YN2B_SCHPO - dbPTM
YN2B_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YN2B_SCHPO
UniProt AC O59746
Protein Name Uncharacterized transcriptional regulatory protein C530.11c
Gene Name SPBC530.11c
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 819
Subcellular Localization Nucleus .
Protein Description
Protein Sequence MLENSTAVHGVRLSDSPEDPFLRKRLASNTQLNQKKIRFTENENDLSPERAQKEPVSIPHGRYTWSTSPDTDSSHLPSTPPTVDIPFHHPHTIHSPTFTLSVSPDSQSSSATHQNDYISSPHADFSFSPPASKIQSHEPLNDMAAVHPLRPSHVSGPLSPPEPKAASVDHSINPAYNASFRLPDGPLWTEGSENLPSLDIQLQLAHIYFIYAHGQPYVLFHRDSFMEALKSQRLPPVLVLAMCAVAIRFWQTDKYDKNELFEQWFNRASAIAMANFDKLDLVYVASFVMLSYVCAATSKYWMFAGMAIRMVVALHPNKTPNLPYYDRPDSPLPFEIRVQLTRRLFWDCFMLDRLNSLYCNTQFLNLEDIHVPLPMRETLFMYKAHAVTETLTGKPSSPDSFTNANPTTAPIVSRNAQDNMGMLAYMIRMVSIWGRVVRCLKSYSQKQSNPYPFWHAKSTFKQLDQELYEWEKNLPNRLRYSRQTLLSYHMMGQGGQFACLHLIFLQIHLYVHRYAASISSVPFSHVKSPPTVFENQSAVLASQCANAICRIIQDCTELSISLAAPFTASSAYLAGTVLLYHYITRGSEVQASKAAVHLPIAKRHLAQLSVYWPALGMYAKALDAIAFHQGALVTPSVPPVIATVSKTNTTNTGVQQRGNVGVTTTGSILTQSSPALPVQPVPLAYSKPAPTTKSSLTELAYNTNVSLPPRSPGTGSLAAGNLPNEKAPSLMTMVNGGPVPGDIGEASIPVVQNLQPSTAHVDPESDLGRVIKICDWYQSPSSDVLLSKPLQLNSSEEMEQQCIDLSRHNTLLNLSSYGI
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
5Phosphorylation---MLENSTAVHGVR
---CCCCCCCCCCEE
14.3621712547
6Phosphorylation--MLENSTAVHGVRL
--CCCCCCCCCCEEC
44.2621712547
14PhosphorylationAVHGVRLSDSPEDPF
CCCCEECCCCCCCHH
26.0229996109
16PhosphorylationHGVRLSDSPEDPFLR
CCEECCCCCCCHHHH
27.1528889911
28PhosphorylationFLRKRLASNTQLNQK
HHHHHHHCCCCCCHH
45.0324763107
30PhosphorylationRKRLASNTQLNQKKI
HHHHHCCCCCCHHHC
31.7521712547
40PhosphorylationNQKKIRFTENENDLS
CHHHCCCCCCCCCCC
28.2229996109
47PhosphorylationTENENDLSPERAQKE
CCCCCCCCHHHHHCC
27.8119547744
136PhosphorylationPPASKIQSHEPLNDM
CCHHHCCCCCCCCCC
33.0421712547
152PhosphorylationAVHPLRPSHVSGPLS
CCCCCCHHHCCCCCC
30.0429996109
155PhosphorylationPLRPSHVSGPLSPPE
CCCHHHCCCCCCCCC
29.3021712547
159PhosphorylationSHVSGPLSPPEPKAA
HHCCCCCCCCCCCCC
41.3521712547
167PhosphorylationPPEPKAASVDHSINP
CCCCCCCCCCCCCCC
32.7025720772
171PhosphorylationKAASVDHSINPAYNA
CCCCCCCCCCCCCCC
21.4329996109
392PhosphorylationHAVTETLTGKPSSPD
HEEHHHCCCCCCCCC
51.0529996109
396PhosphorylationETLTGKPSSPDSFTN
HHCCCCCCCCCCCCC
58.9729996109
397PhosphorylationTLTGKPSSPDSFTNA
HCCCCCCCCCCCCCC
41.0525720772
400PhosphorylationGKPSSPDSFTNANPT
CCCCCCCCCCCCCCC
37.0429996109
402PhosphorylationPSSPDSFTNANPTTA
CCCCCCCCCCCCCCC
37.0629996109
711PhosphorylationNVSLPPRSPGTGSLA
CCCCCCCCCCCCCCC
33.1929996109
714PhosphorylationLPPRSPGTGSLAAGN
CCCCCCCCCCCCCCC
27.2929996109

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 YN2B_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YN2B_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 YN2B_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TIP20_SCHPOdrp1physical
26771498

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YN2B_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-16, AND MASSSPECTROMETRY.

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