MOUSE:VINC

Species (Taxon ID)	Mus musculus (Mouse). (10090)
Gene Name(s)	Vcl
Protein Name(s)	Vinculin Metavinculin
External Links
UniProt	Q64727
EMBL	L13300 L13299 L18880 AK035184 AK077850 BC008520 BC008554
CCDS	CCDS26860.1
PIR	A60965 T10108
RefSeq	NP_033528.3
UniGene	Mm.279361
ProteinModelPortal	Q64727
SMR	Q64727
BioGrid	204506
IntAct	Q64727
MINT	MINT-1634466
PhosphoSite	Q64727
REPRODUCTION-2DPAGE	Q64727
MaxQB	Q64727
PaxDb	Q64727
PRIDE	Q64727
Ensembl	ENSMUST00000022369
GeneID	22330
KEGG	mmu:22330
UCSC	uc007skz.1
CTD	7414
MGI	MGI:98927
eggNOG	NOG329927
GeneTree	ENSGT00550000074411
HOGENOM	HOG000007828
HOVERGEN	HBG079758
InParanoid	Q64727
KO	K05700
OMA	YDEDEWD
OrthoDB	EOG73NG2V
PhylomeDB	Q64727
TreeFam	TF313686
Reactome	REACT_235059
ChiTaRS	Vcl
NextBio	302571
PMAP-CutDB	Q64727
PRO	PR:Q64727
Proteomes	UP000000589
Bgee	Q64727
CleanEx	MM_VCL
Genevestigator	Q64727
GO	GO:0015629 GO:0005912 GO:0005911 GO:0043034 GO:0005737 GO:0070062 GO:0005916 GO:0005925 GO:0005886 GO:0043234 GO:0005198 GO:0034333 GO:0043297 GO:0048675 GO:0007155 GO:0090136 GO:0030032 GO:0002009 GO:0034394 GO:0030334
InterPro	IPR017997 IPR006077 IPR000633
PANTHER	PTHR18914 PTHR18914:SF22
Pfam	PF01044
SUPFAM	SSF47220
PROSITE	PS00663 PS00664

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
part_of	GO:0042383	sarcolemma	PMID:26359501^[1]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:1990357	terminal web	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P12003	C		Seeded From UniProt	complete
part_of	GO:0090637	inner dense plaque of desmosome	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P12003	C		Seeded From UniProt	complete
part_of	GO:0090636	outer dense plaque of desmosome	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P12003	C		Seeded From UniProt	complete
part_of	GO:0005915	zonula adherens	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P12003	C		Seeded From UniProt	complete
part_of	GO:0005903	brush border	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P12003	C		Seeded From UniProt	complete
part_of	GO:0005925	focal adhesion	PMID:24036928^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:24036928^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005925	focal adhesion	PMID:15883197^[3]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0090136	epithelial cell-cell adhesion	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P18206	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0048675	axon extension	PMID:24623780^[4]	ECO:0000316	genetic interaction evidence used in manual assertion	MGI:MGI:106658 MGI:MGI:1861437	P	occurs_in:(CL:0002608)	Seeded From UniProt	complete
enables	GO:0045294	alpha-catenin binding	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P18206	F		Seeded From UniProt	complete
part_of	GO:0045121	membrane raft	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P18206	C		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0043297	apical junction assembly	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P18206	P		Seeded From UniProt	complete
part_of	GO:0043034	costamere	PMID:15128702^[5]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000188)	Seeded From UniProt	complete
part_of	GO:0043034	costamere	GO_REF:0000008	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P18206	C		Seeded From UniProt	complete
part_of	GO:0042383	sarcolemma	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:1311217	C		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0034394	protein localization to cell surface	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P18206	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0034333	adherens junction assembly	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P18206	P		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P18206	C		Seeded From UniProt	complete
enables	GO:0031625	ubiquitin protein ligase binding	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P18206	F		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0030334	regulation of cell migration	PMID:12473693^[6]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0030032	lamellipodium assembly	PMID:12473693^[6]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0030018	Z disc	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:1311217	C		Seeded From UniProt	complete
enables	GO:0017048	Rho GTPase binding	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:1311217	F		Seeded From UniProt	complete
part_of	GO:0015629	actin cytoskeleton	PMID:21048959^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0014704	intercalated disc	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:1311217	C		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0007155	cell adhesion	PMID:12473693^[6]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005925	focal adhesion	PMID:25217619^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005925	focal adhesion	PMID:29162887^[9]	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P18206	C		Seeded From UniProt	complete
part_of	GO:0005925	focal adhesion	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P18206	C		Seeded From UniProt	complete
colocalizes_with	GO:0005925	focal adhesion	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:1311217	C		Seeded From UniProt	complete
part_of	GO:0005916	fascia adherens	PMID:16481394^[10]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(EMAPA:17339) part_of:(CL:0000746)	Seeded From UniProt	complete
part_of	GO:0005916	fascia adherens	PMID:11732910^[11]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005913	cell-cell adherens junction	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P18206	C		Seeded From UniProt	complete
part_of	GO:0005912	adherens junction	PMID:12203715^[12]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000188)	Seeded From UniProt	complete
part_of	GO:0005911	cell-cell junction	PMID:22984613^[13]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005911	cell-cell junction	PMID:14657280^[14]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:16481394^[10]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(EMAPA:17339) part_of:(CL:0000746)	Seeded From UniProt	complete
colocalizes_with	GO:0005884	actin filament	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:1311217	C		Seeded From UniProt	complete
enables	GO:0002162	dystroglycan binding	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P18206	F		Seeded From UniProt	complete
part_of	GO:0002102	podosome	PMID:17893324^[15]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000057)	Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0002009	morphogenesis of an epithelium	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P18206	P		Seeded From UniProt	complete
colocalizes_with	GO:0001725	stress fiber	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:1311217	C		Seeded From UniProt	complete
involved_in	GO:0090136	epithelial cell-cell adhesion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P18206 ensembl:ENSP00000211998	P		Seeded From UniProt	complete
enables	GO:0045294	alpha-catenin binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P18206 ensembl:ENSP00000211998	F		Seeded From UniProt	complete
involved_in	GO:0043297	apical junction assembly	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P18206 ensembl:ENSP00000211998	P		Seeded From UniProt	complete
part_of	GO:0043034	costamere	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P18206 ensembl:ENSP00000211998	C		Seeded From UniProt	complete
involved_in	GO:0034394	protein localization to cell surface	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P18206 ensembl:ENSP00000211998	P		Seeded From UniProt	complete
involved_in	GO:0034333	adherens junction assembly	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P18206 ensembl:ENSP00000211998	P		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P18206 ensembl:ENSP00000211998	C		Seeded From UniProt	complete
enables	GO:0031625	ubiquitin protein ligase binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P18206 ensembl:ENSP00000211998	F		Seeded From UniProt	complete
part_of	GO:0005925	focal adhesion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P18206 ensembl:ENSP00000211998	C		Seeded From UniProt	complete
part_of	GO:0005913	cell-cell adherens junction	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P18206 ensembl:ENSP00000211998	C		Seeded From UniProt	complete
enables	GO:0003779	actin binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P18206 ensembl:ENSP00000211998	F		Seeded From UniProt	complete
enables	GO:0002162	dystroglycan binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P18206 ensembl:ENSP00000211998	F		Seeded From UniProt	complete
involved_in	GO:0002009	morphogenesis of an epithelium	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P18206 ensembl:ENSP00000211998	P		Seeded From UniProt	complete
part_of	GO:0005925	focal adhesion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:V9HWK2 ensembl:ENSP00000211998	C		Seeded From UniProt	complete
enables	GO:0003779	actin binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR017997	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:IPR000633	F		Seeded From UniProt	complete
involved_in	GO:0007155	cell adhesion	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000633 InterPro:IPR006077 InterPro:IPR036723	P		Seeded From UniProt	complete
part_of	GO:0015629	actin cytoskeleton	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000633	C		Seeded From UniProt	complete
enables	GO:0051015	actin filament binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006077 InterPro:IPR036723	F		Seeded From UniProt	complete
involved_in	GO:0007155	cell adhesion	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0130	P		Seeded From UniProt	complete
enables	GO:0003779	actin binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0009	F		Seeded From UniProt	complete
part_of	GO:0030054	cell junction	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0965	C		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963	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:0005886	plasma membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1003 UniProtKB-SubCell:SL-0039	C		Seeded From UniProt	complete
part_of	GO:0042383	sarcolemma	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0238	C		Seeded From UniProt	complete
part_of	GO:0005925	focal adhesion	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0118	C		Seeded From UniProt	complete
part_of	GO:0005912	adherens junction	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0009	C		Seeded From UniProt	complete
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Notes

References

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

↑ Cattin, ME et al. (2015) Deletion of MLIP (muscle-enriched A-type lamin-interacting protein) leads to cardiac hyperactivation of Akt/mammalian target of rapamycin (mTOR) and impaired cardiac adaptation. J. Biol. Chem. 290 26699-714 PubMed GONUTS page
↑ ^2.0 ^2.1 Bianchi-Smiraglia, A et al. (2013) Integrin-β5 and zyxin mediate formation of ventral stress fibers in response to transforming growth factor β. Cell Cycle 12 3377-89 PubMed GONUTS page
↑ Chen, H et al. (2005) Spatial distribution and functional significance of activated vinculin in living cells. J. Cell Biol. 169 459-70 PubMed GONUTS page
↑ Li, CL et al. (2014) SRF phosphorylation by glycogen synthase kinase-3 promotes axon growth in hippocampal neurons. J. Neurosci. 34 4027-42 PubMed GONUTS page
↑ Mientjes, EJ et al. (2004) Fxr1 knockout mice show a striated muscle phenotype: implications for Fxr1p function in vivo. Hum. Mol. Genet. 13 1291-302 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 DeMali, KA et al. (2002) Recruitment of the Arp2/3 complex to vinculin: coupling membrane protrusion to matrix adhesion. J. Cell Biol. 159 881-91 PubMed GONUTS page
↑ Pirih, FQ et al. (2010) Parathyroid hormone mediates hematopoietic cell expansion through interleukin-6. PLoS ONE 5 e13657 PubMed GONUTS page
↑ Cariaga-Martínez, AE et al. (2014) Phosphoinositide 3-kinase p85beta regulates invadopodium formation. Biol Open 3 924-36 PubMed GONUTS page
↑ Rogg, M et al. (2017) The WD40-domain containing protein CORO2B is specifically enriched in glomerular podocytes and regulates the ventral actin cytoskeleton. Sci Rep 7 15910 PubMed GONUTS page
↑ ^10.0 ^10.1 Bennett, PM et al. (2006) The transitional junction: a new functional subcellular domain at the intercalated disc. Mol. Biol. Cell 17 2091-100 PubMed GONUTS page
↑ Zhang, JQ et al. (2001) Ultrastructural and biochemical localization of N-RAP at the interface between myofibrils and intercalated disks in the mouse heart. Biochemistry 40 14898-906 PubMed GONUTS page
↑ Sinn, HW et al. (2002) Localization of the novel Xin protein to the adherens junction complex in cardiac and skeletal muscle during development. Dev. Dyn. 225 1-13 PubMed GONUTS page
↑ Balasubramanian, S et al. (2012) β3 integrin in cardiac fibroblast is critical for extracellular matrix accumulation during pressure overload hypertrophy in mouse. PLoS ONE 7 e45076 PubMed GONUTS page
↑ Gavard, J et al. (2004) Lamellipodium extension and cadherin adhesion: two cell responses to cadherin activation relying on distinct signalling pathways. J. Cell. Sci. 117 257-70 PubMed GONUTS page
↑ Bharti, S et al. (2007) Src-dependent phosphorylation of ASAP1 regulates podosomes. Mol. Cell. Biol. 27 8271-83 PubMed GONUTS page

[PMID:26359501-1] Cattin, ME et al. (2015) Deletion of MLIP (muscle-enriched A-type lamin-interacting protein) leads to cardiac hyperactivation of Akt/mammalian target of rapamycin (mTOR) and impaired cardiac adaptation. J. Biol. Chem. 290 26699-714 PubMed GONUTS page

[PMID:24036928-2] 2.0 ^2.1 Bianchi-Smiraglia, A et al. (2013) Integrin-β5 and zyxin mediate formation of ventral stress fibers in response to transforming growth factor β. Cell Cycle 12 3377-89 PubMed GONUTS page

[PMID:15883197-3] Chen, H et al. (2005) Spatial distribution and functional significance of activated vinculin in living cells. J. Cell Biol. 169 459-70 PubMed GONUTS page

[PMID:24623780-4] Li, CL et al. (2014) SRF phosphorylation by glycogen synthase kinase-3 promotes axon growth in hippocampal neurons. J. Neurosci. 34 4027-42 PubMed GONUTS page

[PMID:15128702-5] Mientjes, EJ et al. (2004) Fxr1 knockout mice show a striated muscle phenotype: implications for Fxr1p function in vivo. Hum. Mol. Genet. 13 1291-302 PubMed GONUTS page

[PMID:12473693-6] 6.0 ^6.1 ^6.2 DeMali, KA et al. (2002) Recruitment of the Arp2/3 complex to vinculin: coupling membrane protrusion to matrix adhesion. J. Cell Biol. 159 881-91 PubMed GONUTS page

[PMID:21048959-7] Pirih, FQ et al. (2010) Parathyroid hormone mediates hematopoietic cell expansion through interleukin-6. PLoS ONE 5 e13657 PubMed GONUTS page

[PMID:25217619-8] Cariaga-Martínez, AE et al. (2014) Phosphoinositide 3-kinase p85beta regulates invadopodium formation. Biol Open 3 924-36 PubMed GONUTS page

[PMID:29162887-9] Rogg, M et al. (2017) The WD40-domain containing protein CORO2B is specifically enriched in glomerular podocytes and regulates the ventral actin cytoskeleton. Sci Rep 7 15910 PubMed GONUTS page

[PMID:16481394-10] 10.0 ^10.1 Bennett, PM et al. (2006) The transitional junction: a new functional subcellular domain at the intercalated disc. Mol. Biol. Cell 17 2091-100 PubMed GONUTS page

[PMID:11732910-11] Zhang, JQ et al. (2001) Ultrastructural and biochemical localization of N-RAP at the interface between myofibrils and intercalated disks in the mouse heart. Biochemistry 40 14898-906 PubMed GONUTS page

[PMID:12203715-12] Sinn, HW et al. (2002) Localization of the novel Xin protein to the adherens junction complex in cardiac and skeletal muscle during development. Dev. Dyn. 225 1-13 PubMed GONUTS page

[PMID:22984613-13] Balasubramanian, S et al. (2012) β3 integrin in cardiac fibroblast is critical for extracellular matrix accumulation during pressure overload hypertrophy in mouse. PLoS ONE 7 e45076 PubMed GONUTS page

[PMID:14657280-14] Gavard, J et al. (2004) Lamellipodium extension and cadherin adhesion: two cell responses to cadherin activation relying on distinct signalling pathways. J. Cell. Sci. 117 257-70 PubMed GONUTS page

[PMID:17893324-15] Bharti, S et al. (2007) Src-dependent phosphorylation of ASAP1 regulates podosomes. Mol. Cell. Biol. 27 8271-83 PubMed GONUTS page

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MOUSE:VINC

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