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)

P46108

- CRK_HUMAN

UniProt

P46108 - CRK_HUMAN

Protein

Adapter molecule crk

Gene

CRK

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 156 (01 Oct 2014)
      Sequence version 2 (24 Jul 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    The Crk-I and Crk-II forms differ in their biological activities. Crk-II has less transforming activity than Crk-I. Crk-II mediates attachment-induced MAPK8 activation, membrane ruffling and cell motility in a Rac-dependent manner. Involved in phagocytosis of apoptotic cells and cell motility via its interaction with DOCK1 and DOCK4. May regulate the EFNA5-EPHA3 signaling.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei237 – 2371Proline switchBy similarity

    GO - Molecular functioni

    1. ephrin receptor binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. SH2 domain binding Source: UniProtKB

    GO - Biological processi

    1. activation of MAPKK activity Source: Reactome
    2. blood coagulation Source: Reactome
    3. ephrin receptor signaling pathway Source: UniProtKB
    4. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
    5. innate immune response Source: Reactome
    6. insulin receptor signaling pathway Source: Reactome
    7. neurotrophin TRK receptor signaling pathway Source: Reactome
    8. platelet activation Source: Reactome
    9. positive regulation of signal transduction Source: GOC
    10. regulation of actin cytoskeleton organization Source: UniProtKB
    11. regulation of Rac protein signal transduction Source: Ensembl
    12. regulation of Rho GTPase activity Source: UniProtKB
    13. regulation of transcription from RNA polymerase II promoter Source: ProtInc

    Enzyme and pathway databases

    ReactomeiREACT_12002. ARMS-mediated activation.
    REACT_15381. p130Cas linkage to MAPK signaling for integrins.
    REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    REACT_17025. Downstream signal transduction.
    REACT_23787. Regulation of signaling by CBL.
    REACT_508. Signal attenuation.
    SignaLinkiP46108.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Adapter molecule crk
    Alternative name(s):
    Proto-oncogene c-Crk
    p38
    Gene namesi
    Name:CRK
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:2362. CRK.

    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
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. nucleus Source: ProtInc
    5. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi150 – 1501D → K: Abolishes interaction with DOCK1. 1 Publication

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    PharmGKBiPA26880.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 304303Adapter molecule crkPRO_0000079351Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei41 – 411Phosphoserine2 Publications
    Modified residuei74 – 741Phosphoserine3 Publications
    Modified residuei83 – 831Phosphoserine2 Publications
    Modified residuei221 – 2211Phosphotyrosine; by ABL12 Publications
    Modified residuei239 – 2391Phosphotyrosine2 Publications

    Post-translational modificationi

    Phosphorylation of Crk-II (40 kDa) gives rise to a 42 kDa form. Isoform Crk-II is phosphorylated by KIT.
    Phosphorylated on Tyr-221 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-221 with the SH2 domain. This leads finally to the down-regulation of the Crk signaling pathway.1 Publication
    Proline isomerization at Pro-237 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.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP46108.
    PaxDbiP46108.
    PRIDEiP46108.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00399054.
    SWISS-2DPAGEP46108.

    PTM databases

    PhosphoSiteiP46108.

    Expressioni

    Gene expression databases

    ArrayExpressiP46108.
    BgeeiP46108.
    CleanExiHS_CRK.
    GenevestigatoriP46108.

    Organism-specific databases

    HPAiCAB010485.

    Interactioni

    Subunit structurei

    Interacts with ABL1, C3G, DOCK3, MAP4K1, MAPK8 and SOS via its first SH3 domain. Interacts (via SH2 domain) with BCAR1, CBL, CBLB, PXN, IRS4 and GAB1 upon stimulus-induced tyrosine phosphorylation. Interacts (via SH2 domain) with several tyrosine-phosphorylated growth factor receptors such as EGFR and INSR. Interacts with FLT1 (tyrosine-phosphorylated). Interacts with DOCK1 and DOCK4. Interacts with SHB. Interacts with PEAK1. Interacts with FASLG. Isoform Crk-II interacts with KIT. Interacts with EPHA3; upon activation of EPHA3 by the ligand EFNA5 and EPHA3 tyrosine kinase activity-dependent. Interacts with EPHA3 (phosphorylated); mediates EFNA5-EPHA3 signaling through RHOA GTPase activation. Interacts with FLT4 (tyrosine-phosphorylated). Isoform Crk-II (via SH2 domain) interacts with PDGFRA (tyrosine phosphorylated) and PDGFRB (tyrosine phosphorylated). Part of a collagen stimulated complex involved in cell migration composed of CDC42, CRK, TNK2 and p130cas/BCAR1. Interacts (via SH2 domain) with the 'Tyr-9' phosphorylated form of PDPK1. Interacts with CBLC. Found in a complex with ABL1, ABL2, CRK and UNC119; leading to the inhibition of CRK phosphorylation by ABL kinases.16 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ABL1P005192EBI-886,EBI-375543
    ABL2P426845EBI-886,EBI-1102694
    ARHGEF11O150852EBI-886,EBI-311099
    ASAP1Q9ULH12EBI-886,EBI-346622
    ATXN1P542533EBI-886,EBI-930964
    BCAR1P569455EBI-886,EBI-702093
    CBLP226816EBI-886,EBI-518228
    EGFRP005332EBI-886,EBI-297353
    ERBB3P218602EBI-886,EBI-720706
    FGFR1P113622EBI-886,EBI-1028277
    FLNAP213333EBI-886,EBI-350432
    FLNCQ143152EBI-886,EBI-489954
    GAB1Q134802EBI-886,EBI-517684
    IRS4O146548EBI-886,EBI-356594
    KDRP359682EBI-886,EBI-1005487
    KITP107214EBI-886,EBI-1379503
    MAP4K1Q929183EBI-886,EBI-881
    MAP4K5Q9Y4K45EBI-886,EBI-1279
    MAPK8P459832EBI-886,EBI-286483
    OGNP207742EBI-886,EBI-1753690
    PDGFRAP162344EBI-886,EBI-2861522
    PIK3R1P279862EBI-886,EBI-79464
    PTPN4P290743EBI-886,EBI-710431
    RAPGEF1Q139053EBI-886,EBI-976876
    SHANK2Q9UPX82EBI-886,EBI-1570571
    SHC1P293533EBI-886,EBI-78835
    SNX3O604932EBI-886,EBI-727209
    SOS1Q078893EBI-886,EBI-297487
    SOS2Q078902EBI-886,EBI-298181

    Protein-protein interaction databases

    BioGridi107788. 160 interactions.
    DIPiDIP-199N.
    IntActiP46108. 176 interactions.
    MINTiMINT-1208745.
    STRINGi9606.ENSP00000300574.

    Structurei

    Secondary structure

    1
    304
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 137
    Beta strandi14 – 163
    Helixi20 – 278
    Beta strandi30 – 334
    Beta strandi34 – 396
    Beta strandi41 – 433
    Beta strandi46 – 527
    Beta strandi54 – 563
    Beta strandi57 – 637
    Beta strandi66 – 694
    Beta strandi70 – 778
    Turni78 – 803
    Beta strandi87 – 893
    Beta strandi92 – 965
    Helixi97 – 10610
    Beta strandi109 – 1124
    Beta strandi116 – 1183
    Beta strandi120 – 1234
    Helixi126 – 1283
    Beta strandi135 – 1384
    Beta strandi146 – 1505
    Beta strandi158 – 1669
    Beta strandi167 – 1737
    Beta strandi179 – 1835
    Helixi184 – 1863
    Beta strandi187 – 1893
    Beta strandi208 – 2103
    Beta strandi224 – 2274
    Beta strandi229 – 2313
    Beta strandi239 – 2424
    Beta strandi253 – 2553
    Beta strandi260 – 26910
    Beta strandi273 – 2797
    Beta strandi282 – 2876
    Helixi288 – 2903

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JU5NMR-A12-120[»]
    2DVJNMR-A1-228[»]
    2EYVNMR-A6-124[»]
    2EYWNMR-A125-198[»]
    2EYXNMR-A232-298[»]
    2EYYNMR-A1-204[»]
    2EYZNMR-A1-304[»]
    DisProtiDP00748.
    ProteinModelPortaliP46108.
    SMRiP46108. Positions 1-304.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP46108.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini13 – 118106SH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini132 – 19261SH3 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini237 – 29660SH3 2PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The C-terminal SH3 domain function as a negative modulator for transformation and the N-terminal SH3 domain appears to function as a positive regulator for transformation.By similarity
    The SH2 domain mediates interaction with tyrosine phosphorylated proteins. Mediates interaction with SHB.

    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.
    HOGENOMiHOG000236288.
    HOVERGENiHBG105616.
    InParanoidiP46108.
    KOiK04438.
    OMAiNQDSSHP.
    OrthoDBiEOG7NW69P.
    PhylomeDBiP46108.
    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. 3 hits.
    SSF55550. SSF55550. 2 hits.
    PROSITEiPS50001. SH2. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Crk-II (identifier: P46108-1) [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

    MAGNFDSEER SSWYWGRLSR QEAVALLQGQ RHGVFLVRDS STSPGDYVLS    50
    VSENSRVSHY IINSSGPRPP VPPSPAQPPP GVSPSRLRIG DQEFDSLPAL 100
    LEFYKIHYLD TTTLIEPVSR SRQGSGVILR QEEAEYVRAL FDFNGNDEED 150
    LPFKKGDILR IRDKPEEQWW NAEDSEGKRG MIPVPYVEKY RPASASVSAL 200
    IGGNQEGSHP QPLGGPEPGP YAQPSVNTPL PNLQNGPIYA RVIQKRVPNA 250
    YDKTALALEV GELVKVTKIN VSGQWEGECN GKRGHFPFTH VRLLDQQNPD 300
    EDFS 304
    Length:304
    Mass (Da):33,831
    Last modified:July 24, 2007 - v2
    Checksum:i4CFBFB65BFC2E265
    GO
    Isoform Crk-I (identifier: P46108-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         204-204: N → R
         205-304: Missing.

    Note: Contains a phosphoserine at position 194.

    Show »
    Length:204
    Mass (Da):22,906
    Checksum:iB4C5BF23887B6B80
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti109 – 1091L → W in BAA01505. (PubMed:1630456)Curated
    Sequence conflicti109 – 1091L → W in AAB28213. (PubMed:8378094)Curated
    Sequence conflicti215 – 2151G → P in BAA01505. (PubMed:1630456)Curated
    Sequence conflicti215 – 2151G → P in AAB28213. (PubMed:8378094)Curated
    Sequence conflicti278 – 2781E → G in BAA01505. (PubMed:1630456)Curated
    Sequence conflicti278 – 2781E → G in AAB28213. (PubMed:8378094)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei204 – 2041N → R in isoform Crk-I. 2 PublicationsVSP_041153
    Alternative sequencei205 – 304100Missing in isoform Crk-I. 2 PublicationsVSP_041154Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D10656 mRNA. Translation: BAA01505.1.
    S65701 Genomic DNA. Translation: AAB28213.1.
    BT007277 mRNA. Translation: AAP35941.1.
    EU332838 Genomic DNA. Translation: ABY87527.1.
    AK291060 mRNA. Translation: BAF83749.1.
    AC032044 Genomic DNA. No translation available.
    AC100748 Genomic DNA. No translation available.
    CH471108 Genomic DNA. Translation: EAW90621.1.
    CH471108 Genomic DNA. Translation: EAW90624.1.
    CH471108 Genomic DNA. Translation: EAW90625.1.
    BC001718 mRNA. Translation: AAH01718.1.
    BC008506 mRNA. Translation: AAH08506.1.
    BC009837 mRNA. Translation: AAH09837.1.
    CCDSiCCDS11002.1. [P46108-1]
    CCDS45561.1. [P46108-2]
    PIRiA45022.
    RefSeqiNP_005197.3. NM_005206.4. [P46108-2]
    NP_058431.2. NM_016823.3. [P46108-1]
    UniGeneiHs.461896.

    Genome annotation databases

    EnsembliENST00000300574; ENSP00000300574; ENSG00000167193. [P46108-1]
    ENST00000398970; ENSP00000381942; ENSG00000167193. [P46108-2]
    GeneIDi1398.
    KEGGihsa:1398.
    UCSCiuc002fsl.3. human. [P46108-1]
    uc002fsm.3. human. [P46108-2]

    Polymorphism databases

    DMDMi158939322.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D10656 mRNA. Translation: BAA01505.1 .
    S65701 Genomic DNA. Translation: AAB28213.1 .
    BT007277 mRNA. Translation: AAP35941.1 .
    EU332838 Genomic DNA. Translation: ABY87527.1 .
    AK291060 mRNA. Translation: BAF83749.1 .
    AC032044 Genomic DNA. No translation available.
    AC100748 Genomic DNA. No translation available.
    CH471108 Genomic DNA. Translation: EAW90621.1 .
    CH471108 Genomic DNA. Translation: EAW90624.1 .
    CH471108 Genomic DNA. Translation: EAW90625.1 .
    BC001718 mRNA. Translation: AAH01718.1 .
    BC008506 mRNA. Translation: AAH08506.1 .
    BC009837 mRNA. Translation: AAH09837.1 .
    CCDSi CCDS11002.1. [P46108-1 ]
    CCDS45561.1. [P46108-2 ]
    PIRi A45022.
    RefSeqi NP_005197.3. NM_005206.4. [P46108-2 ]
    NP_058431.2. NM_016823.3. [P46108-1 ]
    UniGenei Hs.461896.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JU5 NMR - A 12-120 [» ]
    2DVJ NMR - A 1-228 [» ]
    2EYV NMR - A 6-124 [» ]
    2EYW NMR - A 125-198 [» ]
    2EYX NMR - A 232-298 [» ]
    2EYY NMR - A 1-204 [» ]
    2EYZ NMR - A 1-304 [» ]
    DisProti DP00748.
    ProteinModelPortali P46108.
    SMRi P46108. Positions 1-304.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107788. 160 interactions.
    DIPi DIP-199N.
    IntActi P46108. 176 interactions.
    MINTi MINT-1208745.
    STRINGi 9606.ENSP00000300574.

    Chemistry

    ChEMBLi CHEMBL5005.

    PTM databases

    PhosphoSitei P46108.

    Polymorphism databases

    DMDMi 158939322.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00399054.
    SWISS-2DPAGE P46108.

    Proteomic databases

    MaxQBi P46108.
    PaxDbi P46108.
    PRIDEi P46108.

    Protocols and materials databases

    DNASUi 1398.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000300574 ; ENSP00000300574 ; ENSG00000167193 . [P46108-1 ]
    ENST00000398970 ; ENSP00000381942 ; ENSG00000167193 . [P46108-2 ]
    GeneIDi 1398.
    KEGGi hsa:1398.
    UCSCi uc002fsl.3. human. [P46108-1 ]
    uc002fsm.3. human. [P46108-2 ]

    Organism-specific databases

    CTDi 1398.
    GeneCardsi GC17M001323.
    HGNCi HGNC:2362. CRK.
    HPAi CAB010485.
    MIMi 164762. gene.
    neXtProti NX_P46108.
    PharmGKBi PA26880.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG292767.
    HOGENOMi HOG000236288.
    HOVERGENi HBG105616.
    InParanoidi P46108.
    KOi K04438.
    OMAi NQDSSHP.
    OrthoDBi EOG7NW69P.
    PhylomeDBi P46108.
    TreeFami TF321436.

    Enzyme and pathway databases

    Reactomei REACT_12002. ARMS-mediated activation.
    REACT_15381. p130Cas linkage to MAPK signaling for integrins.
    REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    REACT_17025. Downstream signal transduction.
    REACT_23787. Regulation of signaling by CBL.
    REACT_508. Signal attenuation.
    SignaLinki P46108.

    Miscellaneous databases

    ChiTaRSi CRK. human.
    EvolutionaryTracei P46108.
    GeneWikii CRK_(gene).
    GenomeRNAii 1398.
    NextBioi 5721.
    PROi P46108.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P46108.
    Bgeei P46108.
    CleanExi HS_CRK.
    Genevestigatori P46108.

    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. 3 hits.
    SSF55550. SSF55550. 2 hits.
    PROSITEi PS50001. SH2. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Two species of human CRK cDNA encode proteins with distinct biological activities."
      Matsuda M., Tanaka S., Nagata S., Kojima A., Kurata T., Shibuya M.
      Mol. Cell. Biol. 12:3482-3489(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CRK-II), FUNCTION, ALTERNATIVE SPLICING.
      Tissue: Embryonic lung and Placenta.
    2. "CRK proto-oncogene maps to human chromosome band 17p13."
      Fioretos T., Heisterkamp N., Groffen J., Benjes S., Morris C.
      Oncogene 8:2853-2855(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CRK-II).
    4. SeattleSNPs variation discovery resource
      Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "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] (ISOFORM CRK-I).
    6. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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 CRK-I AND CRK-II).
      Tissue: Eye, Lung and Placenta.
    9. "DOCK180, a major CRK-binding protein, alters cell morphology upon translocation to the cell membrane."
      Hasegawa H., Kiyokawa E., Tanaka S., Nagashima K., Gotoh N., Shibuya M., Kurata T., Matsuda M.
      Mol. Cell. Biol. 16:1770-1776(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DOCK1.
    10. "Interaction between the amino-terminal SH3 domain of CRK and its natural target proteins."
      Matsuda M., Ota S., Tanimura R., Nakamura H., Matuoka K., Takenawa T., Nagashima K., Kurata T.
      J. Biol. Chem. 271:14468-14472(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DOCK1; C3G AND EPS15, MUTAGENESIS OF ASP-150.
    11. "Interplay of the proto-oncogene proteins CrkL and CrkII in insulin-like growth factor-I receptor-mediated signal transduction."
      Koval A.P., Karas M., Zick Y., LeRoith D.
      J. Biol. Chem. 273:14780-14787(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IRS4.
    12. Cited for: INTERACTION WITH CBLC.
    13. "Differential interaction of CrkII adaptor protein with platelet-derived growth factor alpha- and beta-receptors is determined by its internal tyrosine phosphorylation."
      Matsumoto T., Yokote K., Take A., Takemoto M., Asaumi S., Hashimoto Y., Matsuda M., Saito Y., Mori S.
      Biochem. Biophys. Res. Commun. 270:28-33(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PDGFRA AND PDGFRB.
    14. "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 SHB.
    15. "Ephrin-A5 induces rounding, blebbing and de-adhesion of EphA3-expressing 293T and melanoma cells by CrkII and Rho-mediated signalling."
      Lawrenson I.D., Wimmer-Kleikamp S.H., Lock P., Schoenwaelder S.M., Down M., Boyd A.W., Alewood P.F., Lackmann M.
      J. Cell Sci. 115:1059-1072(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL-CELL ADHESION, INTERACTION WITH EPHA3.
    16. Cited for: INTERACTION WITH DOCK4.
    17. "Identification of Tyr900 in the kinase domain of c-Kit as a Src-dependent phosphorylation site mediating interaction with c-Crk."
      Lennartsson J., Wernstedt C., Engstrom U., Hellman U., Ronnstrand L.
      Exp. Cell Res. 288:110-118(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KIT, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION.
    18. "Direct recruitment of CRK and GRB2 to VEGFR-3 induces proliferation, migration, and survival of endothelial cells through the activation of ERK, AKT, and JNK pathways."
      Salameh A., Galvagni F., Bardelli M., Bussolino F., Oliviero S.
      Blood 106:3423-3431(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FLT4.
    19. "Signaling by Kit protein-tyrosine kinase--the stem cell factor receptor."
      Roskoski R. Jr.
      Biochem. Biophys. Res. Commun. 337:1-13(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON ROLE IN KIT SIGNALING.
    20. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-239, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Ack1 mediates Cdc42-dependent cell migration and signaling to p130Cas."
      Modzelewska K., Newman L.P., Desai R., Keely P.J.
      J. Biol. Chem. 281:37527-37535(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BCAR1; CDC42 AND TNK2.
    22. "Regulation of 3-phosphoinositide-dependent protein kinase-1 (PDK1) by Src involves tyrosine phosphorylation of PDK1 and Src homology 2 domain binding."
      Yang K.J., Shin S., Piao L., Shin E., Li Y., Park K.A., Byun H.S., Won M., Hong J., Kweon G.R., Hur G.M., Seok J.H., Chun T., Brazil D.P., Hemmings B.A., Park J.
      J. Biol. Chem. 283:1480-1491(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PDPK1.
    23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74 AND SER-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. "Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
      Voss M., Lettau M., Janssen O.
      BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FASLG.
    25. "Unc119 protects from Shigella infection by inhibiting the Abl family kinases."
      Vepachedu R., Karim Z., Patel O., Goplen N., Alam R.
      PLoS ONE 4:E5211-E5211(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH ABL1; ABL2 AND UNC119.
    26. Cited for: INTERACTION WITH PEAK1.
    27. "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-41 AND SER-74, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194 (ISOFORM CRK-I), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    28. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    31. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    32. "Structure of a regulatory complex involving the Abl SH3 domain, the Crk SH2 domain, and a Crk-derived phosphopeptide."
      Donaldson L.W., Gish G., Pawson T., Kay L.E., Forman-Kay J.D.
      Proc. Natl. Acad. Sci. U.S.A. 99:14053-14058(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 12-120 IN COMPLEX WITH ABL1, INTERACTION OF THE CRK SH2 DOMAIN WITH PHOSPHORYLATED TYR-221.
    33. "Structural basis for the transforming activity of human cancer-related signaling adaptor protein CRK."
      Kobashigawa Y., Sakai M., Naito M., Yokochi M., Kumeta H., Makino Y., Ogura K., Tanaka S., Inagaki F.
      Nat. Struct. Mol. Biol. 14:503-510(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR (ISOFORMS CRK-I AND CRK-II), FUNCTION, PHOSPHORYLATION AT TYR-221.

    Entry informationi

    Entry nameiCRK_HUMAN
    AccessioniPrimary (citable) accession number: P46108
    Secondary accession number(s): A8MWE8
    , B0LPE8, D3DTH6, Q96GA9, Q96HJ0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: July 24, 2007
    Last modified: October 1, 2014
    This is version 156 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 17
      Human chromosome 17: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3