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Q24145 (SHARK_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. 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:
Tyrosine-protein kinase shark

EC=2.7.10.2
Gene names
Name:shark
Synonyms:Tk7
ORF Names:CG18247
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length939 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

May be involved in signal transduction on the apical surface of ectodermal epithelia regulating their polarity during invagination. Crumbs (crb) may be the intracellular signal. Ref.1

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Subcellular location

Cytoplasm. Note: Apical expression in cephalic furrow and tracheal cells. Limited to luminal surface and absent from the basal surface. Ref.1

Tissue specificity

Gastrulation embryos show expression in ectodermal cells along the cephalic furrow and ventral midline. Proctodeum, stomodeum and their derived structures (foregut, atrium, pharynx, esophagus and hindgut) continue to show expression from stage 8-9 to late embryos. Other ectodermally derived structures (frontal sac, salivary gland and labium) and developing tracheal system also show expression. Ref.1

Developmental stage

Embryos only. Ref.1

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family.

Contains 3 ANK repeats.

Contains 1 protein kinase domain.

Contains 2 SH2 domains.

Ontologies

Keywords
   Cellular componentCytoplasm
   DomainANK repeat
Repeat
SH2 domain
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
Tyrosine-protein kinase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processJNK cascade

Inferred from mutant phenotype PubMed 10716948. Source: FlyBase

apoptotic cell clearance

Inferred from mutant phenotype PubMed 18432193PubMed 19369546. Source: FlyBase

dorsal appendage formation

Inferred from mutant phenotype PubMed 14602681. Source: FlyBase

dorsal closure

Traceable author statement PubMed 12147138. Source: FlyBase

dorsal closure, elongation of leading edge cells

Inferred from mutant phenotype PubMed 10716948. Source: FlyBase

eggshell chorion assembly

Inferred from mutant phenotype PubMed 14602681. Source: FlyBase

maintenance of epithelial cell apical/basal polarity

Inferred from expression pattern Ref.1. Source: UniProtKB

neuron projection morphogenesis

Inferred from mutant phenotype PubMed 18604272. Source: FlyBase

peptidyl-tyrosine phosphorylation

Non-traceable author statement PubMed 10908587PubMed 12147138. Source: GOC

protein phosphorylation

Non-traceable author statement PubMed 10908587. Source: FlyBase

   Cellular_componentcell cortex

Inferred from direct assay PubMed 16339186. Source: FlyBase

cytoplasm

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

non-membrane spanning protein tyrosine kinase activity

Non-traceable author statement PubMed 12147138. Source: FlyBase

protein tyrosine kinase activity

Non-traceable author statement PubMed 10908587. Source: FlyBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 939939Tyrosine-protein kinase shark
PRO_0000088137

Regions

Domain10 – 10697SH2 1
Repeat153 – 18533ANK 1
Repeat186 – 21833ANK 2
Repeat220 – 25233ANK 3
Domain288 – 403116SH2 2
Domain662 – 921260Protein kinase
Nucleotide binding668 – 6769ATP By similarity

Sites

Active site7891Proton acceptor By similarity
Binding site6981ATP By similarity

Amino acid modifications

Modified residue9271Phosphotyrosine Potential

Experimental info

Sequence conflict191A → V in AAA79851. Ref.1
Sequence conflict391S → R in AAA79851. Ref.1
Sequence conflict501L → F in AAA79851. Ref.1
Sequence conflict851D → E in AAA79851. Ref.1
Sequence conflict1291S → T in AAA79851. Ref.1
Sequence conflict1991P → T in AAA79851. Ref.1
Sequence conflict3411C → S in AAA79851. Ref.1
Sequence conflict505 – 5062GT → RA in AAA79851. Ref.1
Sequence conflict5971M → V in AAA79851. Ref.1
Sequence conflict6111A → P in AAA79851. Ref.1
Sequence conflict7321A → S in AAA79851. Ref.1
Sequence conflict8981A → P in AAA79851. Ref.1
Sequence conflict935 – 9395QTVHI → KRFTFNPVSIFHFFRC in AAA79851. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q24145 [UniParc].

Last modified October 1, 2000. Version 2.
Checksum: 37CC2C3DA25D3F52

FASTA939104,273
        10         20         30         40         50         60 
MSRDSDPMKW YHGNLSREAA DELLKQGYED GTFLVRESST AAGDFVLSLL CQGEVCHYQV 

        70         80         90        100        110        120 
RRHGGEDAFF SIDDKVQTKI LHGLDTLVDY YQQAANGLPT KLTVPLIRDL PPHNTRSHGV 

       130        140        150        160        170        180 
TNLLHRATSK NESKVVFELL KCGYRNFDAK NQDGQTALHL AALHSDEDIL KHLLNAKVQV 

       190        200        210        220        230        240 
NSSDSFGCQP LHYAARSKPA SFIRTLISAQ ANVQGRNIDN GYVPLHEAAK HGNLEAVQEL 

       250        260        270        280        290        300 
LLAEAPPLPR TSSGEFPFDL AKEAGQTAVE EFLLNYKLPP ANTTRDQWYH GTLTREEAVA 

       310        320        330        340        350        360 
ILKKHAKELL AKQPEVDTSG CFLVRYSESP AASGLVLTLL CDQVVKNFRI SQADLYQNGN 

       370        380        390        400        410        420 
KVQSGGSKFL YIDDGPYWPS VEHLIAHFMR FSYGLPVSLK YPVPPQPKPE VPSFATIPRS 

       430        440        450        460        470        480 
NMKPKAASPA TPPTPVSPHS HHQHPHVPAL TITKKKQKEN SSSMFNTLRL TSPKKALFDM 

       490        500        510        520        530        540 
NSLRKNKSKG KRSDSESSVS GSLAGTEQEL QAAAPMLKSL SFSTEFSTFN ADGVTGSGAA 

       550        560        570        580        590        600 
AAGEVYNVPR NNTPIEIDLP PIAQKTEAEV EYFTKSDVAI ERERAGQWIG NGYQPTMDVL 

       610        620        630        640        650        660 
SLLDQQIKAP AVARLNSLGP NASTESEMAS YLHRKCSGTP STPSATEVEA AKLRFFIEPE 

       670        680        690        700        710        720 
KLVLDREIGH GEFGSVHSGW LLRKSGAGEE SRLEVAIKML SDEHSNKQEF LREASVMMRL 

       730        740        750        760        770        780 
EHKCIVRLIG IAKGEMLMMV QELAPLGSML QYILDHGHEI TANAELKVWA SQIACGMHYL 

       790        800        810        820        830        840 
ESQHFVHRDL AARNILLTAR HQAKISDFGM SRSLRPGSTE YQFTQGGRWP IRWYAPESFN 

       850        860        870        880        890        900 
LGIFSHASDV WSFGVTIWEM FSLGAPPYGE ISNVDAIKLV DSGERLPQPN LCPAYIYAVM 

       910        920        930 
QSCWKERPKD RPTFVYLTEF FARDPDYQNL PELVQTVHI 

« Hide

References

« Hide 'large scale' references
[1]"Shark, a Src homology 2, ankyrin repeat, tyrosine kinase, is expressed on the apical surfaces of ectodermal epithelia."
Ferrante A.W. Jr., Reinke R., Stanley E.R.
Proc. Natl. Acad. Sci. U.S.A. 92:1911-1915(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, 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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[5]"Identification of seven novel protein-tyrosine kinase genes of Drosophila by the polymerase chain reaction."
Shishido E., Emori Y., Saigo K.
FEBS Lett. 289:235-238(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 793-849.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U37773 mRNA. Translation: AAA79851.1.
AE013599 Genomic DNA. Translation: AAF58044.1.
AY051937 mRNA. Translation: AAK93361.1.
S55982 Genomic DNA. Translation: AAB19909.1.
PIRS18015.
RefSeqNP_524743.2. NM_080004.3.
UniGeneDm.6764.

3D structure databases

ProteinModelPortalQ24145.
SMRQ24145. Positions 10-274, 285-404, 614-928.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid68999. 1 interaction.
DIPDIP-59843N.

Proteomic databases

PaxDbQ24145.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0087244; FBpp0086382; FBgn0015295.
GeneID44353.
KEGGdme:Dmel_CG18247.

Organism-specific databases

CTD44353.
FlyBaseFBgn0015295. shark.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00740000115195.
InParanoidQ24145.
KOK17512.
OMAHGEDAFF.
OrthoDBEOG70W3CT.
PhylomeDBQ24145.

Enzyme and pathway databases

BRENDA2.7.10.2. 1994.
SignaLinkQ24145.

Gene expression databases

BgeeQ24145.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
3.30.505.10. 2 hits.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamPF00023. Ank. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 2 hits.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTSM00248. ANK. 4 hits.
SM00252. SH2. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
SSF55550. SSF55550. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 3 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSshark. drosophila.
GenomeRNAi44353.
NextBio837182.

Entry information

Entry nameSHARK_DROME
AccessionPrimary (citable) accession number: Q24145
Secondary accession number(s): Q26299, Q9V7K5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2003
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

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