MBO1_SCHPO - dbPTM
MBO1_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MBO1_SCHPO
UniProt AC O94488
Protein Name Microtubule organizer protein 1
Gene Name mbo1
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 1115
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body . Localizes at the interphase MTOC (iMTOC) and at the equatorial MTOC (eMTOC) at the end of mitosis.
Protein Description Required for cytoplasmic astral microtubule growth during mitosis. Involved in localizing components of the gamma-tubulin complex to the non-spindle pole body (non-SPB) microtubule organizing centers (MTOCs). Required for new microtubule nucleation from non-SPB sites during interphase..
Protein Sequence MEENSSELDSNNFNVLVDNLAGLSLTDEEVRRILSPRKEGSRQLPSSTSKDEDSEEASHKYDFEIDRDSLKSDSGSPRLHQNATAPTSSTPLQSPDESVNKLNSEDEEGNSSVAPFFLDTTNFDRLNDNITTDDEQLSPVLTANQGFQSQEQYEEDSYNNYDYTSDPSSPNYISSSLDQLPHLDDEDDLQLTPIKEERNYLHSQDAPTTNALSKKISDILIPASAMKDLKDRKNALAKEFEESQPGSSLTLKEQANVIDNLRKEVFGLKLKCYFLYDQLNKFHDQEVQDIMKQNIDLKTLTMELQRAVAGYEKKISGLESRIKPDQSFNLSTPSPAPSNLITLQSRYSQALSELETTKRAFAALRKEKSKKTNYSVGAYNEDRNVLSNMLDNERREKEALLQELESLRVQLSKKVPMPAKNTDERVIETLQRSNELLRMDISMQNEALLLRKQENDRLVKQVEELTVALNSGKMNAIVEAESSKNELWDSMMVSRMKTQEQSIELTRLYKQLQDIEEDYENKLMRMEQQWREDVDQLQEYVEEITQELQDTKEVLSKSSKESDDYEEVVGKLRTEAEREIEKFEKTIRENEESISLFKEEVEKLTDEITQLSERYNDKCHEFDELQKRLQTLEEENNKAKEDSTSKTSNLLEQLKMTEAEVDSLRKENEENKQVIALKESELVKSNDNKLLLNEQIESLNDQLSQLKTEMESVTTSKESLADYLSNLKERHNDELDSLNKKLREFEGILSSNSSLKSEIEERNNQYVTLRENFDSLQNAIMETFDKQVTHCSVNHLVQQIRKLKDENKKDQSGTDKLMKKIYHCEQSLKEKTNSLETLVSEKKELKNLLDAERRSKKAIQLELENLSSQAFRRNLSGSSSPSERSQSRELKLLQASEKRLKEQVEERNSLIKNIVTRFTQLNTGSKPVNTNVEALTTISSMNQAVNMNFRELDKSIQEFKRKCQSMEREFKTELRKLDGVLEARSKRLSQLEERVKLLGAGSTSSIPNSPRASKRVSLDSEDKKLVPASPDKSAVQRGITALKRDAEGMSHIWQLRLREMEFQLKAEQEGRKRDKLGARERLQDLIRQNRSLSRQIKTDKESNSRSPSISSQEHK
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
35PhosphorylationEEVRRILSPRKEGSR
HHHHHHHCCCCCCCC		21.9325720772
49PhosphorylationRQLPSSTSKDEDSEE
CCCCCCCCCCCCCHH		39.8024763107
61PhosphorylationSEEASHKYDFEIDRD
CHHHHHHCCEEECHH		22.0529996109
69PhosphorylationDFEIDRDSLKSDSGS
CEEECHHHCCCCCCC		38.2921712547
72PhosphorylationIDRDSLKSDSGSPRL
ECHHHCCCCCCCCCC		42.1529996109
76PhosphorylationSLKSDSGSPRLHQNA
HCCCCCCCCCCCCCC		15.7029996109
88PhosphorylationQNATAPTSSTPLQSP
CCCCCCCCCCCCCCC		31.0227738172
89PhosphorylationNATAPTSSTPLQSPD
CCCCCCCCCCCCCCC		36.2029996109
90PhosphorylationATAPTSSTPLQSPDE
CCCCCCCCCCCCCCH		27.9928889911
94PhosphorylationTSSTPLQSPDESVNK
CCCCCCCCCCHHHHH		41.8428889911
98PhosphorylationPLQSPDESVNKLNSE
CCCCCCHHHHHCCCC		38.0729996109
104PhosphorylationESVNKLNSEDEEGNS
HHHHHCCCCCCCCCC		57.7825720772
208PhosphorylationLHSQDAPTTNALSKK
HHCCCCCCCHHHHHH		34.1124763107
209PhosphorylationHSQDAPTTNALSKKI
HCCCCCCCHHHHHHH		19.8921712547
213PhosphorylationAPTTNALSKKISDIL
CCCCHHHHHHHHHHH		29.5021712547
224PhosphorylationSDILIPASAMKDLKD
HHHHCCHHHCHHHHH		24.4429996109
327PhosphorylationSRIKPDQSFNLSTPS
HCCCCCCCCCCCCCC		24.3929996109
331PhosphorylationPDQSFNLSTPSPAPS
CCCCCCCCCCCCCCC		39.1029996109
332PhosphorylationDQSFNLSTPSPAPSN
CCCCCCCCCCCCCCC		30.8329996109
334PhosphorylationSFNLSTPSPAPSNLI
CCCCCCCCCCCCCHH		33.5129996109
880PhosphorylationRNLSGSSSPSERSQS
HHCCCCCCHHHHHHH		33.8629996109
882PhosphorylationLSGSSSPSERSQSRE
CCCCCCHHHHHHHHH		47.8129996109
1002PhosphorylationVKLLGAGSTSSIPNS
HHHHCCCCCCCCCCC		25.2824763107
1003PhosphorylationKLLGAGSTSSIPNSP
HHHCCCCCCCCCCCC		26.1024763107
1004PhosphorylationLLGAGSTSSIPNSPR
HHCCCCCCCCCCCCC		28.1524763107
1005PhosphorylationLGAGSTSSIPNSPRA
HCCCCCCCCCCCCCC		42.0028889911
1009PhosphorylationSTSSIPNSPRASKRV
CCCCCCCCCCCCCCC		15.4828889911
1013PhosphorylationIPNSPRASKRVSLDS
CCCCCCCCCCCCCCC		23.4424763107
1017PhosphorylationPRASKRVSLDSEDKK
CCCCCCCCCCCCCCC		30.4124763107
1020PhosphorylationSKRVSLDSEDKKLVP
CCCCCCCCCCCCCCC		53.6529996109
1029PhosphorylationDKKLVPASPDKSAVQ
CCCCCCCCCCHHHHH		27.8024763107
1102PhosphorylationQIKTDKESNSRSPSI
HHHCCCCCCCCCCCC		45.9321712547
1104PhosphorylationKTDKESNSRSPSISS
HCCCCCCCCCCCCCC		43.3321712547
1106PhosphorylationDKESNSRSPSISSQE
CCCCCCCCCCCCCCC		23.8721712547
1108PhosphorylationESNSRSPSISSQEHK
CCCCCCCCCCCCCCC		36.0321712547
1111PhosphorylationSRSPSISSQEHK---
CCCCCCCCCCCC---		37.6121712547
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 MBO1_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MBO1_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 MBO1_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
YHP6_SCHPOmto2physical
15659644
ALP4_SCHPOalp4physical
15004232
ALP6_SCHPOalp6physical
15004232
ALP16_SCHPOalp16physical
15004232
GFH1_SCHPOgfh1physical
15004232
ALP4_SCHPOalp4physical
15120067
ALP6_SCHPOalp6physical
15120067
YHP6_SCHPOmto2physical
15800064
ALP4_SCHPOalp4physical
15659644
MYO3_SCHPOmyp2physical
20970338
CDC11_SCHPOcdc11physical
20970338
ALP4_SCHPOalp4physical
23401002
YHP6_SCHPOmto2physical
24704079
TBG_SCHPOgtb1physical
24704079
TEA1_SCHPOtea1genetic
25422470
YHP6_SCHPOmto2physical
26243668
TBG_SCHPOgtb1physical
26243668
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MBO1_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-94; SER-1005 ANDSER-1009, AND MASS SPECTROMETRY.

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