dbPTM

SPT16_DROME - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SPT16_DROME
UniProt AC	Q8IRG6
Protein Name	FACT complex subunit spt16
Gene Name	dre4
Organism	Drosophila melanogaster (Fruit fly).
Sequence Length	1083
Subcellular Localization	Nucleus . Chromosome . 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. The FACT complex is required for expression of Hox genes..
Protein Sequence	MSSFVLDKEAFVRRVKRLYTEWRAPSIGHDDALRNLDCIMSIVGVEEDVMYSKSMALQLWLLGYELTDTISVFCSDAVYFLTSKKKIEFLKQTQNITEEGFPEINLLVRDRTDKDQGNFEKLIKALQNSKKGKRLGVFAKDAYPGEFSEAWKKSLTASKFEHVDISTIIAYLMCPKDESEINNIRKASLVSMDIFNKYLKDEIMDIIDSDRKVKHNKLSDGCEAAIGEKKYTSGLDPRLLDMAYPPIIQSGGAYSLKFSAVADKNPLHFGVIVCSLGARYKSYCSNISRTFLVNPTEAMQENYTFLVSVQEEILKLLVPGTKLCDVYEKTLDFVKKEKPSMVDNLPKSFGFAMGLEFRENSIVIGPKCQALLKKNMVFNLHVGISNLTNPEATDKEGKNYALFIGDTVLVGEQSPASVMTPSKKKIKNVGIFIKDDSDEEDVDDKKTAKEDQGTEILGRSKRNAVLESKLRNEINTEEKRKEHQRELAQQLNERAKDRLARQGNSKEVEKVRKNTVSYKSISQMPREPEVKELKLYVDKKYETVIMPVFGIQVPFHISTIKNISQSVEGEYTYLRINFFHPGATMGRNEGGLYPQPEATFVKEVTYRSSNVKEHGEVGAPSANLNNAFRLIKEVQKRFKTREAEEREKEDLVKQDTLILSQNKGNPKLKDLYIRPNIVTKRMTGSLEAHSNGFRYISVRGDKVDILYNNIKSAFFQPCDGEMIILLHFHLKYAIMFGKKKHVDVQFYTEVGEITTDLGKHQHMHDRDDLAAEQAERELRHKLKTAFKSFCEKVETMTKSVVEFDTPFRELGFPGAPFRSTVTLQPTSGSLVNLTEWPPFVITLDDVELVHFERVQFHLRNFDMIFVFKEYNKKVAMVNAIPMNMLDHVKEWLNSCDIRYSEGVQSLNWQKIMKTITDDPEGFFEQGGWTFLDPESGSEGENETAESEEDEAYNPTDAESDEESDEDSEYSEASEDSEESDEDLGSDEESGKDWSDLEREAAEEDRNHDYAADDKPRNGKFDSKKHGKSSKHSPSKSSKDKYNSRDKHHSSSSSGNKSSSKDKDRKRSRDDSRDNGHKSKKSRH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
188	Phosphorylation	INNIRKASLVSMDIF HHHHHHHHHEEHHHH	32.13	21082442
437	Phosphorylation	GIFIKDDSDEEDVDD EEEECCCCCCCCCCC	57.99	21082442
505	Phosphorylation	RLARQGNSKEVEKVR HHHHCCCHHHHHHHH	36.70	27626673
519	Acetylation	RKNTVSYKSISQMPR HHCCCCHHHHHCCCC	33.53	21791702
680	Acetylation	IRPNIVTKRMTGSLE ECCCEEECCCCCCEE	29.31	21791702
994	Phosphorylation	EESGKDWSDLEREAA CCCCCCHHHHHHHHH	42.31	19429919
1032	Phosphorylation	HGKSSKHSPSKSSKD CCCCCCCCCCCCCCC	34.31	30478224
1050 (in isoform 2)	Phosphorylation	-	29.86	27626673
1052 (in isoform 2)	Phosphorylation	-	44.18	21082442
1067	Phosphorylation	KDKDRKRSRDDSRDN CHHHHHHCCCCCCCC	43.00	19429919
1071	Phosphorylation	RKRSRDDSRDNGHKS HHHCCCCCCCCCCCC	45.91	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 SPT16_DROME !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SPT16_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 SPT16_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GAGA_DROME	Trl	physical	12815073
SSRP1_DROME	Ssrp	physical	22036573
SSRP1_DROME	Ssrp	physical	12815073
SSRP1_DROME	Ssrp	physical	19605348
SSRP1_DROME	Ssrp	physical	20889714

Drug and Disease Associations

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

Regulatory Network of SPT16_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-437, AND MASSSPECTROMETRY.	18327897 [Abstract]