MYO52_SCHPO - dbPTM
MYO52_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MYO52_SCHPO
UniProt AC O94477
Protein Name Myosin-52
Gene Name myo52
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 1516
Subcellular Localization Cytoplasm . Localized at the cell poles and septum.
Protein Description Involved in cell wall deposition where it has a role in the localization of mok1..
Protein Sequence MTSGIYYKGLQCWIPDEQSQWIPGSIKDCRVEGEKAFLTVQDENENETVITVKPDDLNYEGRNGLPFLRSINSDADDLTDLSYLNEPSVLDALSTRYNQLQIYTYSGIVLIAVNPFQRLPNLYTHEIVRAYSEKSRDELDPHLYAIAEDSYKCMNQEHKNQTIIISGESGAGKTVSARYIMRYFASVQALIQSTDSNFHEAPQLTAVENEILATNPIMEAFGNSKTSRNDNSSRFGKYIQILFDGNATIIGAKIQTYLLERSRLVFQPNQERNYHIFYQILAGSSSEQLEKWKLVENSQEFNYLKQGNCSTIEGVNDKEEFKATVDALKTVGIDNDTCECIFSLLAALLHIGNIEVKHSRNDAYIDSKNENLINATSLLGVDPSSLVKWLTKRKIKMASEGILKPLNEFQAVVARDSVAKFLYASLFDWLVATINKALMYSADKSNQTAKSFIGVLDIYGFEHFKKNSFEQFCINYANEKLQQEFYRHVFKLEQEEYAAEGLNWSYIDYQDNQQCISMIESRLGILSLLDEECRMPTNSDENWVSKLNDAFSKPEFKNSYQKSRFGNKEFTIKHYALDVVYCAEGFIDKNRDTISDELLELFTNSDVPFVKDLVLFRLEQTAPPADTKKIKTKPKSNTLGSMFKSSLVSLMSTINETNAHYIRCIKPNEEKEAWKFDNQMVVSQLRACGVLETIKISCAGFPSRWTFDEFVSRYYMLVPSAVRTTESLTFSKAILEKHADPTKYQIGKTKIFFRSGVTPLLESARDKALKHAAHLLYEAFAVNYYRTRFLLSRKRVRSFQAVAHGFLSRRHTEYELLSSNIIKLQSLWRTALKRKEFIQTKNSILKVQSIIRGFLLRQTLEEKTKHDATLIIQSLWLTFKAHKHYKELQYYAVRIQSLWRMKLAKRQLTELKIESTKASHLKQVSYRLESRLFEISKQLDNSEQENNKFRERIAELESHLSNYAEAKLAQERELEQTRVLISDQSQDGELKELLEEKENALIMMEEEMRQVNDANTELLRVNATLKSQLKNYDMIIVEQTSQLKEKNRIIASLTKATKILNSASSIEQSRNSEEKSRRDSSLMEMRTQKEMLVLLMNDGLKHDLDKLTEYAGRTFTTLKTLLLKDNDVEAQKLDHLFLAKLLFIIISQMWKSNLCQESVALVERYCVHTLEYVFQKTSSANERPDIGFWVANTHALLAFVYTKQQAFKHSSAFTLLSTESHESVQTIFEMIESHLSKIFFEWVRQVNNFLKPLIVQAMIITGTNTDAGDENRKLRIKFFEKPKYKITDVIHVLNKVHDSCQAYKVNYEIYNALIRSIYRFINVEAFNSLFIDERGSWKRGTNISYNYHVLKDWCLESGVPEAYLQLEELLQTSKILQFVKDDPNYVARVRDFYALNFLQIKTLLHRYDYADYEAHVPKKTMSELSKNIVAEGINQREQLTYEVLDYRLQDSFEESPSLEKIKIPDDCNVTYLRRIIDLASAEESVEQALITVGNVADNDVQNSSDEENQVPNGIKV
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
399PhosphorylationKRKIKMASEGILKPL
HHCCCHHCCCCCCCH		32.6224763107
714PhosphorylationFDEFVSRYYMLVPSA
HHHHHHHHHHHCCHH		5.9225720772
720PhosphorylationRYYMLVPSAVRTTES
HHHHHCCHHCCCCCC		31.7325720772
724PhosphorylationLVPSAVRTTESLTFS
HCCHHCCCCCCCCCC		28.4625720772
727PhosphorylationSAVRTTESLTFSKAI
HHCCCCCCCCCCHHH		30.5325720772
729PhosphorylationVRTTESLTFSKAILE
CCCCCCCCCCHHHHH		34.8325720772
731PhosphorylationTTESLTFSKAILEKH
CCCCCCCCHHHHHHC		18.8825720772
755PhosphorylationKTKIFFRSGVTPLLE
CEEEEECCCCHHHHH		32.2425720772
798PhosphorylationLSRKRVRSFQAVAHG
HCHHHHHHHHHHHHH		20.8925720772
985PhosphorylationRVLISDQSQDGELKE
EEEECCCCCCCHHHH		34.9221712547
1062PhosphorylationKATKILNSASSIEQS
HHHHHHHCHHHHHHH		26.5329996109
1064PhosphorylationTKILNSASSIEQSRN
HHHHHCHHHHHHHCC		31.5021712547
1065PhosphorylationKILNSASSIEQSRNS
HHHHCHHHHHHHCCH		29.8428889911
1069PhosphorylationSASSIEQSRNSEEKS
CHHHHHHHCCHHHHH		22.1921712547
1072PhosphorylationSIEQSRNSEEKSRRD
HHHHHCCHHHHHHHH		46.1228889911
1076PhosphorylationSRNSEEKSRRDSSLM
HCCHHHHHHHHHHHH		35.5129996109
1080PhosphorylationEEKSRRDSSLMEMRT
HHHHHHHHHHHHHHH		24.4529996109
1081PhosphorylationEKSRRDSSLMEMRTQ
HHHHHHHHHHHHHHH		35.7029996109
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 MYO52_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MYO52_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 MYO52_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MYO52_SCHPOmyo52physical
18003699
CALM_SCHPOcam1physical
18003699
PKD2_SCHPOpkd2physical
19543678
TIP1_SCHPOtip1physical
19808886
DSK2_SCHPOdph1physical
19808886
MYO1_SCHPOmyo1physical
19805578
RNG2_SCHPOrng2physical
19805578
MYO3_SCHPOmyp2physical
19805578
MYO2_SCHPOmyo2physical
19805578
MYO52_SCHPOmyo52physical
19805578
SEC8_SCHPOsec8genetic
21148300
EXO70_SCHPOexo70genetic
21148300
YPT3_SCHPOypt3physical
22137473
MAL3_SCHPOmal3genetic
23051734
FOR3_SCHPOfor3physical
23051734
RHO3_SCHPOrho3genetic
21652630
EXO70_SCHPOexo70genetic
21652630
FOR3_SCHPOfor3genetic
21652630
MYO52_SCHPOmyo52physical
24196839
ACT_SCHPOact1physical
24196839
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MYO52_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-1065 AND SER-1072, ANDMASS SPECTROMETRY.

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