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Q04929

- CRK_CHICK

UniProt

Q04929 - CRK_CHICK

Protein

Adapter molecule crk

Gene

CRK

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    May mediate attachment-induced MAPK8 activation, membrane ruffling and cell motility in a Rac-dependent manner. May regulate the EFNA5-EPHA3 signaling By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei238 – 2381Proline switch

    GO - Biological processi

    1. ephrin receptor signaling pathway Source: UniProtKB
    2. positive regulation of signal transduction Source: GOC
    3. regulation of actin cytoskeleton organization Source: UniProtKB
    4. regulation of Rho GTPase activity Source: UniProtKB

    Enzyme and pathway databases

    ReactomeiREACT_197520. Regulation of signaling by CBL.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Adapter molecule crk
    Alternative name(s):
    Proto-oncogene c-Crk
    p38
    Gene namesi
    Name:CRK
    OrganismiGallus gallus (Chicken)
    Taxonomic identifieri9031 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Chromosome 19

    Subcellular locationi

    Cytoplasm By similarity. Cell membrane By similarity
    Note: Translocated to the plasma membrane upon cell adhesion.By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Keywords - Diseasei

    Proto-oncogene

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 305305Adapter molecule crkPRO_0000079349Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei222 – 2221PhosphotyrosineBy similarity

    Post-translational modificationi

    Phosphorylated on Tyr-222 upon cell adhesion. Results in the negative regulation of the association with SH2- and SH3-binding partners, possibly by the formation of an intramolecular interaction of phosphorylated Tyr-222 with the SH2 domain. This leads finally to the down-regulation of the Crk signaling pathway By similarity.By similarity
    Proline isomerization at Pro-238 by PPIA acts as a switch between two conformations: an autoinhibitory conformation in the cis form, where the tandem SH3 domains interact intramolecularly, and an activated conformation in the trans form.

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ04929.
    PRIDEiQ04929.

    Interactioni

    Subunit structurei

    Interacts with ABL1, C3G, SOS, MAP4K1, MAPK8 and DOCK1 via its first SH3 domain. Interacts with BCAR1, CBL, PXN and GAB1 via its SH2 domain upon stimulus-induced tyrosine phosphorylation. Interacts with several tyrosine-phosphorylated growth factor receptors such as EGFR, PDGFR and INSR via its SH2 domain By similarity.By similarity

    Protein-protein interaction databases

    BioGridi678886. 1 interaction.
    IntActiQ04929. 2 interactions.
    MINTiMINT-8019929.
    STRINGi9031.ENSGALP00000004174.

    Structurei

    Secondary structure

    1
    305
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi137 – 1404
    Beta strandi148 – 1514
    Beta strandi156 – 1649
    Beta strandi166 – 1749
    Beta strandi176 – 1783
    Beta strandi180 – 1845
    Helixi185 – 1873
    Beta strandi200 – 2034
    Beta strandi226 – 2283
    Beta strandi234 – 2363
    Beta strandi239 – 2457
    Beta strandi253 – 2553
    Beta strandi263 – 2697
    Beta strandi272 – 2743
    Beta strandi277 – 2804
    Beta strandi283 – 2864
    Helixi289 – 2913
    Beta strandi292 – 2954

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2L3PNMR-A220-297[»]
    2L3QNMR-A220-297[»]
    2L3SNMR-A135-297[»]
    ProteinModelPortaliQ04929.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ04929.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini13 – 119107SH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini133 – 19361SH3 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini238 – 29760SH3 2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the CRK family.Curated
    Contains 1 SH2 domain.PROSITE-ProRule annotation
    Contains 2 SH3 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, SH2 domain, SH3 domain

    Phylogenomic databases

    eggNOGiNOG292767.
    GeneTreeiENSGT00390000001475.
    HOGENOMiHOG000236288.
    HOVERGENiHBG105616.
    InParanoidiQ04929.
    KOiK04438.
    OMAiNQDSSHP.
    OrthoDBiEOG7NW69P.
    PhylomeDBiQ04929.
    TreeFamiTF321436.

    Family and domain databases

    Gene3Di3.30.505.10. 1 hit.
    InterProiIPR000980. SH2.
    IPR011511. SH3_2.
    IPR001452. SH3_domain.
    [Graphical view]
    PfamiPF00017. SH2. 1 hit.
    PF00018. SH3_1. 1 hit.
    PF07653. SH3_2. 1 hit.
    [Graphical view]
    PRINTSiPR00401. SH2DOMAIN.
    PR00452. SH3DOMAIN.
    SMARTiSM00252. SH2. 1 hit.
    SM00326. SH3. 2 hits.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 2 hits.
    SSF55550. SSF55550. 2 hits.
    PROSITEiPS50001. SH2. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q04929-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGQFDSEDR GSWYWGRLSR GDAVSLLQGQ RHGTFLVRDS GSIPGDFVLS    50
    VSESSRVSHY IVNSLGPAGG RRAGGEGPGA PGLNPTRFRI GDQEFDSLPS 100
    LLEFYKIHYL DTTTLIEPVS RSRQNSGVIL RQEEVEYVRA LFDFNGNDDE 150
    DLPFKKGDIL KIRDKPEEQW WNAEDMDGKR GMIPVPYVEK CRPSSASVST 200
    LTGGNQDSSH PQPLGGPEPG PYAQPSINTP LPNLQNGPFY ARVIQKRVPN 250
    AYDKTALALE VGELVKVTKI NMSGQWEGEC NGKRGHFPFT HVRLLDQQNP 300
    DEDFS 305
    Length:305
    Mass (Da):33,806
    Last modified:November 1, 1995 - v1
    Checksum:i0A79AD232E824768
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L08168 mRNA. Translation: AAA49001.1.
    PIRiA49011.
    RefSeqiNP_001007847.1. NM_001007846.1.
    UniGeneiGga.27345.

    Genome annotation databases

    EnsembliENSGALT00000004183; ENSGALP00000004174; ENSGALG00000002656.
    GeneIDi417553.
    KEGGigga:417553.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L08168 mRNA. Translation: AAA49001.1 .
    PIRi A49011.
    RefSeqi NP_001007847.1. NM_001007846.1.
    UniGenei Gga.27345.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2L3P NMR - A 220-297 [» ]
    2L3Q NMR - A 220-297 [» ]
    2L3S NMR - A 135-297 [» ]
    ProteinModelPortali Q04929.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 678886. 1 interaction.
    IntActi Q04929. 2 interactions.
    MINTi MINT-8019929.
    STRINGi 9031.ENSGALP00000004174.

    Proteomic databases

    PaxDbi Q04929.
    PRIDEi Q04929.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSGALT00000004183 ; ENSGALP00000004174 ; ENSGALG00000002656 .
    GeneIDi 417553.
    KEGGi gga:417553.

    Organism-specific databases

    CTDi 1398.

    Phylogenomic databases

    eggNOGi NOG292767.
    GeneTreei ENSGT00390000001475.
    HOGENOMi HOG000236288.
    HOVERGENi HBG105616.
    InParanoidi Q04929.
    KOi K04438.
    OMAi NQDSSHP.
    OrthoDBi EOG7NW69P.
    PhylomeDBi Q04929.
    TreeFami TF321436.

    Enzyme and pathway databases

    Reactomei REACT_197520. Regulation of signaling by CBL.

    Miscellaneous databases

    EvolutionaryTracei Q04929.
    NextBioi 20820838.
    PROi Q04929.

    Family and domain databases

    Gene3Di 3.30.505.10. 1 hit.
    InterProi IPR000980. SH2.
    IPR011511. SH3_2.
    IPR001452. SH3_domain.
    [Graphical view ]
    Pfami PF00017. SH2. 1 hit.
    PF00018. SH3_1. 1 hit.
    PF07653. SH3_2. 1 hit.
    [Graphical view ]
    PRINTSi PR00401. SH2DOMAIN.
    PR00452. SH3DOMAIN.
    SMARTi SM00252. SH2. 1 hit.
    SM00326. SH3. 2 hits.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 2 hits.
    SSF55550. SSF55550. 2 hits.
    PROSITEi PS50001. SH2. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The product of the cellular crk gene consists primarily of SH2 and SH3 regions."
      Reichman C.T., Mayer B.J., Khawer S., Hanafusa H.
      Cell Growth Differ. 3:451-460(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Structural basis for regulation of the Crk signaling protein by a proline switch."
      Sarkar P., Saleh T., Tzeng S.R., Birge R.B., Kalodimos C.G.
      Nat. Chem. Biol. 7:51-57(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 135-297, ISOMERIZATION AT PRO-238.

    Entry informationi

    Entry nameiCRK_CHICK
    AccessioniPrimary (citable) accession number: Q04929
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 93 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3