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Q04929 (CRK_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·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
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length305 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May mediate attachment-induced MAPK8 activation, membrane ruffling and cell motility in a Rac-dependent manner. May regulate the EFNA5-EPHA3 signaling By similarity.

Subunit structure

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. Ref.2

Subcellular location

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

Post-translational modification

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.

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.

Sequence similarities

Belongs to the CRK family.

Contains 1 SH2 domain.

Contains 2 SH3 domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 305305Adapter molecule crk
PRO_0000079349

Regions

Domain13 – 119107SH2
Domain133 – 19361SH3 1
Domain238 – 29760SH3 2

Sites

Site2381Proline switch

Amino acid modifications

Modified residue2221Phosphotyrosine By similarity

Secondary structure

................................... 305
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q04929 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 0A79AD232E824768

FASTA30533,806
        10         20         30         40         50         60 
MAGQFDSEDR GSWYWGRLSR GDAVSLLQGQ RHGTFLVRDS GSIPGDFVLS VSESSRVSHY 

        70         80         90        100        110        120 
IVNSLGPAGG RRAGGEGPGA PGLNPTRFRI GDQEFDSLPS LLEFYKIHYL DTTTLIEPVS 

       130        140        150        160        170        180 
RSRQNSGVIL RQEEVEYVRA LFDFNGNDDE DLPFKKGDIL KIRDKPEEQW WNAEDMDGKR 

       190        200        210        220        230        240 
GMIPVPYVEK CRPSSASVST LTGGNQDSSH PQPLGGPEPG PYAQPSINTP LPNLQNGPFY 

       250        260        270        280        290        300 
ARVIQKRVPN AYDKTALALE VGELVKVTKI NMSGQWEGEC NGKRGHFPFT HVRLLDQQNP 


DEDFS 

« Hide

References

[1]"The product of the cellular crk gene consists primarily of SH2 and SH3 regions."
Reichman C.T., Mayer B.J., Khawer S., Hanafusa H.
Cell Growth Differ. 3:451-460(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Structural basis for regulation of the Crk signaling protein by a proline switch."
Sarkar P., Saleh T., Tzeng S.R., Birge R.B., Kalodimos C.G.
Nat. Chem. Biol. 7:51-57(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 135-297, ISOMERIZATION AT PRO-238.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L08168 mRNA. Translation: AAA49001.1.
PIRA49011.
RefSeqNP_001007847.1. NM_001007846.1.
UniGeneGga.27345.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2L3PNMR-A220-297[»]
2L3QNMR-A220-297[»]
2L3SNMR-A135-297[»]
ProteinModelPortalQ04929.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid678886. 1 interaction.
IntActQ04929. 2 interactions.
MINTMINT-8019929.
STRING9031.ENSGALP00000004174.

Proteomic databases

PaxDbQ04929.
PRIDEQ04929.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSGALT00000004183; ENSGALP00000004174; ENSGALG00000002656.
GeneID417553.
KEGGgga:417553.

Organism-specific databases

CTD1398.

Phylogenomic databases

eggNOGNOG292767.
GeneTreeENSGT00390000001475.
HOGENOMHOG000236288.
HOVERGENHBG105616.
InParanoidQ04929.
KOK04438.
OMANQDSSHP.
OrthoDBEOG7NW69P.
PhylomeDBQ04929.
TreeFamTF321436.

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. 2 hits.
SSF55550. SSF55550. 2 hits.
PROSITEPS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ04929.
NextBio20820838.
PROQ04929.

Entry information

Entry nameCRK_CHICK
AccessionPrimary (citable) accession number: Q04929
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references