BLT1_SCHPO - dbPTM
BLT1_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BLT1_SCHPO
UniProt AC O74338
Protein Name Mitosis inducer protein blt1
Gene Name blt1
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 700
Subcellular Localization Cell septum .
Protein Description At the onset of mitosis, forms a medial ring structure before the arrangement of the medial actin ring. Essential for the central positioning of the division septum before the cell divides..
Protein Sequence MSKSAFTSKSQLKGIDGSFNDPFRQPSMNLPTPPHDDGLPSIPRSTALPNLSNRLSPYSHRNYLPIPEADSRNLEVLNSISLTTGSVVNQINKLYQRSCDNANYLQDLRSLILQTPTAEANATQVTESLNQIQKILQEASSKDREQIVQVIKELNKGNSLEVRRELGNCLAHLKKGTLNIDNALQASLQKYWKELQYFNVSKDKLLSLEESIKLLSARLEETDTPSSTHWIEINAGFKEVGDELSENFQRKQEILSGLQNNVILRTNNRKPVGSDGSNSNFNGGEEQMDSKDQEEIQDYLNSLLSVHEKDGVLLQKFHNSYVQYQKLAVALSKYENFDADKLFQQMNLAKQSNETLLQTLTEQTDQLLSFKETMDSFKFILGPSMENQALQQGILAEQQDLVAQLRDIVLRSETLAENPSNMPGSCLPGASSNTADEFTEQLNLLKNEVARLSAICPSPNSGINASVLTNADNLEKENLLLVNNNAFKVDDRSVSSVALDDHNRQLQMNVEELEGKKADLTSKINRLDKDFVKLNTTYSLLTDQVKTKQLALQEIESRVIRLEERLNMLQKLSMQPAISSSSEFVPIESHPSSSAVVPIEEPKNSIIEKKRVPHNAARNSVNLEVTLPNSKKRFSSFSGSSSKLPVRPSTALTDKRKPSWSRRLAAAIGFSSGSPEKKHVITSSDAGHQRSKSRSFSSKM
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
27PhosphorylationNDPFRQPSMNLPTPP
CCCCCCCCCCCCCCC		16.3829996109
32PhosphorylationQPSMNLPTPPHDDGL
CCCCCCCCCCCCCCC		53.2529996109
52PhosphorylationSTALPNLSNRLSPYS
CCCCCCCCCCCCCCC		26.9229996109
56PhosphorylationPNLSNRLSPYSHRNY
CCCCCCCCCCCCCCC		20.6829996109
458PhosphorylationRLSAICPSPNSGINA
HHHHHCCCCCCCCCH		32.1021712547
461PhosphorylationAICPSPNSGINASVL
HHCCCCCCCCCHHHH		44.4221712547
466PhosphorylationPNSGINASVLTNADN
CCCCCCHHHHCCCCC		17.1121712547
469PhosphorylationGINASVLTNADNLEK
CCCHHHHCCCCCCCC		26.6321712547
493PhosphorylationAFKVDDRSVSSVALD
CEECCCCCCCCEEEC		33.0925720772
495PhosphorylationKVDDRSVSSVALDDH
ECCCCCCCCEEECHH		21.9721712547
496PhosphorylationVDDRSVSSVALDDHN
CCCCCCCCEEECHHH		14.8425720772
573PhosphorylationLNMLQKLSMQPAISS
HHHHHHHHCCCCCCC		23.5429996109
579PhosphorylationLSMQPAISSSSEFVP
HHCCCCCCCCCCCCC		26.6925720772
580PhosphorylationSMQPAISSSSEFVPI
HCCCCCCCCCCCCCC		31.6029996109
581PhosphorylationMQPAISSSSEFVPIE
CCCCCCCCCCCCCCC		27.3929996109
582PhosphorylationQPAISSSSEFVPIES
CCCCCCCCCCCCCCC		36.6825720772
589PhosphorylationSEFVPIESHPSSSAV
CCCCCCCCCCCCCCE		41.2225720772
592PhosphorylationVPIESHPSSSAVVPI
CCCCCCCCCCCEEEC		31.3427738172
594PhosphorylationIESHPSSSAVVPIEE
CCCCCCCCCEEECCC		29.4425720772
605PhosphorylationPIEEPKNSIIEKKRV
ECCCCCCCHHHCCCC		30.9421712547
620PhosphorylationPHNAARNSVNLEVTL
CCCCCCCCCEEEEEC		13.5628889911
635PhosphorylationPNSKKRFSSFSGSSS
CCCCCCCCCCCCCCC		34.2121712547
636PhosphorylationNSKKRFSSFSGSSSK
CCCCCCCCCCCCCCC		22.2528889911
638PhosphorylationKKRFSSFSGSSSKLP
CCCCCCCCCCCCCCC		39.4525720772
640PhosphorylationRFSSFSGSSSKLPVR
CCCCCCCCCCCCCCC		30.1828889911
641PhosphorylationFSSFSGSSSKLPVRP
CCCCCCCCCCCCCCC		34.7129996109
642PhosphorylationSSFSGSSSKLPVRPS
CCCCCCCCCCCCCCC		39.6529996109
649PhosphorylationSKLPVRPSTALTDKR
CCCCCCCCCCCCCCC		18.7529996109
650PhosphorylationKLPVRPSTALTDKRK
CCCCCCCCCCCCCCC		28.5029996109
653PhosphorylationVRPSTALTDKRKPSW
CCCCCCCCCCCCCCH		36.6924763107
659PhosphorylationLTDKRKPSWSRRLAA
CCCCCCCCHHHHHHH		40.4929996109
671PhosphorylationLAAAIGFSSGSPEKK
HHHHHCCCCCCCCCC		28.6929996109
672PhosphorylationAAAIGFSSGSPEKKH
HHHHCCCCCCCCCCE		40.8229996109
674PhosphorylationAIGFSSGSPEKKHVI
HHCCCCCCCCCCEEE		31.6529996109
682PhosphorylationPEKKHVITSSDAGHQ
CCCCEEEECCHHCCC		22.5329996109
683PhosphorylationEKKHVITSSDAGHQR
CCCEEEECCHHCCCH		18.3329996109
684PhosphorylationKKHVITSSDAGHQRS
CCEEEECCHHCCCHH		23.8829996109
693PhosphorylationAGHQRSKSRSFSSKM
HCCCHHHCCCCCCCC		34.1124763107
697PhosphorylationRSKSRSFSSKM----
HHHCCCCCCCC----		30.2324763107
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 BLT1_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BLT1_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 BLT1_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MID1_SCHPOmid1physical
23149940
MID1_SCHPOmid1genetic
23149940
GEF2_SCHPOgef2physical
23149940
CDR2_SCHPOcdr2genetic
23149940
YDEA_SCHPOnod1physical
23349808
GEF2_SCHPOgef2physical
23349808
BLT1_SCHPOblt1physical
24790095
MOB1_SCHPOmob1genetic
24790095
SID2_SCHPOsid2genetic
24790095
CDC15_SCHPOcdc15physical
24790095
MOB1_SCHPOmob1physical
24790095
SID2_SCHPOsid2physical
24790095
CDC11_SCHPOcdc11genetic
24790095
CDC14_SCHPOcdc14genetic
24790095
CDC15_SCHPOcdc15genetic
24790095
CDC16_SCHPOcdc16genetic
24790095
CDK1_SCHPOcdc2genetic
24790095
MPIP_SCHPOcdc25genetic
24790095
PROF_SCHPOcdc3genetic
24790095
MLR4_SCHPOcdc4genetic
24790095
CDC7_SCHPOcdc7genetic
24790095
TPM_SCHPOcdc8genetic
24790095
MID1_SCHPOmid1genetic
24790095
BGS1_SCHPObgs1genetic
24790095
MYO2_SCHPOmyo2genetic
24790095
PLO1_SCHPOplo1genetic
24790095
RNG2_SCHPOrng2genetic
24790095
SID1_SCHPOsid1genetic
24790095
SID4_SCHPOsid4genetic
24790095
SPG1_SCHPOspg1genetic
24790095
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BLT1_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-636, AND MASSSPECTROMETRY.

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