YI14_SCHPO - dbPTM
YI14_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YI14_SCHPO
UniProt AC Q9P7B3
Protein Name Putative cation exchanger C521.04c
Gene Name SPAC521.04c
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 881
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein .
Protein Description Putative cation exchanger..
Protein Sequence MSQPADINQSESSAETITQGRRADRPEETPSSSVYEQNLRFGDFLMPTVGDADATDSLSQSTNDRDIYSPREIDQYTRKVSSRTDPSTSTISNARQHPRNSVSRLSRSSSNVRQQRDIPKQNFKVRPLSPLRGQSPASLRSEESFTLKERQNAINKTRAFGMRLWKPALYKKFRSINRDADIDIHDEPLKRPNTSISNVIWLICFGAPLFLVIFICYIFFTVLSFFNVPDAIVYSKLCRGLMFYLLYPFGQHVRHKVKRLSVRSPAHPIYQTQHSHYDETPTSHHPDPARLNFLSFSFCVNPMNQSLDCNTTPHRRNASSIIYTLMYYLIIAPTLLITSAICMFTIFFVPCARTLWAICRHLRTCPLSLSFRPNLALPLSMDSSDVVLLCVKKAASWKYYKYTIDGIYIIYFDMLALIIPTIFFGFFGSQGHWFTSSVFLFTASLVSIIPLAYFIGMAVASISAQSSMGMGAFINAFFGSVIEVFLYSVALRKGNAGLVEGSVIGSILAGLLLMPGLSMCAGAIRKKFQFFNIKSAGATSTMLLFAVLGAFAPTMLFRIYGPFRLDCEPCGANCQKCTKHYVLENDSLYKNRVLPFTYCCSIMLVLAYAIGLWFTLRTHASHIWQNFTADDISFLKAEEEVGEPVNQDTAGNMSDSSEGGEAVVNGNSQHHHNRDDASSGLSSNGSENESLEHEPTNELPQRPLVNQSQNSHGDDAPNWSRSKSAIILLSATFLYSLIAEILVEHVDTVLDKFAISEKFLGLTLFALVPNTTEFMNAISFALNENIALSMEIGSAYALQVCLLQIPCLMGYSLFQYYRSGDSISFKHLFTMVFPTWDMICVMICVFLLTYVHSEGKSNYFKGSILVLAYLVSMLGFTFFNY
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 Orthologous
Protein Cluster
29PhosphorylationRADRPEETPSSSVYE
CCCCCCCCCCCCHHH
27.1529996109
31PhosphorylationDRPEETPSSSVYEQN
CCCCCCCCCCHHHCC
42.5425720772
32PhosphorylationRPEETPSSSVYEQNL
CCCCCCCCCHHHCCC
25.6525720772
33PhosphorylationPEETPSSSVYEQNLR
CCCCCCCCHHHCCCC
32.8129996109
35PhosphorylationETPSSSVYEQNLRFG
CCCCCCHHHCCCCCC
17.4725720772
57PhosphorylationGDADATDSLSQSTND
CCCCCCCCCCCCCCC
26.0929996109
59PhosphorylationADATDSLSQSTNDRD
CCCCCCCCCCCCCCC
26.4929996109
101PhosphorylationARQHPRNSVSRLSRS
HHHCCCCHHHHHHHC
23.8125720772
103PhosphorylationQHPRNSVSRLSRSSS
HCCCCHHHHHHHCCC
27.5925720772
106PhosphorylationRNSVSRLSRSSSNVR
CCHHHHHHHCCCCHH
29.0729996109
108PhosphorylationSVSRLSRSSSNVRQQ
HHHHHHHCCCCHHHH
34.4425720772
109PhosphorylationVSRLSRSSSNVRQQR
HHHHHHCCCCHHHHC
25.4825720772
110PhosphorylationSRLSRSSSNVRQQRD
HHHHHCCCCHHHHCC
40.3625720772
129PhosphorylationNFKVRPLSPLRGQSP
CCEEECCCCCCCCCC
25.2728889911
135PhosphorylationLSPLRGQSPASLRSE
CCCCCCCCCCHHCCC
25.8428889911
138PhosphorylationLRGQSPASLRSEESF
CCCCCCCHHCCCCCC
27.9225720772
141PhosphorylationQSPASLRSEESFTLK
CCCCHHCCCCCCCHH
51.5124763107
144PhosphorylationASLRSEESFTLKERQ
CHHCCCCCCCHHHHH
21.3424763107
146PhosphorylationLRSEESFTLKERQNA
HCCCCCCCHHHHHHH
46.3124763107

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 YI14_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YI14_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 YI14_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATG11_SCHPOatg11physical
26771498
SAD1_SCHPOsad1physical
26771498

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YI14_SCHPO

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-129, AND MASSSPECTROMETRY.

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