dbPTM

TPSX_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TPSX_SCHPO
UniProt AC	O14081
Protein Name	Putative alpha,alpha-trehalose-phosphate synthase [UDP-forming] 106 kDa subunit
Gene Name	SPAC2E11.16c, SPACUNK4.16c
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	944
Subcellular Localization
Protein Description
Protein Sequence	MGRILIAHLFLPSSVGFSFDTVPHDEVGSKFMQKEESKDWIADTPLDESAIVSEEESDDDSLLSDLPEEIDSTNAQSNIATPSPGTVAAAISGIQPPPKTPSSDSPSLENSLSNLNDLFKSRGRHMAFSKNDGTNLSLPPSRHQSPPPSSVLASQRHHRRHDSELEEFARRASRSLSFSMNGTPQRRMTFDAEAWKNVIFKIKPSSFGNASFYNAISAATRSKQFDDHLFVGTCGIPTDSLPDSLKERISHDYITEHSSLVVYPTDTDFVGHYNHYCKNILWPTFHYQIPDNPKSKAYEDHSWANYVKVNKAFADTIVDNYEQDDMIWINDYHLLLVPEMVRERLPRAKIGFFLHIPFPSSEVFRCLATRQEILKGMLGANILGFQIPEFAYHFLQTCSRLVNIDIRKNGVVSFENRQIDVIALPISIDPGFIDRCLASPPVEHWAKVLQDRFRGKHIILSHDKLDPIRGLRSKLISFERFLQKYPEYRENTILLQVAPESLQDSEHLPHISDIVTRINSAYSNIASRHVPVILLRQKLGYAQFLALMMISDALIDNSLREGISLTSHQFIYVQRKRHRPLILSEFVGSASILNDNAIIVNPWDYSKTAEAFRTALTMSEEECQKRNKAMCNLILRHDAASWAVTFQSLIKESWKEQIDMQRIPAFTAQLIKEPYQNAQKRLILLYFEGTISTWGSQYHNVMTSLQRTINLLNMLTSDPKNTVYVFSALSCQELEQLFQRVPKLGIVAENGCFVRSPPKGDATMPVSKKEIAELWKNKVLGTDLTWMKTVSEIFEYYAERTTGAYVENKDATVILHLREAEDDEAAMWAAKECCESVNNFNVPCSATIQNDMVVCRSNKVSKRLAAEDIYSANGGDYDFIFAASNDPDDDTVFSWMKNFKQSKKEVVPFTFSVCVSEHGNSTNADAESSGVFGFLQALEKVYSA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
100	Phosphorylation	GIQPPPKTPSSDSPS CCCCCCCCCCCCCCC	33.89	24763107
102	Phosphorylation	QPPPKTPSSDSPSLE CCCCCCCCCCCCCHH	52.59	25720772
103	Phosphorylation	PPPKTPSSDSPSLEN CCCCCCCCCCCCHHH	43.22	21712547
105	Phosphorylation	PKTPSSDSPSLENSL CCCCCCCCCCHHHHH	20.52	29996109
107	Phosphorylation	TPSSDSPSLENSLSN CCCCCCCCHHHHHHH	52.87	21712547
111	Phosphorylation	DSPSLENSLSNLNDL CCCCHHHHHHHHHHH	24.65	25720772
113	Phosphorylation	PSLENSLSNLNDLFK CCHHHHHHHHHHHHH	38.81	29996109
134	Phosphorylation	AFSKNDGTNLSLPPS EECCCCCCCCCCCCC	35.53	25720772
137	Phosphorylation	KNDGTNLSLPPSRHQ CCCCCCCCCCCCCCC	40.68	28889911
141	Phosphorylation	TNLSLPPSRHQSPPP CCCCCCCCCCCCCCC	40.22	28889911
145	Phosphorylation	LPPSRHQSPPPSSVL CCCCCCCCCCCCHHH	33.00	28889911
149	Phosphorylation	RHQSPPPSSVLASQR CCCCCCCCHHHHHHH	38.56	28889911
150	Phosphorylation	HQSPPPSSVLASQRH CCCCCCCHHHHHHHH	27.24	28889911
163	Phosphorylation	RHHRRHDSELEEFAR HHHHCCHHHHHHHHH	37.65	28889911
173	Phosphorylation	EEFARRASRSLSFSM HHHHHHHHHHHCCCC	22.16	25720772
175	Phosphorylation	FARRASRSLSFSMNG HHHHHHHHHCCCCCC	26.35	28889911
177	Phosphorylation	RRASRSLSFSMNGTP HHHHHHHCCCCCCCC	19.27	28889911
179	Phosphorylation	ASRSLSFSMNGTPQR HHHHHCCCCCCCCCC	14.15	28889911
183	Phosphorylation	LSFSMNGTPQRRMTF HCCCCCCCCCCCEEE	15.96	29996109
189	Phosphorylation	GTPQRRMTFDAEAWK CCCCCCEEECHHHHH	19.29	28889911
473	Phosphorylation	DPIRGLRSKLISFER CCCHHHHHHHHCHHH	36.54	25720772

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 TPSX_SCHPO !!

Functions of PTM Sites

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

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 TPSX_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
H2AZ_SCHPO	pht1	genetic	18818364
VPS71_SCHPO	vps71	genetic	18818364
CTBL1_SCHPO	SPAC1952.06c	genetic	22681890
ULP2_SCHPO	ulp2	genetic	22681890
HUS1_SCHPO	hus1	genetic	22681890

Drug and Disease Associations

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

Regulatory Network of TPSX_SCHPO

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-141; SER-145; SER-149;SER-150; SER-163; SER-177 AND THR-189, AND MASS SPECTROMETRY.	18257517 [Abstract]