Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

Q24592

- JAK_DROME

UniProt

Q24592 - JAK_DROME

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 2 (01 Mar 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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. endomembrane system Source: UniProtKB-SubCell
    4. membrane Source: UniProtKB-KW

    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 574-839, 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.
    GeneTreeiENSGT00740000115195.
    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

    MALANGGEDR MDDSSSGRTS LADSASLTNS SLRSGTSSQS IHTNDGTIRV     50
    FNFTTGEFER FHPNMLCEEI CNTMCRQLGI APIAQLLYGI REHSTSRRPS 100
    PLVRLDLTWC LPGERLNCQL VYCFRMRFRV PELDSQLELI DGRSHKFLYR 150
    QMRYDMRTEQ IPEIRYPEHK DKSTGLAVMD MLIDDQEQSE DQQAMRSIEK 200
    LYKLYLPPSL WRAHSFFVGS KIREVFRSLK ANSLSVERLK WHYVHQVSHL 250
    APTYMTEQFT CTVQYLPNEE VARGSGPIGT SLAHSTSTLA SSGSTNTLST 300
    LTTNTNSVAL GGSGKKAKRR STSGGIDVYV RVFPHDSLEP GLKVARVTSE 350
    ATLKWILVGA VEGIFMISKI NDTSVRLEIV GLPKGYEMQF QTEKEMKSFI 400
    SYLGIYIRLS SKWMQDLCHS YRTPSLEELS SLHCHGPIGG AYSLMKLHEN 450
    GDKCGSYIVR ECDREYNIYY IDINTKIMAK KTDQERCKTE TFRIVRKDSQ 500
    WKLSYNNGEH VLNSLHEVAH IIQADSPDRY RIPASKYDKP PLLLLLLPKN 550
    LKAKKTDLQL SEAELQRRNP QIFNPRTDLQ WYPDSISLSD DGMMFTMRGD 600
    WIQQSPVKDV SVTMKMLKSD GNFMEFFRLA QTWSLIQSPQ FLKLYGLTLA 650
    DPYTMVMEYS RYGPLNKFLH SMPNVTLHCL LDLMHGLVRG MHYLEDNKII 700
    HNYIRCSNLY VTKYDPNSYV LDAKISDPGY PRPYRESDSP WIPVKYYRNL 750
    QAAKTDQFAQ LWAFATTIYE IFSRCKEDLS TLRQEQLLRQ KNLDGNILKM 800
    LDQDICPAPI FETIMDGWSD DETKRFSHHD IFSRLNTIKA EILPNYMPPP 850
    EIATNGTGDE TVIDRSDIPF LPFPRSNMLM VIPLTSECRV IYNMENMIGR 900
    GHYGTVYKGH LEFNDKDQPR EQVAIKMLNT MQVSTDFHRE IGIMRTLSHP 950
    NIVKFKYWAE KSHCIIMEYL QSGSFDIYLR FTAPNLNNPR LVSFALDIAN 1000
    GMKYLSDMGL IHRDLAARNI LVDHNGDGDC VKISDFGLAQ FANSDGYYYA 1050
    KSKRDIPIRW YSPEAISTCR FSSYSDVWSY GVTLFEMFSR GEEPNLVPIQ 1100
    TSQEDFLNRL QSGERLNRPA SCPDFIYDLM QLCWHATPRS RPSFATIVDI 1150
    ITREVATKVT HPTDGHQSPP NQPTDAE 1177
    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_078564.2.
    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_078564.2.
    UniGenei Dm.2926.

    3D structure databases

    ProteinModelPortali Q24592.
    SMRi Q24592. Positions 574-839, 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 ENSGT00740000115195.
    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

    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 1, 2014
    This is version 142 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