PSC_DROME - dbPTM
PSC_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PSC_DROME
UniProt AC P35820
Protein Name Polycomb group protein Psc
Gene Name Psc
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1601
Subcellular Localization Nucleus .
Protein Description Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. Component of the PcG multiprotein PRC1 complex, a complex that acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-118', rendering chromatin heritably changed in its expressibility. Needed to maintain expression patterns of the homeotic selector genes of the Antennapedia (Antp-C) and Bithorax (BX-C) complexes, and hence for the maintenance of segmental determination..
Protein Sequence MMTPESKAIQPAAATTKQTAEATATTTMAHTQQKSQLSTLAKTTTTTATNKAAKSVVSNANSSGNNSSKKLALSQSQKTTTTTTPPTTTTTTTAAAAAEATTNADKMQKQQQLKQQLFAACSIKVKSENTLATTANAALAAATTTTTTATPALATGKAAKTILENGIKKESTPPAVESVEASSSSSSSSSSSSSSSSSWPTTRRATSEDASSNGGASADEEKSEEDPTAAVAASSTATTTSDLATTSRPRPVLLTAVNPHIICHLCQGYLINATTIVECLHSFCHSCLINHLRKERFCPRCEMVINNAKPNIKSDTTLQAIVYKLVPGLYERELMRKRAFYKDRPEEAALATPEQRGDDTEHLIFSPSDDMSLSLEYAELGELKTDSEPELVDTLRPRYLQCPAMCRVSHLKKFVYDKFEIDAQRFSIDIMYKVKTIVLLDYYTLMDIAYIYTWKRDAPMRFYYRVYESPQPLVKPAPRRVLPLKLEKQERENQEQQLAVEVASSKVEPVSLPEDQKAEASIKVEEQESTREIVKEVIKDVAATPPTETLKLVINRNMLDKREKSHSPQMSSKSSSKSSPCTPVSSPSEPNIKLKIDLSKQNSVTIIDMSDPERREIVKPLKPEKESRSKKKDKDGSPKSSSSSSSSSSGERKRKSPSPLTVPPLTIRTERIMSPSGVSTLSPRVTSGAFSEDPKSEFLKSFALKPIKVKVESPERTLNNRAITPPSPSVQQSASPKSKGNNLDDSILMKPPSCMPPKSIASSKRKSKEPVKAVSKKQKLSPPLPTVDFKIRLPVTNGNSSGTASPKIEKPLMPPPAKPPMLAPRKLQPSAQFAPPPSPIHHHAGVQMSAPGNRTPIAKRYQPILPKASRPNPFANIPNDVNRLLKDAGTEIKSIGGGSVENNSNAAQKPHLYGPKGESKMGPPALPATTPSQGNKNVGKQAGNLPMSAPPNKGNSSNNYLNLALFNSSKCKGKEAPPGCRTPMYTPNSPIYSPSSPQYVPSYNIPTMPTYKYTPKPTPNSGSGNGGSGSYLQNMLGGGNGGSLGGLFPSPPTKSDQNTNPAQGGGGSSSATQSGGNNGIVNNNIYMPNEDAPEKQQVKVKSLLNSCNINIPSSLSITISRDNGDSSSPNNGQHPKHKSPVNNYIEIVKLPDQPQDQVQAAKEAQKRQSPPAAVPGHLAAKLPPPPPSKAIPSPQHLVSRMTPPQLPKVATPPPPSSPRVITPPKTSPPANAAKVTPLKPVLTPTQVDKKTPSPEKRTAAQMGSHSPTASENKSPKGGPAGVANSTGGAQNGDPAAKKFRPILPRQNGMPELAPKLPTLAPFVGFNPLQNPAAGKKVPPSKKSPNAGAAAHQSGQQKLVNGGQSQPAQQKTSPPAQKNQQQVKKVSKNPTPPPPSLPAVGKMMPHPVMHSQNAPLSIASSASAAAVASGQLDLSNFLKENLRRVHAAQAAQAAQVAAAANQSNMMYNLAQMGHMTPAMYNYQQAYFREQLSRMQRVGNEVFNDYLQKLKTAAATGGGGPVEGELKPMLPTVTLPSPGATPPAASPKTSPLPAGKLTAAATAPQTKGNSSSGAANARQQTAATGNNGATVPAASLPPATKSK
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
656PhosphorylationSGERKRKSPSPLTVP
CCCCCCCCCCCCCCC		34.3419429919
658PhosphorylationERKRKSPSPLTVPPL
CCCCCCCCCCCCCCC		39.3619429919
661PhosphorylationRKSPSPLTVPPLTIR
CCCCCCCCCCCCEEE		34.0619429919
666PhosphorylationPLTVPPLTIRTERIM
CCCCCCCEEEEEEEE		17.7419429919
674PhosphorylationIRTERIMSPSGVSTL
EEEEEEECCCCCCCC		17.3419429919
682PhosphorylationPSGVSTLSPRVTSGA
CCCCCCCCCCCCCCC		15.6819429919
713PhosphorylationPIKVKVESPERTLNN
CEEEEECCCCCCCCC		34.7425749252
1139PhosphorylationGQHPKHKSPVNNYIE
CCCCCCCCCCCCEEE		33.5219429919
1169PhosphorylationKEAQKRQSPPAAVPG
HHHHHHCCCCCCCCC		36.5619429919
1211PhosphorylationPQLPKVATPPPPSSP
CCCCCCCCCCCCCCC		39.0422668510
1222PhosphorylationPSSPRVITPPKTSPP
CCCCCCCCCCCCCCC		30.5922817900
1227PhosphorylationVITPPKTSPPANAAK
CCCCCCCCCCCCCCC		34.7022817900
1236PhosphorylationPANAAKVTPLKPVLT
CCCCCCCCCCCCCCC		23.3822817900
1243PhosphorylationTPLKPVLTPTQVDKK
CCCCCCCCCCCCCCC		25.2319429919
1251PhosphorylationPTQVDKKTPSPEKRT
CCCCCCCCCCHHHCH		34.4419429919
1253PhosphorylationQVDKKTPSPEKRTAA
CCCCCCCCHHHCHHH		51.4219429919
1266PhosphorylationAAQMGSHSPTASENK
HHHHCCCCCCCCCCC		26.1619429919
1268PhosphorylationQMGSHSPTASENKSP
HHCCCCCCCCCCCCC		45.9219429919
1274PhosphorylationPTASENKSPKGGPAG
CCCCCCCCCCCCCCC		43.3522817900
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 PSC_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PSC_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 PSC_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ESC_DROMEescgenetic
7854314
SUZ2_DROMESu(z)2genetic
27510973
BRM_DROMEbrmgenetic
7854314
RING1_DROMEScegenetic
8313990
PHP_DROMEph-pphysical
11172718
PHP_DROMEph-pphysical
11493924
PHP_DROMEph-pphysical
15280237
PHP_DROMEph-pphysical
18923078
PHP_DROMEph-pphysical
25415640
PHP_DROMEph-pphysical
9372908
PHP_DROMEph-pphysical
10412979
PHP_DROMEph-pphysical
9566890
TPR_DROMEMtorphysical
18923078
PSC_DROMEPscphysical
22749399
PSC_DROMEPscphysical
9566890
PC_DROMEPcphysical
11493924
PC_DROMEPcphysical
11581156
PC_DROMEPcphysical
15280237
PC_DROMEPcphysical
18923078
PC_DROMEPcphysical
25415640
PC_DROMEPcphysical
9372908
PC_DROMEPcphysical
9566890
JHD1_DROMEKdm2physical
18923078
JHD1_DROMEKdm2physical
25415640
SCM_DROMEScmphysical
15280237
SCM_DROMEScmphysical
10412979
RING1_DROMEScephysical
15280237
RING1_DROMEScephysical
18923078
RING1_DROMEScephysical
25415640
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PSC_DROME

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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-656; SER-658; SER-1139;THR-1222; THR-1236; THR-1251; SER-1253; SER-1266 AND SER-1274, ANDMASS SPECTROMETRY.

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