SCM_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SCM_DROME
• UniProt AC: Q9VHA0
• Protein Name: Polycomb protein Scm
• Gene Name: Scm {ECO:0000312|EMBL:AAF54419.2}
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 877
• 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. They probably act via the methylation of histones, rendering chromatin heritably changed in its expressibility..
• Protein Sequence: MSGGRDSSTSSGSNSAAPGASTNATSSASASASSTSTSASPGSTTSPASTQRQRGRPAKRATCTWCGEGKLPLQYVLPTQTGKKEFCSETCIAEFRKAYSKGACTQCDNVIRDGAPNKEFCSIMCMNKHQKKNCSTRHSGGSASGKGLAESERKLLASGAPAPTGPFQYESFHVFDWDAYLEETGSEAAPAKCFKQAQNPPNNDFKIGMKLEALDPRNVTSTCIATVVGVLGSRLRLRLDGSDSQNDFWRLVDSTEIHAIGHCEKNGGMLQPPLGFRMNASSWPGYLCKILNNAMVAPEEIFQPEPPEPEENLFKVGQKLEAVDKKNPQLICCATVDAIKDDQIHVTFDGWRGAFDYWCNYRSRDIFPAGWCARSCHPMQPPGHKSRMDSSSSKQRCPRPRYTVVAESEAMVPASPATAHFHPNCKGGPFINNSKLPCMVTGPTYQTLAKLCLQEVLAASTDTQQLSKLLFALEGDVHIVTAAGKNFTVKIPSPMRMKDDESLAQFIETLCTTCRACANLISLVHETEECKKCANSRKRQLTQSATPPSSPVLADKRNRQSNSATTSPSEKIIKQELAVKSPVESKSKTSTNNGKEPASQQNSNHSLNNNNNSASKSSNKVVIKSEPNGANAQTSSTTQALRKVRFQHHANTNTNSSATNGNQDTSQTTHVSTSHCSSSSTSSSTSLAGGSANTSTIGKYLAPLVAEVHPEQANVKPSNSYYKSPTTLSSSASLPTSVSTPFTGCQSASSTALAAGGVTAAKAATAPAGAAATAGASPSYTAITSPVSTPTSALANSHLRSQPIDWTIEEVIQYIESNDNSLAVHGDLFRKHEIDGKALLLLNSEMMMKYMGLKLGPALKICNLVNKVNGRRNNLAL

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
210	Sumoylation	NDFKIGMKLEALDPR CCCCCEEEEEECCCC	37.65	-
542	Phosphorylation	NSRKRQLTQSATPPS HHHHHHHHHCCCCCC	16.49	19429919
544	Phosphorylation	RKRQLTQSATPPSSP HHHHHHHCCCCCCCC	28.95	19429919
546	Phosphorylation	RQLTQSATPPSSPVL HHHHHCCCCCCCCCC	40.76	19429919
549	Phosphorylation	TQSATPPSSPVLADK HHCCCCCCCCCCCCC	48.77	19429919
550	Phosphorylation	QSATPPSSPVLADKR HCCCCCCCCCCCCCC	25.46	19429919
574	Sumoylation	SPSEKIIKQELAVKS CCCHHHHHHHHHCCC	40.99	-
581	Phosphorylation	KQELAVKSPVESKSK HHHHHCCCCCCCCCC	27.81	22817900
585	Phosphorylation	AVKSPVESKSKTSTN HCCCCCCCCCCCCCC	42.32	15280237
624	Sumoylation	SSNKVVIKSEPNGAN CCCCEEEECCCCCCC	36.84	-
779	Phosphorylation	ATAGASPSYTAITSP HHCCCCCCCEEECCC	32.40	21082442
784	Phosphorylation	SPSYTAITSPVSTPT CCCCEEECCCCCCCC	25.23	21082442
785	Phosphorylation	PSYTAITSPVSTPTS CCCEEECCCCCCCCH	19.72	21082442

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SCM_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 SCM_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DOT1L_DROME	gpp	genetic	15371351
PHP_DROME	ph-p	physical	26063573
PHP_DROME	ph-p	physical	19494831
PHP_DROME	ph-p	physical	9343432
PHP_DROME	ph-p	physical	15905166
PHP_DROME	ph-p	physical	10412979
PHP_DROME	ph-p	physical	15280237
RCOR_DROME	CoRest	physical	26063573
ESC_DROME	esc	physical	26063573
SMBT_DROME	Sfmbt	physical	26063573
SMBT_DROME	Sfmbt	physical	19494831
SMBT_DROME	Sfmbt	physical	27151979
PSC_DROME	Psc	physical	26063573
SUZ2_DROME	Su(z)2	physical	26063573
PCL_DROME	Pcl	physical	26063573
EZ_DROME	E(z)	physical	26063573
LSDA_DROME	Su(var)3-3	physical	26063573
PC_DROME	Pc	physical	26063573
SCM_DROME	Scm	physical	15280237
SCM_DROME	Scm	physical	9343432
RING1_DROME	Sce	physical	26063573
PHO_DROME	pho	physical	26063573
SUZ12_DROME	Su(z)12	physical	26063573

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 THR-546; SER-549; SER-550AND SER-585, AND MASS SPECTROMETRY.
PubMed: 18327897