Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q96B97

- SH3K1_HUMAN

UniProt

Q96B97 - SH3K1_HUMAN

Protein

SH3 domain-containing kinase-binding protein 1

Gene

SH3KBP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 2 (23 May 2003)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Adapter protein involved in regulating diverse signal transduction pathways. Involved in the regulation of endocytosis and lysosomal degradation of ligand-induced receptor tyrosine kinases, including EGFR and MET/hepatocyte growth factor receptor, through a association with CBL and endophilins. The association with CBL, and thus the receptor internalization, may inhibited by an interaction with PDCD6IP and/or SPRY2. Involved in regulation of ligand-dependent endocytosis of the IgE receptor. Attenuates phosphatidylinositol 3-kinase activity by interaction with its regulatory subunit By similarity. May be involved in regulation of cell adhesion; promotes the interaction between TTK2B and PDCD6IP. May be involved in the regulation of cellular stress response via the MAPK pathways through its interaction with MAP3K4. Is involved in modulation of tumor necrosis factor mediated apoptosis. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration.By similarity10 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. cell-cell signaling Source: UniProtKB
    3. cell migration Source: UniProtKB
    4. cytoskeleton organization Source: UniProtKB
    5. endocytosis Source: UniProtKB-KW
    6. epidermal growth factor receptor signaling pathway Source: Reactome
    7. negative regulation of epidermal growth factor receptor signaling pathway Source: Reactome
    8. regulation of cell shape Source: UniProtKB

    Keywords - Biological processi

    Apoptosis, Endocytosis

    Enzyme and pathway databases

    ReactomeiREACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_12484. EGFR downregulation.
    SignaLinkiQ96B97.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    SH3 domain-containing kinase-binding protein 1
    Alternative name(s):
    CD2-binding protein 3
    Short name:
    CD2BP3
    Cbl-interacting protein of 85 kDa
    Human Src family kinase-binding protein 1
    Short name:
    HSB-1
    Gene namesi
    Name:SH3KBP1
    Synonyms:CIN85
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:13867. SH3KBP1.

    Subcellular locationi

    Cytoplasmcytoskeleton. Cytoplasmic vesicle membrane; Peripheral membrane protein. Cell junctionsynapsesynaptosome. Cell junctionfocal adhesion By similarity
    Note: Localized in endocytic vesicles containing clustered receptors. Colocalizes with ASAP1 in vesicular structures. Colocalized with actin microfilaments and focal adhesions By similarity. Colocalized with MAGI2 in synaptosomes By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
    2. cytoskeleton Source: UniProtKB-SubCell
    3. cytosol Source: Reactome
    4. focal adhesion Source: UniProtKB-SubCell
    5. neuron projection Source: UniProtKB-SubCell
    6. plasma membrane Source: Reactome
    7. synapse Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cell junction, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Membrane, Synapse, Synaptosome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37822.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 665665SH3 domain-containing kinase-binding protein 1PRO_0000097728Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei230 – 2301Phosphoserine6 Publications
    Modified residuei254 – 2541Phosphothreonine1 Publication
    Modified residuei436 – 4361Phosphoserine2 Publications
    Modified residuei509 – 5091Phosphoserine1 Publication
    Modified residuei511 – 5111Phosphoserine1 Publication
    Modified residuei521 – 5211Phosphoserine1 Publication
    Modified residuei587 – 5871Phosphoserine2 Publications

    Post-translational modificationi

    Monoubiquitinated by CBL and CBLB after EGF stimulation; probably on its C-terminus.

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ96B97.
    PaxDbiQ96B97.
    PRIDEiQ96B97.

    PTM databases

    PhosphoSiteiQ96B97.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. Also expressed in some cancer cell lines.

    Gene expression databases

    ArrayExpressiQ96B97.
    BgeeiQ96B97.
    CleanExiHS_SH3KBP1.
    GenevestigatoriQ96B97.

    Organism-specific databases

    HPAiCAB021892.
    HPA003351.
    HPA003355.

    Interactioni

    Subunit structurei

    Can self-associate and form homotetramers. Interacts with CD2, F-actin capping protein, PIK3R3, GRB2, EGFR, MET, BLNK, MAP3K4, PDCD6IP, SPRY2, ARHGAP17, ARHGAP27, MAGI2, CRK, BCAR1, SOS1, ASAP1, ARAP3, HIP1R, SYNJ2, INPP5D and STAP1. Interacts with CBL and CBLB, but does not interact with CBLC. Two molecules of SH3KBP1 seem to bind through their respective SH3 1 domain to one molecule of CBLB. The interaction with CBL or CBLB and EGFR is increased upon EGF stimulation. The interaction with CBL is attenuated by PDCD6IP. Interacts through its proline-rich region with the SH3 domain of endophilins SH3GL1, SH3GL2 and SH3GL3. The SH3KBP1-endophilin complex seems to associate with a complex containing the phosphorylated receptor (EGFR or MET) and phosphorylated CBL. Probably associates with ASAP1 and phosphorylated EGFR. Probably part of a complex consisting of at least SH3KBP1, ASAP1 and ARAP3. Interacts with focal adhesion kinases PTK2/FAK1 AND PTK2B/PYK2, probably as a dimer. Interacts with DAB2 and probably associates with chathrin through its interaction with DAB2. Part of a complex consisting of SH3KBP1, DAB2, and clathrin heavy chain. DAB2 and clathrin dissociate from SH3KBP1 following growth factor treatment, enabling interaction with CBL. Interacts with DDN and probably associates with MAGI2 through its interaction with DDN. Interacts with the SH3 domains of SRC tyrosine-protein kinases SRC, LCK, LYN, FGR, FYN and HCK. Interacts with TRADD, BIRC2, TRAF1, TRAF2 and TNFR1, and the association with a TNFR1-associated complex upon stimulation with TNF-alpha seems to be mediated by SRC. Probably interacts with SH3KBP1.17 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARAP3Q8WWN82EBI-346595,EBI-4402732
    ASAP1Q9ULH18EBI-346595,EBI-346622
    CAPZA1P529072EBI-346595,EBI-355586
    CBLP2268118EBI-346595,EBI-518228
    CBLBQ1319119EBI-346595,EBI-744027
    CD2P067293EBI-346595,EBI-3912464
    Dab2P980789EBI-346595,EBI-1391846From a different organism.
    DDNO948505EBI-346595,EBI-5240523
    DNM2P505705EBI-346595,EBI-346547
    Dnm2P390524EBI-346595,EBI-349613From a different organism.
    Hip1rQ9JKY53EBI-346595,EBI-642457From a different organism.
    INPP5DQ928356EBI-346595,EBI-1380477
    MAP3K4Q9Y6R45EBI-346595,EBI-448104
    SH3BP2P783148EBI-346595,EBI-727062
    SH3GL2Q999622EBI-346595,EBI-77938
    SPRY2O435972EBI-346595,EBI-742487
    SQSTM1Q135014EBI-346595,EBI-307104
    STAP1Q9ULZ24EBI-346595,EBI-6083058
    SYNJ2O150563EBI-346595,EBI-310513
    UBCP0CG486EBI-346595,EBI-3390054

    Protein-protein interaction databases

    BioGridi119029. 240 interactions.
    DIPiDIP-31803N.
    IntActiQ96B97. 42 interactions.
    MINTiMINT-233697.
    STRINGi9606.ENSP00000380921.

    Structurei

    Secondary structure

    1
    665
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 85
    Beta strandi25 – 306
    Turni33 – 353
    Beta strandi36 – 416
    Beta strandi44 – 496
    Helixi50 – 523
    Beta strandi53 – 553
    Beta strandi102 – 1054
    Beta strandi113 – 1153
    Beta strandi124 – 1263
    Helixi130 – 1323
    Beta strandi149 – 1535
    Turni161 – 1644
    Beta strandi270 – 2767
    Beta strandi283 – 2853
    Beta strandi293 – 2997
    Beta strandi301 – 3033
    Beta strandi306 – 3116
    Beta strandi314 – 3196
    Helixi320 – 3223
    Beta strandi323 – 3253

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2BZ8X-ray2.00A/B1-58[»]
    2K6DNMR-A267-328[»]
    2K9GNMR-A262-333[»]
    2O2ONMR-A92-168[»]
    2YDLX-ray2.05A270-328[»]
    ProteinModelPortaliQ96B97.
    SMRiQ96B97. Positions 2-58, 92-182, 262-345.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96B97.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 5858SH3 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini98 – 15760SH3 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini267 – 32862SH3 3PROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili602 – 66463Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi327 – 428102Pro-richAdd
    BLAST

    Domaini

    The SH3 domains mediate interaction with SHKBP1.By similarity

    Sequence similaritiesi

    Contains 3 SH3 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat, SH3 domain, SH3-binding

    Phylogenomic databases

    eggNOGiNOG319250.
    HOGENOMiHOG000231405.
    HOVERGENiHBG057824.
    InParanoidiQ96B97.
    KOiK12470.
    OMAiMDSRTKT.
    OrthoDBiEOG7W41BC.
    PhylomeDBiQ96B97.
    TreeFamiTF350191.

    Family and domain databases

    InterProiIPR001452. SH3_domain.
    [Graphical view]
    PfamiPF14604. SH3_9. 3 hits.
    [Graphical view]
    PRINTSiPR00452. SH3DOMAIN.
    SMARTiSM00326. SH3. 3 hits.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 3 hits.
    PROSITEiPS50002. SH3. 3 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96B97-1) [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

    MVEAIVEFDY QAQHDDELTI SVGEIITNIR KEDGGWWEGQ INGRRGLFPD    50
    NFVREIKKEM KKDPLTNKAP EKPLHEVPSG NSLLSSETIL RTNKRGERRR 100
    RRCQVAFSYL PQNDDELELK VGDIIEVVGE VEEGWWEGVL NGKTGMFPSN 150
    FIKELSGESD ELGISQDEQL SKSSLRETTG SESDGGDSSS TKSEGANGTV 200
    ATAAIQPKKV KGVGFGDIFK DKPIKLRPRS IEVENDFLPV EKTIGKKLPA 250
    TTATPDSSKT EMDSRTKSKD YCKVIFPYEA QNDDELTIKE GDIVTLINKD 300
    CIDVGWWEGE LNGRRGVFPD NFVKLLPPDF EKEGNRPKKP PPPSAPVIKQ 350
    GAGTTERKHE IKKIPPERPE MLPNRTEEKE RPEREPKLDL QKPSVPAIPP 400
    KKPRPPKTNS LSRPGALPPR RPERPVGPLT HTRGDSPKID LAGSSLSGIL 450
    DKDLSDRSND IDLEGFDSVV SSTEKLSHPT TSRPKATGRR PPSQSLTSSS 500
    LSSPDIFDSP SPEEDKEEHI SLAHRGVDAS KKTSKTVTIS QVSDNKASLP 550
    PKPGTMAAGG GGPAPLSSAA PSPLSSSLGT AGHRANSPSL FGTEGKPKME 600
    PAASSQAAVE ELRTQVRELR SIIETMKDQQ KREIKQLLSE LDEEKKIRLR 650
    LQMEVNDIKK ALQSK 665

    Note: Interacts with CBL.

    Length:665
    Mass (Da):73,126
    Last modified:May 23, 2003 - v2
    Checksum:i3BD350FCDB14BD4C
    GO
    Isoform 2 (identifier: Q96B97-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-54: MVEAIVEFDYQAQHDDELTISVGEIITNIRKEDGGWWEGQINGRRGLFPDNFVR → MEVSAAKAPSAADLSEI

    Note: Interacts with CD2 cytoplasmic tail and does not interact with F-actin.

    Show »
    Length:628
    Mass (Da):68,550
    Checksum:i8AD93481480879D6
    GO
    Isoform 3 (identifier: Q96B97-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-4: MVEA → MGEE
         5-242: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:427
    Mass (Da):46,610
    Checksum:iCDD6AC2770E695F4
    GO

    Sequence cautioni

    The sequence AAH50663.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti288 – 2881I → T in BAH11471. (PubMed:14702039)Curated
    Sequence conflicti426 – 4261V → A in BAH11471. (PubMed:14702039)Curated
    Sequence conflicti570 – 5701A → V in AAH15806. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti382 – 3821P → L.1 Publication
    VAR_015667

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5454MVEAI…DNFVR → MEVSAAKAPSAADLSEI in isoform 2. 2 PublicationsVSP_007504Add
    BLAST
    Alternative sequencei1 – 44MVEA → MGEE in isoform 3. 1 PublicationVSP_044655
    Alternative sequencei5 – 242238Missing in isoform 3. 1 PublicationVSP_044656Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF230904 mRNA. Translation: AAF37854.1.
    AF542051 mRNA. Translation: AAN77231.1.
    AK293234 mRNA. Translation: BAH11470.1.
    AK293237 mRNA. Translation: BAH11471.1.
    AL732423, AL732325, AL732327 Genomic DNA. Translation: CAI40277.1.
    AL732423, AL732327 Genomic DNA. Translation: CAI40278.1.
    AL732327, AL732325, AL732423 Genomic DNA. Translation: CAI40511.1.
    AL732327, AL732423 Genomic DNA. Translation: CAI40512.1.
    AL732325, AL732327, AL732423 Genomic DNA. Translation: CAI41254.1.
    AL732409 Genomic DNA. No translation available.
    AL772197 Genomic DNA. No translation available.
    BC015806 mRNA. Translation: AAH15806.1.
    BC050663 mRNA. Translation: AAH50663.1. Sequence problems.
    AF329267 mRNA. Translation: AAK95587.1.
    AF329268 mRNA. Translation: AAO13348.1.
    CCDSiCCDS14193.1. [Q96B97-1]
    CCDS35213.1. [Q96B97-2]
    CCDS55383.1. [Q96B97-3]
    PIRiJC7191.
    RefSeqiNP_001019837.1. NM_001024666.2. [Q96B97-2]
    NP_001171889.1. NM_001184960.1. [Q96B97-3]
    NP_114098.1. NM_031892.2. [Q96B97-1]
    UniGeneiHs.726365.

    Genome annotation databases

    EnsembliENST00000379698; ENSP00000369020; ENSG00000147010. [Q96B97-2]
    ENST00000379716; ENSP00000369039; ENSG00000147010. [Q96B97-3]
    ENST00000397821; ENSP00000380921; ENSG00000147010. [Q96B97-1]
    GeneIDi30011.
    KEGGihsa:30011.
    UCSCiuc004czl.3. human. [Q96B97-2]
    uc004czm.3. human. [Q96B97-1]
    uc011mjf.2. human.

    Polymorphism databases

    DMDMi31077034.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF230904 mRNA. Translation: AAF37854.1 .
    AF542051 mRNA. Translation: AAN77231.1 .
    AK293234 mRNA. Translation: BAH11470.1 .
    AK293237 mRNA. Translation: BAH11471.1 .
    AL732423 , AL732325 , AL732327 Genomic DNA. Translation: CAI40277.1 .
    AL732423 , AL732327 Genomic DNA. Translation: CAI40278.1 .
    AL732327 , AL732325 , AL732423 Genomic DNA. Translation: CAI40511.1 .
    AL732327 , AL732423 Genomic DNA. Translation: CAI40512.1 .
    AL732325 , AL732327 , AL732423 Genomic DNA. Translation: CAI41254.1 .
    AL732409 Genomic DNA. No translation available.
    AL772197 Genomic DNA. No translation available.
    BC015806 mRNA. Translation: AAH15806.1 .
    BC050663 mRNA. Translation: AAH50663.1 . Sequence problems.
    AF329267 mRNA. Translation: AAK95587.1 .
    AF329268 mRNA. Translation: AAO13348.1 .
    CCDSi CCDS14193.1. [Q96B97-1 ]
    CCDS35213.1. [Q96B97-2 ]
    CCDS55383.1. [Q96B97-3 ]
    PIRi JC7191.
    RefSeqi NP_001019837.1. NM_001024666.2. [Q96B97-2 ]
    NP_001171889.1. NM_001184960.1. [Q96B97-3 ]
    NP_114098.1. NM_031892.2. [Q96B97-1 ]
    UniGenei Hs.726365.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2BZ8 X-ray 2.00 A/B 1-58 [» ]
    2K6D NMR - A 267-328 [» ]
    2K9G NMR - A 262-333 [» ]
    2O2O NMR - A 92-168 [» ]
    2YDL X-ray 2.05 A 270-328 [» ]
    ProteinModelPortali Q96B97.
    SMRi Q96B97. Positions 2-58, 92-182, 262-345.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119029. 240 interactions.
    DIPi DIP-31803N.
    IntActi Q96B97. 42 interactions.
    MINTi MINT-233697.
    STRINGi 9606.ENSP00000380921.

    PTM databases

    PhosphoSitei Q96B97.

    Polymorphism databases

    DMDMi 31077034.

    Proteomic databases

    MaxQBi Q96B97.
    PaxDbi Q96B97.
    PRIDEi Q96B97.

    Protocols and materials databases

    DNASUi 30011.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000379698 ; ENSP00000369020 ; ENSG00000147010 . [Q96B97-2 ]
    ENST00000379716 ; ENSP00000369039 ; ENSG00000147010 . [Q96B97-3 ]
    ENST00000397821 ; ENSP00000380921 ; ENSG00000147010 . [Q96B97-1 ]
    GeneIDi 30011.
    KEGGi hsa:30011.
    UCSCi uc004czl.3. human. [Q96B97-2 ]
    uc004czm.3. human. [Q96B97-1 ]
    uc011mjf.2. human.

    Organism-specific databases

    CTDi 30011.
    GeneCardsi GC0XM019552.
    HGNCi HGNC:13867. SH3KBP1.
    HPAi CAB021892.
    HPA003351.
    HPA003355.
    MIMi 300374. gene.
    neXtProti NX_Q96B97.
    PharmGKBi PA37822.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG319250.
    HOGENOMi HOG000231405.
    HOVERGENi HBG057824.
    InParanoidi Q96B97.
    KOi K12470.
    OMAi MDSRTKT.
    OrthoDBi EOG7W41BC.
    PhylomeDBi Q96B97.
    TreeFami TF350191.

    Enzyme and pathway databases

    Reactomei REACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_12484. EGFR downregulation.
    SignaLinki Q96B97.

    Miscellaneous databases

    ChiTaRSi SH3KBP1. human.
    EvolutionaryTracei Q96B97.
    GeneWikii SH3KBP1.
    GenomeRNAii 30011.
    NextBioi 52832.
    PROi Q96B97.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96B97.
    Bgeei Q96B97.
    CleanExi HS_SH3KBP1.
    Genevestigatori Q96B97.

    Family and domain databases

    InterProi IPR001452. SH3_domain.
    [Graphical view ]
    Pfami PF14604. SH3_9. 3 hits.
    [Graphical view ]
    PRINTSi PR00452. SH3DOMAIN.
    SMARTi SM00326. SH3. 3 hits.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 3 hits.
    PROSITEi PS50002. SH3. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of a novel adaptor protein, CIN85, that interacts with c-Cbl."
      Take H., Watanabe S., Takeda K., Yu Z.-X., Iwata N., Kajigaya S.
      Biochem. Biophys. Res. Commun. 268:321-328(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CBL.
    2. "CD2BP3, CIN85 and the structurally related adaptor protein CMS bind to the same CD2 cytoplasmic segment but elicit divergent functional activities."
      Tibaldi E.V., Reinherz E.L.
      Int. Immunol. 15:313-329(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: T-cell.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    4. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      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] (ISOFORM 1).
      Tissue: Adrenal cortex and Uterus.
    6. "Assignment of SH3KBP1 to human chromosome band Xp22.1-->p21.3 by in situ hybridization."
      Narita T., Amano F., Yoshizaki K., Nishimoto N., Nishimura T., Tajima T., Namiki H., Taniyama T.
      Cytogenet. Cell Genet. 93:133-134(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 262-665, VARIANT LEU-382.
    7. "Characterization of the CIN85 adaptor protein and identification of components involved in CIN85 complexes."
      Watanabe S., Take H., Takeda K., Yu Z.X., Iwata N., Kajigaya S.
      Biochem. Biophys. Res. Commun. 278:167-174(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BLNK; CRK; BCAR1; PIK3R3; GRB2 AND SOS1, SELF-ASSOCIATION.
    8. "CIN85 participates in Cbl-b-mediated down-regulation of receptor tyrosine kinases."
      Szymkiewicz I., Kowanetz K., Soubeyran P., Dinarina A., Lipkowitz S., Dikic I.
      J. Biol. Chem. 277:39666-39672(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CBLB AND ENDOPHILINS, LACK OF INTERACTION WITH CBLC, FUNCTION IN RECEPTOR INTERNALIZATION, SUBCELLULAR LOCATION.
    9. "Cbl-CIN85-endophilin complex mediates ligand-induced downregulation of EGF receptors."
      Soubeyran P., Kowanetz K., Szymkiewicz I., Langdon W.Y., Dikic I.
      Nature 416:183-187(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN RECEPTOR INTERNALIZATION, INTERACTION WITH EGFR; SH3GL1; SH3GL2; SH3GL3 AND CBL, SUBCELLULAR LOCATION.
    10. "The endophilin-CIN85-Cbl complex mediates ligand-dependent downregulation of c-Met."
      Petrelli A., Gilestro G.F., Lanzardo S., Comoglio P.M., Migone N., Giordano S.
      Nature 416:187-190(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN RECEPTOR INTERNALIZATION, INTERACTION WITH SH3GL1; SH3GL2; SH3GL3; CBL AND MET.
    11. "Cbl-directed monoubiquitination of CIN85 is involved in regulation of ligand-induced degradation of EGF receptors."
      Haglund K., Shimokawa N., Szymkiewicz I., Dikic I.
      Proc. Natl. Acad. Sci. U.S.A. 99:12191-12196(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION BY CBL AND CBLB.
    12. "Dab2 links CIN85 with clathrin-mediated receptor internalization."
      Kowanetz K., Terzic J., Dikic I.
      FEBS Lett. 554:81-87(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DAB2, IDENTIFICATION IN A COMPLEX WITH DAB2 AND CLATHRIN.
    13. "SETA/CIN85/Ruk and its binding partner AIP1 associate with diverse cytoskeletal elements, including FAKs, and modulate cell adhesion."
      Schmidt M.H., Chen B., Randazzo L.M., Boegler O.
      J. Cell Sci. 116:2845-2855(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL ADHESION, INTERACTION WITH PDCD6IP; PTK2/FAK1 AND PTK2B/PYK2.
    14. "Linking the T cell surface protein CD2 to the actin-capping protein CAPZ via CMS and CIN85."
      Hutchings N.J., Clarkson N., Chalkley R., Barclay A.N., Brown M.H.
      J. Biol. Chem. 278:22396-22403(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CD2 AND F-ACTIN CAPPING PROTEIN.
    15. "Epidermal growth factor receptor signaling intensity determines intracellular protein interactions, ubiquitination, and internalization."
      Schmidt M.H., Furnari F.B., Cavenee W.K., Bogler O.
      Proc. Natl. Acad. Sci. U.S.A. 100:6505-6510(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN RECEPTOR INTERNALIZATION.
    16. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    17. "CIN85 associates with multiple effectors controlling intracellular trafficking of epidermal growth factor receptors."
      Kowanetz K., Husnjak K., Holler D., Kowanetz M., Soubeyran P., Hirsch D., Schmidt M.H., Pavelic K., De Camilli P., Randazzo P.A., Dikic I.
      Mol. Biol. Cell 15:3155-3166(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN RECEPTOR INTERNALIZATION, INTERACTION WITH ASAP1; ARAP3; HIP1R; SYNJ2; INPP5D; STAP1 AND EGFR, IDENTIFICATION IN A COMPLEX WITH ASAP1 AND ARAP3, SUBCELLULAR LOCATION.
    18. "Alix/AIP1 antagonizes epidermal growth factor receptor downregulation by the Cbl-SETA/CIN85 complex."
      Schmidt M.H., Hoeller D., Yu J., Furnari F.B., Cavenee W.K., Dikic I., Bogler O.
      Mol. Cell. Biol. 24:8981-8993(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PDCD6IP; EGFR; CBL AND CBLB.
    19. "CIN85 regulates the ability of MEKK4 to activate the p38 MAP kinase pathway."
      Aissouni Y., Zapart G., Iovanna J.L., Dikic I., Soubeyran P.
      Biochem. Biophys. Res. Commun. 338:808-814(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MAP3K4.
    20. "Sprouty2 acts at the Cbl/CIN85 interface to inhibit epidermal growth factor receptor downregulation."
      Haglund K., Schmidt M.H., Wong E.S., Guy G.R., Dikic I.
      EMBO Rep. 6:635-641(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SPRY2.
    21. "CIN85 associates with TNF receptor 1 via Src and modulates TNF-alpha-induced apoptosis."
      Narita T., Nishimura T., Yoshizaki K., Taniyama T.
      Exp. Cell Res. 304:256-264(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN APOPTOSIS, INTERACTION WITH SRC; LCK; LYN; FGR; FYN; HCK; TRADD; BIRC2; TRAF1; TRAF2 AND TNFR1.
    22. "CIN85 regulates the ligand-dependent endocytosis of the IgE receptor: a new molecular mechanism to dampen mast cell function."
      Molfetta R., Belleudi F., Peruzzi G., Morrone S., Leone L., Dikic I., Piccoli M., Frati L., Torrisi M.R., Santoni A., Paolini R.
      J. Immunol. 175:4208-4216(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN RECEPTOR INTERNALIZATION.
    23. "A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity proteins in epithelial cells."
      Wells C.D., Fawcett J.P., Traweger A., Yamanaka Y., Goudreault M., Elder K., Kulkarni S., Gish G., Virag C., Lim C., Colwill K., Starostine A., Metalnikov P., Pawson T.
      Cell 125:535-548(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARHGAP17.
    24. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    25. "CIN85 is localized at synapses and forms a complex with S-SCAM via dendrin."
      Kawata A., Iida J., Ikeda M., Sato Y., Mori H., Kansaku A., Sumita K., Fujiwara N., Rokukawa C., Hamano M., Hirabayashi S., Hata Y.
      J. Biochem. 139:931-939(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DDN AND MAGI2, SUBCELLULAR LOCATION.
    26. "CFBP is a novel tyrosine-phosphorylated protein that might function as a regulator of CIN85/CD2AP."
      Konishi H., Tashiro K., Murata Y., Nabeshi H., Yamauchi E., Taniguchi H.
      J. Biol. Chem. 281:28919-28931(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MVB12A.
    27. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    28. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-254; SER-436; SER-509; SER-511; SER-521 AND SER-587, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    29. "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-230, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    30. "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-230; SER-436 AND SER-587, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    31. "Identification and characterization of a set of conserved and new regulators of cytoskeletal organisation, cell morphology and migration."
      Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V., Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.
      BMC Biol. 9:54-54(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    32. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    33. "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-230, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    34. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-58 IN COMPLEX WITH CBLB.

    Entry informationi

    Entry nameiSH3K1_HUMAN
    AccessioniPrimary (citable) accession number: Q96B97
    Secondary accession number(s): B7Z1D5
    , Q5JPT4, Q5JPT5, Q8IWX6, Q8IX98, Q96RN4, Q9NYR0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 23, 2003
    Last sequence update: May 23, 2003
    Last modified: October 1, 2014
    This is version 133 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3