dbPTM

SPT5H_DROME - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SPT5H_DROME
UniProt AC	Q9V460
Protein Name	Transcription elongation factor SPT5
Gene Name	Spt5
Organism	Drosophila melanogaster (Fruit fly).
Sequence Length	1078
Subcellular Localization	Nucleus. Chromosome. Localizes predominantly to transcriptionally active regions of polytene chromosomes.
Protein Description	Component of the DRB sensitivity-inducing factor complex (DSIF complex), which regulates transcription elongation by RNA polymerase II. DSIF enhances transcriptional pausing at sites proximal to the promoter, which may facilitate the assembly of an elongation competent RNA polymerase II complex. DSIF may also promote transcriptional elongation within coding regions. DSIF is required for the transcriptional induction of heat shock response genes and regulation of genes which control anterior-posterior patterning during embryonic development..
Protein Sequence	MSDSEVSNMSDSGSEDGSISNKSQRSARSKSRSRSRSGSRGSRSVSRSRSRSQSGHSRSGSESPQRRDNRGKSDESGEEEEEPPGEDIDSEEYDEEENDDHPRKKKKKERFGGFIIDEAEVDDEVDEDDEWEEGANEIGIVGNEIDELGPTARDIEIRRRGTNLWDTQKEDEIEEYLRKKYADESIAKRHFGDGGEEMSDEITQQTLLPGIKDPNLWMVKCRIGEEKATALLLMRKYLTYLNTDDPLQIKSIIAPEGVKGYIYLEAYKQTHVKTCIDNVGNLRMGKWKQEMVPIKEMTDVLKVVKEQVGLKVKQWVRLKRGLYKDDIAQVDYVDLAQNQVHLKLLPRIDYTRMRGALRTTATESDDSKRKKKRRPAAKPFDPEAVRAIGGEVHSDGDFLLFEGNRYSRKGFLYKNFTMSAILSDGVKPTLAELERFEESPEEVNLEIMGTVKDDPTMAHSFSMGDNVEVCVGDLENLQAKIVAIDGTMITVMPKHQDLKDPLIFKASELRKYFKTGDHARVLAGRYEGETGLIIRVEPTRVVLVSDLTNHELEVLPRDLQLCSDVATGVDCLGQFQWGDMVQLDSQNVGVIVRLERENFHVLGMNGKCIECKPTALHKRKENRHTVALDADQNQIRRRDVVKVMEGPHAGRSGEIKHLYRSLAFLHCRMYTENGGIFVCKTRHLQLAGGSKTTVSNAGIVGGLGFMSPRIQSPMHPSGGRGARGGARGGRGGFRVTRDREILGKTIKISGGPYKGAVGIVKDATESTARVELHTSCQTISVDRNHIAIVGVTGKEGSVSTYGRTPARTPGYGAQTPSYTAAGSKTPLVGSQTPNWDTDTRTPYGTMTPSHDGSMTPRHGAWDPTANTTPARNNDFDYSLEEPSPSPGYNPSTPGYQMTSQFAPQTPGTLYGSDRSYSPFNPSPSPAPSPYPVGYMNTPSPSTYSPNTPGGIPQSPYNPQTPGASLDSSMGDWCTTDIEVRIHTHDDTDLVGQTGIIRTVSNGVCSVFLRQEDRSVSIVSEHLAPVLPCNGDEFKIIYGDDRESVGRVLSKDGDVFVCRINEEIKLLPINFLCKMKSID

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
73	Phosphorylation	RRDNRGKSDESGEEE CCCCCCCCCCCCCCC	49.81	22817900
76	Phosphorylation	NRGKSDESGEEEEEP CCCCCCCCCCCCCCC	57.40	22817900
90	Phosphorylation	PPGEDIDSEEYDEEE CCCCCCCHHHCCCCC	32.44	22817900
162	Phosphorylation	IEIRRRGTNLWDTQK HHHHHCCCCCCCCCC	25.90	22817900
364	Phosphorylation	LRTTATESDDSKRKK HHCCCCCCCCHHHHH	42.22	27626673
707	Phosphorylation	VGGLGFMSPRIQSPM CCCCCCCCCCCCCCC	14.57	25749252
717	Phosphorylation	IQSPMHPSGGRGARG CCCCCCCCCCCCCCC	38.92	27626673
744	Acetylation	RDREILGKTIKISGG CCHHHCCCEEEECCC	43.56	21791702
804	Phosphorylation	SVSTYGRTPARTPGY CCEECCCCCCCCCCC	19.55	22817900
808	Phosphorylation	YGRTPARTPGYGAQT CCCCCCCCCCCCCCC	24.15	25749252
815	Phosphorylation	TPGYGAQTPSYTAAG CCCCCCCCCCCCCCC	17.42	25749252
825	Phosphorylation	YTAAGSKTPLVGSQT CCCCCCCCCCCCCCC	24.45	19429919
830	Phosphorylation	SKTPLVGSQTPNWDT CCCCCCCCCCCCCCC	24.33	29892262
832	Phosphorylation	TPLVGSQTPNWDTDT CCCCCCCCCCCCCCC	21.93	19429919
845	Phosphorylation	DTRTPYGTMTPSHDG CCCCCCCCCCCCCCC	16.42	21082442
847	Phosphorylation	RTPYGTMTPSHDGSM CCCCCCCCCCCCCCC	22.83	25749252
849	Phosphorylation	PYGTMTPSHDGSMTP CCCCCCCCCCCCCCC	25.66	27626673
853	Phosphorylation	MTPSHDGSMTPRHGA CCCCCCCCCCCCCCC	26.07	22817900
855	Phosphorylation	PSHDGSMTPRHGAWD CCCCCCCCCCCCCCC	20.90	22817900
867	Phosphorylation	AWDPTANTTPARNND CCCCCCCCCCCCCCC	31.52	22817900
868	Phosphorylation	WDPTANTTPARNNDF CCCCCCCCCCCCCCC	18.11	15380072

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
815	T	Phosphorylation	Kinase	CDK9	-	Uniprot
825	T	Phosphorylation	Kinase	CDK9	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SPT5H_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 SPT5H_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MSL1_DROME	msl-1	physical	23209435
SPT4H_DROME	spt4	physical	23894613
PHO_DROME	pho	physical	23894613

Drug and Disease Associations

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

Regulatory Network of SPT5H_DROME

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-73; SER-76; SER-90;THR-162; THR-808; THR-815; THR-847; THR-855; THR-867 AND THR-868, ANDMASS SPECTROMETRY.	18327897 [Abstract]
"An integrated chemical, mass spectrometric and computational strategyfor (quantitative) phosphoproteomics: application to Drosophilamelanogaster Kc167 cells."; Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,Juenger M.A., Eng J.K., Aebersold R., Tao W.A.; Mol. Biosyst. 3:275-286(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-707, AND MASSSPECTROMETRY.	17372656 [Abstract]