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Protein

Adapter molecule Crk

Gene

Crk

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Adapter protein which interacts with C-terminal portion of mbc, homolog of human DOCK180. May play a role in cellular processes throughout development.1 Publication

GO - Molecular functioni

  • SH3/SH2 adaptor activity Source: FlyBase

GO - Biological processi

  • border follicle cell migration Source: FlyBase
  • ephrin receptor signaling pathway Source: UniProtKB
  • imaginal disc fusion, thorax closure Source: FlyBase
  • myoblast fusion Source: FlyBase
  • phagocytosis, engulfment Source: FlyBase
  • positive regulation of JNK cascade Source: FlyBase
  • regulation of actin cytoskeleton organization Source: UniProtKB
  • regulation of GTPase activity Source: UniProtKB
  • signal transduction Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Enzyme and pathway databases

ReactomeiR-DME-372708. p130Cas linkage to MAPK signaling for integrins.
R-DME-4420097. VEGFA-VEGFR2 Pathway.
R-DME-912631. Regulation of signaling by CBL.
SignaLinkiQ9XYM0.

Names & Taxonomyi

Protein namesi
Recommended name:
Adapter molecule Crk
Gene namesi
Name:Crk
ORF Names:CG1587
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 4

Organism-specific databases

FlyBaseiFBgn0024811. Crk.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 271271Adapter molecule CrkPRO_0000079350Add
BLAST

Proteomic databases

PaxDbiQ9XYM0.
PRIDEiQ9XYM0.

Expressioni

Tissue specificityi

Embryonic zygotic expression is seen in invaginating presumptive mesoderm and ectodermally derived tissues during gastrulation. At stage 8, expression is also seen in anterior and posterior midgut and cephalic furrow. By stage 9, expression is highest in visceral mesoderm of anterior and posterior midgut, ventral nerve cord and somatic mesoderm.1 Publication

Developmental stagei

Expressed both maternally and zygotically throughout embryogenesis, declines during larval stages and reappears during pupation.1 Publication

Gene expression databases

BgeeiQ9XYM0.
GenevisibleiQ9XYM0. DM.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
mbcQ9VCH43EBI-99477,EBI-177001

GO - Molecular functioni

  • SH3/SH2 adaptor activity Source: FlyBase

Protein-protein interaction databases

BioGridi68612. 9 interactions.
DIPiDIP-21287N.
IntActiQ9XYM0. 4 interactions.
MINTiMINT-308673.
STRINGi7227.FBpp0088181.

Structurei

3D structure databases

ProteinModelPortaliQ9XYM0.
SMRiQ9XYM0. Positions 4-266.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 10493SH2PROSITE-ProRule annotationAdd
BLAST
Domaini106 – 16661SH3 1PROSITE-ProRule annotationAdd
BLAST
Domaini201 – 26060SH3 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

eggNOGiKOG4792. Eukaryota.
ENOG4110574. LUCA.
GeneTreeiENSGT00820000127055.
InParanoidiQ9XYM0.
OMAiICEGILN.
OrthoDBiEOG7NW69P.
PhylomeDBiQ9XYM0.

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

Sequencei

Sequence statusi: Complete.

Q9XYM0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDTFDVSDRN SWYFGPMSRQ DATEVLMNER ERGVFLVRDS NSIAGDYVLC
60 70 80 90 100
VREDTKVSNY IINKVQQQDQ IVYRIGDQSF DNLPKLLTFY TLHYLDTTPL
110 120 130 140 150
KRPACRRVEK VIGKFDFVGS DQDDLPFQRG EVLTIVRKDE DQWWTARNSS
160 170 180 190 200
GKIGQIPVPY IQQYDDYMDE DAIDKNEPSI SGSSNVFEST LKRTDLNRKL
210 220 230 240 250
PAYARVKQSR VPNAYDKTAL KLEIGDIIKV TKTNINGQWE GELNGKNGHF
260 270
PFTHVEFVDD CDLSKNSTEI C
Length:271
Mass (Da):31,205
Last modified:November 1, 1999 - v1
Checksum:iD1B4FE43150932DC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF112976 mRNA. Translation: AAD28428.1.
AE014135 Genomic DNA. Translation: AAF59362.1.
AE014135 Genomic DNA. Translation: AAN06519.1.
BT012456 mRNA. Translation: AAS93727.1.
RefSeqiNP_651908.1. NM_143651.6.
NP_726549.1. NM_166743.3.
UniGeneiDm.3226.

Genome annotation databases

EnsemblMetazoaiFBtr0089112; FBpp0088181; FBgn0024811.
FBtr0089113; FBpp0088182; FBgn0024811.
GeneIDi43775.
UCSCiCG1587-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF112976 mRNA. Translation: AAD28428.1.
AE014135 Genomic DNA. Translation: AAF59362.1.
AE014135 Genomic DNA. Translation: AAN06519.1.
BT012456 mRNA. Translation: AAS93727.1.
RefSeqiNP_651908.1. NM_143651.6.
NP_726549.1. NM_166743.3.
UniGeneiDm.3226.

3D structure databases

ProteinModelPortaliQ9XYM0.
SMRiQ9XYM0. Positions 4-266.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi68612. 9 interactions.
DIPiDIP-21287N.
IntActiQ9XYM0. 4 interactions.
MINTiMINT-308673.
STRINGi7227.FBpp0088181.

Proteomic databases

PaxDbiQ9XYM0.
PRIDEiQ9XYM0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0089112; FBpp0088181; FBgn0024811.
FBtr0089113; FBpp0088182; FBgn0024811.
GeneIDi43775.
UCSCiCG1587-RA. d. melanogaster.

Organism-specific databases

CTDi1398.
FlyBaseiFBgn0024811. Crk.

Phylogenomic databases

eggNOGiKOG4792. Eukaryota.
ENOG4110574. LUCA.
GeneTreeiENSGT00820000127055.
InParanoidiQ9XYM0.
OMAiICEGILN.
OrthoDBiEOG7NW69P.
PhylomeDBiQ9XYM0.

Enzyme and pathway databases

ReactomeiR-DME-372708. p130Cas linkage to MAPK signaling for integrins.
R-DME-4420097. VEGFA-VEGFR2 Pathway.
R-DME-912631. Regulation of signaling by CBL.
SignaLinkiQ9XYM0.

Miscellaneous databases

GenomeRNAii43775.
NextBioi835750.
PROiQ9XYM0.

Gene expression databases

BgeeiQ9XYM0.
GenevisibleiQ9XYM0. DM.

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

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a Drosophila homologue to vertebrate Crk by interaction with MBC."
    Galletta B.J., Niu X.-P., Erickson M.R., Abmayr S.M.
    Gene 228:243-252(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Tissue: Embryo.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Stapleton M., Carlson J., Chavez C., Frise E., George R., Pacleb J., Park S., Wan K., Yu C., Rubin G.M., Celniker S.
    Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.

Entry informationi

Entry nameiCRK_DROME
AccessioniPrimary (citable) accession number: Q9XYM0
Secondary accession number(s): Q53XD2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 1, 1999
Last modified: May 11, 2016
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  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.