dbPTM

SSRP1_DROME - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SSRP1_DROME
UniProt AC	Q05344
Protein Name	FACT complex subunit Ssrp1
Gene Name	Ssrp
Organism	Drosophila melanogaster (Fruit fly).
Sequence Length	723
Subcellular Localization	Nucleus . Chromosome . Nucleus, nucleolus . Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci.
Protein Description	Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. Binds specifically to single-stranded DNA and RNA with highest affinity for nucleotides G and U. The FACT complex is required for expression of Hox genes..
Protein Sequence	MTDSLEYNDINAEVRGVLCSGRLKMTEQNIIFKNTKTGKVEQISAEDIDLINSQKFVGTWGLRVFTKGGVLHRFTGFRDSEHEKLGKFIKAAYSQEMVEKEMCVKGWNWGTARFMGSVLSFDKESKTIFEVPLSHVSQCVTGKNEVTLEFHQNDDAPVGLLEMRFHIPAVESAEEDPVDKFHQNVMSKASVISASGESIAIFREIQILTPRGRYDIKIFSTFFQLHGKTFDYKIPMDSVLRLFMLPHKDSRQMFFVLSLDPPIKQGQTRYHYLVLLFAPDEETTIELPFSEAELRDKYEGKLEKEISGPVYEVMGKVMKVLIGRKITGPGNFIGHSGTAAVGCSFKAAAGYLYPLERGFIYIHKPPLHIRFEEISSVNFARSGGSTRSFDFEVTLKNGTVHIFSSIEKEEYAKLFDYITQKKLHVSNMGKDKSGYKDVDFGDSDNENEPDAYLARLKAEAREKEEDDDDGDSDEESTDEDFKPNENESDVAEEYDSNVESDSDDDSDASGGGGDSDGAKKKKEKKSEKKEKKEKKHKEKERTKKPSKKKKDSGKPKRATTAFMLWLNDTRESIKRENPGIKVTEIAKKGGEMWKELKDKSKWEDAAAKDKQRYHDEMRNYKPEAGGDSDNEKGGKSSKKRKTEPSPSKKANTSGSGFKSKEYISDDDSTSSDDEKDNEPAKKKSKPPSDGDAKKKKAKSESEPEESEEDSNASDEDEEDEASD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
33	Acetylation	TEQNIIFKNTKTGKV CCEEEEEECCCCCCE	53.98	21791702
67	Acetylation	WGLRVFTKGGVLHRF CEEEEEEECCCEEEE	42.05	21791702
123	Acetylation	GSVLSFDKESKTIFE HEECEECCCCCEEEE	62.97	21791702
364	Acetylation	RGFIYIHKPPLHIRF CCEEEEECCCEEEEE	38.48	21791702
433	Phosphorylation	SNMGKDKSGYKDVDF HCCCCCCCCCCCCCC	58.45	22817900
435	Phosphorylation	MGKDKSGYKDVDFGD CCCCCCCCCCCCCCC	15.88	22817900
443	Phosphorylation	KDVDFGDSDNENEPD CCCCCCCCCCCCCHH	42.59	21082442
628	Phosphorylation	KPEAGGDSDNEKGGK CCCCCCCCCCCCCCC	45.68	21082442
645	Phosphorylation	KKRKTEPSPSKKANT CCCCCCCCCCCCCCC	35.26	25749252
652	Phosphorylation	SPSKKANTSGSGFKS CCCCCCCCCCCCCCC	39.05	25749252
653	Phosphorylation	PSKKANTSGSGFKSK CCCCCCCCCCCCCCC	30.67	22817900
655	Phosphorylation	KKANTSGSGFKSKEY CCCCCCCCCCCCCEE	40.60	25749252
662	Phosphorylation	SGFKSKEYISDDDST CCCCCCEECCCCCCC	14.95	19429919
664	Phosphorylation	FKSKEYISDDDSTSS CCCCEECCCCCCCCC	33.80	19429919
668	Phosphorylation	EYISDDDSTSSDDEK EECCCCCCCCCCCCC	36.86	19429919
669	Phosphorylation	YISDDDSTSSDDEKD ECCCCCCCCCCCCCC	38.96	19429919
670	Phosphorylation	ISDDDSTSSDDEKDN CCCCCCCCCCCCCCC	35.40	19429919
671	Phosphorylation	SDDDSTSSDDEKDNE CCCCCCCCCCCCCCC	49.52	19429919

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 SSRP1_DROME !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SSRP1_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 SSRP1_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GAGA_DROME	Trl	physical	12815073
HP1_DROME	Su(var)205	physical	20889714
SSRP1_DROME	Ssrp	physical	19605348
SSRP1_DROME	Ssrp	physical	23708362
SPT16_DROME	dre4	physical	20889714

Drug and Disease Associations

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

Regulatory Network of SSRP1_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-443; SER-664; SER-668;THR-669; SER-670 AND SER-671, AND MASS 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-443 AND SER-628, ANDMASS SPECTROMETRY.	17372656 [Abstract]