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Q15464

- SHB_HUMAN

UniProt

Q15464 - SHB_HUMAN

Protein

SH2 domain-containing adapter protein B

Gene

SHB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 2 (25 Jul 2006)
      Previous versions | rss
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    Functioni

    Adapter protein which regulates several signal transduction cascades by linking activated receptors to downstream signaling components. May play a role in angiogenesis by regulating FGFR1, VEGFR2 and PDGFR signaling. May also play a role in T-cell antigen receptor/TCR signaling, interleukin-2 signaling, apoptosis and neuronal cells differentiation by mediating basic-FGF and NGF-induced signaling cascades. May also regulate IRS1 and IRS2 signaling in insulin-producing cells.10 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. SH3/SH2 adaptor activity Source: ProtInc

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. apoptotic process Source: UniProtKB-KW
    3. B cell proliferation Source: Ensembl
    4. cell differentiation Source: UniProtKB-KW
    5. hemopoiesis Source: Ensembl
    6. negative regulation of oocyte maturation Source: Ensembl
    7. positive regulation of signal transduction Source: GOC
    8. signal transduction Source: ProtInc

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Angiogenesis, Apoptosis, Differentiation

    Enzyme and pathway databases

    SignaLinkiQ15464.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    SH2 domain-containing adapter protein B
    Gene namesi
    Name:SHB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:10838. SHB.

    Subcellular locationi

    Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side
    Note: Associates with membrane lipid rafts upon TCR stimulation.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi435 – 4351R → K: Loss of interaction with CD3Z. Alters LAT, PLCG1, VAV1 and LCP2 phosphorylation, MAP kinase signaling, Rac1 and JNK activation, intracellular calcium increase, activation of the nuclear factor for activation of T-cells and subsequent interleukin-2 expression which normally occur upon T-cells stimulation. 1 Publication

    Organism-specific databases

    PharmGKBiPA35744.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 509509SH2 domain-containing adapter protein BPRO_0000246324Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei317 – 3171Phosphoserine2 Publications
    Modified residuei388 – 3881Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated upon PDGFRA, PDGFRB, TCR, IL2 receptor, FGFR1 or VEGFR2 activation.3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ15464.
    PaxDbiQ15464.
    PRIDEiQ15464.

    PTM databases

    PhosphoSiteiQ15464.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    BgeeiQ15464.
    CleanExiHS_SHB.
    GenevestigatoriQ15464.

    Organism-specific databases

    HPAiCAB010161.
    HPA049911.

    Interactioni

    Subunit structurei

    Interacts with PTPN11 By similarity. Interacts with phosphorylated 'Tyr-720' of the ligand-activated receptor PDGFRA via its SH2 domain. Interacts with the ligand-activated receptors PDGFRB, FGFR1, KDR/VEGFR2, IL2RB and IL2RG. Interacts with EPS8 and V-SRC. Interacts with GRB2 and GRAP. Interacts with CD3Z. Interacts with tyrosine-phosphorylated LAT upon T-cell antigen receptor activation. Interacts with PLCG1. Interacts with ZAP70, LCP2/SLP-76, VAV1 and GRAP2. Interacts with JAK1 and JAK3. Interacts with PTK2/FAK1. Interacts with CRK/CrKII. Interacts with IRS2.By similarity12 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ABL1P005195EBI-4402156,EBI-375543
    KITP107212EBI-4402156,EBI-1379503
    METP085814EBI-4402156,EBI-1039152

    Protein-protein interaction databases

    BioGridi112358. 16 interactions.
    IntActiQ15464. 8 interactions.
    MINTiMINT-7046528.
    STRINGi9606.ENSP00000366936.

    Structurei

    3D structure databases

    ProteinModelPortaliQ15464.
    SMRiQ15464. Positions 405-487.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini410 – 50495SH2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 410410Mediates interaction with LAT, PTK2/FAK1, JAK1 and JAK3Add
    BLAST

    Domaini

    The SH2 domain preferentially binds phosphopeptides with the consensus sequence Y-[TVI]-X-L and mediates interaction with PDGFRA, PDGFRB, FGRFR1, IL2RB, IL2RG, CD3Z and CRK/CrKII.

    Sequence similaritiesi

    Contains 1 SH2 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH2 domain

    Phylogenomic databases

    eggNOGiNOG80632.
    HOGENOMiHOG000038038.
    HOVERGENiHBG066172.
    InParanoidiQ15464.
    OMAiRPDYREQ.
    OrthoDBiEOG793B9C.
    PhylomeDBiQ15464.
    TreeFamiTF325799.

    Family and domain databases

    Gene3Di3.30.505.10. 1 hit.
    InterProiIPR000980. SH2.
    [Graphical view]
    PfamiPF00017. SH2. 1 hit.
    [Graphical view]
    PRINTSiPR00401. SH2DOMAIN.
    SMARTiSM00252. SH2. 1 hit.
    [Graphical view]
    SUPFAMiSSF55550. SSF55550. 1 hit.
    PROSITEiPS50001. SH2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q15464-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MAKWLNKYFS LGNSKTKSPP QPPRPDYREQ RRRGERPSQP PQAVPQASSA    50
    ASASCGPATA SCFSASSGSL PDDSGSTSDL IRAYRAQKER DFEDPYNGPG 100
    SSLRKLRAMC RLDYCGGSGE PGGVQRAFSA SSASGAAGCC CASSGAGAAA 150
    SSSSSSGSPH LYRSSSERRP ATPAEVRYIS PKHRLIKVES AAGGGAGDPL 200
    GGACAGGRTW SPTACGGKKL LNKCAASAAE ESGAGKKDKV TIADDYSDPF 250
    DAKNDLKSKA GKGESAGYME PYEAQRIMTE FQRQESVRSQ HKGIQLYDTP 300
    YEPEGQSVDS DSESTVSPRL RESKLPQDDD RPADEYDQPW EWNRVTIPAL 350
    AAQFNGNEKR QSSPSPSRDR RRQLRAPGGG FKPIKHGSPE FCGILGERVD 400
    PAVPLEKQIW YHGAISRGDA ENLLRLCKEC SYLVRNSQTS KHDYSLSLRS 450
    NQGFMHMKLA KTKEKYVLGQ NSPPFDSVPE VIHYYTTRKL PIKGAEHLSL 500
    LYPVAVRTL 509
    Length:509
    Mass (Da):55,042
    Last modified:July 25, 2006 - v2
    Checksum:i15C392A6EEB761D6
    GO
    Isoform 2 (identifier: Q15464-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         280-297: EFQRQESVRSQHKGIQLY → GLQEAWRHSPSGCFPVGP
         298-509: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:297
    Mass (Da):30,703
    Checksum:i81ECB44A67B0D8AD
    GO

    Sequence cautioni

    The sequence AAH94765.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAA53091.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti91 – 933DFE → HFQ in CAA53091. (PubMed:8302579)Curated
    Sequence conflicti347 – 3471I → S in CAA53091. (PubMed:8302579)Curated
    Sequence conflicti445 – 4451S → P in CAA53091. (PubMed:8302579)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei280 – 29718EFQRQ…GIQLY → GLQEAWRHSPSGCFPVGP in isoform 2. 1 PublicationVSP_019846Add
    BLAST
    Alternative sequencei298 – 509212Missing in isoform 2. 1 PublicationVSP_019847Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X75342 mRNA. Translation: CAA53091.1. Different initiation.
    AL583849, AL138752, AL161448 Genomic DNA. Translation: CAH73120.1.
    AL161448, AL138752, AL583849 Genomic DNA. Translation: CAH73192.1.
    AL138752, AL161448, AL583849 Genomic DNA. Translation: CAI13876.1.
    CH471071 Genomic DNA. Translation: EAW58254.1.
    CH471071 Genomic DNA. Translation: EAW58255.1.
    BC094765 mRNA. Translation: AAH94765.1. Different initiation.
    BC136581 mRNA. Translation: AAI36582.1.
    BC136582 mRNA. Translation: AAI36583.1.
    CCDSiCCDS43806.1. [Q15464-1]
    PIRiI38228.
    RefSeqiNP_003019.2. NM_003028.2. [Q15464-1]
    UniGeneiHs.521482.

    Genome annotation databases

    EnsembliENST00000377707; ENSP00000366936; ENSG00000107338. [Q15464-1]
    GeneIDi6461.
    KEGGihsa:6461.
    UCSCiuc004aax.3. human. [Q15464-1]

    Polymorphism databases

    DMDMi110816415.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X75342 mRNA. Translation: CAA53091.1 . Different initiation.
    AL583849 , AL138752 , AL161448 Genomic DNA. Translation: CAH73120.1 .
    AL161448 , AL138752 , AL583849 Genomic DNA. Translation: CAH73192.1 .
    AL138752 , AL161448 , AL583849 Genomic DNA. Translation: CAI13876.1 .
    CH471071 Genomic DNA. Translation: EAW58254.1 .
    CH471071 Genomic DNA. Translation: EAW58255.1 .
    BC094765 mRNA. Translation: AAH94765.1 . Different initiation.
    BC136581 mRNA. Translation: AAI36582.1 .
    BC136582 mRNA. Translation: AAI36583.1 .
    CCDSi CCDS43806.1. [Q15464-1 ]
    PIRi I38228.
    RefSeqi NP_003019.2. NM_003028.2. [Q15464-1 ]
    UniGenei Hs.521482.

    3D structure databases

    ProteinModelPortali Q15464.
    SMRi Q15464. Positions 405-487.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112358. 16 interactions.
    IntActi Q15464. 8 interactions.
    MINTi MINT-7046528.
    STRINGi 9606.ENSP00000366936.

    PTM databases

    PhosphoSitei Q15464.

    Polymorphism databases

    DMDMi 110816415.

    Proteomic databases

    MaxQBi Q15464.
    PaxDbi Q15464.
    PRIDEi Q15464.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000377707 ; ENSP00000366936 ; ENSG00000107338 . [Q15464-1 ]
    GeneIDi 6461.
    KEGGi hsa:6461.
    UCSCi uc004aax.3. human. [Q15464-1 ]

    Organism-specific databases

    CTDi 6461.
    GeneCardsi GC09M037953.
    H-InvDB HIX0008049.
    HIX0079163.
    HIX0189186.
    HGNCi HGNC:10838. SHB.
    HPAi CAB010161.
    HPA049911.
    MIMi 600314. gene.
    neXtProti NX_Q15464.
    PharmGKBi PA35744.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG80632.
    HOGENOMi HOG000038038.
    HOVERGENi HBG066172.
    InParanoidi Q15464.
    OMAi RPDYREQ.
    OrthoDBi EOG793B9C.
    PhylomeDBi Q15464.
    TreeFami TF325799.

    Enzyme and pathway databases

    SignaLinki Q15464.

    Miscellaneous databases

    ChiTaRSi SHB. human.
    GeneWikii SHB_(gene).
    GenomeRNAii 6461.
    NextBioi 25105.
    PROi Q15464.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q15464.
    CleanExi HS_SHB.
    Genevestigatori Q15464.

    Family and domain databases

    Gene3Di 3.30.505.10. 1 hit.
    InterProi IPR000980. SH2.
    [Graphical view ]
    Pfami PF00017. SH2. 1 hit.
    [Graphical view ]
    PRINTSi PR00401. SH2DOMAIN.
    SMARTi SM00252. SH2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55550. SSF55550. 1 hit.
    PROSITEi PS50001. SH2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Shb is a ubiquitously expressed Src homology 2 protein."
      Welsh M., Mares J., Karlsson T., Lavergne C., Breant B., Claesson-Welsh L.
      Oncogene 9:19-27(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INTERACTION WITH PDGFRB.
      Tissue: Fetal brain.
    2. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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 1 AND 2).
      Tissue: Placenta and Testis.
    5. "Molecular interactions of the Src homology 2 domain protein Shb with phosphotyrosine residues, tyrosine kinase receptors and Src homology 3 domain proteins."
      Karlsson T., Songyang Z., Landgren E., Lavergne C., Di Fiore P.P., Anafi M., Pawson T., Cantley L.C., Claesson-Welsh L., Welsh M.
      Oncogene 10:1475-1483(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PDGFRB; FGFR1; EPS8 AND V-SRC.
    6. "Apoptosis of NIH3T3 cells overexpressing the Src homology 2 domain protein Shb."
      Karlsson T., Welsh M.
      Oncogene 13:955-961(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "The Src homology 2 domain protein Shb transmits basic fibroblast growth factor- and nerve growth factor-dependent differentiation signals in PC12 cells."
      Karlsson T., Kullander K., Welsh M.
      Cell Growth Differ. 9:757-766(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Stimulation through the T cell receptor leads to interactions between SHB and several signaling proteins."
      Welsh M., Songyang Z., Frantz J.D., Trueb T., Reedquist K.A., Karlsson T., Miyazaki M., Cantley L.C., Band H., Shoelson S.E.
      Oncogene 16:891-901(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH GRB2; GRAP AND CD3Z, MUTAGENESIS OF ARG-435.
    9. "Requirement of the Src homology 2 domain protein Shb for T cell receptor-dependent activation of the interleukin-2 gene nuclear factor for activation of T cells element in Jurkat T cells."
      Lindholm C.K., Gylfe E., Zhang W., Samelson L.E., Welsh M.
      J. Biol. Chem. 274:28050-28057(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, INTERACTION WITH LAT AND PLCG1.
    10. "Endostatin-induced tyrosine kinase signaling through the Shb adaptor protein regulates endothelial cell apoptosis."
      Dixelius J., Larsson H., Sasaki T., Holmqvist K., Lu L., Engstroem A., Timpl R., Welsh M., Claesson-Welsh L.
      Blood 95:3403-3411(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Platelet-derived growth factor-mediated signaling through the Shb adaptor protein: effects on cytoskeletal organization."
      Hooshmand-Rad R., Lu L., Heldin C.-H., Claesson-Welsh L., Welsh M.
      Exp. Cell Res. 257:245-254(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PDGFRA.
    12. "NGF-dependent neurite outgrowth in PC12 cells overexpressing the Src homology 2-domain protein shb requires activation of the Rap1 pathway."
      Lu L., Anneren C., Reedquist K.A., Bos J.L., Welsh M.
      Exp. Cell Res. 259:370-377(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CRK.
    13. "IL-2 receptor signaling through the Shb adapter protein in T and NK cells."
      Lindholm C.K.
      Biochem. Biophys. Res. Commun. 296:929-936(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IL2RB; IL2RG; JAK1 AND JAK3.
    14. "Shb links SLP-76 and Vav with the CD3 complex in Jurkat T cells."
      Lindholm C.K., Henriksson M.L., Hallberg B., Welsh M.
      Eur. J. Biochem. 269:3279-3288(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ZAP70; LCP2; VAV1 AND GRAP2, SUBCELLULAR LOCATION.
    15. "The Shb adaptor protein binds to tyrosine 766 in the FGFR-1 and regulates the Ras/MEK/MAPK pathway via FRS2 phosphorylation in endothelial cells."
      Cross M.J., Lu L., Magnusson P., Nyqvist D., Holmqvist K., Welsh M., Claesson-Welsh L.
      Mol. Biol. Cell 13:2881-2893(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FGFR1.
    16. "Overexpression of the Shb SH2 domain-protein in insulin-producing cells leads to altered signaling through the IRS-1 and IRS-2 proteins."
      Welsh N., Makeeva N., Welsh M.
      Mol. Med. 8:695-704(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH IRS2.
    17. "The Shb adaptor protein causes Src-dependent cell spreading and activation of focal adhesion kinase in murine brain endothelial cells."
      Holmqvist K., Cross M.J., Riley D., Welsh M.
      Cell. Signal. 15:171-179(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PTK2/FAK1.
    18. "The adaptor protein shb binds to tyrosine 1175 in vascular endothelial growth factor (VEGF) receptor-2 and regulates VEGF-dependent cellular migration."
      Holmqvist K., Cross M.J., Rolny C., Haegerkvist R., Rahimi N., Matsumoto T., Claesson-Welsh L., Welsh M.
      J. Biol. Chem. 279:22267-22275(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH KDR.
    19. "Shb promotes blood vessel formation in embryoid bodies by augmenting vascular endothelial growth factor receptor-2 and platelet-derived growth factor receptor-beta signaling."
      Rolny C., Lu L., Aagren N., Nilsson I., Roe C., Webb G.C., Welsh M.
      Exp. Cell Res. 308:381-393(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.

    Entry informationi

    Entry nameiSHB_HUMAN
    AccessioniPrimary (citable) accession number: Q15464
    Secondary accession number(s): B9EGM0
    , D3DRQ5, Q504U5, Q5VUM8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 25, 2006
    Last sequence update: July 25, 2006
    Last modified: October 1, 2014
    This is version 107 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

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