O60504 (VINEX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Vinexin

Alternative name(s):
SH3-containing adapter molecule 1
Short name=SCAM-1
Sorbin and SH3 domain-containing protein 3

Gene names

Name:	SORBS3
Synonyms:	SCAM1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	671 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Vinexin alpha isoform promotes up-regulation of actin stress fiber formation. Vinexin beta isoform plays a role in cell spreading and enhances the activation of JNK/SAPK in response to EGF stimulation by using its third SH3 domain.
Subunit structure	Interacts with DLG5 through its third SH3 domain By similarity. Interacts with vinculin by the first two SH3 domains and the proline rich region of vinculin. Binds to SOS (guanine nucleotide exchange factor of RAS and RAC), through its third SH3 domain. The formation of this complex is down-regulated by phosphorylation of SOS. Interacts with INPPL1/SHIP2, SAFB2, SOCS7 and SRCIN1. Interacts with FASLG. Interacts with MAPK1/ERK2 By similarity. Ref.6 Ref.7 Ref.8 Ref.9 Ref.12 Ref.14
Subcellular location	Isoform Alpha: Cell junction By similarity. Cytoplasm › cytoskeleton By similarity. Note: Localized at cell-extracellular matrix junctions By similarity. Both isoforms were localized at focal adhesion and cell-cell adhesion sites. Isoform Beta: Cell junction By similarity. Nucleus. Cytoplasm › cytoskeleton By similarity. Note: Localized at cell-extracellular matrix junctions By similarity. Both isoforms were localized at focal adhesion and cell-cell adhesion sites, vinexin beta was also found in the nucleus.
Tissue specificity	Both isoforms are expressed in different tissues like heart, placenta, brain, skeletal muscle and pancreas. Isoform beta is especially found in liver.
Post-translational modification	Phosphorylated at Ser-530 by MAPK1/ERK2 during cell spreading By similarity.
Sequence similarities	Contains 3 SH3 domains. Contains 1 SoHo domain.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell junction Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat SH3 domain
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell adhesion Traceable author statement Ref.1. Source: ProtInc cell-substrate adhesion Inferred from electronic annotation. Source: Compara muscle contraction Traceable author statement. Source: Reactome negative regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara positive regulation of MAPK cascade Inferred from electronic annotation. Source: Compara positive regulation of stress fiber assembly Inferred from direct assay Ref.1. Source: UniProtKB
Cellular_component	cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome focal adhesion Inferred from electronic annotation. Source: Compara nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	structural constituent of cytoskeleton Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SAFB2	Q14151	3	EBI-1222956,EBI-352869
Srcin1	Q9QWI6-2	4	EBI-1222956,EBI-775607	From a different organism.
WASL	O00401	2	EBI-1222956,EBI-957615

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Alpha (identifier: O60504-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform Beta (identifier: O60504-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-342: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 671

671

Vinexin

PRO_0000065830

Regions

Domain

115 – 187

73

SoHo

Domain

380 – 439

60

SH3 1

Domain

454 – 515

62

SH3 2

Domain

612 – 671

60

SH3 3

Region

380 – 515

136

Binds to vinculin

Region

612 – 671

60

Binds to SOS

Amino acid modifications

Modified residue

348

1

Phosphoserine Ref.15 Ref.17

Modified residue

395

1

Phosphoserine Ref.17

Modified residue

530

1

Phosphoserine; by MAPK1 Ref.11 Ref.13 Ref.16 Ref.17

Modified residue

544

1

Phosphoserine Ref.18

Modified residue

545

1

Phosphoserine Ref.17 Ref.18

Modified residue

551

1

Phosphoserine Ref.13 Ref.17

Modified residue

563

1

Phosphoserine Ref.13 Ref.16 Ref.17 Ref.18

Natural variations

Alternative sequence

1 – 342

342

Missing in isoform Beta.

VSP_004489

Natural variant

255

1

P → L.
Corresponds to variant rs3758036 [ dbSNP | Ensembl ].

VAR_057019

Natural variant

556

1

I → T. Ref.1 Ref.2 Ref.3 Ref.5 Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20 Ref.21
Corresponds to variant rs2449331 [ dbSNP | Ensembl ].

VAR_055019

Natural variant

573

1

T → A.
Corresponds to variant rs1047030 [ dbSNP | Ensembl ].

VAR_055020

Experimental info

Mutagenesis

649

1

W → F: Loss of SOS-binding ability.

Mutagenesis

667

1

Y → V: Loss of SOS-binding ability.

Sequence conflict

583

1

L → F in AAD32304. Ref.1

Secondary structure

1

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671

Helix Strand Turn

Details...

Beta strand

385 – 389

5

Beta strand

395 – 398

4

Beta strand

406 – 414

9

Beta strand

417 – 422

6

Beta strand

425 – 435

11

Helix

453 – 455

3

Beta strand

456 – 461

6

Beta strand

469 – 472

4

Beta strand

480 – 485

6

Beta strand

489 – 495

7

Turn

497 – 499

3

Beta strand

502 – 506

5

Helix

507 – 509

3

Beta strand

510 – 514

5

Beta strand

615 – 621

7

Beta strand

637 – 644

8

Beta strand

646 – 648

3

Beta strand

650 – 657

8

Beta strand

660 – 663

4

Turn

665 – 667

3

Beta strand

668 – 670

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform Alpha [UniParc]. Last modified January 11, 2011. Version 2. Checksum: 2D8A8718E0367BE9	FASTA	671	75,341
	10 20 30 40 50 60 MQGPPRSLRA GLSLDDFIPG HLQSHIGSSS RGTRVPVIRN GGSNTLNFQF HDPAPRTVCN 70 80 90 100 110 120 GGYTPRRDAS QHPDPAWYQT WPGPGSKPSA STKIPASQHT QNWSATWTKD SKRRDKRWVK 130 140 150 160 170 180 YEGIGPVDES GMPIAPRSSV DRPRDWYRRM FQQIHRKMPD LQLDWTFEEP PRDPRHLGAQ 190 200 210 220 230 240 QRPAHRPGPA TSSSGRSWDH SEELPRSTFN YRPGAFSTVL QPSNQVLRRR EKVDNVWTEE 250 260 270 280 290 300 SWNQFLQELE TGQRPKKPLV DDPGEKPSQP IEVLLERELA ELSAELDKDL RAIETRLPSP 310 320 330 340 350 360 KSSPAPRRAP EQRPPAGPAS AWSSSYPHAP YLGSARSLSP HKMADGGSPF LGRRDFVYPS 370 380 390 400 410 420 STRDPSASNG GGSPARREEK KRKAARLKFD FQAQSPKELT LQKGDIVYIH KEVDKNWLEG 430 440 450 460 470 480 EHHGRLGIFP ANYVEVLPAD EIPKPIKPPT YQVLEYGEAV AQYTFKGDLE VELSFRKGEH 490 500 510 520 530 540 ICLIRKVNEN WYEGRITGTG RQGIFPASYV QVSREPRLRL CDDGPQLPTS PRLTAAARSA 550 560 570 580 590 600 RHPSSPSALR SPADPIDLGG QTSPRRTGFS FPTQEPRPQT QNLGTPGPAL SHSRGPSHPL 610 620 630 640 650 660 DLGTSSPNTS QIHWTPYRAM YQYRPQNEDE LELREGDRVD VMQQCDDGWF VGVSRRTQKF 670 GTFPGNYVAP V
	Isoform Beta [UniParc]. Checksum: 852B1FDC07859AC2	FASTA	329	36,742
	10 20 30 40 50 60 MADGGSPFLG RRDFVYPSST RDPSASNGGG SPARREEKKR KAARLKFDFQ AQSPKELTLQ 70 80 90 100 110 120 KGDIVYIHKE VDKNWLEGEH HGRLGIFPAN YVEVLPADEI PKPIKPPTYQ VLEYGEAVAQ 130 140 150 160 170 180 YTFKGDLEVE LSFRKGEHIC LIRKVNENWY EGRITGTGRQ GIFPASYVQV SREPRLRLCD 190 200 210 220 230 240 DGPQLPTSPR LTAAARSARH PSSPSALRSP ADPIDLGGQT SPRRTGFSFP TQEPRPQTQN 250 260 270 280 290 300 LGTPGPALSH SRGPSHPLDL GTSSPNTSQI HWTPYRAMYQ YRPQNEDELE LREGDRVDVM 310 320 QQCDDGWFVG VSRRTQKFGT FPGNYVAPV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Vinexin: a novel vinculin-binding protein with multiple SH3 domains enhances actin cytoskeletal organization." Kioka N., Sakata S., Kawauchi T., Amachi T., Akiyama S.K., Okazaki K., Yaen C., Yamada K.M., Aota S. J. Cell Biol. 144:59-69(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA), ALTERNATIVE SPLICING, MUTAGENESIS, VARIANT THR-556. Tissue: Placenta.
[2]	Her J.-H., Gorman D., Miyajima A., Bolen J.B. Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), VARIANT THR-556.
[3]	"DNA sequence and analysis of human chromosome 8." Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S. Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT THR-556.
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS ALPHA AND BETA), VARIANT THR-556. Tissue: PNS and Uterus.
[6]	"Vinexin forms a signaling complex with Sos and modulates epidermal growth factor-induced c-Jun N-terminal kinase/stress-activated protein kinase activities." Akamatsu M., Aota S., Suwa A., Ueda K., Amachi T., Yamada K.M., Akiyama S.K., Kioka N. J. Biol. Chem. 274:35933-35937(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SOS.
[7]	"SAFB2, a new scaffold attachment factor homolog and estrogen receptor corepressor." Townson S.M., Dobrzycka K.M., Lee A.V., Air M., Deng W., Kang K., Jiang S., Kioka N., Michaelis K., Oesterreich S. J. Biol. Chem. 278:20059-20068(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SAFB2.
[8]	"The suppressor of cytokine signaling (SOCS)-7 interacts with the actin cytoskeleton through vinexin." Martens N., Wery M., Wang P., Braet F., Gertler A., Hooghe R., Vandenhaute J., Hooghe-Peters E.L. Exp. Cell Res. 298:239-248(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SOCS7.
[9]	"SHIP2 interaction with the cytoskeletal protein Vinexin." Paternotte N., Zhang J., Vandenbroere I., Backers K., Blero D., Kioka N., Vanderwinden J.-M., Pirson I., Erneux C. FEBS J. 272:6052-6066(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH INPPL1.
[10]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[11]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-530, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Characterization of a multidomain adaptor protein, p140Cap, as part of a pre-synaptic complex." Ito H., Atsuzawa K., Sudo K., Di Stefano P., Iwamoto I., Morishita R., Takei S., Semba R., Defilippi P., Asano T., Usuda N., Nagata K. J. Neurochem. 107:61-72(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SRCIN1.
[13]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-530; SER-551 AND SER-563, VARIANT [LARGE SCALE ANALYSIS] THR-556, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening." Voss M., Lettau M., Janssen O. BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FASLG.
[15]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-348, VARIANT [LARGE SCALE ANALYSIS] THR-556, MASS SPECTROMETRY.
[16]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-530 AND SER-563, VARIANT [LARGE SCALE ANALYSIS] THR-556, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[17]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-348; SER-395; SER-530; SER-545; SER-551 AND SER-563, VARIANT [LARGE SCALE ANALYSIS] THR-556, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544; SER-545 AND SER-563, VARIANT [LARGE SCALE ANALYSIS] THR-556, MASS SPECTROMETRY.
[19]	"Solution structure of SH3 domains of human vinexin." RIKEN structural genomics initiative (RSGI) Submitted (OCT-2006) to the PDB data bank Cited for: STRUCTURE BY NMR OF 383-437 AND 615-671.
[20]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-556, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-556, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF064807 mRNA. Translation: AAD32304.1.
AF037261 mRNA. Translation: AAC09244.1.
AC037459 Genomic DNA. No translation available.
CH471080 Genomic DNA. Translation: EAW63675.1.
BC067260 mRNA. Translation: AAH67260.2.
BC091514 mRNA. Translation: AAH91514.1.
BC010146 mRNA. Translation: AAH10146.1.

IPI

IPI00419847.
IPI00939882.

RefSeq

NP_001018003.1. NM_001018003.2.
NP_005766.3. NM_005775.4.

UniGene

Hs.528572.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CT3	NMR	-	A	615-671	[»]
2DLM	NMR	-	A	383-437	[»]
2NWM	NMR	-	A	383-438	[»]
2YUP	NMR	-	A	447-523	[»]

ProteinModelPortal

O60504.

SMR

O60504. Positions 354-525, 615-671.

ModBase

Search...

Protein-protein interaction databases

IntAct

O60504. 18 interactions.

MINT

MINT-262486.

STRING

9606.ENSP00000240123.

PTM databases

PhosphoSite

O60504.

Proteomic databases

PaxDb

O60504.

PRIDE

O60504.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000240123; ENSP00000240123; ENSG00000120896.
ENST00000428103; ENSP00000408476; ENSG00000120896.

GeneID

10174.

KEGG

hsa:10174.

UCSC

uc003xbv.3. human.
uc003xbw.4. human.

Organism-specific databases

CTD

10174.

GeneCards

GC08P022409.

H-InvDB

HIX0201306.

HGNC

HGNC:30907. SORBS3.

HPA

HPA015849.

MIM

610795. gene.

neXtProt

NX_O60504.

PharmGKB

PA128394570.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG256936.

HOGENOM

HOG000294090.

HOVERGEN

HBG054842.

InParanoid

O60504.

OMA

TPYRAMY.

OrthoDB

EOG457563.

PhylomeDB

O60504.

Enzyme and pathway databases

Reactome

REACT_17044. Muscle contraction.

Gene expression databases

ArrayExpress

O60504.

Bgee

O60504.

CleanEx

HS_SORBS3.

Genevestigator

O60504.

GermOnline

ENSG00000120896. Homo sapiens.

Family and domain databases

InterPro

IPR000108. p67phox.
IPR011511. SH3_2.
IPR001452. SH3_domain.
IPR003127. Sorb.
[Graphical view]

Pfam

PF00018. SH3_1. 2 hits.
PF07653. SH3_2. 1 hit.
PF02208. Sorb. 1 hit.
[Graphical view]

PRINTS

PR00499. P67PHOX.
PR00452. SH3DOMAIN.

SMART

SM00326. SH3. 3 hits.
SM00459. Sorb. 1 hit.
[Graphical view]

SUPFAM

SSF50044. SH3. 3 hits.

PROSITE

PS50002. SH3. 3 hits.
PS50831. SOHO. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SORBS3. human.

EvolutionaryTrace

O60504.

GenomeRNAi

10174.

NextBio

38520.

SOURCE

Search...

Entry information

Entry name

VINEX_HUMAN

Accession

Primary (citable) accession number: O60504
Secondary accession number(s): Q5BJE4 , Q6NX54, Q96FY4, Q9UQE4

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2001
Last sequence update:	January 11, 2011
Last modified:	May 1, 2013
This is version 134 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.