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Q24592

- JAK_DROME

UniProt

Q24592 - JAK_DROME

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Protein

Tyrosine-protein kinase hopscotch

Gene

hop

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - 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. JAK-STAT cascade Source: FlyBase
  24. lamellocyte differentiation Source: FlyBase
  25. larval lymph gland hemopoiesis Source: FlyBase
  26. locomotor rhythm Source: FlyBase
  27. long-term memory Source: FlyBase
  28. mediolateral intercalation Source: FlyBase
  29. nervous system development Source: FlyBase
  30. ommatidial rotation Source: FlyBase
  31. oogenesis Source: FlyBase
  32. open tracheal system development Source: FlyBase
  33. ovarian follicle cell development Source: FlyBase
  34. ovarian follicle cell stalk formation Source: FlyBase
  35. periodic partitioning Source: FlyBase
  36. primary sex determination Source: FlyBase
  37. protein phosphorylation Source: FlyBase
  38. regulation of embryonic cell shape Source: FlyBase
  39. regulation of hemocyte differentiation Source: FlyBase
  40. regulation of hemocyte proliferation Source: FlyBase
  41. regulation of JAK-STAT cascade Source: FlyBase
  42. regulation of transcription, DNA-templated Source: UniProtKB-KW
  43. sex determination Source: FlyBase
  44. somatic stem cell division Source: FlyBase
  45. STAT protein import into nucleus Source: FlyBase
  46. stem cell maintenance Source: FlyBase
  47. transcription, DNA-templated Source: UniProtKB-KW
  48. 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.
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: 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. membrane Source: UniProtKB-KW
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 592-825, 844-1156.
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.
OMAiEIRYPEH.
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:March 1, 2005 - v2
Checksum:iBF8587C420BF3A8F
GO

Sequence cautioni

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

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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi A36984.
RefSeqi NP_511119.2. NM_078564.3.
UniGenei Dm.2926.

3D structure databases

ProteinModelPortali Q24592.
SMRi Q24592. Positions 592-825, 844-1156.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 58492. 11 interactions.

Proteomic databases

PaxDbi Q24592.
PRIDEi Q24592.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0073457 ; FBpp0073313 ; FBgn0004864 .
GeneIDi 32080.
KEGGi dme:Dmel_CG1594.

Organism-specific databases

CTDi 15392.
FlyBasei FBgn0004864. hop.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118799.
InParanoidi Q24592.
KOi K04447.
OMAi EIRYPEH.
OrthoDBi EOG7DZ8J7.
PhylomeDBi Q24592.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 1994.
SignaLinki Q24592.

Miscellaneous databases

GenomeRNAii 32080.
NextBioi 776713.

Gene expression databases

Bgeei Q24592.

Family and domain databases

InterProi IPR019749. 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 ]
Pfami PF07714. Pkinase_Tyr. 2 hits.
[Graphical view ]
PRINTSi PR00109. TYRKINASE.
SMARTi SM00295. B41. 1 hit.
SM00252. SH2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 2 hits.
PROSITEi PS50057. FERM_3. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 2 hits.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(1994) [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(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: 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(1998) [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(2008) [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(2011) [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: November 1, 1997
Last sequence update: March 1, 2005
Last modified: October 29, 2014
This is version 143 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