Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Tyrosine-protein kinase shark

Gene

shark

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

Functioni

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.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei698 – 6981ATPPROSITE-ProRule annotation
Active sitei789 – 7891Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi668 – 6769ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • apoptotic cell clearance Source: FlyBase
  • cell differentiation Source: GO_Central
  • cell migration Source: GO_Central
  • dorsal appendage formation Source: FlyBase
  • dorsal closure Source: FlyBase
  • dorsal closure, elongation of leading edge cells Source: FlyBase
  • eggshell chorion assembly Source: FlyBase
  • innate immune response Source: GO_Central
  • JNK cascade Source: FlyBase
  • maintenance of epithelial cell apical/basal polarity Source: UniProtKB
  • neuron projection morphogenesis Source: FlyBase
  • peptidyl-tyrosine autophosphorylation Source: GO_Central
  • protein phosphorylation Source: FlyBase
  • regulation of cell proliferation Source: GO_Central
  • transmembrane receptor protein tyrosine kinase signaling pathway Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 1994.
ReactomeiREACT_277617. GPVI-mediated activation cascade.
REACT_318429. Integrin alphaIIb beta3 signaling.
SignaLinkiQ24145.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase shark (EC:2.7.10.2)
Gene namesi
Name:shark
Synonyms:Tk7
ORF Names:CG18247
OrganismiDrosophila melanogaster (Fruit fly)Imported
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0015295. shark.

Subcellular locationi

  • Cytoplasm 1 Publication

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

GO - Cellular componenti

  • cell cortex Source: FlyBase
  • cytoplasm Source: UniProtKB
  • extrinsic component of cytoplasmic side of plasma membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 939939Tyrosine-protein kinase sharkPRO_0000088137Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei927 – 9271PhosphotyrosineSequence Analysis

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ24145.

Expressioni

Tissue specificityi

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.1 Publication

Developmental stagei

Embryos only.1 Publication

Gene expression databases

BgeeiQ24145.
GenevisibleiQ24145. DM.

Interactioni

Protein-protein interaction databases

BioGridi68999. 1 interaction.
DIPiDIP-59843N.
IntActiQ24145. 1 interaction.
STRINGi7227.FBpp0086382.

Structurei

3D structure databases

ProteinModelPortaliQ24145.
SMRiQ24145. Positions 10-305, 614-928.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 10697SH2 1PROSITE-ProRule annotationCuratedAdd
BLAST
Repeati153 – 18533ANK 1CuratedAdd
BLAST
Repeati186 – 21833ANK 2CuratedAdd
BLAST
Repeati220 – 25233ANK 3CuratedAdd
BLAST
Domaini288 – 403116SH2 2PROSITE-ProRule annotationCuratedAdd
BLAST
Domaini662 – 921260Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family.PROSITE-ProRule annotation
Contains 3 ANK repeats.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 2 SH2 domains.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat, SH2 domain

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118799.
InParanoidiQ24145.
KOiK17512.
OMAiRWYAPES.
OrthoDBiEOG70W3CT.
PhylomeDBiQ24145.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
3.30.505.10. 2 hits.
InterProiIPR002110. 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]
PfamiPF00023. Ank. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 2 hits.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00248. ANK. 4 hits.
SM00252. SH2. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF55550. SSF55550. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50297. 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]

Sequencei

Sequence statusi: Complete.

Q24145-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRDSDPMKW YHGNLSREAA DELLKQGYED GTFLVRESST AAGDFVLSLL
60 70 80 90 100
CQGEVCHYQV RRHGGEDAFF SIDDKVQTKI LHGLDTLVDY YQQAANGLPT
110 120 130 140 150
KLTVPLIRDL PPHNTRSHGV TNLLHRATSK NESKVVFELL KCGYRNFDAK
160 170 180 190 200
NQDGQTALHL AALHSDEDIL KHLLNAKVQV NSSDSFGCQP LHYAARSKPA
210 220 230 240 250
SFIRTLISAQ ANVQGRNIDN GYVPLHEAAK HGNLEAVQEL LLAEAPPLPR
260 270 280 290 300
TSSGEFPFDL AKEAGQTAVE EFLLNYKLPP ANTTRDQWYH GTLTREEAVA
310 320 330 340 350
ILKKHAKELL AKQPEVDTSG CFLVRYSESP AASGLVLTLL CDQVVKNFRI
360 370 380 390 400
SQADLYQNGN KVQSGGSKFL YIDDGPYWPS VEHLIAHFMR FSYGLPVSLK
410 420 430 440 450
YPVPPQPKPE VPSFATIPRS NMKPKAASPA TPPTPVSPHS HHQHPHVPAL
460 470 480 490 500
TITKKKQKEN SSSMFNTLRL TSPKKALFDM NSLRKNKSKG KRSDSESSVS
510 520 530 540 550
GSLAGTEQEL QAAAPMLKSL SFSTEFSTFN ADGVTGSGAA AAGEVYNVPR
560 570 580 590 600
NNTPIEIDLP PIAQKTEAEV EYFTKSDVAI ERERAGQWIG NGYQPTMDVL
610 620 630 640 650
SLLDQQIKAP AVARLNSLGP NASTESEMAS YLHRKCSGTP STPSATEVEA
660 670 680 690 700
AKLRFFIEPE KLVLDREIGH GEFGSVHSGW LLRKSGAGEE SRLEVAIKML
710 720 730 740 750
SDEHSNKQEF LREASVMMRL EHKCIVRLIG IAKGEMLMMV QELAPLGSML
760 770 780 790 800
QYILDHGHEI TANAELKVWA SQIACGMHYL ESQHFVHRDL AARNILLTAR
810 820 830 840 850
HQAKISDFGM SRSLRPGSTE YQFTQGGRWP IRWYAPESFN LGIFSHASDV
860 870 880 890 900
WSFGVTIWEM FSLGAPPYGE ISNVDAIKLV DSGERLPQPN LCPAYIYAVM
910 920 930
QSCWKERPKD RPTFVYLTEF FARDPDYQNL PELVQTVHI
Length:939
Mass (Da):104,273
Last modified:October 1, 2000 - v2
Checksum:i37CC2C3DA25D3F52
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191A → V in AAA79851 (PubMed:7892198).Curated
Sequence conflicti39 – 391S → R in AAA79851 (PubMed:7892198).Curated
Sequence conflicti50 – 501L → F in AAA79851 (PubMed:7892198).Curated
Sequence conflicti85 – 851D → E in AAA79851 (PubMed:7892198).Curated
Sequence conflicti129 – 1291S → T in AAA79851 (PubMed:7892198).Curated
Sequence conflicti199 – 1991P → T in AAA79851 (PubMed:7892198).Curated
Sequence conflicti341 – 3411C → S in AAA79851 (PubMed:7892198).Curated
Sequence conflicti505 – 5062GT → RA in AAA79851 (PubMed:7892198).Curated
Sequence conflicti597 – 5971M → V in AAA79851 (PubMed:7892198).Curated
Sequence conflicti611 – 6111A → P in AAA79851 (PubMed:7892198).Curated
Sequence conflicti732 – 7321A → S in AAA79851 (PubMed:7892198).Curated
Sequence conflicti898 – 8981A → P in AAA79851 (PubMed:7892198).Curated
Sequence conflicti935 – 9395QTVHI → KRFTFNPVSIFHFFRC in AAA79851 (PubMed:7892198).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37773 mRNA. Translation: AAA79851.1.
AE013599 Genomic DNA. Translation: AAF58044.1.
AY051937 mRNA. Translation: AAK93361.1.
S55982 Genomic DNA. Translation: AAB19909.1.
PIRiS18015.
RefSeqiNP_524743.2. NM_080004.4.
UniGeneiDm.6764.

Genome annotation databases

EnsemblMetazoaiFBtr0087244; FBpp0086382; FBgn0015295.
GeneIDi44353.
KEGGidme:Dmel_CG18247.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37773 mRNA. Translation: AAA79851.1.
AE013599 Genomic DNA. Translation: AAF58044.1.
AY051937 mRNA. Translation: AAK93361.1.
S55982 Genomic DNA. Translation: AAB19909.1.
PIRiS18015.
RefSeqiNP_524743.2. NM_080004.4.
UniGeneiDm.6764.

3D structure databases

ProteinModelPortaliQ24145.
SMRiQ24145. Positions 10-305, 614-928.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi68999. 1 interaction.
DIPiDIP-59843N.
IntActiQ24145. 1 interaction.
STRINGi7227.FBpp0086382.

Proteomic databases

PaxDbiQ24145.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0087244; FBpp0086382; FBgn0015295.
GeneIDi44353.
KEGGidme:Dmel_CG18247.

Organism-specific databases

CTDi44353.
FlyBaseiFBgn0015295. shark.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118799.
InParanoidiQ24145.
KOiK17512.
OMAiRWYAPES.
OrthoDBiEOG70W3CT.
PhylomeDBiQ24145.

Enzyme and pathway databases

BRENDAi2.7.10.2. 1994.
ReactomeiREACT_277617. GPVI-mediated activation cascade.
REACT_318429. Integrin alphaIIb beta3 signaling.
SignaLinkiQ24145.

Miscellaneous databases

ChiTaRSishark. fly.
GenomeRNAii44353.
NextBioi837182.
PROiQ24145.

Gene expression databases

BgeeiQ24145.
GenevisibleiQ24145. DM.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
3.30.505.10. 2 hits.
InterProiIPR002110. 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]
PfamiPF00023. Ank. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 2 hits.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00248. ANK. 4 hits.
SM00252. SH2. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF55550. SSF55550. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50297. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiSHARK_DROME
AccessioniPrimary (citable) accession number: Q24145
Secondary accession number(s): Q26299, Q9V7K5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2003
Last sequence update: October 1, 2000
Last modified: July 22, 2015
This is version 139 of the entry and version 2 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

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.