Skip Header

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

Q24145

- SHARK_DROME

UniProt

Q24145 - SHARK_DROME

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Tyrosine-protein kinase shark

Gene

shark

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - 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

  1. ATP binding Source: UniProtKB-KW
  2. non-membrane spanning protein tyrosine kinase activity Source: FlyBase
  3. protein tyrosine kinase activity Source: FlyBase

GO - Biological processi

  1. apoptotic cell clearance Source: FlyBase
  2. dorsal appendage formation Source: FlyBase
  3. dorsal closure Source: FlyBase
  4. dorsal closure, elongation of leading edge cells Source: FlyBase
  5. eggshell chorion assembly Source: FlyBase
  6. JNK cascade Source: FlyBase
  7. maintenance of epithelial cell apical/basal polarity Source: UniProtKB
  8. neuron projection morphogenesis Source: FlyBase
  9. peptidyl-tyrosine phosphorylation Source: GOC
  10. protein phosphorylation Source: FlyBase
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.
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: 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

  1. cell cortex Source: FlyBase
  2. cytoplasm Source: UniProtKB
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.

Interactioni

Protein-protein interaction databases

BioGridi68999. 1 interaction.
DIPiDIP-59843N.

Structurei

3D structure databases

ProteinModelPortaliQ24145.
SMRiQ24145. Positions 10-274, 614-928.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 10697SH2 1CuratedPROSITE-ProRule annotationAdd
BLAST
Repeati153 – 18533ANK 1CuratedAdd
BLAST
Repeati186 – 21833ANK 2CuratedAdd
BLAST
Repeati220 – 25233ANK 3CuratedAdd
BLAST
Domaini288 – 403116SH2 2CuratedPROSITE-ProRule annotationAdd
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.
OMAiHGEDAFF.
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
U37773 mRNA. Translation: AAA79851.1 .
AE013599 Genomic DNA. Translation: AAF58044.1 .
AY051937 mRNA. Translation: AAK93361.1 .
S55982 Genomic DNA. Translation: AAB19909.1 .
PIRi S18015.
RefSeqi NP_524743.2. NM_080004.4.
UniGenei Dm.6764.

3D structure databases

ProteinModelPortali Q24145.
SMRi Q24145. Positions 10-274, 614-928.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 68999. 1 interaction.
DIPi DIP-59843N.

Proteomic databases

PaxDbi Q24145.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0087244 ; FBpp0086382 ; FBgn0015295 .
GeneIDi 44353.
KEGGi dme:Dmel_CG18247.

Organism-specific databases

CTDi 44353.
FlyBasei FBgn0015295. shark.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118799.
InParanoidi Q24145.
KOi K17512.
OMAi HGEDAFF.
OrthoDBi EOG70W3CT.
PhylomeDBi Q24145.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 1994.
SignaLinki Q24145.

Miscellaneous databases

ChiTaRSi shark. drosophila.
GenomeRNAii 44353.
NextBioi 837182.

Gene expression databases

Bgeei Q24145.

Family and domain databases

Gene3Di 1.25.40.20. 1 hit.
3.30.505.10. 2 hits.
InterProi IPR002110. 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 ]
Pfami PF00023. Ank. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 2 hits.
[Graphical view ]
PRINTSi PR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTi SM00248. ANK. 4 hits.
SM00252. SH2. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF48403. SSF48403. 1 hit.
SSF55550. SSF55550. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEi PS50297. 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 ]
ProtoNeti Search...

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: October 29, 2014
This is version 131 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