Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P46108

- CRK_HUMAN

UniProt

P46108 - CRK_HUMAN

(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)

Protein

Adapter molecule crk

Gene

CRK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. 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: Ensembl
  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
Complete GO annotation...

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-KW
Complete GO annotation...

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 – 411Phosphoserine1 Publication
Modified residuei74 – 741Phosphoserine2 Publications
Modified residuei83 – 831Phosphoserine1 Publication
Modified residuei221 – 2211Phosphotyrosine; by ABL11 Publication
Modified residuei239 – 2391Phosphotyrosine1 Publication

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

BgeeiP46108.
CleanExiHS_CRK.
ExpressionAtlasiP46108. baseline and differential.
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
EGFRP005333EBI-287556,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 – 137Combined sources
Beta strandi14 – 163Combined sources
Helixi20 – 278Combined sources
Beta strandi30 – 334Combined sources
Beta strandi34 – 396Combined sources
Beta strandi41 – 433Combined sources
Beta strandi46 – 527Combined sources
Beta strandi54 – 563Combined sources
Beta strandi57 – 637Combined sources
Beta strandi66 – 694Combined sources
Beta strandi70 – 778Combined sources
Turni78 – 803Combined sources
Beta strandi87 – 893Combined sources
Beta strandi92 – 965Combined sources
Helixi97 – 10610Combined sources
Beta strandi109 – 1124Combined sources
Beta strandi116 – 1183Combined sources
Beta strandi120 – 1234Combined sources
Helixi126 – 1283Combined sources
Beta strandi135 – 1384Combined sources
Beta strandi146 – 1505Combined sources
Beta strandi158 – 1669Combined sources
Beta strandi167 – 1737Combined sources
Beta strandi179 – 1835Combined sources
Helixi184 – 1863Combined sources
Beta strandi187 – 1893Combined sources
Beta strandi208 – 2103Combined sources
Beta strandi224 – 2274Combined sources
Beta strandi229 – 2313Combined sources
Beta strandi239 – 2424Combined sources
Beta strandi253 – 2553Combined sources
Beta strandi260 – 26910Combined sources
Beta strandi273 – 2797Combined sources
Beta strandi282 – 2876Combined sources
Helixi288 – 2903Combined sources

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.
GeneTreeiENSGT00390000001475.
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

        10         20         30         40         50
MAGNFDSEER SSWYWGRLSR QEAVALLQGQ RHGVFLVRDS STSPGDYVLS
60 70 80 90 100
VSENSRVSHY IINSSGPRPP VPPSPAQPPP GVSPSRLRIG DQEFDSLPAL
110 120 130 140 150
LEFYKIHYLD TTTLIEPVSR SRQGSGVILR QEEAEYVRAL FDFNGNDEED
160 170 180 190 200
LPFKKGDILR IRDKPEEQWW NAEDSEGKRG MIPVPYVEKY RPASASVSAL
210 220 230 240 250
IGGNQEGSHP QPLGGPEPGP YAQPSVNTPL PNLQNGPIYA RVIQKRVPNA
260 270 280 290 300
YDKTALALEV GELVKVTKIN VSGQWEGECN GKRGHFPFTH VRLLDQQNPD

EDFS
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.
GeneTreei ENSGT00390000001475.
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

Bgeei P46108.
CleanExi HS_CRK.
ExpressionAtlasi P46108. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 157 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