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Protein

Adapter molecule crk

Gene

CRK

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-GGA-170984. ARMS-mediated activation.
R-GGA-186763. Downstream signal transduction.
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-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

  • Cytoplasm By similarity
  • Cell membrane By similarity

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

GO - Cellular componenti

Complete GO annotation...

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.

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.
MINTiMINT-8019929.
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
Domaini238 – 297SH3 2PROSITE-ProRule annotationAdd BLAST60

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

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

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q04929-1 [UniParc]FASTAAdd to basket

« Hide

        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.
UniGeneiGga.27345.

Genome annotation databases

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

Cross-referencesi

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.
UniGeneiGga.27345.

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...

Protein-protein interaction databases

BioGridi678886. 2 interactors.
IntActiQ04929. 2 interactors.
MINTiMINT-8019929.
STRINGi9031.ENSGALP00000004174.

PTM databases

iPTMnetiQ04929.

Proteomic databases

PaxDbiQ04929.
PRIDEiQ04929.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1398.

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiR-GGA-170984. ARMS-mediated activation.
R-GGA-186763. Downstream signal transduction.
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-912631. Regulation of signaling by CBL.

Miscellaneous databases

EvolutionaryTraceiQ04929.
PROiQ04929.

Gene expression databases

BgeeiENSGALG00000002656.

Family and domain databases

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

Entry informationi

Entry nameiCRK_CHICK
AccessioniPrimary (citable) accession number: Q04929
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 30, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.