SPO15_SCHPO - dbPTM
SPO15_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPO15_SCHPO
UniProt AC Q10411
Protein Name Sporulation-specific protein 15
Gene Name spo15
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 1957
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body .
Protein Description Has a role in the initiation of spore membrane formation..
Protein Sequence MSNQSSSGSNTSDLDEESASSLVSSAASPFIDSDLETPRPNISRASTGQLAEDGDTSSQHEDSSEELKRQEVRGMRRHSDLSIDAKLGSSEGSTASSALPLTPRSPSNASWLLVRGGLLDSPILDINSVTQKSNLLNELKQVRSKLAALEHENGILSLQLSSSNKKDKNTSSVTTLTSEEDVSYFQKKLTNMESNFSAKQSEAYDLSRQLLTVTEKLDKKEKDYEKIKEDVSSIKASLAEEQASNKSLRGEQERLEKLLVSSNKTVSTLRQTENSLRAECKTLQEKLEKCAINEEDSKLLEELKHNVANYSDAIVHKDKLIEDLSTRISEFDNLKSERDTLSIKNEKLEKLLRNTIGSLKDSRTSNSQLEEEMVELKESNRTIHSQLTDAESKLSSFEQENKSLKGSIDEYQNNLSSKDKMVKQVSSQLEEARSSLAHATGKLAEINSERDFQNKKIKDFEKIEQDLRACLNSSSNELKEKSALIDKKDQELNNLREQIKEQKKVSESTQSSLQSLQRDILNEKKKHEVYESQLNELKGELQTEISNSEHLSSQLSTLAAEKEAAVATNNELSESKNSLQTLCNAFQEKLAKSVMQLKENEQNFSSLDTSFKKLNESHQELENNHQTITKQLKDTSSKLQQLQLERANFEQKESTLSDENNDLRTKLLKLEESNKSLIKKQEDVDSLEKNIQTLKEDLRKSEEALRFSKLEAKNLREVIDNLKGKHETLEAQRNDLHSSLSDAKNTNAILSSELTKSSEDVKRLTANVETLTQDSKAMKQSFTSLVNSYQSISNLYHELRDDHVNMQSQNNTLLESESKLKTDCENLTQQNMTLIDNVQKLMHKHVNQESKVSELKEVNGKLSLDLKNLRSSLNVAISDNDQILTQLAELSKNYDSLEQESAQLNSGLKSLEAEKQLLHTENEELHIRLDKLTGKLKIEESKSSDLGKKLTARQEEISNLKEENMSQSQAITSVKSKLDETLSKSSKLEADIEHLKNKVSEVEVERNALLASNERLMDDLKNNGENIASLQTEIEKKRAENDDLQSKLSVVSSEYENLLLISSQTNKSLEDKTNQLKYIEKNVQKLLDEKDQRNVELEELTSKYGKLGEENAQIKDELLALRKKSKKQHDLCANFVDDLKEKSDALEQLTNEKNELIVSLEQSNSNNEALVEERSDLANRLSDMKKSLSDSDNVISVIRSDLVRVNDELDTLKKDKDSLSTQYSEVCQDRDDLLDSLKGCEESFNKYAVSLRELCTKSEIDVPVSEILDDNFVFNAGNFSELSRLTVLSLENYLDAFNQVNFKKMELDNRLTTTDAEFTKVVADLEKLQHEHDDWLIQRGDLEKALKDSEKNFLRKEAEMTENIHSLEEGKEETKKEIAELSSRLEDNQLATNKLKNQLDHLNQEIRLKEDVLKEKESLIISLEESLSNQRQKESSLLDAKNELEHMLDDTSRKNSSLMEKIESINSSLDDKSFELASAVEKLGALQKLHSESLSLMENIKSQLQEAKEKIQVDESTIQELDHEITASKNNYEGKLNDKDSIIRDLSENIEQLNNLLAEEKSAVKRLSTEKESEILQFNSRLADLEYHKSQVESELGRSKLKLASTTEELQLAENERLSLTTRMLDLQNQVKDLSNIKDSLSEDLRTLRSLEDSVASLQKECKIKSNTVESLQDVLTSVQARNAELEDEVSRSVDKIRRRDDRCEHLSGKLKKLHSQLEEQHETFFRAEQQRMTQLGFLKETVKKQEKLLKKLNLRQEQLIPRSSILVYESYIRDIEKEIIVLQERLNGIELSQQLPKGYFGYFFKTNRVEMEVLDSFKQQVAKLQFLAGAEFIVKFKEDLEKCAAEEKEKQATFDNYSEKVENLGKSIEALYFALNREISFRKSLALSKSAYHNLLVRDSPKFNPDSQITYSIPVTNTKQSLLRSAILCVISLQRLRLLGQRHSFCEEVIENLSCV
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
46PhosphorylationRPNISRASTGQLAED
CCCCCCCCCCCCCCC
31.7729996109
47PhosphorylationPNISRASTGQLAEDG
CCCCCCCCCCCCCCC
28.1429996109
56PhosphorylationQLAEDGDTSSQHEDS
CCCCCCCCCCCCCCC
35.4925720772
57PhosphorylationLAEDGDTSSQHEDSS
CCCCCCCCCCCCCCH
32.5129996109
58PhosphorylationAEDGDTSSQHEDSSE
CCCCCCCCCCCCCHH
37.3329996109
63PhosphorylationTSSQHEDSSEELKRQ
CCCCCCCCHHHHHHH
36.3425720772
64PhosphorylationSSQHEDSSEELKRQE
CCCCCCCHHHHHHHH
47.6225720772
79PhosphorylationVRGMRRHSDLSIDAK
HHHHHHCCCCCEEEE
38.1328889911
82PhosphorylationMRRHSDLSIDAKLGS
HHHCCCCCEEEECCC
24.3429996109
93PhosphorylationKLGSSEGSTASSALP
ECCCCCCCCCCCCCC
19.4221712547
94PhosphorylationLGSSEGSTASSALPL
CCCCCCCCCCCCCCC
41.2229996109
96PhosphorylationSSEGSTASSALPLTP
CCCCCCCCCCCCCCC
19.0721712547
102PhosphorylationASSALPLTPRSPSNA
CCCCCCCCCCCCCCC
18.0825720772
105PhosphorylationALPLTPRSPSNASWL
CCCCCCCCCCCCCEE
33.6128889911
107PhosphorylationPLTPRSPSNASWLLV
CCCCCCCCCCCEEEE
46.4025720772
110PhosphorylationPRSPSNASWLLVRGG
CCCCCCCCEEEEECC
23.6225720772
121PhosphorylationVRGGLLDSPILDINS
EECCCCCCCCCCHHH
17.5125720772
416PhosphorylationDEYQNNLSSKDKMVK
HHHHHCCCHHHHHHH
37.1524763107
417PhosphorylationEYQNNLSSKDKMVKQ
HHHHCCCHHHHHHHH
48.3024763107
863PhosphorylationKEVNGKLSLDLKNLR
HHHCCEEEECHHHHH
24.2725720772
943PhosphorylationLKIEESKSSDLGKKL
EEECCCCCCHHHHHH
38.0628889911
951PhosphorylationSDLGKKLTARQEEIS
CHHHHHHHHHHHHHH
28.7728889911
1187PhosphorylationRLSDMKKSLSDSDNV
HHHHHHHHCCCCCCH
27.8225720772
1189PhosphorylationSDMKKSLSDSDNVIS
HHHHHHCCCCCCHHH
42.0025720772
1191PhosphorylationMKKSLSDSDNVISVI
HHHHCCCCCCHHHHH
27.9225720772
1516PhosphorylationEKIQVDESTIQELDH
HHHCCCHHHHHHHHH
26.7521712547
1657PhosphorylationSLEDSVASLQKECKI
HHHHHHHHHHHHHCC
29.2228889911
1868PhosphorylationKVENLGKSIEALYFA
HHHHHHHHHHHHHHH
24.7025720772

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 SPO15_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPO15_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 SPO15_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SAD1_SCHPOsad1physical
10639340

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SPO15_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-105, AND MASSSPECTROMETRY.

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