JIL1_DROME - dbPTM
JIL1_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID JIL1_DROME
UniProt AC Q9V3I5
Protein Name Chromosomal serine/threonine-protein kinase JIL-1
Gene Name JIL-1 {ECO:0000312|FlyBase:FBgn0020412}
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1207
Subcellular Localization Nucleus . Chromosome . 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.
Protein Description 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..
Protein Sequence MSRLQKQNYEILSGTSTSRLKNHQHPRESESLAYEEPDQMVRNHLNGQLVANGNGKTRKNSNSETMTNGKKSKLNTEGSGSGSGKTLNYNNNNNNNNSISATNGQYTNSSSKTTSASARDYTYRETISPPTPPSPPTTNVADIVCISDAESEDGRDPEREYYDQDMEEDEPNGIEIDESSSSLSKAKSNNAAAAAAAAAAAAAAAASKASSSTTPSYAMPTSNSTPLDLDNEAHQRDLEAVTDLKYYVKLYSDEAVSLNDFKIIRVLGTGAYGRVFLVRKLTRHDAGKLYAMKVLNKITVVQKRKTAEHTKTERVVLEAIQRNPFLVSLHYAFQSSSKLYLVLDFANGGELFTHLYHSENFEESRVRVYIAEVVLALEQLHQLGIIYRDIKLENILLDGEGHIVLSDFGLSKILTAENEYRAHSFCGTLEYMAPEIIRTGPPGHDSAVDWWSVGVLTFELLTGASPFATSDGQVQQSEISRRIQKEQPMIPSSFSANARDFVLKMLEKNPKRRLGGNHRDASEIKEHPFFNGINWQELRTKRRKAPYKPTLTAEDDVQNFSNEFTDQVPEDPECDAPPSRIRLFRGYTYVAPEHLEQMRRDNHCEIQYFNTGLQNIPCRPDDLELGTRTSNGAYGTCHFVVDSSTDLVFLAKIIPLSKFRPSEVDALISCALDTTNHKNIVSYHGTFREKCETWIVMEYLSGPELTASIRMDEDSCREIFLQLVMAVRHIHSKHFIHGDLKPENIMFENREDRTVKLIDFGSACYNNRFKSWKDKPRYTLDYAPPEMLADANLVTYSPAVDIYGLGATLYTMLVGHRPYRQNEDDVDHSAAAHHELRKRMRRGTFNQRSMRWESASPAFRHLVSWCLQRDPADRPTLSDILDSEWLQYGSNDPDVDIILPQQMVVDLSEDTMEQPTGGMFDDQQQLEFMHDKSAEDEGITLVSEPMDTTVATHESRRNAAAFSSVVAPTTDDEIVHERFDPAFEVQADFYGFDENAPPLPLPEEYYSELPLPEEDRQYIPPPPALIPVEPETTFRRPRTRQQRRTESQLVQPVSVATYEDSKASLRVLMQQLPPPGDNVVARIPKRTHRVVRTLPPTFGTTKREENFYGFSKTAISWRKTRASWRHFCLLINGVQQVLKVRFKKARRVYCLPHIKEEKLDHAYEKPLTFPRPKAQLKRTKREPKVPRPPTRVQPERARAMRQLYQFQ
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 Orthologous
Protein Cluster
29PhosphorylationNHQHPRESESLAYEE
CCCCCCHHCCCCCCC		33.4922817900
31PhosphorylationQHPRESESLAYEEPD
CCCCHHCCCCCCCCC		27.8118327897
61PhosphorylationNGKTRKNSNSETMTN
CCCCCCCCCCCCCCC		44.7819429919
63PhosphorylationKTRKNSNSETMTNGK
CCCCCCCCCCCCCCC		33.9719429919
65PhosphorylationRKNSNSETMTNGKKS
CCCCCCCCCCCCCCC		29.1719429919
147PhosphorylationVADIVCISDAESEDG
CCCEEEEECCCCCCC		26.1622817900
188PhosphorylationSSLSKAKSNNAAAAA
CHHHHHHHCHHHHHH		39.9322817900
424PhosphorylationENEYRAHSFCGTLEY
CCHHHHHCCHHCHHH		22.6522817900
587PhosphorylationRIRLFRGYTYVAPEH
CEEEECCEEEECHHH		7.2219429919
588PhosphorylationIRLFRGYTYVAPEHL
EEEECCEEEECHHHH		17.8419429919
589PhosphorylationRLFRGYTYVAPEHLE
EEECCEEEECHHHHH		6.0219429919
1045PhosphorylationRTRQQRRTESQLVQP
CCHHHHCCHHHCCCC		42.0222817900
1047PhosphorylationRQQRRTESQLVQPVS
HHHHCCHHHCCCCEE		28.3525749252
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of JIL1_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of JIL1_DROME !!
Disease-associated PTM Sites based on SAP

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

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of JIL1_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MSL1_DROMEmsl-1physical
10831604
MSL2_DROMEmsl-2physical
10831604
SUV39_DROMESu(var)3-9genetic
16339185
SUV39_DROMESu(var)3-9genetic
17660558
LOLA1_DROMElolagenetic
12538650
LOLA2_DROMElolagenetic
12538650
LOLA3_DROMElolagenetic
12538650
LOLA4_DROMElolagenetic
12538650
LOLA6_DROMElolagenetic
12538650
LOLA5_DROMElolagenetic
12538650
LAM0_DROMELamphysical
16254246
MSL3_DROMEmsl-3physical
10831604
LOLA1_DROMElolaphysical
12538650
LOLA2_DROMElolaphysical
12538650
LOLA3_DROMElolaphysical
12538650
LOLA4_DROMElolaphysical
12538650
LOLA6_DROMElolaphysical
12538650
LOLA5_DROMElolaphysical
12538650
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of JIL1_DROME

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-29; SER-31; SER-424;THR-588; THR-1045 AND SER-1047, AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory