STU1_SCHPO - dbPTM
STU1_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STU1_SCHPO
UniProt AC O42874
Protein Name Protein peg1
Gene Name peg1
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 1462
Subcellular Localization Cytoplasm, cytoskeleton . Cytoplasm, cytoskeleton, spindle . Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body . Colocalizes with cytoplasmic microtubules and associates with the mitotic spindle throughout mitosis.
Protein Description Microtubule binding protein that regulates the stability of dynamic microtubules. Required for mitotic spindle formation..
Protein Sequence MADKDAQDFLKFLKSNASTDEKTRCLDTLRSFFNKNNIPNADLGLFVECFRLALTTVNPLLLRSSVACFETFLRRLRAQYPTWLKFRVPMLKNLVIDHIASRDLQKRVLNILIDLWHFNPSEIEKSLIHLSTTSKSAETRIQCFKWFVLAHNAHLSFDVKSLRPALYINLENANPSVREEAKEVLLLIYKNLSTSAKMQFITDVETTSGLRREILQSLVEELSLISSSSEVIIVQNSASSFQPAPFMTAVATLYPGVELENVKPLLANFSKQLEQDSASMLPAFEGRETEQNWSVRQDSVLRLRQYLRGNACIDYLPELLSVLKTLLPGILLALLSLRTTLSSSAIQLIKEMAIILKSNIDPFLELILPNLLKVCSVTKKLASQAANVTFAAILVNCGVLSRNLSFISLAAHDTNAQLRVFSSNWIFMLISLSPELKNLASLQTNLKAFEKLICRGLADSNSQVREVYRKSFWKLSEYFPSVQEELTNTLEPSVLKQLHLANPNRQAASFNFSGPKRAPIRPLSNLRSFSKSQKEETSSNSSNSSGTRRLGLPQRATPASRERVLPYTRSQAFHSTSLPPSLPSGHSPSIAIPSKRSVSATIKDESKTFELLKNIQRKYELILSGSSVDLPSAEFLSSNLTDALYSGSSICYSLIFSHSLLDLTFQYVDIASLLSQFLLCVYDPSNVGHSFALASFPYVKSHYDAHKYFPIVFDVLMNISNMAPHVKVFPFNTNQKRLIIHGCLLWLKEISDTKLNQLENKPFFVTDKLRYYSSKILAMTAKTKLTSKNWIPLSGLLFSLRAHDTFMFDGLLDRLNEESRTKLVSSWSKQDAFDYSKSSTHQEHLSKNLPTLNTSSSSNSSQTDLLVPHGKGETKETEMQSPIESKEGLLSKDTHIESPQGTSLEKENEEEGKNPVESNCSEESLDDHNIDQTLVNKKETLAQDSESLLQKNNALNEKGFENQFGLSSSAAKVLNKDTLDHVSGPISNSVSSSFKDFTRTPFKEINGERETGFELTSYVNALSKKDDINVQKTENVDESVGLNAMFMDNVNQDSLNSVDQSSGKDKLLLTSSTPNKPTTFFMPANEEILGSPAKDYDIHDQSYSVHELHSENMRENVGQSSLIYNNRDYMNTPMNDFSLSFSEIKGGILESPVESPMTGTISPIDADESVLHDIPAYESLNKSESNKYQEQAYSTPLHHTLNVLPKNKWILSRMHKMENGSPINVDKNLDDAVAALEAAVKELNDGSVNTKTLKFCIKVCKETPSMLYHSHGLLPAILHYIESNNSAMHISDCLILLHEFLVQGYQGVDMHTYHNIICILIEKAEKCKDEPVILAGIEDNITLIAEIADLQGLYEFTQQRLQSLNTETGEKSAPLLLMLLSAILMRLKDLEFLETKDLLRHVVLKYIDHTNPEIRKATFNVCLAVNTIVNNVDETFSILGGLNEGQRLLFMHYLKMKSDEKN
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
599PhosphorylationIPSKRSVSATIKDES
CCCCCCCCEEECCCH		22.4228889911
851PhosphorylationHLSKNLPTLNTSSSS
HHHHHCCCCCCCCCC		35.4924763107
854PhosphorylationKNLPTLNTSSSSNSS
HHCCCCCCCCCCCCC		32.8525720772
855PhosphorylationNLPTLNTSSSSNSSQ
HCCCCCCCCCCCCCC		27.4424763107
856PhosphorylationLPTLNTSSSSNSSQT
CCCCCCCCCCCCCCC		35.4324763107
857PhosphorylationPTLNTSSSSNSSQTD
CCCCCCCCCCCCCCC		33.0521712547
858PhosphorylationTLNTSSSSNSSQTDL
CCCCCCCCCCCCCCE		42.5525720772
860PhosphorylationNTSSSSNSSQTDLLV
CCCCCCCCCCCCEEE		26.2721712547
861PhosphorylationTSSSSNSSQTDLLVP
CCCCCCCCCCCEEEE		41.1521712547
863PhosphorylationSSSNSSQTDLLVPHG
CCCCCCCCCEEEECC		30.4821712547
877PhosphorylationGKGETKETEMQSPIE
CCCCCCCCEECCCCC		38.0129996109
881PhosphorylationTKETEMQSPIESKEG
CCCCEECCCCCCCCC		26.9128889911
894PhosphorylationEGLLSKDTHIESPQG
CCCCCCCCCCCCCCC		28.6121712547
898PhosphorylationSKDTHIESPQGTSLE
CCCCCCCCCCCCCCC		23.1724763107
902PhosphorylationHIESPQGTSLEKENE
CCCCCCCCCCCCCCH		25.5429996109
903PhosphorylationIESPQGTSLEKENEE
CCCCCCCCCCCCCHH		41.1629996109
989PhosphorylationVSGPISNSVSSSFKD
CCCCCCCCCCCCCCC		19.3121712547
991PhosphorylationGPISNSVSSSFKDFT
CCCCCCCCCCCCCCC		21.7821712547
992PhosphorylationPISNSVSSSFKDFTR
CCCCCCCCCCCCCCC		37.3221712547
993PhosphorylationISNSVSSSFKDFTRT
CCCCCCCCCCCCCCC		28.8921712547
1000PhosphorylationSFKDFTRTPFKEING
CCCCCCCCCCHHCCC		29.9824763107
1071PhosphorylationKDKLLLTSSTPNKPT
CCEEEEECCCCCCCC		31.9821712547
1072PhosphorylationDKLLLTSSTPNKPTT
CEEEEECCCCCCCCE		42.5224763107
1073PhosphorylationKLLLTSSTPNKPTTF
EEEEECCCCCCCCEE		30.5521712547
1091PhosphorylationANEEILGSPAKDYDI
CCHHHCCCCCCCCCC		20.4524763107
1120PhosphorylationMRENVGQSSLIYNNR
HHHHCCCCCEEECCC		22.6029996109
1121PhosphorylationRENVGQSSLIYNNRD
HHHCCCCCEEECCCC		15.7625720772
1151PhosphorylationIKGGILESPVESPMT
CCCCCCCCCCCCCCC		30.6925720772
1155PhosphorylationILESPVESPMTGTIS
CCCCCCCCCCCCCCC		21.8725720772
1158PhosphorylationSPVESPMTGTISPID
CCCCCCCCCCCCCCC		34.2627738172
1160PhosphorylationVESPMTGTISPIDAD
CCCCCCCCCCCCCCC		14.7627738172
1162PhosphorylationSPMTGTISPIDADES
CCCCCCCCCCCCCCC		18.6825720772
1221PhosphorylationMHKMENGSPINVDKN
HHHCCCCCCCCCCCC		33.9016951255
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 STU1_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STU1_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 STU1_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MAL3_SCHPOmal3genetic
16951255
DYHC_SCHPOdhc1physical
16951255
MAL3_SCHPOmal3physical
16951255
TIP1_SCHPOtip1physical
16951255
STU1_SCHPOpeg1physical
16951255
ASE1_SCHPOase1physical
18061564
TBA1_SCHPOnda2physical
20708587
ASE1_SCHPOase1genetic
18818364
ASK1_SCHPOask1genetic
18818364
YJ03_SCHPOrhn1genetic
18818364
MAD1_SCHPOmad1genetic
18818364
TBA2_SCHPOatb2genetic
18818364
MPH1L_SCHPOmph1genetic
22681890
ATP10_SCHPOatp10genetic
22681890
YJ03_SCHPOrhn1genetic
22681890
SEY1_SCHPOSPAC222.14cgenetic
22681890
SEC14_SCHPOspo20genetic
22681890
ASK1_SCHPOask1genetic
22681890
DGK1_SCHPOptp4genetic
22681890
ASE1_SCHPOase1genetic
22681890
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of STU1_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-599 AND SER-1221, ANDMASS SPECTROMETRY.

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