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Protein

Tyrosine-protein kinase hopscotch

Gene

hop

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

Functioni

Tyrosine kinase of the non-receptor type, phosphorylates the marelle protein. Required maternally for the establishment of the normal array of embryonic segments: involved in the control of pair-rule gene transcription in a stripe-specific manner. Together with Hsp83 and piwi, mediates canalization, also known as developmental robustness, likely via epigenetic silencing of existing genetic variants and suppression of transposon-induced new genetic variation.2 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei926 – 9261ATPPROSITE-ProRule annotation
Active sitei1014 – 10141Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi898 – 9069ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein tyrosine kinase activity Source: FlyBase

GO - Biological processi

  1. apical constriction Source: FlyBase
  2. blastoderm segmentation Source: FlyBase
  3. border follicle cell migration Source: FlyBase
  4. cell proliferation Source: FlyBase
  5. cellular defense response Source: FlyBase
  6. compound eye development Source: FlyBase
  7. compound eye morphogenesis Source: FlyBase
  8. compound eye photoreceptor cell differentiation Source: FlyBase
  9. defense response to virus Source: FlyBase
  10. encapsulation of foreign target Source: FlyBase
  11. equator specification Source: FlyBase
  12. establishment of ommatidial planar polarity Source: FlyBase
  13. eye-antennal disc morphogenesis Source: FlyBase
  14. germ-line stem cell division Source: FlyBase
  15. hemocyte differentiation Source: FlyBase
  16. hemocyte proliferation Source: FlyBase
  17. hemopoiesis Source: FlyBase
  18. hindgut morphogenesis Source: FlyBase
  19. humoral immune response Source: FlyBase
  20. imaginal disc-derived leg morphogenesis Source: FlyBase
  21. imaginal disc-derived wing morphogenesis Source: FlyBase
  22. immune response Source: FlyBase
  23. innate immune response Source: GO_Central
  24. JAK-STAT cascade Source: FlyBase
  25. lamellocyte differentiation Source: FlyBase
  26. larval lymph gland hemopoiesis Source: FlyBase
  27. locomotor rhythm Source: FlyBase
  28. long-term memory Source: FlyBase
  29. mediolateral intercalation Source: FlyBase
  30. nervous system development Source: FlyBase
  31. ommatidial rotation Source: FlyBase
  32. oogenesis Source: FlyBase
  33. open tracheal system development Source: FlyBase
  34. ovarian follicle cell development Source: FlyBase
  35. ovarian follicle cell stalk formation Source: FlyBase
  36. peptidyl-tyrosine autophosphorylation Source: GO_Central
  37. periodic partitioning Source: FlyBase
  38. primary sex determination Source: FlyBase
  39. protein phosphorylation Source: FlyBase
  40. regulation of embryonic cell shape Source: FlyBase
  41. regulation of hemocyte differentiation Source: FlyBase
  42. regulation of hemocyte proliferation Source: FlyBase
  43. regulation of JAK-STAT cascade Source: FlyBase
  44. regulation of transcription, DNA-templated Source: UniProtKB-KW
  45. sex determination Source: FlyBase
  46. somatic stem cell division Source: FlyBase
  47. STAT protein import into nucleus Source: FlyBase
  48. stem cell maintenance Source: FlyBase
  49. transcription, DNA-templated Source: UniProtKB-KW
  50. transmembrane receptor protein tyrosine kinase signaling pathway Source: GO_Central
  51. tyrosine phosphorylation of STAT protein Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 1994.
ReactomeiREACT_287092. Factors involved in megakaryocyte development and platelet production.
REACT_305574. RMTs methylate histone arginines.
REACT_334486. Signaling by SCF-KIT.
SignaLinkiQ24592.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase hopscotch (EC:2.7.10.2)
Gene namesi
Name:hop
Synonyms:HD-160
ORF Names:CG1594
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0004864. hop.

Subcellular locationi

Endomembrane system By similarity; Peripheral membrane protein By similarity
Note: Wholly intracellular, possibly membrane associated.By similarity

GO - Cellular componenti

  1. cytoplasm Source: FlyBase
  2. cytoskeleton Source: InterPro
  3. endomembrane system Source: UniProtKB-SubCell
  4. extrinsic component of cytoplasmic side of plasma membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11771177Tyrosine-protein kinase hopscotchPRO_0000088118Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei40 – 401Phosphoserine1 Publication
Modified residuei321 – 3211Phosphoserine1 Publication
Modified residuei1047 – 10471Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1048 – 10481Phosphotyrosine; by autocatalysisBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ24592.
PRIDEiQ24592.

Expressioni

Developmental stagei

Expressed both maternally and zygotically throughout development.1 Publication

Gene expression databases

BgeeiQ24592.

Interactioni

Subunit structurei

Forms a complex with Hsp83 and piwi; probably Hop mediates the interaction between piwi and Hsp83.

Protein-protein interaction databases

BioGridi58492. 11 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ24592.
SMRiQ24592. Positions 592-1156.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 414369FERMPROSITE-ProRule annotationAdd
BLAST
Domaini433 – 539107SH2; atypicalAdd
BLAST
Domaini582 – 843262Protein kinase 1PROSITE-ProRule annotationAdd
BLAST
Domaini892 – 1164273Protein kinase 2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi542 – 5476Poly-Leu

Domaini

Possesses two phosphotransferase domains. The second one probably contains the catalytic domain (By similarity), while the presence of slight differences suggest a different role for domain 1 (By similarity).By similarity

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. JAK subfamily.PROSITE-ProRule annotation
Contains 1 FERM domain.PROSITE-ProRule annotation
Contains 2 protein kinase domains.PROSITE-ProRule annotation
Contains 1 SH2 domain.Curated

Keywords - Domaini

Repeat, SH2 domain

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118799.
InParanoidiQ24592.
KOiK04447.
OMAiIAWTQGE.
OrthoDBiEOG7DZ8J7.
PhylomeDBiQ24592.

Family and domain databases

InterProiIPR019749. Band_41_domain.
IPR000299. FERM_domain.
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]
PfamiPF07714. Pkinase_Tyr. 2 hits.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00295. B41. 1 hit.
SM00252. SH2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 2 hits.
PROSITEiPS50057. FERM_3. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 2 hits.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q24592-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALANGGEDR MDDSSSGRTS LADSASLTNS SLRSGTSSQS IHTNDGTIRV
60 70 80 90 100
FNFTTGEFER FHPNMLCEEI CNTMCRQLGI APIAQLLYGI REHSTSRRPS
110 120 130 140 150
PLVRLDLTWC LPGERLNCQL VYCFRMRFRV PELDSQLELI DGRSHKFLYR
160 170 180 190 200
QMRYDMRTEQ IPEIRYPEHK DKSTGLAVMD MLIDDQEQSE DQQAMRSIEK
210 220 230 240 250
LYKLYLPPSL WRAHSFFVGS KIREVFRSLK ANSLSVERLK WHYVHQVSHL
260 270 280 290 300
APTYMTEQFT CTVQYLPNEE VARGSGPIGT SLAHSTSTLA SSGSTNTLST
310 320 330 340 350
LTTNTNSVAL GGSGKKAKRR STSGGIDVYV RVFPHDSLEP GLKVARVTSE
360 370 380 390 400
ATLKWILVGA VEGIFMISKI NDTSVRLEIV GLPKGYEMQF QTEKEMKSFI
410 420 430 440 450
SYLGIYIRLS SKWMQDLCHS YRTPSLEELS SLHCHGPIGG AYSLMKLHEN
460 470 480 490 500
GDKCGSYIVR ECDREYNIYY IDINTKIMAK KTDQERCKTE TFRIVRKDSQ
510 520 530 540 550
WKLSYNNGEH VLNSLHEVAH IIQADSPDRY RIPASKYDKP PLLLLLLPKN
560 570 580 590 600
LKAKKTDLQL SEAELQRRNP QIFNPRTDLQ WYPDSISLSD DGMMFTMRGD
610 620 630 640 650
WIQQSPVKDV SVTMKMLKSD GNFMEFFRLA QTWSLIQSPQ FLKLYGLTLA
660 670 680 690 700
DPYTMVMEYS RYGPLNKFLH SMPNVTLHCL LDLMHGLVRG MHYLEDNKII
710 720 730 740 750
HNYIRCSNLY VTKYDPNSYV LDAKISDPGY PRPYRESDSP WIPVKYYRNL
760 770 780 790 800
QAAKTDQFAQ LWAFATTIYE IFSRCKEDLS TLRQEQLLRQ KNLDGNILKM
810 820 830 840 850
LDQDICPAPI FETIMDGWSD DETKRFSHHD IFSRLNTIKA EILPNYMPPP
860 870 880 890 900
EIATNGTGDE TVIDRSDIPF LPFPRSNMLM VIPLTSECRV IYNMENMIGR
910 920 930 940 950
GHYGTVYKGH LEFNDKDQPR EQVAIKMLNT MQVSTDFHRE IGIMRTLSHP
960 970 980 990 1000
NIVKFKYWAE KSHCIIMEYL QSGSFDIYLR FTAPNLNNPR LVSFALDIAN
1010 1020 1030 1040 1050
GMKYLSDMGL IHRDLAARNI LVDHNGDGDC VKISDFGLAQ FANSDGYYYA
1060 1070 1080 1090 1100
KSKRDIPIRW YSPEAISTCR FSSYSDVWSY GVTLFEMFSR GEEPNLVPIQ
1110 1120 1130 1140 1150
TSQEDFLNRL QSGERLNRPA SCPDFIYDLM QLCWHATPRS RPSFATIVDI
1160 1170
ITREVATKVT HPTDGHQSPP NQPTDAE
Length:1,177
Mass (Da):135,062
Last modified:February 28, 2005 - v2
Checksum:iBF8587C420BF3A8F
GO

Sequence cautioni

The sequence AAL48491.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti365 – 3651F → V in AAA62441 (PubMed:8314084).Curated
Sequence conflicti592 – 5921G → A in AAA62441 (PubMed:8314084).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L26975 mRNA. Translation: AAA62441.1.
AE014298 Genomic DNA. Translation: AAF48035.1.
BT006331 mRNA. Translation: AAP20030.1.
AY070869 mRNA. Translation: AAL48491.1. Different initiation.
AJ002915 Genomic DNA. Translation: CAA05750.1.
PIRiA36984.
RefSeqiNP_511119.2. NM_078564.3.
UniGeneiDm.2926.

Genome annotation databases

EnsemblMetazoaiFBtr0073457; FBpp0073313; FBgn0004864.
GeneIDi32080.
KEGGidme:Dmel_CG1594.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L26975 mRNA. Translation: AAA62441.1.
AE014298 Genomic DNA. Translation: AAF48035.1.
BT006331 mRNA. Translation: AAP20030.1.
AY070869 mRNA. Translation: AAL48491.1. Different initiation.
AJ002915 Genomic DNA. Translation: CAA05750.1.
PIRiA36984.
RefSeqiNP_511119.2. NM_078564.3.
UniGeneiDm.2926.

3D structure databases

ProteinModelPortaliQ24592.
SMRiQ24592. Positions 592-1156.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi58492. 11 interactions.

Proteomic databases

PaxDbiQ24592.
PRIDEiQ24592.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0073457; FBpp0073313; FBgn0004864.
GeneIDi32080.
KEGGidme:Dmel_CG1594.

Organism-specific databases

CTDi15392.
FlyBaseiFBgn0004864. hop.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118799.
InParanoidiQ24592.
KOiK04447.
OMAiIAWTQGE.
OrthoDBiEOG7DZ8J7.
PhylomeDBiQ24592.

Enzyme and pathway databases

BRENDAi2.7.10.2. 1994.
ReactomeiREACT_287092. Factors involved in megakaryocyte development and platelet production.
REACT_305574. RMTs methylate histone arginines.
REACT_334486. Signaling by SCF-KIT.
SignaLinkiQ24592.

Miscellaneous databases

GenomeRNAii32080.
NextBioi776713.

Gene expression databases

BgeeiQ24592.

Family and domain databases

InterProiIPR019749. Band_41_domain.
IPR000299. FERM_domain.
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]
PfamiPF07714. Pkinase_Tyr. 2 hits.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00295. B41. 1 hit.
SM00252. SH2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 2 hits.
PROSITEiPS50057. FERM_3. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 2 hits.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Stripe-specific regulation of pair-rule genes by hopscotch, a putative Jak family tyrosine kinase in Drosophila."
    Binari R., Perrimon N.
    Genes Dev. 8:300-312(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE.
  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(1999) [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: Head.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 596-1177.
    Strain: Berkeley.
    Tissue: Head.
  6. "Sampling the genomic pool of protein tyrosine kinase genes using the polymerase chain reaction with genomic DNA."
    Oates A.C., Wollberg P., Achen M.G., Wilks A.F.
    Biochem. Biophys. Res. Commun. 249:660-667(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1020-1075.
  7. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40 AND SER-321, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  8. "Drosophila Piwi functions in Hsp90-mediated suppression of phenotypic variation."
    Gangaraju V.K., Yin H., Weiner M.M., Wang J., Huang X.A., Lin H.
    Nat. Genet. 43:153-158(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH PIWI AND HSP83.

Entry informationi

Entry nameiJAK_DROME
AccessioniPrimary (citable) accession number: Q24592
Secondary accession number(s): Q712V3, Q8SZI9, Q9VYZ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 1997
Last sequence update: February 28, 2005
Last modified: March 31, 2015
This is version 147 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.