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Q8R550

- SH3K1_MOUSE

UniProt

Q8R550 - SH3K1_MOUSE

Protein

SH3 domain-containing kinase-binding protein 1

Gene

Sh3kbp1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 1 (01 Jun 2002)
      Previous versions | rss
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    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. 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 similarity.By similarity

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. cell migration Source: UniProtKB
    3. cytoskeleton organization Source: UniProtKB
    4. endocytosis Source: UniProtKB-KW
    5. regulation of cell shape Source: UniProtKB

    Keywords - Biological processi

    Apoptosis, Endocytosis

    Enzyme and pathway databases

    ReactomeiREACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_203917. EGFR downregulation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    SH3 domain-containing kinase-binding protein 1
    Alternative name(s):
    Regulator of ubiquitous kinase
    Short name:
    Ruk
    SH3-containing, expressed in tumorigenic astrocytes
    Gene namesi
    Name:Sh3kbp1
    Synonyms:Ruk, Seta
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:1889583. Sh3kbp1.

    Subcellular locationi

    Cytoplasmcytoskeleton By similarity. Cytoplasmic vesicle membrane By similarity; Peripheral membrane protein By similarity. Cell junctionsynapsesynaptosome By similarity. 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. cell-cell junction Source: MGI
    2. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
    3. cytoskeleton Source: UniProtKB-SubCell
    4. focal adhesion Source: UniProtKB-SubCell
    5. neuron projection Source: UniProtKB-SubCell
    6. synapse Source: UniProtKB-KW

    Keywords - Cellular componenti

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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 709709SH3 domain-containing kinase-binding protein 1PRO_0000097729Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei274 – 2741Phosphoserine2 Publications
    Modified residuei298 – 2981PhosphothreonineBy similarity
    Modified residuei480 – 4801PhosphoserineBy similarity
    Modified residuei553 – 5531PhosphoserineBy similarity
    Modified residuei555 – 5551PhosphoserineBy similarity
    Modified residuei565 – 5651PhosphoserineBy similarity
    Modified residuei631 – 6311PhosphoserineBy similarity

    Post-translational modificationi

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

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ8R550.
    PaxDbiQ8R550.
    PRIDEiQ8R550.

    PTM databases

    PhosphoSiteiQ8R550.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8R550.
    BgeeiQ8R550.
    CleanExiMM_SH3KBP1.
    GenevestigatoriQ8R550.

    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, 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 part of a complex consisting of at least SH3KBP1, ASAP1 and ARAP3 By similarity. Interacts with SHKBP1. Interacts with ATX2.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Dlg4Q621083EBI-642709,EBI-300895

    Protein-protein interaction databases

    BioGridi208383. 6 interactions.
    IntActiQ8R550. 9 interactions.
    MINTiMINT-1591643.

    Structurei

    Secondary structure

    1
    709
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi103 – 1075
    Beta strandi129 – 1324
    Beta strandi135 – 1384
    Beta strandi145 – 1484
    Beta strandi151 – 1544
    Beta strandi314 – 3185
    Beta strandi336 – 3427
    Beta strandi350 – 3545
    Beta strandi359 – 3635
    Helixi364 – 3663
    Beta strandi367 – 3693

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WI7NMR-A101-155[»]
    2DA9NMR-A314-370[»]
    ProteinModelPortaliQ8R550.
    SMRiQ8R550. Positions 2-166, 314-389.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8R550.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 5858SH3 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini98 – 15760SH3 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini311 – 37262SH3 3PROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili646 – 70863Sequence AnalysisAdd
    BLAST

    Domaini

    The SH3 domains mediate interaction with SHKBP1.

    Sequence similaritiesi

    Contains 3 SH3 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat, SH3 domain, SH3-binding

    Phylogenomic databases

    eggNOGiNOG319250.
    GeneTreeiENSGT00530000063594.
    HOVERGENiHBG057824.
    InParanoidiQ8R550.
    KOiK12470.
    OMAiMDSRTKT.
    OrthoDBiEOG7W41BC.
    PhylomeDBiQ8R550.
    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 (8)i

    Sequence statusi: Complete.

    This entry describes 8 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8R550-1) [UniParc]FASTAAdd to Basket

    Also known as: Ruk-xl

    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 SVGEVITNIR KEDGGWWEGQ INGRRGLFPD    50
    NFVREIKKDM KKDLLSNKAP EKPMHDVSSG NALLSSETIL RTNKRGERRR 100
    RRCQVAFSYL PQNDDELELK VGDIIEVVGE VEEGWWEGVL NGKTGMFPSN 150
    FIKELSGESD ELGISQDEQL SKSRPEGFLP ASLLPFPAHG AKGKTTFEGT 200
    ILYRAAPGKT EGHRRYYSLR ETTGSESDGG DSSSTKSEGA NGTMATAAIQ 250
    PKKVKGVGFG DIFKDKPIKL RPRSIEVEND FLPVEKTIGK KLPPATSTPD 300
    PSKTEMDSRT KTKDYCKVIF PYEAQNDDEL TIKEGDIVTL INKDCIDVGW 350
    WEGELNGRRG VFPDNFVKLL PSDFDKEGNR PKKPPPPSAP VVKQGAGTTE 400
    RKHEIKKIPP ERPETLPNRT EEKERPEREP KLDLQKPSVP AIPPKKPRPP 450
    KTNSLNRPGA LPPRRPERPV GPLTHTRGDS PKIDLAGSAL SGILDKDLSD 500
    RSNDIDLEGF DSVISSTEKL SHPTTSRPKA TGRRPPSQSL TSSSLSSPDI 550
    FDSPSPEEDK EEHISLAHRG IDVSKKTSKT VTISQVSDNK TSLPPKPGTM 600
    AAASSGPASL SSVASSPMSS SLGTAGQRAS SPSLFSTEGK PKMEPAVSSQ 650
    AAIEELKMQV RELRTIIETM KDQQKREIKQ LLSELDEEKK IRLRLQMEVN 700
    DIKKALQSK 709
    Length:709
    Mass (Da):78,170
    Last modified:June 1, 2002 - v1
    Checksum:iAC2DDFB3248A458B
    GO
    Isoform 2 (identifier: Q8R550-2) [UniParc]FASTAAdd to Basket

    Also known as: Ruk-l

    The sequence of this isoform differs from the canonical sequence as follows:
         174-217: Missing.

    Show »
    Length:665
    Mass (Da):73,328
    Checksum:i724607807A66B043
    GO
    Isoform 3 (identifier: Q8R550-3) [UniParc]FASTAAdd to Basket

    Also known as: Ruk-deltaA

    The sequence of this isoform differs from the canonical sequence as follows:
         1-54: MVEAIVEFDYQAQHDDELTISVGEVITNIRKEDGGWWEGQINGRRGLFPDNFVR → MELSAAKAPSPTDLPES
         174-217: Missing.

    Show »
    Length:628
    Mass (Da):68,820
    Checksum:i1C4AEC6BE48D5D17
    GO
    Isoform 4 (identifier: Q8R550-4) [UniParc]FASTAAdd to Basket

    Also known as: Ruk-m1

    The sequence of this isoform differs from the canonical sequence as follows:
         1-286: MVEAIVEFDY...VENDFLPVEK → MGEEVSLGEK...FGVFLVNEET

    Show »
    Length:464
    Mass (Da):50,755
    Checksum:i54F018C499D51044
    GO
    Isoform 5 (identifier: Q8R550-5) [UniParc]FASTAAdd to Basket

    Also known as: Ruk-m3

    The sequence of this isoform differs from the canonical sequence as follows:
         1-286: MVEAIVEFDY...VENDFLPVEK → MGEE

    Show »
    Length:427
    Mass (Da):46,827
    Checksum:i460A56431A4FDDCD
    GO
    Isoform 6 (identifier: Q8R550-6) [UniParc]FASTAAdd to Basket

    Also known as: Ruk-t

    The sequence of this isoform differs from the canonical sequence as follows:
         1-477: MVEAIVEFDY...RPVGPLTHTR → MFPFRKGARPPSMNLFRQTCW

    Show »
    Length:253
    Mass (Da):27,442
    Checksum:iD1B221FDDE4C72C7
    GO
    Isoform 7 (identifier: Q8R550-7) [UniParc]FASTAAdd to Basket

    Also known as: Ruk-h

    The sequence of this isoform differs from the canonical sequence as follows:
         1-599: Missing.

    Show »
    Length:110
    Mass (Da):11,992
    Checksum:i6536493B3B3761DE
    GO
    Isoform 8 (identifier: Q8R550-8) [UniParc]FASTAAdd to Basket

    Also known as: Ruk-deltaCP

    The sequence of this isoform differs from the canonical sequence as follows:
         174-217: Missing.
         320-630: Missing.

    Show »
    Length:354
    Mass (Da):39,765
    Checksum:iB580135B37F9B571
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti251 – 2599PKKVKGVGF → NDDELTIKE1 PublicationCurated
    Sequence conflicti478 – 52851GDSPK…TTSRP → YCHVLTKAGGHGMIMKIGEG MRTKLCLKIPATFFSSEKVV ARCWGATWCRL in BAC30033. (PubMed:16141072)CuratedAdd
    BLAST
    Sequence conflicti529 – 709181Missing in BAC30033. (PubMed:16141072)CuratedAdd
    BLAST

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 599599Missing in isoform 7. CuratedVSP_007509Add
    BLAST
    Alternative sequencei1 – 477477MVEAI…LTHTR → MFPFRKGARPPSMNLFRQTC W in isoform 6. CuratedVSP_007508Add
    BLAST
    Alternative sequencei1 – 286286MVEAI…LPVEK → MGEEVSLGEKNISPEQASCG ALHPRGWGSQTFGVFLVNEE T in isoform 4. CuratedVSP_007507Add
    BLAST
    Alternative sequencei1 – 286286MVEAI…LPVEK → MGEE in isoform 5. CuratedVSP_007506Add
    BLAST
    Alternative sequencei1 – 5454MVEAI…DNFVR → MELSAAKAPSPTDLPES in isoform 3. 1 PublicationVSP_007505Add
    BLAST
    Alternative sequencei174 – 21744Missing in isoform 2, isoform 3 and isoform 8. 2 PublicationsVSP_007510Add
    BLAST
    Alternative sequencei320 – 630311Missing in isoform 8. 1 PublicationVSP_007511Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF472327
    , AF472306, AF472307, AF472308, AF472309, AF472312, AF472315, AF472316, AF472317, AF472318, AF472319, AF472320, AF472322, AF472323, AF472324, AF472325, AF472326 Genomic DNA. Translation: AAL82456.1.
    AF472327, AF472325, AF472326 Genomic DNA. Translation: AAL82457.1.
    AF472327
    , AF472304, AF472305, AF472307, AF472308, AF472309, AF472312, AF472315, AF472316, AF472317, AF472318, AF472319, AF472320, AF472322, AF472323, AF472324, AF472325, AF472326 Genomic DNA. Translation: AAL82458.1.
    AF472327
    , AF472313, AF472314, AF472315, AF472316, AF472317, AF472318, AF472319, AF472320, AF472322, AF472323, AF472324, AF472325, AF472326 Genomic DNA. Translation: AAL82459.1.
    AF472327
    , AF472313, AF472315, AF472316, AF472317, AF472318, AF472319, AF472320, AF472322, AF472323, AF472324, AF472325, AF472326 Genomic DNA. Translation: AAL82460.1.
    AF472327
    , AF472321, AF472322, AF472323, AF472324, AF472325, AF472326 Genomic DNA. Translation: AAL82461.1.
    AF472327
    , AF472304, AF472305, AF472307, AF472308, AF472309, AF472310, AF472311, AF472312, AF472315, AF472316, AF472317, AF472318, AF472319, AF472320, AF472322, AF472323, AF472324, AF472325, AF472326 Genomic DNA. Translation: AAL82462.1.
    AK004636 mRNA. Translation: BAB23427.2.
    AK020782 mRNA. Translation: BAB32209.2.
    AK038540 mRNA. Translation: BAC30033.1.
    AK049182 mRNA. Translation: BAC33592.1.
    AL929452 Genomic DNA. Translation: CAM21669.1.
    AL929452 Genomic DNA. Translation: CAM21670.1.
    AF243508 Genomic DNA. Translation: AAF68439.1.
    AI428677 mRNA. No translation available.
    CCDSiCCDS41194.1. [Q8R550-3]
    CCDS53234.1. [Q8R550-2]
    CCDS53235.1. [Q8R550-5]
    RefSeqiNP_001129199.1. NM_001135727.2. [Q8R550-2]
    NP_001129200.1. NM_001135728.2. [Q8R550-5]
    NP_001277590.1. NM_001290661.1. [Q8R550-7]
    NP_001277593.1. NM_001290664.1. [Q8R550-7]
    NP_067364.2. NM_021389.6. [Q8R550-3]
    XP_006528987.1. XM_006528924.1. [Q8R550-1]
    UniGeneiMm.286495.

    Genome annotation databases

    EnsembliENSMUST00000073094; ENSMUSP00000072840; ENSMUSG00000040990. [Q8R550-1]
    ENSMUST00000080394; ENSMUSP00000079257; ENSMUSG00000040990. [Q8R550-3]
    ENSMUST00000112451; ENSMUSP00000108070; ENSMUSG00000040990. [Q8R550-5]
    ENSMUST00000112453; ENSMUSP00000108072; ENSMUSG00000040990. [Q8R550-4]
    ENSMUST00000112456; ENSMUSP00000108075; ENSMUSG00000040990. [Q8R550-2]
    GeneIDi58194.
    KEGGimmu:58194.
    UCSCiuc009uss.2. mouse. [Q8R550-1]
    uc009usx.2. mouse. [Q8R550-5]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF472327
    , AF472306 , AF472307 , AF472308 , AF472309 , AF472312 , AF472315 , AF472316 , AF472317 , AF472318 , AF472319 , AF472320 , AF472322 , AF472323 , AF472324 , AF472325 , AF472326 Genomic DNA. Translation: AAL82456.1 .
    AF472327 , AF472325 , AF472326 Genomic DNA. Translation: AAL82457.1 .
    AF472327
    , AF472304 , AF472305 , AF472307 , AF472308 , AF472309 , AF472312 , AF472315 , AF472316 , AF472317 , AF472318 , AF472319 , AF472320 , AF472322 , AF472323 , AF472324 , AF472325 , AF472326 Genomic DNA. Translation: AAL82458.1 .
    AF472327
    , AF472313 , AF472314 , AF472315 , AF472316 , AF472317 , AF472318 , AF472319 , AF472320 , AF472322 , AF472323 , AF472324 , AF472325 , AF472326 Genomic DNA. Translation: AAL82459.1 .
    AF472327
    , AF472313 , AF472315 , AF472316 , AF472317 , AF472318 , AF472319 , AF472320 , AF472322 , AF472323 , AF472324 , AF472325 , AF472326 Genomic DNA. Translation: AAL82460.1 .
    AF472327
    , AF472321 , AF472322 , AF472323 , AF472324 , AF472325 , AF472326 Genomic DNA. Translation: AAL82461.1 .
    AF472327
    , AF472304 , AF472305 , AF472307 , AF472308 , AF472309 , AF472310 , AF472311 , AF472312 , AF472315 , AF472316 , AF472317 , AF472318 , AF472319 , AF472320 , AF472322 , AF472323 , AF472324 , AF472325 , AF472326 Genomic DNA. Translation: AAL82462.1 .
    AK004636 mRNA. Translation: BAB23427.2 .
    AK020782 mRNA. Translation: BAB32209.2 .
    AK038540 mRNA. Translation: BAC30033.1 .
    AK049182 mRNA. Translation: BAC33592.1 .
    AL929452 Genomic DNA. Translation: CAM21669.1 .
    AL929452 Genomic DNA. Translation: CAM21670.1 .
    AF243508 Genomic DNA. Translation: AAF68439.1 .
    AI428677 mRNA. No translation available.
    CCDSi CCDS41194.1. [Q8R550-3 ]
    CCDS53234.1. [Q8R550-2 ]
    CCDS53235.1. [Q8R550-5 ]
    RefSeqi NP_001129199.1. NM_001135727.2. [Q8R550-2 ]
    NP_001129200.1. NM_001135728.2. [Q8R550-5 ]
    NP_001277590.1. NM_001290661.1. [Q8R550-7 ]
    NP_001277593.1. NM_001290664.1. [Q8R550-7 ]
    NP_067364.2. NM_021389.6. [Q8R550-3 ]
    XP_006528987.1. XM_006528924.1. [Q8R550-1 ]
    UniGenei Mm.286495.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WI7 NMR - A 101-155 [» ]
    2DA9 NMR - A 314-370 [» ]
    ProteinModelPortali Q8R550.
    SMRi Q8R550. Positions 2-166, 314-389.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 208383. 6 interactions.
    IntActi Q8R550. 9 interactions.
    MINTi MINT-1591643.

    PTM databases

    PhosphoSitei Q8R550.

    Proteomic databases

    MaxQBi Q8R550.
    PaxDbi Q8R550.
    PRIDEi Q8R550.

    Protocols and materials databases

    DNASUi 58194.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000073094 ; ENSMUSP00000072840 ; ENSMUSG00000040990 . [Q8R550-1 ]
    ENSMUST00000080394 ; ENSMUSP00000079257 ; ENSMUSG00000040990 . [Q8R550-3 ]
    ENSMUST00000112451 ; ENSMUSP00000108070 ; ENSMUSG00000040990 . [Q8R550-5 ]
    ENSMUST00000112453 ; ENSMUSP00000108072 ; ENSMUSG00000040990 . [Q8R550-4 ]
    ENSMUST00000112456 ; ENSMUSP00000108075 ; ENSMUSG00000040990 . [Q8R550-2 ]
    GeneIDi 58194.
    KEGGi mmu:58194.
    UCSCi uc009uss.2. mouse. [Q8R550-1 ]
    uc009usx.2. mouse. [Q8R550-5 ]

    Organism-specific databases

    CTDi 30011.
    MGIi MGI:1889583. Sh3kbp1.

    Phylogenomic databases

    eggNOGi NOG319250.
    GeneTreei ENSGT00530000063594.
    HOVERGENi HBG057824.
    InParanoidi Q8R550.
    KOi K12470.
    OMAi MDSRTKT.
    OrthoDBi EOG7W41BC.
    PhylomeDBi Q8R550.
    TreeFami TF350191.

    Enzyme and pathway databases

    Reactomei REACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_203917. EGFR downregulation.

    Miscellaneous databases

    ChiTaRSi SH3KBP1. mouse.
    EvolutionaryTracei Q8R550.
    NextBioi 314169.
    PROi Q8R550.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8R550.
    Bgeei Q8R550.
    CleanExi MM_SH3KBP1.
    Genevestigatori Q8R550.

    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. "Organization of the mouse Ruk locus and expression of isoforms in mouse tissues."
      Buchman V.L., Luke C., Borthwick E.B., Gout I., Ninkina N.
      Gene 295:13-17(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2; 3; 4; 5; 6 AND 7).
      Strain: 129/Ola.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
      Strain: C57BL/6J.
      Tissue: Embryonic stem cell, Hypothalamus, Lung and Thymus.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "Assignment of SETA to distal mouse X chromosome by radiation hybrid mapping."
      Hyatt M.A., Sykes V.W., Boyer A.D., Arden K.C., Boegler O.
      Cytogenet. Cell Genet. 89:278-278(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 247-286.
      Strain: 129/SvJ.
    5. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 250-709 (ISOFORM 8).
      Strain: C57BL/6J.
      Tissue: Thymus.
    6. "SETA is a multifunctional adapter protein with three SH3 domains that binds Grb2, Cbl, and the novel SB1 proteins."
      Borinstein S.C., Hyatt M.A., Sykes V.W., Straub R.E., Lipkowitz S., Boulter J., Boegler O.
      Cell. Signal. 12:769-779(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SHKBP1.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    8. "Ataxin-2 associates with the endocytosis complex and affects EGF receptor trafficking."
      Nonis D., Schmidt M.H., van de Loo S., Eich F., Dikic I., Nowock J., Auburger G.
      Cell. Signal. 20:1725-1739(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATX2.
    9. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Solution structure of the SH3 domains of SH3-domain kinase binding protein 1."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JUN-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 101-159 AND 314-370.

    Entry informationi

    Entry nameiSH3K1_MOUSE
    AccessioniPrimary (citable) accession number: Q8R550
    Secondary accession number(s): B1AZ86
    , B1AZ87, Q8CAL8, Q8CEF6, Q8R545, Q8R546, Q8R547, Q8R548, Q8R549, Q8R551, Q9CTQ9, Q9DC14, Q9JKC3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 23, 2003
    Last sequence update: June 1, 2002
    Last modified: October 1, 2014
    This is version 120 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3