Q24592 (JAK_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine-protein kinase hopscotch
EC=2.7.10.2

Gene names

Name:	hop
Synonyms:	HD-160
ORF Names:	CG1594

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	1177 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Transcription Transcription regulation
Cellular component	Membrane
Domain	Repeat SH2 domain
Ligand	ATP-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	JAK-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_component	cytoplasm 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_function	ATP 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1177	1177	Tyrosine-protein kinase hopscotch		PRO_0000088118
Regions
	Domain	46 – 414	369	FERM
	Domain	433 – 539	107	SH2; atypical
	Domain	582 – 843	262	Protein kinase 1
	Domain	892 – 1164	273	Protein kinase 2
	Nucleotide binding	898 – 906	9	ATP By similarity
	Compositional bias	542 – 547	6	Poly-Leu
Sites
	Active site	1014	1	Proton acceptor By similarity
	Binding site	926	1	ATP By similarity
Amino acid modifications
	Modified residue	40	1	Phosphoserine Ref.7
	Modified residue	321	1	Phosphoserine Ref.7
	Modified residue	1047	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	1048	1	Phosphotyrosine; by autocatalysis By similarity
Experimental info
	Sequence conflict	365	1	F → V in AAA62441. Ref.1
	Sequence conflict	592	1	G → A in AAA62441. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q24592 [UniParc]. Last modified March 1, 2005. Version 2. Checksum: BF8587C420BF3A8F	FASTA	1,177	135,062
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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.
PIR	A36984.
RefSeq	NP_511119.2. NM_078564.2.
UniGene	Dm.2926.
3D structure databases
ProteinModelPortal	Q24592.
SMR	Q24592. Positions 592-825, 844-1156.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	58492. 11 interactions.
Proteomic databases
PaxDb	Q24592.
PRIDE	Q24592.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0073457; FBpp0073313; FBgn0004864.
GeneID	32080.
KEGG	dme:Dmel_CG1594.
Organism-specific databases
CTD	15392.
FlyBase	FBgn0004864. hop.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00740000115195.
InParanoid	Q24592.
KO	K04447.
OMA	EIRYPEH.
OrthoDB	EOG7DZ8J7.
PhylomeDB	Q24592.
Enzyme and pathway databases
BRENDA	2.7.10.2. 1994.
SignaLink	Q24592.
Gene expression databases
Bgee	Q24592.
Family and domain databases
InterPro	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]
Pfam	PF07714. Pkinase_Tyr. 2 hits. [Graphical view]
PRINTS	PR00109. TYRKINASE.
SMART	SM00295. B41. 1 hit. SM00252. SH2. 1 hit. SM00219. TyrKc. 1 hit. [Graphical view]
SUPFAM	SSF55550. SSF55550. 1 hit. SSF56112. SSF56112. 2 hits.
PROSITE	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]
ProtoNet	Search...
Other
GenomeRNAi	32080.
NextBio	776713.

Entry information

Entry name

JAK_DROME

Accession

Primary (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:	April 16, 2014
This is version 139 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project