SORBS3

Protein-coding gene in the species Homo sapiens
SORBS3
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2CT3, 2DLM, 2NWM, 2YUP

Identifiers
AliasesSORBS3, SCAM-1, SCAM1, SH3D4, sorbin and SH3 domain containing 3
External IDsOMIM: 610795; MGI: 700013; HomoloGene: 4218; GeneCards: SORBS3; OMA:SORBS3 - orthologs
Gene location (Human)
Chromosome 8 (human)
Chr.Chromosome 8 (human)[1]
Chromosome 8 (human)
Genomic location for SORBS3
Genomic location for SORBS3
Band8p21.3Start22,544,986 bp[1]
End22,575,788 bp[1]
Gene location (Mouse)
Chromosome 14 (mouse)
Chr.Chromosome 14 (mouse)[2]
Chromosome 14 (mouse)
Genomic location for SORBS3
Genomic location for SORBS3
Band14 D2|14 36.27 cMStart70,417,917 bp[2]
End70,449,438 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • right testis

  • left testis

  • right coronary artery

  • popliteal artery

  • tibial arteries

  • tibial nerve

  • gastric mucosa

  • left coronary artery

  • canal of the cervix

  • ascending aorta
Top expressed in
  • external carotid artery

  • muscle of thigh

  • internal carotid artery

  • genital tubercle

  • retinal pigment epithelium

  • vestibular membrane of cochlear duct

  • ankle

  • right lung

  • right lung lobe

  • choroid plexus of fourth ventricle
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • vinculin binding
  • transcription factor binding
  • structural constituent of cytoskeleton
  • protein binding
Cellular component
  • cytoplasm
  • cytosol
  • cell junction
  • cytoskeleton
  • nucleus
  • focal adhesion
Biological process
  • cell-substrate adhesion
  • cell adhesion
  • muscle contraction
  • negative regulation of transcription by RNA polymerase II
  • positive regulation of stress fiber assembly
  • positive regulation of cytoskeleton organization
  • positive regulation of MAPK cascade
  • actin filament organization
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

10174

20410

Ensembl

ENSG00000120896

ENSMUSG00000022091

UniProt

O60504

Q9R1Z8

RefSeq (mRNA)

NM_001018003
NM_005775

NM_001271407
NM_001271408
NM_001271409
NM_011366

RefSeq (protein)

NP_001018003
NP_005766

NP_001258336
NP_001258337
NP_001258338
NP_035496

Location (UCSC)Chr 8: 22.54 – 22.58 MbChr 14: 70.42 – 70.45 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Vinexin is a protein that in humans is encoded by the SORBS3 gene.[5][6][7]


Interactions

SORBS3 has been shown to interact with DLG5[8] and MAPK1.[9]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000120896 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000022091 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Kioka N, Sakata S, Kawauchi T, Amachi T, Akiyama SK, Okazaki K, Yaen C, Yamada KM, Aota S (Mar 1999). "Vinexin: a novel vinculin-binding protein with multiple SH3 domains enhances actin cytoskeletal organization". J Cell Biol. 144 (1): 59–69. doi:10.1083/jcb.144.1.59. PMC 2148117. PMID 9885244.
  6. ^ Kioka N (Jan 2003). "[A novel adaptor protein family regulating cytoskeletal organization and signal transduction--Vinexin, CAP/ponsin, ArgBP2]". Seikagaku. 74 (11): 1356–60. PMID 12510380.
  7. ^ "Entrez Gene: SORBS3 sorbin and SH3 domain containing 3".
  8. ^ Wakabayashi M, Ito Takuya, Mitsushima Masaru, Aizawa Sanae, Ueda Kazumitsu, Amachi Teruo, Kioka Noriyuki (Jun 2003). "Interaction of lp-dlg/KIAA0583, a membrane-associated guanylate kinase family protein, with vinexin and beta-catenin at sites of cell-cell contact". J. Biol. Chem. 278 (24): 21709–14. doi:10.1074/jbc.M211004200. ISSN 0021-9258. PMID 12657639.
  9. ^ Mitsushima M, Suwa Akira, Amachi Teruo, Ueda Kazumitsu, Kioka Noriyuki (Aug 2004). "Extracellular signal-regulated kinase activated by epidermal growth factor and cell adhesion interacts with and phosphorylates vinexin". J. Biol. Chem. 279 (33): 34570–7. doi:10.1074/jbc.M402304200. ISSN 0021-9258. PMID 15184391.

Further reading

  • Akamatsu M, Aota S, Suwa A, et al. (2000). "Vinexin forms a signaling complex with Sos and modulates epidermal growth factor-induced c-Jun N-terminal kinase/stress-activated protein kinase activities". J. Biol. Chem. 274 (50): 35933–7. doi:10.1074/jbc.274.50.35933. PMID 10585480.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Wakabayashi M, Ito T, Mitsushima M, et al. (2003). "Interaction of lp-dlg/KIAA0583, a membrane-associated guanylate kinase family protein, with vinexin and beta-catenin at sites of cell-cell contact". J. Biol. Chem. 278 (24): 21709–14. doi:10.1074/jbc.M211004200. PMID 12657639.
  • Townson SM, Dobrzycka KM, Lee AV, et al. (2003). "SAFB2, a new scaffold attachment factor homolog and estrogen receptor corepressor". J. Biol. Chem. 278 (22): 20059–68. doi:10.1074/jbc.M212988200. PMID 12660241.
  • Mitsushima M, Suwa A, Amachi T, et al. (2004). "Extracellular signal-regulated kinase activated by epidermal growth factor and cell adhesion interacts with and phosphorylates vinexin". J. Biol. Chem. 279 (33): 34570–7. doi:10.1074/jbc.M402304200. PMID 15184391.
  • Martens N, Wery M, Wang P, et al. (2004). "The suppressor of cytokine signaling (SOCS)-7 interacts with the actin cytoskeleton through vinexin". Exp. Cell Res. 298 (1): 239–48. doi:10.1016/j.yexcr.2004.04.002. PMID 15242778.
  • Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Bour G, Plassat JL, Bauer A, et al. (2005). "Vinexin beta interacts with the non-phosphorylated AF-1 domain of retinoid receptor gamma (RARgamma) and represses RARgamma-mediated transcription". J. Biol. Chem. 280 (17): 17027–37. doi:10.1074/jbc.M501344200. PMID 15734736.
  • Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
  • Mitsushima M, Ueda K, Kioka N (2006). "Vinexin beta regulates the phosphorylation of epidermal growth factor receptor on the cell surface". Genes Cells. 11 (9): 971–82. doi:10.1111/j.1365-2443.2006.00995.x. PMID 16923119. S2CID 24238810.
  • Beausoleil SA, Villén J, Gerber SA, et al. (2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nat. Biotechnol. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243. S2CID 14294292.
  • Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.
  • Mizutani K, Ito H, Iwamoto I, et al. (2007). "Essential roles of ERK-mediated phosphorylation of vinexin in cell spreading, migration and anchorage-independent growth". Oncogene. 26 (50): 7122–31. doi:10.1038/sj.onc.1210512. hdl:20.500.12099/23093. PMID 17486060. S2CID 9284621.
  • v
  • t
  • e
  • 2ct3: Solution Structure of the SH3 domain of the Vinexin protein
    2ct3: Solution Structure of the SH3 domain of the Vinexin protein
  • 2dlm: Solution structure of the first SH3 domain of human vinexin
    2dlm: Solution structure of the first SH3 domain of human vinexin
  • 2nwm: Solution structure of the first SH3 domain of human Vinexin and its interaction with the peptides from Vinculin
    2nwm: Solution structure of the first SH3 domain of human Vinexin and its interaction with the peptides from Vinculin


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