Reviewed, UniProtKB/Swiss-Prot Q7KRY6 (NHK1_DROME)

Names and origin

Protein names

Recommended name:
    Nucleosomal histone kinase 1
    EC=2.7.11.1
Alternative name(s):
    Protein baellchen

Gene names

Name:	ball
Synonyms:	ballchen, nhk-1
ORF Names:	CG6386

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

General annotation (Comments)

Function	Serine/threonine kinase involved in somatic mitosis and female meiosis. Required for spindle organization in mitosis, and for the establishment or maintenance of meiosis-specific chromosomal configurations, including the prophase I karyosome and the metaphase I spindle. Specifically phosphorylates nucleosomal H2A on 'Thr-119'. Ref.4 Ref.5 Ref.6
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subcellular location	Cytoplasm. Nucleus. Note: Chromatin-associated during mitosis. Ref.4
Tissue specificity	Present in ovary (at protein level). Ref.5 Ref.6
Developmental stage	Present throughout development, with highest level in early embryo (at protein level). Ref.4
Post-translational modification	Phosphorylated during mitosis and female meiosis. Ref.6 Ref.7
Sequence similarities	Belongs to the protein kinase superfamily. CK1 Ser/Thr protein kinase family. VRK subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Meiosis Mitosis
Cellular component	Chromosomal protein Cytoplasm Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chromatin regulator Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cell division Inferred from electronic annotation. Source: UniProtKB-KW female meiosis Ref.5 Ref.6 Inferred from mutant phenotype. Source: UniProtKB histone phosphorylation Ref.4 Inferred from direct assay. Source: FlyBase karyosome formation Inferred from mutant phenotype. Source: FlyBase mitotic sister chromatid segregation Ref.6 Inferred from mutant phenotype. Source: UniProtKB mitotic spindle organization Ref.6 Inferred from mutant phenotype. Source: UniProtKB peptidyl-threonine phosphorylation Ref.4 Inferred from direct assay. Source: FlyBase synaptonemal complex assembly Ref.5 Inferred from mutant phenotype. Source: UniProtKB
Cellular component	chromatin Ref.4 Inferred from direct assay. Source: UniProtKB cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Ref.4 Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW histone threonine kinase activity Ref.4 Inferred from direct assay. Source: FlyBase protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	Q9W1K1	1	EBI-170817,EBI-93866
baf	Q9VLU0	1	EBI-170817,EBI-105147
norpA	P13217	1	EBI-170817,EBI-101510

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 599	599	Nucleosomal histone kinase 1		PRO_0000086441
Regions
	Domain	47 – 328	282	Protein kinase
	Nucleotide binding	53 – 61	9	ATP By similarity
	Compositional bias	394 – 398	5	Poly-Glu
Sites
	Active site	183	1	Proton acceptor By similarity
	Binding site	77	1	ATP By similarity
Amino acid modifications
	Modified residue	376	1	Phosphoserine Ref.7
	Modified residue	381	1	Phosphoserine Ref.7
	Modified residue	382	1	Phosphoserine Ref.7
	Modified residue	388	1	Phosphoserine Ref.7
	Modified residue	390	1	Phosphoserine Ref.7
	Modified residue	483	1	Phosphoserine Ref.7
	Modified residue	564	1	Phosphoserine Ref.7
	Modified residue	586	1	Phosphoserine Ref.7
	Modified residue	589	1	Phosphothreonine Ref.7
Experimental info
	Mutagenesis	117	1	P → L in Z3-0437; induces female and male sterility and abolishes T-119 phosphorylation of H2A in the oocyte. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q7KRY6-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: B32EE3004477EBDB	FASTA	599	65,994
	10 20 30 40 50 60 MPRVAKPKAA APAKKVVSAK KAKSKLYKMP EKVKEGTVFT DLAKGQWRIG PSIGVGGFGE 70 80 90 100 110 120 IYAACKVGEK NYDAVVKCEP HGNGPLFVEM HFYLRNAKLE DIKQFMQKHG LKSLGMPYIL 130 140 150 160 170 180 ANGSVEVNGE KHRFIVMPRY GSDLTKFLEQ NGKRLPEGTV YRLAIQMLDV YQYMHSNGYV 190 200 210 220 230 240 HADLKAANIL LGLEKGGAAQ AYLVDFGLAS HFVTGDFKPD PKKMHNGTIE YTSRDAHLGV 250 260 270 280 290 300 PTRRADLEIL GYNLIEWLGA ELPWVTQKLL AVPPKVQKAK EAFMDNIGES LKTLFPKGVP 310 320 330 340 350 360 PPIGDFMKYV SKLTHNQEPD YDKCRSWFSS ALKQLKIPNN GDLDFKMKPQ TSSNNNLSPP 370 380 390 400 410 420 GTSKAATARK AKKIDSPVLN SSLDEKISAS EDDEEEEEKS HRKKTAKKVT PSARNAKVSP 430 440 450 460 470 480 LKRVADSSPP SQKRVKTEPK STPRERATPK ASPKPRSTPK ASPKPQTPTA ARLRTPNAKI 490 500 510 520 530 540 NFSPSISLRG RPGGKTVIND DLTPQPRSKK TYEFNFELDV SMDANVIVNV KRKKKADQDK 550 560 570 580 590 ATAVDSRTPS SRSALASSSK EEASPVTRVN LRKVNGHGDS STPGRSPRTP AVTVRKYQG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	"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.
[3]	"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]. Strain: Berkeley. Tissue: Embryo.
[4]	"Nucleosomal histone kinase-1 phosphorylates H2A Thr 119 during mitosis in the early Drosophila embryo." Aihara H., Nakagawa T., Yasui K., Ohta T., Hirose S., Dhomae N., Takio K., Kaneko M., Takeshima Y., Muramatsu M., Ito T. Genes Dev. 18:877-888(2004) [PubMed: 15078818] [Abstract] Cited for: PROTEIN SEQUENCE OF 35-44 AND 186-195, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, FUNCTION. Strain: Berkeley. Tissue: Embryo.
[5]	"A histone code in meiosis: the histone kinase, NHK-1, is required for proper chromosomal architecture in Drosophila oocytes." Ivanovska I., Khandan T., Ito T., Orr-Weaver T.L. Genes Dev. 19:2571-2582(2005) [PubMed: 16230526] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF PRO-117, TISSUE SPECIFICITY.
[6]	"The conserved kinase NHK-1 is essential for mitotic progression and unifying acentrosomal meiotic spindles in Drosophila melanogaster." Cullen C.F., Brittle A.L., Ito T., Ohkura H. J. Cell Biol. 171:593-602(2005) [PubMed: 16301329] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION.
[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: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-376; SER-381; SER-382; SER-388; SER-390; SER-483; SER-564; SER-586 AND THR-589, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE014297 Genomic DNA. Translation: AAF56630.2. AF160917 mRNA. Translation: AAD46857.2. Different initiation.
RefSeq	NP_651508.1. NP_733171.1.
UniGene	Dm.1346
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q7KRY6. 6 interactions.
STRING	Q7KRY6.
Proteomic databases
PRIDE	Q7KRY6.
Genome annotation databases
Ensembl	FBtr0085095; FBpp0084465; FBgn0027889; Drosophila melanogaster. [Genome view] FBtr0085096; FBpp0084466; FBgn0027889; Drosophila melanogaster. [Genome view]
GeneID	43228.
KEGG	dme:Dmel_CG6386.
Organism-specific databases
CTD	43228.
FlyBase	FBgn0027889. ball.
Phylogenomic databases
HOGENOM	Q7KRY6.
OMA	MIIKETS
OrthoDB	EOG94MXZK
Enzyme and pathway databases
BRENDA	2.7.11.1. 48.
Gene expression databases
GermOnline	CG6386. Drosophila melanogaster.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_prot_kinase-like_dom. IPR008271. Ser/Thr_prot_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	832818.

Entry information

Entry name

NHK1_DROME

Accession

Primary (citable) accession number: Q7KRY6
Secondary accession number(s): Q9U9Q0, Q9VBB2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	July 5, 2004
Last modified:	November 24, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project