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P46108 (CRK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Adapter molecule crk
Alternative name(s):
Proto-oncogene c-Crk
p38
Gene names
Name:CRK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length304 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.15 Ref.33

Subunit structure

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. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.21 Ref.22 Ref.24 Ref.25 Ref.32

Subcellular location

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

Domain

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. Ref.32

The SH2 domain mediates interaction with tyrosine phosphorylated proteins. Mediates interaction with SHB. Ref.32

Post-translational modification

Phosphorylation of Crk-II (40 kDa) gives rise to a 42 kDa form. Isoform Crk-II is phosphorylated by KIT. Ref.17 Ref.33

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. Ref.17 Ref.33

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.

Sequence similarities

Belongs to the CRK family.

Contains 1 SH2 domain.

Contains 2 SH3 domains.

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Membrane
   Coding sequence diversityAlternative splicing
   DiseaseProto-oncogene
   DomainRepeat
SH2 domain
SH3 domain
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-gamma receptor signaling pathway involved in phagocytosis

Traceable author statement. Source: Reactome

activation of MAPKK activity

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

ephrin receptor signaling pathway

Inferred from direct assay Ref.15. Source: UniProtKB

innate immune response

Traceable author statement. Source: Reactome

insulin receptor signaling pathway

Traceable author statement. Source: Reactome

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

platelet activation

Traceable author statement. Source: Reactome

positive regulation of signal transduction

Inferred from electronic annotation. Source: GOC

regulation of Rac protein signal transduction

Inferred from electronic annotation. Source: Ensembl

regulation of Rho GTPase activity

Inferred from direct assay Ref.15. Source: UniProtKB

regulation of actin cytoskeleton organization

Inferred from direct assay Ref.15. Source: UniProtKB

regulation of transcription from RNA polymerase II promoter

Traceable author statement PubMed 10748058. Source: ProtInc

   Cellular_componentcytoplasm

Inferred by curator Ref.15. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

nucleus

Traceable author statement PubMed 10748058. Source: ProtInc

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionSH2 domain binding

Inferred from physical interaction PubMed 9472046. Source: UniProtKB

ephrin receptor binding

Inferred from physical interaction Ref.15. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Crk-II (identifier: P46108-1)

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.
Isoform Crk-I (identifier: P46108-2)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.30
Chain2 – 304303Adapter molecule crk
PRO_0000079351

Regions

Domain13 – 118106SH2
Domain132 – 19261SH3 1
Domain237 – 29660SH3 2

Sites

Site2371Proline switch By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.30 Ref.31
Modified residue411Phosphoserine Ref.27
Modified residue741Phosphoserine Ref.23 Ref.27
Modified residue831Phosphoserine Ref.23
Modified residue2211Phosphotyrosine; by ABL1 Ref.33
Modified residue2391Phosphotyrosine Ref.20

Natural variations

Alternative sequence2041N → R in isoform Crk-I.
VSP_041153
Alternative sequence205 – 304100Missing in isoform Crk-I.
VSP_041154

Experimental info

Mutagenesis1501D → K: Abolishes interaction with DOCK1. Ref.10
Sequence conflict1091L → W in BAA01505. Ref.1
Sequence conflict1091L → W in AAB28213. Ref.2
Sequence conflict2151G → P in BAA01505. Ref.1
Sequence conflict2151G → P in AAB28213. Ref.2
Sequence conflict2781E → G in BAA01505. Ref.1
Sequence conflict2781E → G in AAB28213. Ref.2

Secondary structure

............................................................. 304
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Crk-II [UniParc].

Last modified July 24, 2007. Version 2.
Checksum: 4CFBFB65BFC2E265

FASTA30433,831
        10         20         30         40         50         60 
MAGNFDSEER SSWYWGRLSR QEAVALLQGQ RHGVFLVRDS STSPGDYVLS VSENSRVSHY 

        70         80         90        100        110        120 
IINSSGPRPP VPPSPAQPPP GVSPSRLRIG DQEFDSLPAL LEFYKIHYLD TTTLIEPVSR 

       130        140        150        160        170        180 
SRQGSGVILR QEEAEYVRAL FDFNGNDEED LPFKKGDILR IRDKPEEQWW NAEDSEGKRG 

       190        200        210        220        230        240 
MIPVPYVEKY RPASASVSAL IGGNQEGSHP QPLGGPEPGP YAQPSVNTPL PNLQNGPIYA 

       250        260        270        280        290        300 
RVIQKRVPNA YDKTALALEV GELVKVTKIN VSGQWEGECN GKRGHFPFTH VRLLDQQNPD 


EDFS 

« Hide

Isoform Crk-I [UniParc].

Checksum: B4C5BF23887B6B80
Show »

FASTA20422,906

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"cbl-3: a new mammalian cbl family protein."
Keane M.M., Ettenberg S.A., Nau M.M., Banerjee P., Cuello M., Penninger J., Lipkowitz S.
Oncogene 18:3365-3375(1999) [PubMed] [Europe PMC] [Abstract]
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]"DOCK4, a GTPase activator, is disrupted during tumorigenesis."
Yajnik V., Paulding C., Sordella R., McClatchey A.I., Saito M., Wahrer D.C.R., Reynolds P., Bell D.W., Lake R., van den Heuvel S., Settleman J., Haber D.A.
Cell 112:673-684(2003) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Pseudopodium-enriched atypical kinase 1 regulates the cytoskeleton and cancer progression."
Wang Y., Kelber J.A., Tran Cao H.S., Cantin G.T., Lin R., Wang W., Kaushal S., Bristow J.M., Edgington T.S., Hoffman R.M., Bouvet M., Yates J.R. III, Klemke R.L.
Proc. Natl. Acad. Sci. U.S.A. 107:10920-10925(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PEAK1.
[26]Erratum
Wang Y., Kelber J.A., Tran Cao H.S., Cantin G.T., Lin R., Wang W., Kaushal S., Bristow J.M., Edgington T.S., Hoffman R.M., Bouvet M., Yates J.R. III, Klemke R.L.
Proc. Natl. Acad. Sci. U.S.A. 107:13556-13556(2010)
[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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA45022.
RefSeqNP_005197.3. NM_005206.4.
NP_058431.2. NM_016823.3.
UniGeneHs.461896.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JU5NMR-A12-120[»]
2DVJNMR-A1-228[»]
2EYVNMR-A6-124[»]
2EYWNMR-A124-198[»]
2EYXNMR-A232-298[»]
2EYYNMR-A1-204[»]
2EYZNMR-A1-304[»]
DisProtDP00748.
ProteinModelPortalP46108.
SMRP46108. Positions 1-304.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107788. 159 interactions.
DIPDIP-199N.
IntActP46108. 171 interactions.
MINTMINT-1208745.
STRING9606.ENSP00000300574.

Chemistry

ChEMBLCHEMBL5005.

PTM databases

PhosphoSiteP46108.

Polymorphism databases

DMDM158939322.

2D gel databases

REPRODUCTION-2DPAGEIPI00399054.
SWISS-2DPAGEP46108.

Proteomic databases

PaxDbP46108.
PRIDEP46108.

Protocols and materials databases

DNASU1398.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000300574; ENSP00000300574; ENSG00000167193. [P46108-1]
ENST00000398970; ENSP00000381942; ENSG00000167193. [P46108-2]
GeneID1398.
KEGGhsa:1398.
UCSCuc002fsl.3. human. [P46108-1]
uc002fsm.3. human. [P46108-2]

Organism-specific databases

CTD1398.
GeneCardsGC17M001323.
HGNCHGNC:2362. CRK.
HPACAB010485.
MIM164762. gene.
neXtProtNX_P46108.
PharmGKBPA26880.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG292767.
HOGENOMHOG000236288.
HOVERGENHBG105616.
InParanoidP46108.
KOK04438.
OMANQDSSHP.
OrthoDBEOG7NW69P.
PhylomeDBP46108.
TreeFamTF321436.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkP46108.

Gene expression databases

ArrayExpressP46108.
BgeeP46108.
CleanExHS_CRK.
GenevestigatorP46108.

Family and domain databases

Gene3D3.30.505.10. 1 hit.
InterProIPR000980. SH2.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamPF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
SMARTSM00252. SH2. 1 hit.
SM00326. SH3. 2 hits.
[Graphical view]
SUPFAMSSF50044. SSF50044. 3 hits.
SSF55550. SSF55550. 2 hits.
PROSITEPS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCRK. human.
EvolutionaryTraceP46108.
GeneWikiCRK_(gene).
GenomeRNAi1398.
NextBio5721.
PROP46108.
SOURCESearch...

Entry information

Entry nameCRK_HUMAN
AccessionPrimary (citable) accession number: P46108
Secondary accession number(s): A8MWE8 expand/collapse secondary AC list , B0LPE8, D3DTH6, Q96GA9, Q96HJ0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: July 24, 2007
Last modified: April 16, 2014
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM