NHK1_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NHK1_DROME
• UniProt AC: Q7KRY6
• Protein Name: Nucleosomal histone kinase 1
• Gene Name: ball
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 599
• Subcellular Localization: Cytoplasm . Nucleus . Chromosome . Cytoplasm, myofibril, sarcomere, Z line . Cytoplasm, myofibril, sarcomere, M line . Chromatin-associated during mitosis (PubMed:15078818). In indirect flight muscle, colocalizes with sls isoform A (kettin) to the sa
• Protein Description: Serine/threonine-protein kinase involved in somatic mitosis and female meiosis. [PubMed: 16230526 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]
• Protein Sequence: MPRVAKPKAAAPAKKVVSAKKAKSKLYKMPEKVKEGTVFTDLAKGQWRIGPSIGVGGFGEIYAACKVGEKNYDAVVKCEPHGNGPLFVEMHFYLRNAKLEDIKQFMQKHGLKSLGMPYILANGSVEVNGEKHRFIVMPRYGSDLTKFLEQNGKRLPEGTVYRLAIQMLDVYQYMHSNGYVHADLKAANILLGLEKGGAAQAYLVDFGLASHFVTGDFKPDPKKMHNGTIEYTSRDAHLGVPTRRADLEILGYNLIEWLGAELPWVTQKLLAVPPKVQKAKEAFMDNIGESLKTLFPKGVPPPIGDFMKYVSKLTHNQEPDYDKCRSWFSSALKQLKIPNNGDLDFKMKPQTSSNNNLSPPGTSKAATARKAKKIDSPVLNSSLDEKISASEDDEEEEEKSHRKKTAKKVTPSARNAKVSPLKRVADSSPPSQKRVKTEPKSTPRERATPKASPKPRSTPKASPKPQTPTAARLRTPNAKINFSPSISLRGRPGGKTVINDDLTPQPRSKKTYEFNFELDVSMDANVIVNVKRKKKADQDKATAVDSRTPSSRSALASSSKEEASPVTRVNLRKVNGHGDSSTPGRSPRTPAVTVRKYQG

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
18	Phosphorylation	APAKKVVSAKKAKSK CCCHHHCCHHHHHHH	37.04	27626673
358	Phosphorylation	TSSNNNLSPPGTSKA CCCCCCCCCCCCCHH	31.04	19429919
376	Phosphorylation	RKAKKIDSPVLNSSL HHHHHCCCCHHCCCH	22.00	19429919
381	Phosphorylation	IDSPVLNSSLDEKIS CCCCHHCCCHHHHCC	28.28	19429919
382	Phosphorylation	DSPVLNSSLDEKISA CCCHHCCCHHHHCCC	38.47	19429919
388	Phosphorylation	SSLDEKISASEDDEE CCHHHHCCCCCCCHH	36.49	19429919
390	Phosphorylation	LDEKISASEDDEEEE HHHHCCCCCCCHHHH	34.46	19429919
427	Phosphorylation	PLKRVADSSPPSQKR CHHHHCCCCCCHHHC	34.70	29892262
428	Phosphorylation	LKRVADSSPPSQKRV HHHHCCCCCCHHHCC	41.18	19429919
431	Phosphorylation	VADSSPPSQKRVKTE HCCCCCCHHHCCCCC	52.28	19429919
452	Phosphorylation	ERATPKASPKPRSTP CCCCCCCCCCCCCCC	39.31	27626673
457	Phosphorylation	KASPKPRSTPKASPK CCCCCCCCCCCCCCC	58.55	28490779
458	Phosphorylation	ASPKPRSTPKASPKP CCCCCCCCCCCCCCC	30.04	28490779
462	Phosphorylation	PRSTPKASPKPQTPT CCCCCCCCCCCCCCC	39.31	19429919
467	Phosphorylation	KASPKPQTPTAARLR CCCCCCCCCCCHHCC	31.00	19429919
469	Phosphorylation	SPKPQTPTAARLRTP CCCCCCCCCHHCCCC	36.02	27626673
483	Phosphorylation	PNAKINFSPSISLRG CCCEEEECCCEECCC	17.16	19429919
485	Phosphorylation	AKINFSPSISLRGRP CEEEECCCEECCCCC	24.50	25749252
487	Phosphorylation	INFSPSISLRGRPGG EEECCCEECCCCCCC	19.15	30478224
496	Phosphorylation	RGRPGGKTVINDDLT CCCCCCCEEECCCCC	29.87	30478224
503	Phosphorylation	TVINDDLTPQPRSKK EEECCCCCCCCCCCC	27.20	19429919
558	Phosphorylation	SRSALASSSKEEASP HHHHHHHCCCCCCCC	39.56	28490779
559	Phosphorylation	RSALASSSKEEASPV HHHHHHCCCCCCCCC	41.41	28490779
564	Phosphorylation	SSSKEEASPVTRVNL HCCCCCCCCCCEEEE	24.15	28490779
567	Phosphorylation	KEEASPVTRVNLRKV CCCCCCCCEEEEEEE	32.08	28490779
580	Phosphorylation	KVNGHGDSSTPGRSP EECCCCCCCCCCCCC	40.48	30478224
586	Phosphorylation	DSSTPGRSPRTPAVT CCCCCCCCCCCCCEE	25.34	22817900
589	Phosphorylation	TPGRSPRTPAVTVRK CCCCCCCCCCEEEEE	20.98	16230526

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of NHK1_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NHK1_DROME !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of NHK1_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BAF_DROME	baf	physical	14605208
BAF_DROME	baf	physical	18039935
BAF_DROME	baf	genetic	25501812

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"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).
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, AND MASSSPECTROMETRY.
PubMed: 18327897