SPT16_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SPT16_SCHPO
• UniProt AC: O94267
• Protein Name: FACT complex subunit spt16
• Gene Name: spt16
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 1019
• Subcellular Localization: Nucleus. Chromosome.
• 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 (By similarity)..
• Protein Sequence: MAEYEIDEITFHKRLGILLTSWKNEEDGKTLFQDCDSILVTVGAHDDTNPYQKSTALHTWLLGYEFPSTLILLEKHRITILTSVNKANMLTKLAETKGAAADVNILKRTKDAEENKKLFEKIIEYIRATNKKVGVFPKDKTQGKFINEWDSIFEPVKSEFNLVDASLGLAKCLAIKDEQELANIKGASRVSVAVMSKYFVDELSTYIDQGKKITHSKFSDQMESLIDNEAFFQTKSLKLGDIDLDQLEWCYTPIIQSGGSYDLKPSAITDDRNLHGDVVLCSLGFRYKSYCSNVGRTYLFDPDSEQQKNYSFLVALQKKLFEYCRDGAVIGDIYTKILGLIRAKRPDLEPNFVRNLGAGIGIEFRESSLLVNAKNPRVLQAGMTLNLSIGFGNLINPHPKNSQSKEYALLLIDTIQITRSDPIVFTDSPKAQGDISYFFGEDDSSLEDGVKPRKPPTRGTATISSHKGKTRSETRDLDDSAEKRRVEHQKQLASRKQAEGLQRFAQGSVPSSGIEKPTVKRFESYKRDSQLPQAIGELRILVDYRAQSIILPIFGRPVPFHISTLKNASKNDEGNFVYLRLNFVSPGQIGGKKDELPFEDPNAQFIRSFTFRSSNNSRMSQVFKDIQDMKKAATKRETERKEFADVIEQDKLIEIKNKRPAHINDVYVRPAIDGKRLPGFIEIHQNGIRYQSPLRSDSHIDLLFSNMKHLFFQPCEGELIVLIHVHLKAPIMVGKRKTQDVQFYREVSDIQFDETGNKKRKYMYGDEDELEQEQEERRRRAQLDREFKSFAEKIAEASEGRIELDIPFRELAFNGVPFRSNVLLQPTTDCLVQLTDTPFTVITLNEIEIAHLERVQFGLKNFDLVFIFQDFRRPPIHINTIPMEQLDNVKEWLDSCDICFYEGPLNLNWTTIMKTVNEDPIAFFEEGGWGFLGAPSDDEGDDSVEEVSEYEASDADPSDEEEEESEEYSEDASEEDGYSESEVEDEESGEDWDELERKARQEDAKHDAFEERPSKKRHR

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
436	Phosphorylation	PKAQGDISYFFGEDD CCCCCCCEEECCCCC	22.19	29996109
437	Phosphorylation	KAQGDISYFFGEDDS CCCCCCEEECCCCCC	11.85	29996109
444	Phosphorylation	YFFGEDDSSLEDGVK EECCCCCCCCCCCCC	49.50	28889911
445	Phosphorylation	FFGEDDSSLEDGVKP ECCCCCCCCCCCCCC	42.65	28889911
474	Phosphorylation	KGKTRSETRDLDDSA CCCCCCCCCCCCCHH	30.63	25720772
508	Phosphorylation	LQRFAQGSVPSSGIE HHHHHHCCCCCCCCC	20.83	21712547
511	Phosphorylation	FAQGSVPSSGIEKPT HHHCCCCCCCCCCCC	38.75	25720772
512	Phosphorylation	AQGSVPSSGIEKPTV HHCCCCCCCCCCCCC	37.41	28889911
518	Phosphorylation	SSGIEKPTVKRFESY CCCCCCCCCCCHHHH	50.13	21712547

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

Oops, there are no upstream regulatory protein records of SPT16_SCHPO !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SPT16_SCHPO !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of SPT16_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CENPA_SCHPO	cnp1	genetic	23028377
YEJJ_SCHPO	abo1	physical	26582768
YEJJ_SCHPO	abo1	genetic	26582768

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 fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444 AND SER-445, ANDMASS SPECTROMETRY.
PubMed: 18257517