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Protein

Adapter molecule crk

Gene

Crk

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The Crk-I and Crk-II forms differ in their biological activities. Crk-II has less transforming activity than Crk-I. Crk-II mediates attachment-induced MAPK8 activation, membrane ruffling and cell motility in a Rac-dependent manner. Involved in phagocytosis of apoptotic cells and cell motility via its interaction with DOCK1 and DOCK4. May regulate the EFNA5-EPHA3 signaling.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei237 – 2371Proline switchBy similarity

GO - Molecular functioni

  • ephrin receptor binding Source: UniProtKB
  • protein phosphorylated amino acid binding Source: MGI
  • SH2 domain binding Source: MGI
  • SH3/SH2 adaptor activity Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_278498. Downstream signal transduction.
REACT_286373. Regulation of signaling by CBL.
REACT_315885. VEGFA-VEGFR2 Pathway.
REACT_316753. p130Cas linkage to MAPK signaling for integrins.
REACT_324620. ARMS-mediated activation.
REACT_333431. Signal attenuation.
REACT_344463. Regulation of actin dynamics for phagocytic cup formation.

Names & Taxonomyi

Protein namesi
Recommended name:
Adapter molecule crk
Alternative name(s):
Proto-oncogene c-Crk
p38
Gene namesi
Name:Crk
Synonyms:Crko
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:88508. Crk.

Subcellular locationi

  • Cytoplasm By similarity
  • Cell membrane By similarity

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

GO - Cellular componenti

  • actin cytoskeleton Source: MGI
  • cytoplasm Source: UniProtKB-SubCell
  • extracellular exosome Source: MGI
  • 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
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 304303Adapter molecule crkPRO_0000079352Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei41 – 411PhosphoserineBy similarity
Modified residuei74 – 741PhosphoserineBy similarity
Modified residuei83 – 831PhosphoserineBy similarity
Modified residuei125 – 1251PhosphoserineBy similarity
Modified residuei221 – 2211Phosphotyrosine; by ABL11 Publication
Modified residuei239 – 2391PhosphotyrosineBy similarity

Post-translational modificationi

Isoform Crk-II is phosphorylated by KIT. Phosphorylated on Tyr-221 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-221 with the SH2 domain. This leads finally to the down-regulation of the Crk signaling pathway.2 Publications
Proline isomerization at Pro-237 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.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ64010.
PaxDbiQ64010.
PRIDEiQ64010.

PTM databases

PhosphoSiteiQ64010.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ64010.
CleanExiMM_CRK.
ExpressionAtlasiQ64010. baseline and differential.
GenevisibleiQ64010. MM.

Interactioni

Subunit structurei

Interacts with ABL1, C3G, DOCK3, MAP4K1, MAPK8 and SOS via its first SH3 domain. Interacts (via SH2 domain) with BCAR1, CBL, CBLB, PXN, IRS4 and GAB1 upon stimulus-induced tyrosine phosphorylation. Interacts (via SH2 domain) with several tyrosine-phosphorylated growth factor receptors such as EGFR and INSR. Interacts with FLT1 (tyrosine-phosphorylated). Interacts with DOCK1 and DOCK4. Interacts with SHB. Interacts with PEAK1. Interacts with FASLG. Isoform Crk-II interacts with KIT. Interacts with EPHA3; upon activation of EPHA3 by the ligand EFNA5 and EPHA3 tyrosine kinase activity-dependent. Interacts with EPHA3 (phosphorylated); mediates EFNA5-EPHA3 signaling through RHOA GTPase activation. Interacts with FLT4 (tyrosine-phosphorylated). Isoform Crk-II (via SH2 domain) interacts with PDGFRA (tyrosine phosphorylated) and PDGFRB (tyrosine phosphorylated). Part of a collagen stimulated complex involved in cell migration composed of CDC42, CRK, TNK2 and p130cas/BCAR1. Interacts (via SH2 domain) with the 'Tyr-9' phosphorylated form of PDPK1. Interacts with CBLC. Found in a complex with ABL1, ABL2, CRK and UNC119; leading to the inhibition of CRK phosphorylation by ABL kinases (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
IGF1RP080693EBI-2906540,EBI-475981From a different organism.

Protein-protein interaction databases

BioGridi198887. 24 interactions.
DIPiDIP-57059N.
IntActiQ64010. 22 interactions.
MINTiMINT-4599411.
STRINGi10090.ENSMUSP00000017920.

Structurei

Secondary structure

1
304
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi136 – 1416Combined sources
Beta strandi147 – 1504Combined sources
Beta strandi158 – 1636Combined sources
Beta strandi165 – 1739Combined sources
Beta strandi179 – 1835Combined sources
Helixi184 – 1863Combined sources
Beta strandi187 – 1893Combined sources
Beta strandi238 – 2447Combined sources
Beta strandi252 – 2543Combined sources
Beta strandi262 – 2687Combined sources
Beta strandi271 – 2733Combined sources
Beta strandi275 – 2795Combined sources
Beta strandi282 – 2865Combined sources
Helixi288 – 2903Combined sources
Beta strandi291 – 2944Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B07X-ray2.50A134-190[»]
1CKAX-ray1.50A134-190[»]
1CKBX-ray1.90A134-190[»]
1JU5NMR-B217-228[»]
1M30NMR-A134-191[»]
1M3ANMR-A135-191[»]
1M3BNMR-A134-191[»]
1M3CNMR-A132-191[»]
2GGRNMR-A230-304[»]
ProteinModelPortaliQ64010.
SMRiQ64010. Positions 1-304.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ64010.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 118106SH2PROSITE-ProRule annotationAdd
BLAST
Domaini132 – 19261SH3 1PROSITE-ProRule annotationAdd
BLAST
Domaini237 – 29660SH3 2PROSITE-ProRule annotationAdd
BLAST

Domaini

The C-terminal SH3 domain function as a negative modulator for transformation and the N-terminal SH3 domain appears to function as a positive regulator for transformation.By similarity
The SH2 domain mediates interaction with tyrosine phosphorylated proteins. Mediates interaction with SHB.

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.
InParanoidiQ64010.
OrthoDBiEOG7NW69P.
PhylomeDBiQ64010.
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. 3 hits.
SSF55550. SSF55550. 2 hits.
PROSITEiPS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Crk-II (identifier: Q64010-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAGNFDSEER SSWYWGRLSR QEAVALLQGQ RHGVFLVRDS STSPGDYVLS
60 70 80 90 100
VSENSRVSHY IINSSGPRPP VPPSPAQPPP GVSPSRLRIG DQEFDSLPAL
110 120 130 140 150
LEFYKIHYLD TTTLIEPVAR SRQGSGVILR QEEAEYVRAL FDFNGNDEED
160 170 180 190 200
LPFKKGDILR IRDKPEEQWW NAEDSEGKRG MIPVPYVEKY RPASASVSAL
210 220 230 240 250
IGGNQEGSHP QPLGGPEPGP YAQPSVNTPL PNLQNGPIYA RVIQKRVPNA
260 270 280 290 300
YDKTALALEV GELVKVTKIN VSGQWEGECN GKRGHFPFTH VRLLDQQNPD

EDFS
Length:304
Mass (Da):33,815
Last modified:November 1, 1996 - v1
Checksum:i5491896FC7A89065
GO
Isoform Crk-I (identifier: Q64010-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     205-304: Missing.

Show »
Length:204
Mass (Da):22,847
Checksum:i35B7AC1188657461
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei205 – 304100Missing in isoform Crk-I. 1 PublicationVSP_004174Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S72408 mRNA. Translation: AAB30755.1.
AK028488 mRNA. Translation: BAC25976.1.
CCDSiCCDS25055.1. [Q64010-1]
RefSeqiNP_598417.2. NM_133656.5. [Q64010-1]
UniGeneiMm.280125.

Genome annotation databases

EnsembliENSMUST00000017920; ENSMUSP00000017920; ENSMUSG00000017776. [Q64010-1]
GeneIDi12928.
UCSCiuc007keq.2. mouse. [Q64010-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S72408 mRNA. Translation: AAB30755.1.
AK028488 mRNA. Translation: BAC25976.1.
CCDSiCCDS25055.1. [Q64010-1]
RefSeqiNP_598417.2. NM_133656.5. [Q64010-1]
UniGeneiMm.280125.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B07X-ray2.50A134-190[»]
1CKAX-ray1.50A134-190[»]
1CKBX-ray1.90A134-190[»]
1JU5NMR-B217-228[»]
1M30NMR-A134-191[»]
1M3ANMR-A135-191[»]
1M3BNMR-A134-191[»]
1M3CNMR-A132-191[»]
2GGRNMR-A230-304[»]
ProteinModelPortaliQ64010.
SMRiQ64010. Positions 1-304.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198887. 24 interactions.
DIPiDIP-57059N.
IntActiQ64010. 22 interactions.
MINTiMINT-4599411.
STRINGi10090.ENSMUSP00000017920.

PTM databases

PhosphoSiteiQ64010.

Proteomic databases

MaxQBiQ64010.
PaxDbiQ64010.
PRIDEiQ64010.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000017920; ENSMUSP00000017920; ENSMUSG00000017776. [Q64010-1]
GeneIDi12928.
UCSCiuc007keq.2. mouse. [Q64010-1]

Organism-specific databases

CTDi1398.
MGIiMGI:88508. Crk.

Phylogenomic databases

eggNOGiNOG292767.
GeneTreeiENSGT00390000001475.
HOGENOMiHOG000236288.
HOVERGENiHBG105616.
InParanoidiQ64010.
OrthoDBiEOG7NW69P.
PhylomeDBiQ64010.
TreeFamiTF321436.

Enzyme and pathway databases

ReactomeiREACT_278498. Downstream signal transduction.
REACT_286373. Regulation of signaling by CBL.
REACT_315885. VEGFA-VEGFR2 Pathway.
REACT_316753. p130Cas linkage to MAPK signaling for integrins.
REACT_324620. ARMS-mediated activation.
REACT_333431. Signal attenuation.
REACT_344463. Regulation of actin dynamics for phagocytic cup formation.

Miscellaneous databases

EvolutionaryTraceiQ64010.
NextBioi282592.
PROiQ64010.
SOURCEiSearch...

Gene expression databases

BgeeiQ64010.
CleanExiMM_CRK.
ExpressionAtlasiQ64010. baseline and differential.
GenevisibleiQ64010. MM.

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. 3 hits.
SSF55550. SSF55550. 2 hits.
PROSITEiPS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The C-terminal SH3 domain of the mouse c-Crk protein negatively regulates tyrosine-phosphorylation of Crk associated p130 in rat 3Y1 cells."
    Ogawa S., Toyoshima H., Kozutsumi H., Hagiwara K., Sakai R., Tanaka T., Hirano N., Mano H., Yazaki Y., Hirai H.
    Oncogene 9:1669-1678(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS CRK-I AND CRK-II).
    Tissue: Liver.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CRK-II).
    Strain: C57BL/6J.
    Tissue: Skin.
  3. "c-Abl kinase regulates the protein binding activity of c-Crk."
    Feller S.M., Knudsen B., Hanafusa H.
    EMBO J. 13:2341-2351(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-221, INTERACTION WITH ABL1.
  4. "An eps homology (EH) domain protein that binds to the ral-GTPase target, RalBP1."
    Yamaguchi A., Urano T., Goi T., Feig L.A.
    J. Biol. Chem. 272:31230-31234(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH REPS1.
    Tissue: Muscle.
  5. "Identification of vascular endothelial growth factor receptor-1 tyrosine phosphorylation sites and binding of SH2 domain-containing molecules."
    Ito N., Wernstedt C., Engstrom U., Claesson-Welsh L.
    J. Biol. Chem. 273:23410-23418(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FLT1.
  6. "ASAP1, a phospholipid-dependent arf GTPase-activating protein that associates with and is phosphorylated by Src."
    Brown M.T., Andrade J., Radhakrishna H., Donaldson J.G., Cooper J.A., Randazzo P.A.
    Mol. Cell. Biol. 18:7038-7051(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DDEF1/ASAP1.
  7. "Isolation and characterization of novel presenilin binding protein."
    Kashiwa A., Yoshida H., Lee S., Paladino T., Liu Y., Chen Q., Dargusch R., Schubert D., Kimura H.
    J. Neurochem. 75:109-116(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DOCK3.
    Tissue: Brain.
  8. "Ephrin-A5 induces rounding, blebbing and de-adhesion of EphA3-expressing 293T and melanoma cells by CrkII and Rho-mediated signalling."
    Lawrenson I.D., Wimmer-Kleikamp S.H., Lock P., Schoenwaelder S.M., Down M., Boyd A.W., Alewood P.F., Lackmann M.
    J. Cell Sci. 115:1059-1072(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EPHA3.
  9. "Identification of Tyr900 in the kinase domain of c-Kit as a Src-dependent phosphorylation site mediating interaction with c-Crk."
    Lennartsson J., Wernstedt C., Engstrom U., Hellman U., Ronnstrand L.
    Exp. Cell Res. 288:110-118(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KIT, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION.
  10. "The roles of Cbl-b and c-Cbl in insulin-stimulated glucose transport."
    Liu J., DeYoung S.M., Hwang J.B., O'Leary E.E., Saltiel A.R.
    J. Biol. Chem. 278:36754-36762(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CBLB.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  14. "Structural basis for the specific interaction of lysine-containing proline-rich peptides with the N-terminal SH3 domain of c-Crk."
    Wu X., Knudsen B., Feller S.M., Zheng J., Sali A., Cowburn D., Hanafusa H., Kuriyan J.
    Structure 3:215-226(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 134-190.
  15. "Exploiting the basis of proline recognition by SH3 and WW domains: design of N-substituted inhibitors."
    Nguyen J.T., Turck C.W., Cohen F.E., Zuckermann R.N., Lim W.A.
    Science 282:2088-2092(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 133-191.

Entry informationi

Entry nameiCRK_MOUSE
AccessioniPrimary (citable) accession number: Q64010
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 22, 2015
This is version 149 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.