Reviewed, UniProtKB/Swiss-Prot Q9V3I5 (JIL1_DROME)

Names and origin

Protein names

Recommended name:
    Chromosomal serine/threonine-protein kinase JIL-1
    EC=2.7.11.1

Gene names

Name:	JIL-1
ORF Names:	CG6297

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	1207 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Phosphorylates 'Ser-10' of histone H3. May regulate gene expression by establishing or maintaining the structure of more open chromatin regions. Also required for normal polytene chromosome structure, for oogenesis and for viability throughout development. Regulates the structure of polytene chromosomes in salivary glands. May phosphorylate 'Ser-1' of histone H2A. Ref.1 Ref.7 Ref.8 Ref.10 Ref.11
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. Ref.1
Cofactor	Magnesium. Ref.1
Subunit structure	Interacts with lola. Interacts with proteins of the male specific lethal (MSL) dosage compensation complex; this interaction is mediated by the kinase domains. Ref.9 Ref.6
Subcellular location	Nucleus. Note: Associates with chromosomes throughout the cell cycle. Localizes to interband regions along the polytene chromosomes and is enriched almost two-fold on the male X chromosome compared to the autosome. Ref.1
Post-translational modification	Autophosphorylated in vitro. Ref.1 Ref.12
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Contains 1 AGC-kinase C-terminal domain. Contains 2 protein kinase domains.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Chromosomal protein Nucleus
Domain	Repeat
Ligand	ATP-binding Magnesium Nucleotide-binding
Molecular function	Chromatin regulator Developmental protein Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	female meiosis chromosome segregation Inferred from mutant phenotype. Source: FlyBase histone phosphorylation Ref.1 Ref.7 Inferred from direct assay. Source: UniProtKB multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of chromatin silencing Inferred from mutant phenotype. Source: FlyBase oogenesis Ref.8 Inferred from mutant phenotype. Source: FlyBase peptidyl-serine phosphorylation Ref.7 Inferred from mutant phenotype. Source: UniProtKB protein amino acid autophosphorylation Ref.1 Inferred from direct assay. Source: UniProtKB transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	X chromosome located dosage compensation complex, transcription activating Ref.6 Inferred from physical interaction. Source: UniProtKB nuclear chromosome Ref.1 Inferred from direct assay. Source: UniProtKB polytene chromosome interband Ref.1 Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW histone kinase activity (H3-S10 specific) Ref.7 Inferred from mutant phenotype. Source: UniProtKB magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Ref.9 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1207	1207	Chromosomal serine/threonine-protein kinase JIL-1		PRO_0000086039
Regions
	Domain	261 – 530	270	Protein kinase 1
	Domain	531 – 599	69	AGC-kinase C-terminal
	Domain	623 – 886	264	Protein kinase 2
	Nucleotide binding	267 – 275	9	ATP By similarity
	Nucleotide binding	629 – 637	9	ATP By similarity
	Compositional bias	43 – 108	66	Asn-rich
	Compositional bias	191 – 209	19	Ala-rich
Sites
	Active site	389	1	Proton acceptor By similarity
	Active site	739	1	Proton acceptor By similarity
	Binding site	293	1	ATP By similarity
	Binding site	652	1	ATP By similarity
Amino acid modifications
	Modified residue	29	1	Phosphoserine Ref.12
	Modified residue	31	1	Phosphoserine Ref.12
	Modified residue	424	1	Phosphoserine Ref.12
	Modified residue	588	1	Phosphothreonine Ref.12
	Modified residue	1045	1	Phosphothreonine Ref.12
	Modified residue	1047	1	Phosphoserine Ref.12

Sequences

	Sequence		Length	Mass (Da)
	Q9V3I5-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: BD99FB932D708743	FASTA	1,207	137,045
	10 20 30 40 50 60 MSRLQKQNYE ILSGTSTSRL KNHQHPRESE SLAYEEPDQM VRNHLNGQLV ANGNGKTRKN 70 80 90 100 110 120 SNSETMTNGK KSKLNTEGSG SGSGKTLNYN NNNNNNNSIS ATNGQYTNSS SKTTSASARD 130 140 150 160 170 180 YTYRETISPP TPPSPPTTNV ADIVCISDAE SEDGRDPERE YYDQDMEEDE PNGIEIDESS 190 200 210 220 230 240 SSLSKAKSNN AAAAAAAAAA AAAAAASKAS SSTTPSYAMP TSNSTPLDLD NEAHQRDLEA 250 260 270 280 290 300 VTDLKYYVKL YSDEAVSLND FKIIRVLGTG AYGRVFLVRK LTRHDAGKLY AMKVLNKITV 310 320 330 340 350 360 VQKRKTAEHT KTERVVLEAI QRNPFLVSLH YAFQSSSKLY LVLDFANGGE LFTHLYHSEN 370 380 390 400 410 420 FEESRVRVYI AEVVLALEQL HQLGIIYRDI KLENILLDGE GHIVLSDFGL SKILTAENEY 430 440 450 460 470 480 RAHSFCGTLE YMAPEIIRTG PPGHDSAVDW WSVGVLTFEL LTGASPFATS DGQVQQSEIS 490 500 510 520 530 540 RRIQKEQPMI PSSFSANARD FVLKMLEKNP KRRLGGNHRD ASEIKEHPFF NGINWQELRT 550 560 570 580 590 600 KRRKAPYKPT LTAEDDVQNF SNEFTDQVPE DPECDAPPSR IRLFRGYTYV APEHLEQMRR 610 620 630 640 650 660 DNHCEIQYFN TGLQNIPCRP DDLELGTRTS NGAYGTCHFV VDSSTDLVFL AKIIPLSKFR 670 680 690 700 710 720 PSEVDALISC ALDTTNHKNI VSYHGTFREK CETWIVMEYL SGPELTASIR MDEDSCREIF 730 740 750 760 770 780 LQLVMAVRHI HSKHFIHGDL KPENIMFENR EDRTVKLIDF GSACYNNRFK SWKDKPRYTL 790 800 810 820 830 840 DYAPPEMLAD ANLVTYSPAV DIYGLGATLY TMLVGHRPYR QNEDDVDHSA AAHHELRKRM 850 860 870 880 890 900 RRGTFNQRSM RWESASPAFR HLVSWCLQRD PADRPTLSDI LDSEWLQYGS NDPDVDIILP 910 920 930 940 950 960 QQMVVDLSED TMEQPTGGMF DDQQQLEFMH DKSAEDEGIT LVSEPMDTTV ATHESRRNAA 970 980 990 1000 1010 1020 AFSSVVAPTT DDEIVHERFD PAFEVQADFY GFDENAPPLP LPEEYYSELP LPEEDRQYIP 1030 1040 1050 1060 1070 1080 PPPALIPVEP ETTFRRPRTR QQRRTESQLV QPVSVATYED SKASLRVLMQ QLPPPGDNVV 1090 1100 1110 1120 1130 1140 ARIPKRTHRV VRTLPPTFGT TKREENFYGF SKTAISWRKT RASWRHFCLL INGVQQVLKV 1150 1160 1170 1180 1190 1200 RFKKARRVYC LPHIKEEKLD HAYEKPLTFP RPKAQLKRTK REPKVPRPPT RVQPERARAM RQLYQFQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"JIL-1: a novel chromosomal tandem kinase implicated in transcriptional regulation in Drosophila." Jin Y., Wang Y., Walker D.L., Dong H., Conley C., Johansen J., Johansen K.M. Mol. Cell 4:129-135(1999) [PubMed: 10445035] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION.
[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: 10731132] [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: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[4]	Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E. Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Testis.
[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: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 962-1207. Strain: Berkeley. Tissue: Embryo.
[6]	"JIL-1, a chromosomal kinase implicated in regulation of chromatin structure, associates with the male specific lethal (MSL) dosage compensation complex." Jin Y., Wang Y., Johansen J., Johansen K.M. J. Cell Biol. 149:1005-1010(2000) [PubMed: 10831604] [Abstract] Cited for: ASSOCIATION WITH THE MSL DOSAGE COMPENSATION COMPLEX.
[7]	"The JIL-1 tandem kinase mediates histone H3 phosphorylation and is required for maintenance of chromatin structure in Drosophila." Wang Y., Zhang W., Jin Y., Johansen J., Johansen K.M. Cell 105:433-443(2001) [PubMed: 11371341] [Abstract] Cited for: FUNCTION.
[8]	"Genetic and phenotypic analysis of alleles of the Drosophila chromosomal JIL-1 kinase reveals a functional requirement at multiple developmental stages." Zhang W., Jin Y., Ji Y., Girton J., Johansen J., Johansen K.M. Genetics 165:1341-1354(2003) [PubMed: 14668387] [Abstract] Cited for: FUNCTION.
[9]	"A developmentally regulated splice variant from the complex lola locus encoding multiple different zinc finger domain proteins interacts with the chromosomal kinase JIL-1." Zhang W., Wang Y., Long J., Girton J., Johansen J., Johansen K.M. J. Biol. Chem. 278:11696-11704(2003) [PubMed: 12538650] [Abstract] Cited for: INTERACTION WITH LOLA.
[10]	"Su(var) genes regulate the balance between euchromatin and heterochromatin in Drosophila." Ebert A., Schotta G., Lein S., Kubicek S., Krauss V., Jenuwein T., Reuter G. Genes Dev. 18:2973-2983(2004) [PubMed: 15574598] [Abstract] Cited for: FUNCTION.
[11]	"The JIL-1 kinase regulates the structure of Drosophila polytene chromosomes." Deng H., Zhang W., Bao X., Martin J.N., Girton J., Johansen J., Johansen K.M. Chromosoma 114:173-182(2005) [PubMed: 15986206] [Abstract] Cited for: FUNCTION.
[12]	"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: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-31; SER-424; THR-588; THR-1045 AND SER-1047, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF142061 mRNA. Translation: AAD48407.1. AE014296 Genomic DNA. Translation: AAF50105.1. AE014296 Genomic DNA. Translation: AAN11898.1. BT044484 mRNA. Translation: ACH95258.1. AY061043 mRNA. Translation: AAL28591.1. Different initiation.
RefSeq	NP_648432.1. NP_729661.1.
UniGene	Dm.3098
3D structure databases
HSSP	HSSP built from PDB template 1MRY based on UniProtKB P31751.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9V3I5. 3 interactions.
Proteomic databases
PRIDE	Q9V3I5.
Genome annotation databases
Ensembl	FBgn0020412. Drosophila melanogaster. [Contig view]
GeneID	39241.
KEGG	dme:Dmel_CG6297.
Organism-specific databases
FlyBase	FBgn0020412. JIL-1.
Phylogenomic databases
HOGENOM	Q9V3I5.
Enzyme and pathway databases
BRENDA	2.7.11.1. 48.
Gene expression databases
ArrayExpress	Q9V3I5.
GermOnline	CG6297. Drosophila melanogaster.
Family and domain databases
InterPro	IPR000961. AGC-kinase_C. IPR017892. Pkinase_C. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR002290. Ser_thr_pkinase. [Graphical view]
Pfam	PF00069. Pkinase. 2 hits. PF00433. Pkinase_C. 1 hit. [Graphical view]
ProDom	PD000001. Prot_kinase. 2 hits. [Graphical view] [Entries sharing at least one domain]
SMART	SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 2 hits. [Graphical view]
PROSITE	PS51285. AGC_KINASE_CTER. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 2 hits. PS00108. PROTEIN_KINASE_ST. 2 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	812663.

Entry information

Entry name

JIL1_DROME

Accession

Primary (citable) accession number: Q9V3I5
Secondary accession number(s): B5RJL0, Q0E8F9, Q95RY3

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	May 1, 2000
Last modified:	June 16, 2009
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project