dbPTM

CSX1_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CSX1_SCHPO
UniProt AC	O13759
Protein Name	RNA-binding post-transcriptional regulator csx1
Gene Name	csx1
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	632
Subcellular Localization	Cytoplasm .
Protein Description	Regulates global gene expression after oxidative stress. Interacts and stabilizes atf1 and pcr1 mRNAs after oxidative stress, thus controlling their turnover..
Protein Sequence	MSIDCLYRRSSLFDTSFVPLHSSIPATSKMSASNSDVNAPISPVVDEGKSELVSPTLERLVAPFNCSPSSTPLQDVAGVGSKMSDTLWMGDLEPWMDATFIQQLWASLNEPVNVKVMRSKASSSETLISYCFVQFSSSAAAERALMKYNNTMIPGAHCTFKLNWATGGGIQHNNFVSRDPEFSIFVGDLLPTTEDSDLFMTFRSIYPSCTSAKIIVDPVTGLSRKYGFVRFSSEKEQQHALMHMQGYLCQGRPLRISVASPKSRASIAADSALGIVPTSTSNRQPNQDLCSMDPLNTTVFVGGLASNLSEKDLQVCFQPFGRILNIKIPFGKGCGFVQYSEKSAAEKAINTMQGALVGTSHIRLAWGHNTLPVSALSQSQSQVSDEGFDRTLSANQIFGMNQSVIGANSGSSNSSGSSLKSAPVSPRTAAAQSLLPNSVVSSINGMNSVNFSTISPPPLSRSASISPTLSGSGSGLTPLSSHFPSAATGLVGGQVYPQSSVLQSSKINGSAKVQPSVKLPEWLQPFSGNNHNSFATQDLLTRVSSLKLVDDEQPASLNGSAFQARASRPWNLGRERQSSLIDLRHELEQNENGLEKSGFGLNLRGRLPPRSYSTFNCTGQYLQPSLRLSRDS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Phosphorylation	IDCLYRRSSLFDTSF HHHCCCCCCCCCCCC	23.53	29996109
11	Phosphorylation	DCLYRRSSLFDTSFV HHCCCCCCCCCCCCC	31.11	25720772
15	Phosphorylation	RRSSLFDTSFVPLHS CCCCCCCCCCCCCCC	19.41	29996109
16	Phosphorylation	RSSLFDTSFVPLHSS CCCCCCCCCCCCCCC	26.54	29996109
31	Phosphorylation	IPATSKMSASNSDVN CCCCCCCCCCCCCCC	32.08	25720772
33	Phosphorylation	ATSKMSASNSDVNAP CCCCCCCCCCCCCCC	29.56	25720772
35	Phosphorylation	SKMSASNSDVNAPIS CCCCCCCCCCCCCCC	40.20	29996109
42	Phosphorylation	SDVNAPISPVVDEGK CCCCCCCCCCCCCCC	15.58	28889911
50	Phosphorylation	PVVDEGKSELVSPTL CCCCCCCCCCCCCCH	47.20	25720772
54	Phosphorylation	EGKSELVSPTLERLV CCCCCCCCCCHHHHH	25.45	28889911
56	Phosphorylation	KSELVSPTLERLVAP CCCCCCCCHHHHHCC	33.47	29996109
67	Phosphorylation	LVAPFNCSPSSTPLQ HHCCCCCCCCCCCHH	28.99	28889911
69	Phosphorylation	APFNCSPSSTPLQDV CCCCCCCCCCCHHHC	30.47	28889911
70	Phosphorylation	PFNCSPSSTPLQDVA CCCCCCCCCCHHHCC	37.11	25720772
71	Phosphorylation	FNCSPSSTPLQDVAG CCCCCCCCCHHHCCC	32.15	29996109
263	Phosphorylation	ISVASPKSRASIAAD EEECCCCHHHHHHHH	36.14	25720772
266	Phosphorylation	ASPKSRASIAADSAL CCCCHHHHHHHHHHC	16.20	25720772
271	Phosphorylation	RASIAADSALGIVPT HHHHHHHHHCCCCCC	22.22	25720772
291	Phosphorylation	QPNQDLCSMDPLNTT CCCCCCCCCCCCCCE	33.25	28889911
381	Phosphorylation	SALSQSQSQVSDEGF HHHCCCHHHCCCCCH	37.48	29996109
384	Phosphorylation	SQSQSQVSDEGFDRT CCCHHHCCCCCHHCE	23.47	29996109
393	Phosphorylation	EGFDRTLSANQIFGM CCHHCEECHHHHHCC	25.26	27738172
414	Phosphorylation	ANSGSSNSSGSSLKS CCCCCCCCCCCCCCC	37.72	25720772
417	Phosphorylation	GSSNSSGSSLKSAPV CCCCCCCCCCCCCCC	34.15	27738172
421	Phosphorylation	SSGSSLKSAPVSPRT CCCCCCCCCCCCHHC	43.00	25720772
425	Phosphorylation	SLKSAPVSPRTAAAQ CCCCCCCCHHCHHHH	13.96	25720772
455	Phosphorylation	SVNFSTISPPPLSRS CCCCEECCCCCCCCC	31.29	28889911
462	Phosphorylation	SPPPLSRSASISPTL CCCCCCCCCCCCCCC	24.00	29996109
464	Phosphorylation	PPLSRSASISPTLSG CCCCCCCCCCCCCCC	25.50	29996109
466	Phosphorylation	LSRSASISPTLSGSG CCCCCCCCCCCCCCC	14.88	29996109
480	Phosphorylation	GSGLTPLSSHFPSAA CCCCCCHHHCCCCCC	23.99	27738172
488	Phosphorylation	SHFPSAATGLVGGQV HCCCCCCCCCCCCEE	30.66	27738172
545	Phosphorylation	DLLTRVSSLKLVDDE HHHHHHHHCEECCCC	27.02	27738172
578	Phosphorylation	NLGRERQSSLIDLRH CCCCHHHHHHHHHHH	33.08	28889911
579	Phosphorylation	LGRERQSSLIDLRHE CCCHHHHHHHHHHHH	22.47	29996109
611	Phosphorylation	RGRLPPRSYSTFNCT CCCCCCCCCCCCCCC	29.25	29996109
612	Phosphorylation	GRLPPRSYSTFNCTG CCCCCCCCCCCCCCC	17.01	25720772
613	Phosphorylation	RLPPRSYSTFNCTGQ CCCCCCCCCCCCCCC	27.98	29996109
614	Phosphorylation	LPPRSYSTFNCTGQY CCCCCCCCCCCCCCC	15.61	25720772
618	Phosphorylation	SYSTFNCTGQYLQPS CCCCCCCCCCCCCCC	28.55	29996109

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
42	S	Phosphorylation	Kinase	STY1	Q09892	GPS
54	S	Phosphorylation	Kinase	STY1	Q09892	GPS
291	S	Phosphorylation	Kinase	STY1	Q09892	GPS
455	S	Phosphorylation	Kinase	STY1	Q09892	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CSX1_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 CSX1_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HOG1_SCHPO	sty1	genetic	14633985
CIP2_SCHPO	cip2	genetic	16407405
CIP1_SCHPO	cip1	genetic	16407405
CIP1_SCHPO	cip1	physical	16407405
CIP2_SCHPO	cip2	physical	16407405
STE11_SCHPO	ste11	physical	22253882
MDV1_SCHPO	caf4	physical	26771498

Drug and Disease Associations

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

Regulatory Network of CSX1_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-42; SER-54; SER-67 ANDSER-69, AND MASS SPECTROMETRY.	18257517 [Abstract]
"RNA-binding protein Csx1 mediates global control of gene expressionin response to oxidative stress."; Rodriguez-Gabriel M.A., Burns G., McDonald W.H., Martin V.,Yates J.R. III, Baehler J., Russell P.; EMBO J. 22:6256-6266(2003). Cited for: FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-42; SER-54;SER-291 AND SER-455.	14633985 [Abstract]