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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)LengthDescriptionGraphical viewFeature identifierActions
Sitei238 – 2381Proline switch

GO - Biological processi

  1. ephrin receptor signaling pathway Source: UniProtKB
  2. positive regulation of signal transduction Source: Ensembl
  3. regulation of actin cytoskeleton organization Source: UniProtKB
  4. regulation of Rho GTPase activity Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_271548. ARMS-mediated activation.
REACT_321609. p130Cas linkage to MAPK signaling for integrins.
REACT_329539. VEGFA-VEGFR2 Pathway.
REACT_333012. Downstream signal transduction.
REACT_351340. 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
ProteomesiUP000000539 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

  1. actin cytoskeleton Source: Ensembl
  2. cytoplasm Source: UniProtKB-SubCell
  3. extracellular vesicular exosome Source: Ensembl
  4. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 305305Adapter molecule crkPRO_0000079349Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei222 – 2221PhosphotyrosineBy similarity

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.

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 interactions.
IntActiQ04929. 2 interactions.
MINTiMINT-8019929.
STRINGi9031.ENSGALP00000004174.

Structurei

Secondary structure

1
305
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi137 – 1404Combined sources
Beta strandi148 – 1514Combined sources
Beta strandi156 – 1649Combined sources
Beta strandi166 – 1749Combined sources
Beta strandi176 – 1783Combined sources
Beta strandi180 – 1845Combined sources
Helixi185 – 1873Combined sources
Beta strandi200 – 2034Combined sources
Beta strandi226 – 2283Combined sources
Beta strandi234 – 2363Combined sources
Beta strandi239 – 2457Combined sources
Beta strandi253 – 2553Combined sources
Beta strandi263 – 2697Combined sources
Beta strandi272 – 2743Combined sources
Beta strandi277 – 2804Combined sources
Beta strandi283 – 2864Combined sources
Helixi289 – 2913Combined sources
Beta strandi292 – 2954Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ04929.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 119107SH2PROSITE-ProRule annotationAdd
BLAST
Domaini133 – 19361SH3 1PROSITE-ProRule annotationAdd
BLAST
Domaini238 – 29760SH3 2PROSITE-ProRule annotationAdd
BLAST

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.
InParanoidiQ04929.
KOiK04438.
OMAiNQDSSHP.
OrthoDBiEOG7NW69P.
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.
UniGeneiGga.27345.

Genome annotation databases

EnsembliENSGALT00000004183; ENSGALP00000004174; ENSGALG00000002656.
GeneIDi417553.
KEGGigga: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.
UniGeneiGga.27345.

3D structure databases

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

Protein-protein interaction databases

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

Proteomic databases

PaxDbiQ04929.
PRIDEiQ04929.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSGALT00000004183; ENSGALP00000004174; ENSGALG00000002656.
GeneIDi417553.
KEGGigga:417553.

Organism-specific databases

CTDi1398.

Phylogenomic databases

eggNOGiNOG292767.
GeneTreeiENSGT00390000001475.
HOGENOMiHOG000236288.
HOVERGENiHBG105616.
InParanoidiQ04929.
KOiK04438.
OMAiNQDSSHP.
OrthoDBiEOG7NW69P.
PhylomeDBiQ04929.
TreeFamiTF321436.

Enzyme and pathway databases

ReactomeiREACT_271548. ARMS-mediated activation.
REACT_321609. p130Cas linkage to MAPK signaling for integrins.
REACT_329539. VEGFA-VEGFR2 Pathway.
REACT_333012. Downstream signal transduction.
REACT_351340. Regulation of signaling by CBL.

Miscellaneous databases

EvolutionaryTraceiQ04929.
NextBioi20820838.
PROiQ04929.

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...

Publicationsi

  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(1991) [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(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 135-297, ISOMERIZATION AT PRO-238.

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: April 1, 2015
This is version 99 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

External Data

Dasty 3

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 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.