Skip Header

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

Adapter molecule crk

Gene

CRK

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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)DescriptionActionsGraphical viewLength
Sitei238Proline switch1 Publication1

GO - Biological processi

Enzyme and pathway databases

ReactomeiR-GGA-170984 ARMS-mediated activation
R-GGA-186763 Downstream signal transduction
R-GGA-2029482 Regulation of actin dynamics for phagocytic cup formation
R-GGA-372708 p130Cas linkage to MAPK signaling for integrins
R-GGA-4420097 VEGFA-VEGFR2 Pathway
R-GGA-8849471 PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases
R-GGA-8875555 MET activates RAP1 and RAC1
R-GGA-8875656 MET receptor recycling
R-GGA-9032759 NTRK2 activates RAC1
R-GGA-912631 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Chromosome 19

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000793491 – 305Adapter molecule crkAdd BLAST305

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei222PhosphotyrosineBy similarity1

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.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ04929
PRIDEiQ04929

PTM databases

iPTMnetiQ04929

Expressioni

Gene expression databases

BgeeiENSGALG00000002656

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, 2 interactors
IntActiQ04929, 2 interactors
MINTiQ04929
STRINGi9031.ENSGALP00000004174

Structurei

Secondary structure

1305
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi137 – 140Combined sources4
Beta strandi148 – 151Combined sources4
Beta strandi156 – 164Combined sources9
Beta strandi166 – 174Combined sources9
Beta strandi176 – 178Combined sources3
Beta strandi180 – 184Combined sources5
Helixi185 – 187Combined sources3
Beta strandi200 – 203Combined sources4
Beta strandi226 – 228Combined sources3
Beta strandi234 – 236Combined sources3
Beta strandi239 – 245Combined sources7
Beta strandi253 – 255Combined sources3
Beta strandi263 – 269Combined sources7
Beta strandi272 – 274Combined sources3
Beta strandi277 – 280Combined sources4
Beta strandi283 – 286Combined sources4
Helixi289 – 291Combined sources3
Beta strandi292 – 295Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2L3PNMR-A220-297[»]
2L3QNMR-A220-297[»]
2L3SNMR-A135-297[»]
ProteinModelPortaliQ04929
SMRiQ04929
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ04929

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini13 – 119SH2PROSITE-ProRule annotationAdd BLAST107
Domaini133 – 193SH3 1PROSITE-ProRule annotationAdd BLAST61
Domaini236 – 297SH3 2PROSITE-ProRule annotationAdd BLAST62

Sequence similaritiesi

Belongs to the CRK family.Curated

Keywords - Domaini

Repeat, SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiKOG4792 Eukaryota
ENOG4110574 LUCA
GeneTreeiENSGT00820000127055
HOGENOMiHOG000236288
HOVERGENiHBG105616
InParanoidiQ04929
KOiK04438
OMAiGSWYWGR
OrthoDBiEOG091G0JPQ
PhylomeDBiQ04929
TreeFamiTF321436

Family and domain databases

CDDicd11759 SH3_CRK_C, 1 hit
cd11758 SH3_CRK_N, 1 hit
Gene3Di3.30.505.10, 2 hits
InterProiView protein in InterPro
IPR035458 CRK_SH3_C
IPR035457 CRK_SH3_N
IPR000980 SH2
IPR036860 SH2_dom_sf
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain
PfamiView protein in Pfam
PF00017 SH2, 1 hit
PF00018 SH3_1, 1 hit
PF07653 SH3_2, 1 hit
PRINTSiPR00401 SH2DOMAIN
PR00452 SH3DOMAIN
SMARTiView protein in SMART
SM00252 SH2, 1 hit
SM00326 SH3, 2 hits
SUPFAMiSSF50044 SSF50044, 2 hits
SSF55550 SSF55550, 2 hits
PROSITEiView protein in PROSITE
PS50001 SH2, 1 hit
PS50002 SH3, 2 hits

Sequencei

Sequence statusi: Complete.

Q04929-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGQFDSEDR GSWYWGRLSR GDAVSLLQGQ RHGTFLVRDS GSIPGDFVLS
60 70 80 90 100
VSESSRVSHY IVNSLGPAGG RRAGGEGPGA PGLNPTRFRI GDQEFDSLPS
110 120 130 140 150
LLEFYKIHYL DTTTLIEPVS RSRQNSGVIL RQEEVEYVRA LFDFNGNDDE
160 170 180 190 200
DLPFKKGDIL KIRDKPEEQW WNAEDMDGKR GMIPVPYVEK CRPSSASVST
210 220 230 240 250
LTGGNQDSSH PQPLGGPEPG PYAQPSINTP LPNLQNGPFY ARVIQKRVPN
260 270 280 290 300
AYDKTALALE VGELVKVTKI NMSGQWEGEC NGKRGHFPFT HVRLLDQQNP

DEDFS
Length:305
Mass (Da):33,806
Last modified:November 1, 1995 - v1
Checksum:i0A79AD232E824768
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L08168 mRNA Translation: AAA49001.1
PIRiA49011
RefSeqiNP_001007847.1, NM_001007846.1
XP_015151517.1, XM_015296031.1

Genome annotation databases

EnsembliENSGALT00000004183; ENSGALP00000004174; ENSGALG00000002656
GeneIDi107054794
KEGGigga:107054794
gga:417553

Similar proteinsi

Entry informationi

Entry nameiCRK_CHICK
AccessioniPrimary (citable) accession number: Q04929
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 23, 2018
This is version 120 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health