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Q24592 (JAK_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein kinase hopscotch

EC=2.7.10.2
Gene names
Name:hop
Synonyms:HD-160
ORF Names:CG1594
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length1177 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.8

Catalytic activity

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

Subunit structure

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

Subcellular location

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

Developmental stage

Expressed both maternally and zygotically throughout development. Ref.1

Domain

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.

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. JAK subfamily.

Contains 1 FERM domain.

Contains 2 protein kinase domains.

Contains 1 SH2 domain.

Sequence caution

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

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentMembrane
   DomainRepeat
SH2 domain
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Transferase
Tyrosine-protein kinase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processJAK-STAT cascade

Inferred from genetic interaction PubMed 8608595. Source: FlyBase

STAT protein import into nucleus

Traceable author statement PubMed 15199955. Source: FlyBase

apical constriction

Inferred from mutant phenotype PubMed 19934015. Source: FlyBase

blastoderm segmentation

Inferred from mutant phenotype PubMed 12586062. Source: FlyBase

border follicle cell migration

Inferred from mutant phenotype PubMed 12586061. Source: FlyBase

cell proliferation

Inferred from mutant phenotype Ref.1. Source: FlyBase

cellular defense response

Non-traceable author statement PubMed 15199955. Source: FlyBase

compound eye development

Inferred from mutant phenotype PubMed 10479459PubMed 11746233. Source: FlyBase

compound eye morphogenesis

Inferred from mutant phenotype PubMed 15170700. Source: FlyBase

compound eye photoreceptor cell differentiation

Inferred from mutant phenotype PubMed 10479459. Source: FlyBase

defense response to virus

Inferred from mutant phenotype PubMed 16086017. Source: FlyBase

encapsulation of foreign target

Non-traceable author statement PubMed 15199955. Source: FlyBase

equator specification

Inferred from mutant phenotype PubMed 10479459PubMed 11746233. Source: FlyBase

establishment of ommatidial planar polarity

Inferred from mutant phenotype PubMed 10479459. Source: FlyBase

eye-antennal disc morphogenesis

Inferred from mutant phenotype PubMed 17079268. Source: FlyBase

germ-line stem cell division

Traceable author statement PubMed 12459723. Source: FlyBase

hemocyte differentiation

Inferred from mutant phenotype PubMed 11919715. Source: FlyBase

hemocyte proliferation

Traceable author statement PubMed 15199955. Source: FlyBase

hemopoiesis

Traceable author statement PubMed 10793472PubMed 11746233PubMed 14602069. Source: FlyBase

hindgut morphogenesis

Inferred from mutant phenotype PubMed 12441298PubMed 14654218. Source: FlyBase

humoral immune response

Traceable author statement PubMed 15199955. Source: FlyBase

imaginal disc-derived leg morphogenesis

Non-traceable author statement PubMed 11746233. Source: FlyBase

imaginal disc-derived wing morphogenesis

Non-traceable author statement PubMed 11746233. Source: FlyBase

immune response

Traceable author statement PubMed 11283698. Source: FlyBase

lamellocyte differentiation

Traceable author statement PubMed 15199955. Source: FlyBase

larval lymph gland hemopoiesis

Inferred from mutant phenotype PubMed 17936744. Source: FlyBase

locomotor rhythm

Inferred from mutant phenotype PubMed 22305007. Source: FlyBase

long-term memory

Inferred from mutant phenotype PubMed 21518857. Source: FlyBase

mediolateral intercalation

Inferred from mutant phenotype PubMed 19934015. Source: FlyBase

nervous system development

Inferred from mutant phenotype PubMed 14654218. Source: FlyBase

ommatidial rotation

Inferred from mutant phenotype PubMed 11746233. Source: FlyBase

oogenesis

Traceable author statement PubMed 12194841. Source: FlyBase

open tracheal system development

Inferred from mutant phenotype PubMed 12586062PubMed 14654218. Source: FlyBase

ovarian follicle cell development

Inferred from mutant phenotype PubMed 12586061. Source: FlyBase

ovarian follicle cell stalk formation

Inferred from mutant phenotype PubMed 17332535. Source: FlyBase

periodic partitioning

Inferred from mutant phenotype Ref.1. Source: FlyBase

primary sex determination

Inferred from mutant phenotype PubMed 10882142. Source: FlyBase

protein phosphorylation

Non-traceable author statement PubMed 10908587. Source: FlyBase

regulation of JAK-STAT cascade

Inferred from mutant phenotype PubMed 20624926. Source: FlyBase

regulation of embryonic cell shape

Inferred from mutant phenotype PubMed 19934015. Source: FlyBase

regulation of hemocyte differentiation

Inferred from mutant phenotype PubMed 15381778. Source: FlyBase

regulation of hemocyte proliferation

Inferred from mutant phenotype PubMed 20688956. Source: FlyBase

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

sex determination

Non-traceable author statement PubMed 11746233. Source: FlyBase

somatic stem cell division

Traceable author statement PubMed 12459723. Source: FlyBase

stem cell maintenance

Inferred from mutant phenotype PubMed 11752574. Source: FlyBase

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

tyrosine phosphorylation of STAT protein

Traceable author statement PubMed 11746233PubMed 15199955. Source: FlyBase

   Cellular_componentcytoplasm

Traceable author statement PubMed 9066269. Source: FlyBase

cytoskeleton

Inferred from electronic annotation. Source: InterPro

endomembrane system

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein tyrosine kinase activity

Non-traceable author statement PubMed 10908587PubMed 11746233. Source: FlyBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11771177Tyrosine-protein kinase hopscotch
PRO_0000088118

Regions

Domain46 – 414369FERM
Domain433 – 539107SH2; atypical
Domain582 – 843262Protein kinase 1
Domain892 – 1164273Protein kinase 2
Nucleotide binding898 – 9069ATP By similarity
Compositional bias542 – 5476Poly-Leu

Sites

Active site10141Proton acceptor By similarity
Binding site9261ATP By similarity

Amino acid modifications

Modified residue401Phosphoserine Ref.7
Modified residue3211Phosphoserine Ref.7
Modified residue10471Phosphotyrosine; by autocatalysis By similarity
Modified residue10481Phosphotyrosine; by autocatalysis By similarity

Experimental info

Sequence conflict3651F → V in AAA62441. Ref.1
Sequence conflict5921G → A in AAA62441. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q24592 [UniParc].

Last modified March 1, 2005. Version 2.
Checksum: BF8587C420BF3A8F

FASTA1,177135,062
        10         20         30         40         50         60 
MALANGGEDR MDDSSSGRTS LADSASLTNS SLRSGTSSQS IHTNDGTIRV FNFTTGEFER 

        70         80         90        100        110        120 
FHPNMLCEEI CNTMCRQLGI APIAQLLYGI REHSTSRRPS PLVRLDLTWC LPGERLNCQL 

       130        140        150        160        170        180 
VYCFRMRFRV PELDSQLELI DGRSHKFLYR QMRYDMRTEQ IPEIRYPEHK DKSTGLAVMD 

       190        200        210        220        230        240 
MLIDDQEQSE DQQAMRSIEK LYKLYLPPSL WRAHSFFVGS KIREVFRSLK ANSLSVERLK 

       250        260        270        280        290        300 
WHYVHQVSHL APTYMTEQFT CTVQYLPNEE VARGSGPIGT SLAHSTSTLA SSGSTNTLST 

       310        320        330        340        350        360 
LTTNTNSVAL GGSGKKAKRR STSGGIDVYV RVFPHDSLEP GLKVARVTSE ATLKWILVGA 

       370        380        390        400        410        420 
VEGIFMISKI NDTSVRLEIV GLPKGYEMQF QTEKEMKSFI SYLGIYIRLS SKWMQDLCHS 

       430        440        450        460        470        480 
YRTPSLEELS SLHCHGPIGG AYSLMKLHEN GDKCGSYIVR ECDREYNIYY IDINTKIMAK 

       490        500        510        520        530        540 
KTDQERCKTE TFRIVRKDSQ WKLSYNNGEH VLNSLHEVAH IIQADSPDRY RIPASKYDKP 

       550        560        570        580        590        600 
PLLLLLLPKN LKAKKTDLQL SEAELQRRNP QIFNPRTDLQ WYPDSISLSD DGMMFTMRGD 

       610        620        630        640        650        660 
WIQQSPVKDV SVTMKMLKSD GNFMEFFRLA QTWSLIQSPQ FLKLYGLTLA DPYTMVMEYS 

       670        680        690        700        710        720 
RYGPLNKFLH SMPNVTLHCL LDLMHGLVRG MHYLEDNKII HNYIRCSNLY VTKYDPNSYV 

       730        740        750        760        770        780 
LDAKISDPGY PRPYRESDSP WIPVKYYRNL QAAKTDQFAQ LWAFATTIYE IFSRCKEDLS 

       790        800        810        820        830        840 
TLRQEQLLRQ KNLDGNILKM LDQDICPAPI FETIMDGWSD DETKRFSHHD IFSRLNTIKA 

       850        860        870        880        890        900 
EILPNYMPPP EIATNGTGDE TVIDRSDIPF LPFPRSNMLM VIPLTSECRV IYNMENMIGR 

       910        920        930        940        950        960 
GHYGTVYKGH LEFNDKDQPR EQVAIKMLNT MQVSTDFHRE IGIMRTLSHP NIVKFKYWAE 

       970        980        990       1000       1010       1020 
KSHCIIMEYL QSGSFDIYLR FTAPNLNNPR LVSFALDIAN GMKYLSDMGL IHRDLAARNI 

      1030       1040       1050       1060       1070       1080 
LVDHNGDGDC VKISDFGLAQ FANSDGYYYA KSKRDIPIRW YSPEAISTCR FSSYSDVWSY 

      1090       1100       1110       1120       1130       1140 
GVTLFEMFSR GEEPNLVPIQ TSQEDFLNRL QSGERLNRPA SCPDFIYDLM QLCWHATPRS 

      1150       1160       1170 
RPSFATIVDI ITREVATKVT HPTDGHQSPP NQPTDAE 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. expand/collapse author list , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Head.
[5]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA36984.
RefSeqNP_511119.2. NM_078564.2.
UniGeneDm.2926.

3D structure databases

ProteinModelPortalQ24592.
SMRQ24592. Positions 574-839, 844-1156.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid58492. 11 interactions.

Proteomic databases

PaxDbQ24592.
PRIDEQ24592.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0073457; FBpp0073313; FBgn0004864.
GeneID32080.
KEGGdme:Dmel_CG1594.

Organism-specific databases

CTD15392.
FlyBaseFBgn0004864. hop.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00740000115195.
InParanoidQ24592.
KOK04447.
OMAEIRYPEH.
OrthoDBEOG7DZ8J7.
PhylomeDBQ24592.

Enzyme and pathway databases

BRENDA2.7.10.2. 1994.
SignaLinkQ24592.

Gene expression databases

BgeeQ24592.

Family and domain databases

InterProIPR019749. 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]
PfamPF07714. Pkinase_Tyr. 2 hits.
[Graphical view]
PRINTSPR00109. TYRKINASE.
SMARTSM00295. B41. 1 hit.
SM00252. SH2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 2 hits.
PROSITEPS50057. FERM_3. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 2 hits.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi32080.
NextBio776713.

Entry information

Entry nameJAK_DROME
AccessionPrimary (citable) accession number: Q24592
Secondary accession number(s): Q712V3, Q8SZI9, Q9VYZ7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 1, 2005
Last modified: July 9, 2014
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase