29104
PMAP-CutDB	P08670
PRO	PR:P08670
Proteomes	UP000005640
Bgee	P08670
ExpressionAtlas	P08670
Genevestigator	P08670
GO	GO:0031252 GO:0005737 GO:0005856 GO:0005829 GO:0070062 GO:0005925 GO:0005882 GO:0045111 GO:0043005 GO:0005777 GO:0005886 GO:0003725 GO:0001948 GO:0042802 GO:0008022 GO:0097110 GO:0005200 GO:0005212 GO:0006915 GO:0014002 GO:0060020 GO:0006921 GO:0006928 GO:0045109 GO:0070307 GO:0030049 GO:0010977 GO:0010628 GO:0016032
InterPro	IPR001664 IPR006821 IPR018039 IPR027699
PANTHER	PTHR23239 PTHR23239:SF27
Pfam	PF00038 PF04732
PROSITE	PS00226

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
involved_in	GO:0071222	cellular response to lipopolysaccharide	PMID:27812135^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0071225	cellular response to muramyl dipeptide	PMID:27812135^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043488	regulation of mRNA stability	PMID:21746880^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045727	positive regulation of translation	PMID:21746880^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032967	positive regulation of collagen biosynthetic process	PMID:21746880^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21746880^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0019904	protein domain specific binding	PMID:21746880^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9BRS8	F		Seeded From UniProt	complete
part_of	GO:1990904	ribonucleoprotein complex	PMID:21746880^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005844	polysome	PMID:21746880^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005844	polysome	PMID:20603131^[3]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:27919618^[4]	ECO:0000314	direct assay evidence used in manual assertion		C	exists_during:(GO:0071257) part_of:(CL:0000312)	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21914078^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:15846844^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:1990254	keratin filament binding	PMID:15846844^[6]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P05787	F		Seeded From UniProt	complete
part_of	GO:0005925	focal adhesion	PMID:21423176^[7]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000057)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:20458337^[8]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000639)	Seeded From UniProt	complete
part_of	GO:0005882	intermediate filament	PMID:29496907^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:29496907^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0097110	scaffold protein binding	PMID:10852826^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q99959	F		Seeded From UniProt	complete
enables	GO:0097110	scaffold protein binding	PMID:10852826^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q13835	F		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:21362503^[11]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0002367)	Seeded From UniProt	complete
part_of	GO:0005882	intermediate filament	PMID:11889032^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005777	peroxisome	PMID:17881773^[13]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(UBERON:0000473) part_of:(CL:0000216)	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:9150946^[14]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0005200	structural constituent of cytoskeleton	PMID:11889032^[12]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005856	cytoskeleton	PMID:16769727^[15]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003725	double-stranded RNA binding	PMID:21266579^[16]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:22869704^[17]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P08670	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:21900206^[18]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P08670	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:17050693^[19]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P08670	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:16169070^[20]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P08670	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:15383276^[21]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P08670	F		Seeded From UniProt	complete
involved_in	GO:0071346	cellular response to interferon-gamma	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20152 ensembl:ENSMUSP00000028062	P		Seeded From UniProt	complete
involved_in	GO:0070307	lens fiber cell development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20152 ensembl:ENSMUSP00000028062	P		Seeded From UniProt	complete
involved_in	GO:0060395	SMAD protein signal transduction	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20152 ensembl:ENSMUSP00000028062	P		Seeded From UniProt	complete
involved_in	GO:0060020	Bergmann glial cell differentiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20152 ensembl:ENSMUSP00000028062	P		Seeded From UniProt	complete
part_of	GO:0045335	phagocytic vesicle	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20152 ensembl:ENSMUSP00000028062	C		Seeded From UniProt	complete
involved_in	GO:0045109	intermediate filament organization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20152 ensembl:ENSMUSP00000028062	P		Seeded From UniProt	complete
involved_in	GO:0045103	intermediate filament-based process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20152 ensembl:ENSMUSP00000028062	P		Seeded From UniProt	complete
part_of	GO:0043005	neuron projection	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20152 ensembl:ENSMUSP00000028062	C		Seeded From UniProt	complete
part_of	GO:0042995	cell projection	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20152 ensembl:ENSMUSP00000028062	C		Seeded From UniProt	complete
part_of	GO:0031252	cell leading edge	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20152 ensembl:ENSMUSP00000028062	C		Seeded From UniProt	complete
involved_in	GO:0014002	astrocyte development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20152 ensembl:ENSMUSP00000028062	P		Seeded From UniProt	complete
involved_in	GO:0010977	negative regulation of neuron projection development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20152 ensembl:ENSMUSP00000028062	P		Seeded From UniProt	complete
involved_in	GO:0010628	positive regulation of gene expression	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20152 ensembl:ENSMUSP00000028062	P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20152 ensembl:ENSMUSP00000028062	C		Seeded From UniProt	complete
part_of	GO:0005882	intermediate filament	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20152 ensembl:ENSMUSP00000028062	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20152 ensembl:ENSMUSP00000028062	C		Seeded From UniProt	complete
enables	GO:0005212	structural constituent of eye lens	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20152 ensembl:ENSMUSP00000028062	F		Seeded From UniProt	complete
enables	GO:0005198	structural molecule activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20152 ensembl:ENSMUSP00000028062	F		Seeded From UniProt	complete
enables	GO:0005198	structural molecule activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001664	F		Seeded From UniProt	complete
part_of	GO:0005882	intermediate filament	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001664 InterPro:IPR006821 InterPro:IPR027699	C		Seeded From UniProt	complete
part_of	GO:0005856	cytoskeleton	PMID:16130169^[22]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-390597 Reactome:R-HSA-390595 Reactome:R-HSA-390593 Reactome:R-HSA-350319 Reactome:R-HSA-350318 Reactome:R-HSA-201628 Reactome:R-HSA-6790041 Reactome:R-HSA-390598	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0030049	muscle filament sliding	Reactome:R-HSA-390522	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0019221	cytokine-mediated signaling pathway	Reactome:R-HSA-6785807	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		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:0005634	nucleus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539	C		Seeded From UniProt	complete
part_of	GO:0005856	cytoskeleton	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0206 UniProtKB-SubCell:SL-0090	C		Seeded From UniProt	complete
part_of	GO:0005882	intermediate filament	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0403	C		Seeded From UniProt	complete
involved_in	GO:0016032	viral process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0945	P		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
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Notes

References

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

↑ ^1.0 ^1.1 Thiébaut, R et al. (2016) Characterization and Genetic Analyses of New Genes Coding for NOD2 Interacting Proteins. PLoS ONE 11 e0165420 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 ^2.6 Challa, AA & Stefanovic, B (2011) A novel role of vimentin filaments: binding and stabilization of collagen mRNAs. Mol. Cell. Biol. 31 3773-89 PubMed GONUTS page
↑ Cai, L et al. (2010) Nonmuscle myosin-dependent synthesis of type I collagen. J. Mol. Biol. 401 564-78 PubMed GONUTS page
↑ Yan, T et al. (2017) Electric field-induced suppression of PTEN drives epithelial-to-mesenchymal transition via mTORC1 activation. J. Dermatol. Sci. 85 96-105 PubMed GONUTS page
↑ Ghosh, S et al. (2011) Association of filamin A and vimentin with hepatitis C virus proteins in infected human hepatocytes. J. Viral Hepat. 18 e568-77 PubMed GONUTS page
↑ ^6.0 ^6.1 Kang, SM et al. (2005) Proteomic profiling of cellular proteins interacting with the hepatitis C virus core protein. Proteomics 5 2227-37 PubMed GONUTS page
↑ Kuo, JC et al. (2011) Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation. Nat. Cell Biol. 13 383-93 PubMed GONUTS page
↑ Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page
↑ ^9.0 ^9.1 Goel, RK et al. (2018) Phosphoproteomics Analysis Identifies Novel Candidate Substrates of the Nonreceptor Tyrosine Kinase, rc-elated Kinase Lacking C-terminal Regulatory Tyrosine and N-terminal yristoylation ites (SRMS). Mol. Cell Proteomics 17 925-947 PubMed GONUTS page
↑ ^10.0 ^10.1 Hofmann, I et al. (2000) Interaction of plakophilins with desmoplakin and intermediate filament proteins: an in vitro analysis. J. Cell. Sci. 113 ( Pt 13) 2471-83 PubMed GONUTS page
↑ Stamer, WD et al. (2011) Protein profile of exosomes from trabecular meshwork cells. J Proteomics 74 796-804 PubMed GONUTS page
↑ ^12.0 ^12.1 Strelkov, SV et al. (2002) Conserved segments 1A and 2B of the intermediate filament dimer: their atomic structures and role in filament assembly. EMBO J. 21 1255-66 PubMed GONUTS page
↑ Nenicu, A et al. (2007) Peroxisomes in human and mouse testis: differential expression of peroxisomal proteins in germ cells and distinct somatic cell types of the testis. Biol. Reprod. 77 1060-72 PubMed GONUTS page
↑ Rasmussen, RK et al. () Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2. Electrophoresis 18 588-98 PubMed GONUTS page
↑ Stefansson, B & Brautigan, DL (2006) Protein phosphatase 6 subunit with conserved Sit4-associated protein domain targets IkappaBepsilon. J. Biol. Chem. 281 22624-34 PubMed GONUTS page
↑ Watanabe, A et al. (2011) Raftlin is involved in the nucleocapture complex to induce poly(I:C)-mediated TLR3 activation. J. Biol. Chem. 286 10702-11 PubMed GONUTS page
↑ Chernyatina, AA et al. (2012) Atomic structure of the vimentin central α-helical domain and its implications for intermediate filament assembly. Proc. Natl. Acad. Sci. U.S.A. 109 13620-5 PubMed GONUTS page
↑ Vinayagam, A et al. (2011) A directed protein interaction network for investigating intracellular signal transduction. Sci Signal 4 rs8 PubMed GONUTS page
↑ Sokolova, AV et al. (2006) Monitoring intermediate filament assembly by small-angle x-ray scattering reveals the molecular architecture of assembly intermediates. Proc. Natl. Acad. Sci. U.S.A. 103 16206-11 PubMed GONUTS page
↑ Stelzl, U et al. (2005) A human protein-protein interaction network: a resource for annotating the proteome. Cell 122 957-68 PubMed GONUTS page
↑ Goehler, H et al. (2004) A protein interaction network links GIT1, an enhancer of huntingtin aggregation, to Huntington's disease. Mol. Cell 15 853-65 PubMed GONUTS page
↑ Bruneel, A et al. (2005) Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis. Proteomics 5 3876-84 PubMed GONUTS page

[PMID:27812135-1] 1.0 ^1.1 Thiébaut, R et al. (2016) Characterization and Genetic Analyses of New Genes Coding for NOD2 Interacting Proteins. PLoS ONE 11 e0165420 PubMed GONUTS page

[PMID:21746880-2] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 ^2.6 Challa, AA & Stefanovic, B (2011) A novel role of vimentin filaments: binding and stabilization of collagen mRNAs. Mol. Cell. Biol. 31 3773-89 PubMed GONUTS page

[PMID:20603131-3] Cai, L et al. (2010) Nonmuscle myosin-dependent synthesis of type I collagen. J. Mol. Biol. 401 564-78 PubMed GONUTS page

[PMID:27919618-4] Yan, T et al. (2017) Electric field-induced suppression of PTEN drives epithelial-to-mesenchymal transition via mTORC1 activation. J. Dermatol. Sci. 85 96-105 PubMed GONUTS page

[PMID:21914078-5] Ghosh, S et al. (2011) Association of filamin A and vimentin with hepatitis C virus proteins in infected human hepatocytes. J. Viral Hepat. 18 e568-77 PubMed GONUTS page

[PMID:15846844-6] 6.0 ^6.1 Kang, SM et al. (2005) Proteomic profiling of cellular proteins interacting with the hepatitis C virus core protein. Proteomics 5 2227-37 PubMed GONUTS page

[PMID:21423176-7] Kuo, JC et al. (2011) Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation. Nat. Cell Biol. 13 383-93 PubMed GONUTS page

[PMID:20458337-8] Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page

[PMID:29496907-9] 9.0 ^9.1 Goel, RK et al. (2018) Phosphoproteomics Analysis Identifies Novel Candidate Substrates of the Nonreceptor Tyrosine Kinase, rc-elated Kinase Lacking C-terminal Regulatory Tyrosine and N-terminal yristoylation ites (SRMS). Mol. Cell Proteomics 17 925-947 PubMed GONUTS page

[PMID:10852826-10] 10.0 ^10.1 Hofmann, I et al. (2000) Interaction of plakophilins with desmoplakin and intermediate filament proteins: an in vitro analysis. J. Cell. Sci. 113 ( Pt 13) 2471-83 PubMed GONUTS page

[PMID:21362503-11] Stamer, WD et al. (2011) Protein profile of exosomes from trabecular meshwork cells. J Proteomics 74 796-804 PubMed GONUTS page

[PMID:11889032-12] 12.0 ^12.1 Strelkov, SV et al. (2002) Conserved segments 1A and 2B of the intermediate filament dimer: their atomic structures and role in filament assembly. EMBO J. 21 1255-66 PubMed GONUTS page

[PMID:17881773-13] Nenicu, A et al. (2007) Peroxisomes in human and mouse testis: differential expression of peroxisomal proteins in germ cells and distinct somatic cell types of the testis. Biol. Reprod. 77 1060-72 PubMed GONUTS page

[PMID:9150946-14] Rasmussen, RK et al. () Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2. Electrophoresis 18 588-98 PubMed GONUTS page

[PMID:16769727-15] Stefansson, B & Brautigan, DL (2006) Protein phosphatase 6 subunit with conserved Sit4-associated protein domain targets IkappaBepsilon. J. Biol. Chem. 281 22624-34 PubMed GONUTS page

[PMID:21266579-16] Watanabe, A et al. (2011) Raftlin is involved in the nucleocapture complex to induce poly(I:C)-mediated TLR3 activation. J. Biol. Chem. 286 10702-11 PubMed GONUTS page

[PMID:22869704-17] Chernyatina, AA et al. (2012) Atomic structure of the vimentin central α-helical domain and its implications for intermediate filament assembly. Proc. Natl. Acad. Sci. U.S.A. 109 13620-5 PubMed GONUTS page

[PMID:21900206-18] Vinayagam, A et al. (2011) A directed protein interaction network for investigating intracellular signal transduction. Sci Signal 4 rs8 PubMed GONUTS page

[PMID:17050693-19] Sokolova, AV et al. (2006) Monitoring intermediate filament assembly by small-angle x-ray scattering reveals the molecular architecture of assembly intermediates. Proc. Natl. Acad. Sci. U.S.A. 103 16206-11 PubMed GONUTS page

[PMID:16169070-20] Stelzl, U et al. (2005) A human protein-protein interaction network: a resource for annotating the proteome. Cell 122 957-68 PubMed GONUTS page

[PMID:15383276-21] Goehler, H et al. (2004) A protein interaction network links GIT1, an enhancer of huntingtin aggregation, to Huntington's disease. Mol. Cell 15 853-65 PubMed GONUTS page

[PMID:16130169-22] Bruneel, A et al. (2005) Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis. Proteomics 5 3876-84 PubMed GONUTS page

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HUMAN:VIME

Contents

Annotations

Notes

References

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