UniProtKB - Q64727 (VINC_MOUSE)

BLAST

>sp|Q64727|VINC_MOUSE Vinculin OS=Mus musculus OX=10090 GN=Vcl PE=1 SV=4
MPVFHTRTIESILEPVAQQISHLVIMHEEGEVDGKAIPDLTAPVAAVQAAVSNLVRVGKE
TVQTTEDQILKRDMPPAFIKVENACTKLVQAAQMLQSDPYSVPARDYLIDGSRGILSGTS
DLLLTFDEAEVRKIIRVCKGILEYLTVAEVVETMEDLVTYTKNLGPGMTKMAKMIDERQQ
ELTHQEHRVMLVNSMNTVKELLPVLISAMKIFVTTKNSKNQGIEEALKNRNFTVEKMSAE
INEIIRVLQLTSWDEDAWASKDTEAMKRALASIDSKLNQAKGWLRDPNASPGDAGEQAIR
QILDEAGKVGELCAGKERREILGTCKMLGQMTDQVADLRARGQGASPVAMQKAQQVSQGL
DVLTAKVENAARKLEAMTNSKQSIAKKIDAAQNWLADPNGGPEGEEQIRGALAEARKIAE
LCDDPKERDDILRSLGEIAALTSKLGDLRRQGKGDSPEARALAKQVATALQNLQTKTNRA
VANSRPAKAAVHLEGKIEQAQRWIDNPTVDDRGVGQAAIRGLVAEGHRLANVMMGPYRQD
LLAKCDRVDQLTAQLADLAARGEGESPQARALASQLQDSLKDLKAQMQEAMTQEVSDVFS
DTTTPIKLLAVAATAPPDAPNREEVFDERAANFENHSGRLGATAEKAAAVGTANKSTVEG
IQASVKTARELTPQVISAARILLRNPGNQAAYEHFETMKNQWIDNVEKMTGLVDEAIDTK
SLLDASEEAIKKDLDKCKVAMANIQPQMLVAGATSIARRANRILLVAKREVENSEDPKFR
EAVKAASDELSKTISPMVMDAKAVAGNISDPGLQKSFLDSGYRILGAVAKVREAFQPQEP
DFPPPPPDLEQLRLTDELAPPKPPLPEGEVPPPRPPPPEEKDEEFPEQKAGEVINQPMMM
AARQLHDEARKWSSKGNDIIAAAKRMALLMAEMSRLVRGGSGTKRALIQCAKDIAKASDE
VTRLAKEVAKQCTDKRIRTNLLQVCERIPTISTQLKILSTVKATMLGRTNISDEESEQAT
EMLVHNAQNLMQSVKETVREAEAASIKIRTDAGFTLRWVRKTPWYQ

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History
Entry version 167 (10 Oct 2018)
Sequence version 4 (23 Jan 2007)
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Protein

Vinculin

Gene

Vcl

Organism

Mus musculus (Mouse)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion (By similarity).By similarity1 Publication

GO - Molecular functionⁱ

actin filament binding Source: InterPro
alpha-catenin binding Source: MGI
dystroglycan binding Source: MGI
Rho GTPase binding Source: MGI
structural molecule activity Source: InterPro
ubiquitin protein ligase binding Source: MGI

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

adherens junction assembly Source: MGI
apical junction assembly Source: MGI
axon extension
Source: MGI
Inferred from genetic interactionⁱ
- 24623780
cell adhesion
Source: MGI
Inferred from direct assayⁱ
- 12473693
epithelial cell-cell adhesion Source: MGI
lamellipodium assembly
Source: MGI
Inferred from direct assayⁱ
- 12473693
morphogenesis of an epithelium Source: MGI
protein localization to cell surface Source: MGI
regulation of cell migration
Source: MGI
Inferred from direct assayⁱ
- 12473693

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Actin-binding
Biological process	Cell adhesion

Enzyme and pathway databases

Reactomeⁱ	R-MMU-114608 Platelet degranulation R-MMU-445355 Smooth Muscle Contraction R-MMU-5674135 MAP2K and MAPK activation R-MMU-6798695 Neutrophil degranulation

Reactomeⁱ

R-MMU-114608 Platelet degranulation
R-MMU-445355 Smooth Muscle Contraction
R-MMU-5674135 MAP2K and MAPK activation
R-MMU-6798695 Neutrophil degranulation

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Vinculin Alternative name(s): Metavinculin
Gene namesⁱ	Name:Vcl
Organismⁱ	Mus musculus (Mouse)
Taxonomic identifierⁱ	10090 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesⁱ	UP000000589 Componentⁱ: Chromosome 14

Organism-specific databases

MGIⁱ	MGI:98927 Vcl

Keywords - Cellular componentⁱ

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000064253	1 – 1066	VinculinAdd BLAST		1066

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	97	PhosphoserineBy similarity	1
Modified residueⁱ	173	N6-acetyllysineBy similarity	1
Modified residueⁱ	260	PhosphoserineCombined sources	1
Modified residueⁱ	272	PhosphoserineBy similarity	1
Modified residueⁱ	275	PhosphoserineBy similarity	1
Modified residueⁱ	290	PhosphoserineCombined sources	1
Modified residueⁱ	346	PhosphoserineCombined sources	1
Modified residueⁱ	434	PhosphoserineBy similarity	1
Modified residueⁱ	496	N6-acetyllysineBy similarity	1
Modified residueⁱ	537	PhosphotyrosineCurated	1
Modified residueⁱ	574	PhosphoserineBy similarity	1
Modified residueⁱ	579	PhosphoserineCombined sources	1
Modified residueⁱ	600	PhosphoserineCombined sources	1
Modified residueⁱ	604	PhosphothreonineBy similarity	1
Modified residueⁱ	672	PhosphothreonineBy similarity	1
Modified residueⁱ	721	PhosphoserineCombined sources	1
Modified residueⁱ	795	PhosphoserineBy similarity	1
Modified residueⁱ	809	PhosphoserineCombined sources	1
Modified residueⁱ	822	PhosphotyrosineCombined sources	1
Modified residueⁱ	1065	Phosphotyrosine; by SRC-type Tyr-kinasesBy similarity	1

Post-translational modificationⁱ

Phosphorylated; on serines, threonines and tyrosines. Phosphorylation on Tyr-1065 in activated platelets affects head-tail interactions and cell spreading but has no effect on actin binding nor on localization to focal adhesion plaques (By similarity).By similarity

Acetylated; mainly by myristic acid but also by a small amount of palmitic acid.By similarity

Keywords - PTMⁱ

Acetylation, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

EPDⁱ	Q64727
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q64727
PaxDbⁱ	Q64727
PeptideAtlas More...PeptideAtlasⁱ	Q64727
PRIDEⁱ	Q64727

2D gel databases

REPRODUCTION-2DPAGE More...REPRODUCTION-2DPAGEⁱ	Q64727

REPRODUCTION-2DPAGEⁱ

Q64727

PTM databases

iPTMnetⁱ	Q64727
PhosphoSitePlusⁱ	Q64727

Miscellaneous databases

PMAP-CutDBⁱ	Q64727

PMAP-CutDBⁱ

Q64727

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSMUSG00000021823 Expressed in 290 organ(s), highest expression level in urinary bladder
CleanExⁱ	MM_VCL
ExpressionAtlasⁱ	Q64727 baseline and differential
Genevisibleⁱ	Q64727 MM

Interactionⁱ

Subunit structureⁱ

Exhibits self-association properties. Interacts with APBB1IP, NRAP and TLN1. Interacts with SYNM. Interacts with CTNNB1 and this interaction is necessary for its localization to the cell-cell junctions and for its function in regulating cell surface expression of E-cadherin (By similarity). Interacts with SORBS1 (PubMed:10085297). Interacts with SYNM (By similarity). Interacts with CTNNA1 (By similarity). Binds to ACTN4; this interaction triggers conformational changes (By similarity).By similarity2 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
Arhgef1	Q61210	3	EBI-432047,EBI-641821
PXN	P49024	4	EBI-432047,EBI-2896280	From Gallus gallus.
Pxn	Q8VI36	3	EBI-432047,EBI-983394
Tjp1	P39447	8	EBI-432047,EBI-79508
Tln1	P26039	2	EBI-432047,EBI-1039593

GO - Molecular functionⁱ

actin filament binding Source: InterPro
alpha-catenin binding Source: MGI
dystroglycan binding Source: MGI
Rho GTPase binding Source: MGI
ubiquitin protein ligase binding Source: MGI

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	204506, 9 interactors
IntActⁱ	Q64727, 16 interactors
Molecular INTeraction database More...MINTⁱ	Q64727
STRINGⁱ	10090.ENSMUSP00000022369

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	3 – 6	Combined sources	4
Helixⁱ	7 – 29	Combined sources	23
Turnⁱ	30 – 34	Combined sources	5
Helixⁱ	41 – 64	Combined sources	24
Helixⁱ	68 – 97	Combined sources	30
Helixⁱ	104 – 146	Combined sources	43
Helixⁱ	159 – 179	Combined sources	21
Helixⁱ	185 – 210	Combined sources	26
Helixⁱ	225 – 249	Combined sources	25

Show more details

3D structure databases

ProteinModelPortalⁱ	Q64727
SMRⁱ	Q64727
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Repeatⁱ	259 – 369	1Sequence analysisAdd BLAST	111
Repeatⁱ	370 – 479	2Sequence analysisAdd BLAST	110
Repeatⁱ	480 – 589	3Sequence analysisAdd BLAST	110

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	1 – 835	N-terminal globular headBy similarityAdd BLAST	835
Regionⁱ	168 – 208	Talin-interactionBy similarityAdd BLAST	41
Regionⁱ	259 – 589	3 X 112 AA tandem repeatsSequence analysisAdd BLAST	331
Regionⁱ	741 – 764	Interaction with ACTN4By similarityAdd BLAST	24
Regionⁱ	836 – 878	Linker (Pro-rich)By similarityAdd BLAST	43
Regionⁱ	879 – 1066	C-terminal tailBy similarityAdd BLAST	188
Regionⁱ	935 – 978	Facilitates phospholipid membrane insertion1 PublicationAdd BLAST	44
Regionⁱ	1052 – 1066	Facilitates phospholipid membrane insertion1 PublicationAdd BLAST	15

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	837 – 878	Pro-richPROSITE-ProRule annotationAdd BLAST		42

Domainⁱ

Exists in at least two conformations. When in the closed, 'inactive' conformation, extensive interactions between the head and tail domains prevent detectable binding to most of its ligands. It takes on an 'active' conformation after cooperative and simultaneous binding of two different ligands. This activation involves displacement of the head-tail interactions and leads to a significant accumulation of ternary complexes. The active form then binds a number of proteins that have both signaling and structural roles that are essential for cell adhesion.By similarity

The N-terminal globular head (Vh) comprises of subdomains D1-D4. The C-terminal tail (Vt) binds F-actin and cross-links actin filaments into bundles. An intramolecular interaction between Vh and Vt masks the F-actin-binding domain located in Vt. The binding of talin and alpha-actinin to the D1 subdomain of vinculin induces a helical bundle conversion of this subdomain, leading to the disruption of the intramolecular interaction and the exposure of the cryptic F-actin-binding domain of Vt. Vt inhibits actin filament barbed end elongation without affecting the critical concentration of actin assembly.By similarity

Sequence similaritiesⁱ

Belongs to the vinculin/alpha-catenin family.Curated

Keywords - Domainⁱ

Repeat

Phylogenomic databases

eggNOGⁱ	KOG3681 Eukaryota ENOG410XSRU LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00550000074411
HOGENOMⁱ	HOG000007828
HOVERGENⁱ	HBG079758
InParanoidⁱ	Q64727
KEGG Orthology (KO) More...KOⁱ	K05700
OMAⁱ	TPGREQN
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G038S
PhylomeDBⁱ	Q64727
TreeFamⁱ	TF313686

Family and domain databases

InterProⁱ	View protein in InterPro IPR036723 Alpha-catenin/vinculin-like_sf IPR017997 Vinculin IPR006077 Vinculin/catenin IPR000633 Vinculin_CS
PANTHERⁱ	PTHR18914 PTHR18914, 2 hits PTHR18914:SF1 PTHR18914:SF1, 2 hits
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01044 Vinculin, 2 hits
SUPFAMⁱ	SSF47220 SSF47220, 6 hits
PROSITEⁱ	View protein in PROSITE PS00663 VINCULIN_1, 1 hit PS00664 VINCULIN_2, 3 hits

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show all Align All

Q64727-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MPVFHTRTIE SILEPVAQQI SHLVIMHEEG EVDGKAIPDL TAPVAAVQAA 
        60         70         80         90        100
VSNLVRVGKE TVQTTEDQIL KRDMPPAFIK VENACTKLVQ AAQMLQSDPY 
       110        120        130        140        150
SVPARDYLID GSRGILSGTS DLLLTFDEAE VRKIIRVCKG ILEYLTVAEV 
       160        170        180        190        200
VETMEDLVTY TKNLGPGMTK MAKMIDERQQ ELTHQEHRVM LVNSMNTVKE 
       210        220        230        240        250
LLPVLISAMK IFVTTKNSKN QGIEEALKNR NFTVEKMSAE INEIIRVLQL 
       260        270        280        290        300
TSWDEDAWAS KDTEAMKRAL ASIDSKLNQA KGWLRDPNAS PGDAGEQAIR 
       310        320        330        340        350
QILDEAGKVG ELCAGKERRE ILGTCKMLGQ MTDQVADLRA RGQGASPVAM 
       360        370        380        390        400
QKAQQVSQGL DVLTAKVENA ARKLEAMTNS KQSIAKKIDA AQNWLADPNG 
       410        420        430        440        450
GPEGEEQIRG ALAEARKIAE LCDDPKERDD ILRSLGEIAA LTSKLGDLRR 
       460        470        480        490        500
QGKGDSPEAR ALAKQVATAL QNLQTKTNRA VANSRPAKAA VHLEGKIEQA 
       510        520        530        540        550
QRWIDNPTVD DRGVGQAAIR GLVAEGHRLA NVMMGPYRQD LLAKCDRVDQ 
       560        570        580        590        600
LTAQLADLAA RGEGESPQAR ALASQLQDSL KDLKAQMQEA MTQEVSDVFS 
       610        620        630        640        650
DTTTPIKLLA VAATAPPDAP NREEVFDERA ANFENHSGRL GATAEKAAAV 
       660        670        680        690        700
GTANKSTVEG IQASVKTARE LTPQVISAAR ILLRNPGNQA AYEHFETMKN 
       710        720        730        740        750
QWIDNVEKMT GLVDEAIDTK SLLDASEEAI KKDLDKCKVA MANIQPQMLV 
       760        770        780        790        800
AGATSIARRA NRILLVAKRE VENSEDPKFR EAVKAASDEL SKTISPMVMD 
       810        820        830        840        850
AKAVAGNISD PGLQKSFLDS GYRILGAVAK VREAFQPQEP DFPPPPPDLE 
       860        870        880        890        900
QLRLTDELAP PKPPLPEGEV PPPRPPPPEE KDEEFPEQKA GEVINQPMMM 
       910        920        930        940        950
AARQLHDEAR KWSSKGNDII AAAKRMALLM AEMSRLVRGG SGTKRALIQC 
       960        970        980        990       1000
AKDIAKASDE VTRLAKEVAK QCTDKRIRTN LLQVCERIPT ISTQLKILST 
      1010       1020       1030       1040       1050
VKATMLGRTN ISDEESEQAT EMLVHNAQNL MQSVKETVRE AEAASIKIRT 
      1060 
DAGFTLRWVR KTPWYQ

Length:1,066

Mass (Da):116,717

Last modified:January 23, 2007 - v4

Checksum:ⁱ067F1B16A5285859

Computationally mapped potential isoform sequencesⁱ

There is 1 potential isoform mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name		Protein names	Gene names	Length	Annotation

	A0A286YDJ4	A0A286YDJ4_MOUSE		Vinculin Vinculin	Vcl	149	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	16	V → E in AAB96843 (PubMed:7568093).Curated	1
Sequence conflictⁱ	215	T → S in AAB96843 (PubMed:7568093).Curated	1
Sequence conflictⁱ	363	L → V in AAB96843 (PubMed:7568093).Curated	1
Sequence conflictⁱ	499	Q → K in BAC37033 (PubMed:16141072).Curated	1
Sequence conflictⁱ	501	Q → R in AAB96843 (PubMed:7568093).Curated	1
Sequence conflictⁱ	799	M → K in BAC37033 (PubMed:16141072).Curated	1
Sequence conflictⁱ	812	G → D in AAB96843 (PubMed:7568093).Curated	1
Sequence conflictⁱ	1044	A → T in BAC37033 (PubMed:16141072).Curated	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	L13300, L13299 Genomic DNA Translation: AAA40557.1 L18880 mRNA Translation: AAB96843.1 AK035184 mRNA Translation: BAC28973.1 AK077850 mRNA Translation: BAC37033.1 BC008520 mRNA Translation: AAH08520.1 BC008554 mRNA Translation: AAH08554.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS26860.1
PIRⁱ	A60965 T10108
NCBI Reference Sequences More...RefSeqⁱ	NP_033528.3, NM_009502.4
UniGeneⁱ	Mm.279361

Genome annotation databases

Ensemblⁱ	ENSMUST00000022369; ENSMUSP00000022369; ENSMUSG00000021823
GeneIDⁱ	22330
KEGGⁱ	mmu:22330
UCSC genome browser More...UCSCⁱ	uc007skz.1 mouse

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q64727	Isoform 1 of Vinculin		CHICK		1066	UniRef90_P12003-1
Vinculin		RAT		1066
Vinculin		CANLF		1074
Chain A, Crystal Structure Of A Cytoskeletal Protein		CROAD		1068
vinculin isoform X1		BALAS		1067
+236

Protein	Similar proteins		Species	Score	Length	Source
Q64727	Isoform 1 of Vinculin		CHICK		1066	UniRef50_P12003-1
Vinculin		RAT		1066
Vinculin (Fragment)		XENLA		235
Vinculin		CANLF		1074
Chain A, Crystal Structure Of A Cytoskeletal Protein		CROAD		1068
+514

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	L13300, L13299 Genomic DNA Translation: AAA40557.1 L18880 mRNA Translation: AAB96843.1 AK035184 mRNA Translation: BAC28973.1 AK077850 mRNA Translation: BAC37033.1 BC008520 mRNA Translation: AAH08520.1 BC008554 mRNA Translation: AAH08554.1
CCDSⁱ	CCDS26860.1
PIRⁱ	A60965 T10108
RefSeqⁱ	NP_033528.3, NM_009502.4
UniGeneⁱ	Mm.279361

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	5Y04	X-ray	2.85	A	1-250	[»]
ProteinModelPortalⁱ	Q64727
SMRⁱ	Q64727
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	204506, 9 interactors
IntActⁱ	Q64727, 16 interactors
MINTⁱ	Q64727
STRINGⁱ	10090.ENSMUSP00000022369

PTM databases

iPTMnetⁱ	Q64727
PhosphoSitePlusⁱ	Q64727

2D gel databases

REPRODUCTION-2DPAGEⁱ	Q64727

REPRODUCTION-2DPAGEⁱ

Q64727

Proteomic databases

EPDⁱ	Q64727
MaxQBⁱ	Q64727
PaxDbⁱ	Q64727
PeptideAtlasⁱ	Q64727
PRIDEⁱ	Q64727

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENSMUST00000022369; ENSMUSP00000022369; ENSMUSG00000021823
GeneIDⁱ	22330
KEGGⁱ	mmu:22330
UCSCⁱ	uc007skz.1 mouse

Organism-specific databases

CTDⁱ	7414
MGIⁱ	MGI:98927 Vcl

Phylogenomic databases

eggNOGⁱ	KOG3681 Eukaryota ENOG410XSRU LUCA
GeneTreeⁱ	ENSGT00550000074411
HOGENOMⁱ	HOG000007828
HOVERGENⁱ	HBG079758
InParanoidⁱ	Q64727
KOⁱ	K05700
OMAⁱ	TPGREQN
OrthoDBⁱ	EOG091G038S
PhylomeDBⁱ	Q64727
TreeFamⁱ	TF313686

Enzyme and pathway databases

Reactomeⁱ	R-MMU-114608 Platelet degranulation R-MMU-445355 Smooth Muscle Contraction R-MMU-5674135 MAP2K and MAPK activation R-MMU-6798695 Neutrophil degranulation

Reactomeⁱ

R-MMU-114608 Platelet degranulation
R-MMU-445355 Smooth Muscle Contraction
R-MMU-5674135 MAP2K and MAPK activation
R-MMU-6798695 Neutrophil degranulation

Miscellaneous databases

ChiTaRSⁱ	Vcl mouse
PMAP-CutDBⁱ	Q64727
Protein Ontology More...PROⁱ	PR:Q64727
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSMUSG00000021823 Expressed in 290 organ(s), highest expression level in urinary bladder
CleanExⁱ	MM_VCL
ExpressionAtlasⁱ	Q64727 baseline and differential
Genevisibleⁱ	Q64727 MM

Family and domain databases

InterProⁱ	View protein in InterPro IPR036723 Alpha-catenin/vinculin-like_sf IPR017997 Vinculin IPR006077 Vinculin/catenin IPR000633 Vinculin_CS
PANTHERⁱ	PTHR18914 PTHR18914, 2 hits PTHR18914:SF1 PTHR18914:SF1, 2 hits
Pfamⁱ	View protein in Pfam PF01044 Vinculin, 2 hits
SUPFAMⁱ	SSF47220 SSF47220, 6 hits
PROSITEⁱ	View protein in PROSITE PS00663 VINCULIN_1, 1 hit PS00664 VINCULIN_2, 3 hits
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	VINC_MOUSE
Accessionⁱ	Q64727Primary (citable) accession number: Q64727 Secondary accession number(s): Q8BP32 , Q8BS46, Q922C5, Q922D9
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
	Last sequence update:	January 23, 2007
	Last modified:	October 10, 2018
	This is version 167 of the entry and version 4 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references

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UniRef

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Supporting data

UniProtKB - Q64727 (VINC_MOUSE)

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Vinculin

Vcl

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Cytoskeleton

Plasma membrane

Other locations

Cytoskeleton

Plasma Membrane

Other locations

Keywords - Cellular componenti

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

2D gel databases

PTM databases

Miscellaneous databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

Compositional bias

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ