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Q04929

- CRK_CHICK

UniProt

Q04929 - CRK_CHICK

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Protein

Adapter molecule crk

Gene
CRK
Organism
Gallus gallus (Chicken)
Status
Reviewed - 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.

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: GOC
  3. regulation of actin cytoskeleton organization Source: UniProtKB
  4. regulation of Rho GTPase activity Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_197520. 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: 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. cytoplasm Source: UniProtKB-SubCell
  2. 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 – 2221Phosphotyrosine By 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.
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.1 Publication

Protein-protein interaction databases

BioGridi678886. 1 interaction.
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 – 1404
Beta strandi148 – 1514
Beta strandi156 – 1649
Beta strandi166 – 1749
Beta strandi176 – 1783
Beta strandi180 – 1845
Helixi185 – 1873
Beta strandi200 – 2034
Beta strandi226 – 2283
Beta strandi234 – 2363
Beta strandi239 – 2457
Beta strandi253 – 2553
Beta strandi263 – 2697
Beta strandi272 – 2743
Beta strandi277 – 2804
Beta strandi283 – 2864
Helixi289 – 2913
Beta strandi292 – 2954

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L3PNMR-A220-297[»]
2L3QNMR-A220-297[»]
2L3SNMR-A135-297[»]
ProteinModelPortaliQ04929.

Miscellaneous databases

EvolutionaryTraceiQ04929.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 119107SH2Add
BLAST
Domaini133 – 19361SH3 1Add
BLAST
Domaini238 – 29760SH3 2Add
BLAST

Sequence similaritiesi

Belongs to the CRK family.
Contains 1 SH2 domain.
Contains 2 SH3 domains.

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

MAGQFDSEDR GSWYWGRLSR GDAVSLLQGQ RHGTFLVRDS GSIPGDFVLS    50
VSESSRVSHY IVNSLGPAGG RRAGGEGPGA PGLNPTRFRI GDQEFDSLPS 100
LLEFYKIHYL DTTTLIEPVS RSRQNSGVIL RQEEVEYVRA LFDFNGNDDE 150
DLPFKKGDIL KIRDKPEEQW WNAEDMDGKR GMIPVPYVEK CRPSSASVST 200
LTGGNQDSSH PQPLGGPEPG PYAQPSINTP LPNLQNGPFY ARVIQKRVPN 250
AYDKTALALE VGELVKVTKI NMSGQWEGEC NGKRGHFPFT HVRLLDQQNP 300
DEDFS 305
Length:305
Mass (Da):33,806
Last modified:November 1, 1995 - v1
Checksum:i0A79AD232E824768
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
L08168 mRNA. Translation: AAA49001.1 .
PIRi A49011.
RefSeqi NP_001007847.1. NM_001007846.1.
UniGenei Gga.27345.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2L3P NMR - A 220-297 [» ]
2L3Q NMR - A 220-297 [» ]
2L3S NMR - A 135-297 [» ]
ProteinModelPortali Q04929.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 678886. 1 interaction.
IntActi Q04929. 2 interactions.
MINTi MINT-8019929.
STRINGi 9031.ENSGALP00000004174.

Proteomic databases

PaxDbi Q04929.
PRIDEi Q04929.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSGALT00000004183 ; ENSGALP00000004174 ; ENSGALG00000002656 .
GeneIDi 417553.
KEGGi gga:417553.

Organism-specific databases

CTDi 1398.

Phylogenomic databases

eggNOGi NOG292767.
GeneTreei ENSGT00390000001475.
HOGENOMi HOG000236288.
HOVERGENi HBG105616.
InParanoidi Q04929.
KOi K04438.
OMAi NQDSSHP.
OrthoDBi EOG7NW69P.
PhylomeDBi Q04929.
TreeFami TF321436.

Enzyme and pathway databases

Reactomei REACT_197520. Regulation of signaling by CBL.

Miscellaneous databases

EvolutionaryTracei Q04929.
NextBioi 20820838.
PROi Q04929.

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. 2 hits.
SSF55550. SSF55550. 2 hits.
PROSITEi PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(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.

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: September 3, 2014
This is version 92 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

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