INO80_SCHPO - dbPTM
INO80_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID INO80_SCHPO
UniProt AC O14148
Protein Name Putative DNA helicase ino80
Gene Name ino80
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 1604
Subcellular Localization Nucleus .
Protein Description DNA helicase component of the INO80 complex which remodels chromatin by shifting nucleosomes and is involved in DNA repair..
Protein Sequence MDPSRETFDGSTRDSYKPPNGAEMMGQSELNTQNRIPYNTSANNRNWQIPLYWQQRGNEFQASPPPPLGYVTPEYGATGTPVNANNASRVDYATTAANVPEEYANDYSSELAYIHNVNDMPHVDGLSNHSPATQPDLFETPAQSDPILFSSYPHAAQARVDPSISKDLYNMVPRPDANTVSPHAARSASSLPVPKEASETPFRDASTDLFDEHAHAAPMHSSISISTLLSDSDRYEPHVSLTENISPVMAPSIDARLSQTILRGLPPAQKLSPNSSQSQITHNRRKHKLPLNATTNNSVVLTPDTSPLLDSDEVVSDDDSNEQQTMMMKFNYLQHLRNKRDEAVHAEKRRLLDIRGSIHDRLVCRYENRYNKLHASEYNHHHDWAVRQAIREEVAAVEAAKIRADEEKKKKEREEQVRLLQESADKDAEMNEASTATSENEDLKDDLSLADLSSKKTANSQATENNNTPSKAKVKAESKVRSKAKSDKSRAKLSSDTNKDSEKNDNNDASLQSAGVASDGESSPETPLTKASKSKKAKASKLANDTSKNANGETKSTPKKSKKKTSKAQQEANSTTAEGKEKLSGDSTETGNSTNKEASTEDTKANATASAPNKKKKTVETLQQQVIKEIARKEIPRVYKIIQQNQYNRSTNARKTSQLCGREARRWQFRTIKNNKDMQTKAKRAMRETMVFWKRNERVERDLRKKAEREALDRAKKEEELRESRRQARKLDFLITQTELYSHFVGRKMDREQDLPSATNTASVSEINFDSDEEEDIRRLAVESAQEAVQKAREHSQLFDANRQQSPNNSSSDMNEGEMNFQNPTLVNAFEVKQPKMLMCKLKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSISVMAYLAETHNIWGPFLVIAPASTLHNWQQEITRFVPKLKCIPYWGSTKDRKILRKFWCRKNMTYDENSPFHVVVTSYQLVVLDAQYFQSVKWQYMILDEAQAIKSSSSSRWKSLLAFKCRNRLLLTGTPIQNTMQELWALLHFIMPSLFDSHNEFSEWFSKDIESHAQSNTQLNEQQLKRLHMILKPFMLRRVKKNVQSELGEKIEKEVYCDLTQRQKILYQALRRQISIAELLEKAILGGDDTVASIMNLVMQFRKVCNHPDLFEREDVRSPLSLATWSKSIYINREGNFLDVPYNTRNFITFSIPRLLYEQGGILSVPGLNTSRGFETKYLYNLMNIWNPEYTNDSIKSNPEGSPFSWLRFVDESPQTLFQTFQNPVVHYLDEAEASSSLKEEQLCRQEFCYGKDYSNVRKMLLLPKSITKVDVLGSDFKEDSPFYHLTHVLEESDSQLDLTLLDSVLVQRASAPPIDIYCPGSRQFTVLQSRFQRDHLWSHYLYQPLKGEEDLIINNQAVSKLPIPRKPLLPSFGIAKGSYSNVRIPSMLRFIADSGKLSKLDKLLVELKANDHRVLIYFQMTRMIDLMEEYLTFRQYKYLRLDGSSKISQRRDMVTEWQTRPELFVFLLSTRAGGLGINLTAADTVIFYDSDWNPSIDSQAMDRAHRIGQQKQVTVYRFITRGTIEERIVIRAKEKEEVQKVVISGGETRPTKQMDLKGNSREMVSWLLEE
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
63PhosphorylationRGNEFQASPPPPLGY
CCCCCCCCCCCCCCC		27.4427738172
169PhosphorylationPSISKDLYNMVPRPD
CCCCHHHHHCCCCCC		16.0229996109
179PhosphorylationVPRPDANTVSPHAAR
CCCCCCCCCCHHHHH		24.8728889911
181PhosphorylationRPDANTVSPHAARSA
CCCCCCCCHHHHHCC		14.6625720772
189PhosphorylationPHAARSASSLPVPKE
HHHHHCCCCCCCCCC		33.3825720772
272PhosphorylationLPPAQKLSPNSSQSQ
CCCHHHCCCCCCCHH		29.1328889911
275PhosphorylationAQKLSPNSSQSQITH
HHHCCCCCCCHHHCC		32.8929996109
278PhosphorylationLSPNSSQSQITHNRR
CCCCCCCHHHCCCCC		26.0425720772
306PhosphorylationVVLTPDTSPLLDSDE
EEECCCCCCCCCCCC		22.4121712547
311PhosphorylationDTSPLLDSDEVVSDD
CCCCCCCCCCCCCCC		35.3221712547
316PhosphorylationLDSDEVVSDDDSNEQ
CCCCCCCCCCCCHHH		40.2621712547
320PhosphorylationEVVSDDDSNEQQTMM
CCCCCCCCHHHHHHH		49.6221712547
434PhosphorylationDAEMNEASTATSENE
HHHHHHHHHCCCCCC		16.6421712547
435PhosphorylationAEMNEASTATSENED
HHHHHHHHCCCCCCC		40.7929996109
437PhosphorylationMNEASTATSENEDLK
HHHHHHCCCCCCCCC		36.3424763107
438PhosphorylationNEASTATSENEDLKD
HHHHHCCCCCCCCCH		35.6424763107
448PhosphorylationEDLKDDLSLADLSSK
CCCCHHCCHHHHCCC		28.6221712547
453PhosphorylationDLSLADLSSKKTANS
HCCHHHHCCCCCCCC		40.4324763107
454PhosphorylationLSLADLSSKKTANSQ
CCHHHHCCCCCCCCC		45.5321712547
463PhosphorylationKTANSQATENNNTPS
CCCCCCCCCCCCCCC		31.4429996109
468PhosphorylationQATENNNTPSKAKVK
CCCCCCCCCCHHHHH		30.9421712547
470PhosphorylationTENNNTPSKAKVKAE
CCCCCCCCHHHHHHH		43.1129996109
510PhosphorylationKNDNNDASLQSAGVA
CCCCCCHHHHHCCCC		29.7927738172
513PhosphorylationNNDASLQSAGVASDG
CCCHHHHHCCCCCCC		32.0825720772
518PhosphorylationLQSAGVASDGESSPE
HHHCCCCCCCCCCCC		43.6828889911
522PhosphorylationGVASDGESSPETPLT
CCCCCCCCCCCCCCC		57.6421712547
526PhosphorylationDGESSPETPLTKASK
CCCCCCCCCCCHHHH		27.2924763107
765PhosphorylationATNTASVSEINFDSD
CCCCCCHHEECCCCC		30.2029996109
771PhosphorylationVSEINFDSDEEEDIR
HHEECCCCCCHHHHH		42.6628889911
806PhosphorylationFDANRQQSPNNSSSD
HCCCCCCCCCCCCCC		22.6621712547
812PhosphorylationQSPNNSSSDMNEGEM
CCCCCCCCCCCCCCC		40.4721712547
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 INO80_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of INO80_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 INO80_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARP4_SCHPOalp5physical
19933844
TAF14_SCHPOtfg3physical
19933844
IES6_SCHPOies6physical
19933844
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of INO80_SCHPO

loading...

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 THR-179 AND SER-518, ANDMASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory