INO80_MOUSE - dbPTM
INO80_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID INO80_MOUSE
UniProt AC Q6ZPV2
Protein Name Chromatin-remodeling ATPase INO80 {ECO:0000305}
Gene Name Ino80
Organism Mus musculus (Mouse).
Sequence Length 1559
Subcellular Localization Cytoplasm . Nucleus . Cytoplasm, cytoskeleton, spindle . Chromosome . Localizes to the cytoplasm in quiescent cell. Associates with spindle microtubules during mitosis. Colocalizes with PCNA at replication forks during S-phase. Recruited to DNA damag
Protein Description ATPase component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and DNA repair. Binds DNA. As part of the INO80 complex, remodels chromatin by shifting nucleosomes. Regulates transcription upon recruitment by YY1 to YY1-activated genes, where it acts as an essential coactivator. Involved in UV-damage excision DNA repair. The contribution to DNA double-strand break repair appears to be largely indirect through transcriptional regulation. Involved in DNA replication. Required for microtubule assembly during mitosis thereby regulating chromosome segregation cycle..
Protein Sequence MASELGAGDDGSSTELAKPLYLQYLERALRLDHFLRQTSAIFNRNISSDDSEDGLDDNNPLLPESGDPLIQVKEEPPNSLLGETSGASSSGLLNPYSLNGVLQSESKSDKGNLYNFSKLKKSRKWLKSILLSDESSEADSQSEDNDDEEEELSLSREELHNMLRLHKYKKLHQNKYSKDKELQQYQYYSAGLLSTYDPFYEQQRHLLGPKKKKFKEDKKLKAKLKKVKKKRRRDEEFSSEESPRHHHHQTKVFAKFSHDAPPPGTKKKHLSIEQLNARRRKVWLSIVKKELPKANKQKSSARNLFLTNSRKLAHQCMKEVRRAALQAQKNCKETLPRARRLTKEMLLYWKKYEKVEKEHRKRAEKEALEQRKLDEEMREAKRQQRKLNFLITQTELYAHFMSRKRDMGHDGIQEEILRKLEDSSTQRQIDIGGGVVVNITQEDYDSNHFKAQALKNAENAYHIHQARTRSFDEDAKESRAAALRAADKSGSGFGESYSLANPSIRAGEDIPQPTIFNGKLKGYQLKGMNWLANLYEQGINGILADEMGLGKTVQSIALLAHLAERENIWGPFLIISPASTLNNWHQEFTRFVPKFKVLPYWGNPHDRKVIRRFWSQKTLYTQDAPFHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVRWKILLQFQCRNRLLLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNEWFSKDIESHAENKSAIDENQLSRLHMILKPFMLRRIKKDVENELSDKIEILTYCQLTSRQKLLYQALKNKISIEDLLQSSMGSTQQAQNTTSSLMNLVMQFRKVCNHPELFERQETWSPFHISLKPYEISKFIYRHGQIRVFNHSRDRWLKVLLSPFAPDYIQQSLFHRKGINEGSCFSFLRFIDVSPAEMANLMLQGLLARWLALFLSLKASYRLHQLRSWAEPDGTSHQSYLRNKDFLLGVDFPLSFPNLCSCPLLKSLVFSSHCKAVSGYSDHVVHQRRSATSSLRCCLLTELPSFLCVASPRVTAVPLDSYCNDRSAEYERGVLKEGGSLAAKQCLLNGAPELATDWLSRRSQFFPEPAGGLLSIRPQNGWSFIRIPGKESLITDSGKLYALDVLLTRLKSQGHRVLIYSQMTRMIDLLEEYMVYRKHTYMRLDGSSKISERRDMVADFQTRNDIFVFLLSTRAGGLGINLTAADTVIFYDSDWNPTVDQQAMDRAHRLGQTKQVTVYRLICKGTIEERILQRAKEKSEIQRMVISGGNFKPDTLKPKEVVSLLLDDEELEKKLRLRQEEKRQQEESNRVKERKRKREKYAEKKKKEDELDGKRRKEGVNLVIPFVPSADNSNLSADGDDSFISVDSAMPSPFSEISISSELHTGSIPPDESSSDMLVIVDDPASSAPQSRATNSPASITGSVSDTVNGISIQEVPAAGRGHSARSRGRPKGSGSTAKGAGKGRSRKSTAGSAAAMAGAKAGAAAASAAAYAAYGYNVSKGISASSPLQTSIVRPAGLADFGPSSASSPLSSPLNKGNNIPGTPKSLHMTSSLASDSLIRKQGKGTNPSGGR
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
3Phosphorylation-----MASELGAGDD
-----CCCCCCCCCC		45.2530352176
12PhosphorylationLGAGDDGSSTELAKP
CCCCCCCCHHHHHHH		40.8730352176
13PhosphorylationGAGDDGSSTELAKPL
CCCCCCCHHHHHHHH		31.2826643407
14PhosphorylationAGDDGSSTELAKPLY
CCCCCCHHHHHHHHH		36.3926643407
47PhosphorylationAIFNRNISSDDSEDG
HHHCCCCCCCCCCCC		31.1223429704
48PhosphorylationIFNRNISSDDSEDGL
HHCCCCCCCCCCCCC		41.4623429704
51PhosphorylationRNISSDDSEDGLDDN
CCCCCCCCCCCCCCC		42.4521082442
65PhosphorylationNNPLLPESGDPLIQV
CCCCCCCCCCCCEEE		46.7025293948
118AcetylationGNLYNFSKLKKSRKW
CCCCCHHHHHHHHHH		61.25-
132PhosphorylationWLKSILLSDESSEAD
HHHHHHHCCCCCCCC		35.5720531401
135PhosphorylationSILLSDESSEADSQS
HHHHCCCCCCCCCCC		38.1720531401
136PhosphorylationILLSDESSEADSQSE
HHHCCCCCCCCCCCC		34.4520531401
140PhosphorylationDESSEADSQSEDNDD
CCCCCCCCCCCCCCH		42.5320531401
142PhosphorylationSSEADSQSEDNDDEE
CCCCCCCCCCCCHHH		51.3620531401
238PhosphorylationRRRDEEFSSEESPRH
HHCCCCCCCCCCCCC		39.8721149613
239PhosphorylationRRDEEFSSEESPRHH
HCCCCCCCCCCCCCC		51.1821149613
242PhosphorylationEEFSSEESPRHHHHQ
CCCCCCCCCCCCCCC		24.1521149613
257PhosphorylationTKVFAKFSHDAPPPG
CCEEEEECCCCCCCC		21.54-
468PhosphorylationYHIHQARTRSFDEDA
HHHHHHHCCCCCHHH		33.4130635358
470PhosphorylationIHQARTRSFDEDAKE
HHHHHCCCCCHHHHH		36.1122802335
642PhosphorylationLVVQDVKYFQRVKWQ
EHHCCHHHHHHCCEE		12.56-
889PhosphorylationRKGINEGSCFSFLRF
CCCCCCCCHHHHHEE		13.0522817900
892PhosphorylationINEGSCFSFLRFIDV
CCCCCHHHHHEECCC		27.9122817900
926PhosphorylationLFLSLKASYRLHQLR
HHHHHHHHHHHHHHH		14.8123737553
927PhosphorylationFLSLKASYRLHQLRS
HHHHHHHHHHHHHHH		23.2723737553
1027PhosphorylationVTAVPLDSYCNDRSA
EEEEECHHHCCCCCH		38.99-
1033PhosphorylationDSYCNDRSAEYERGV
HHHCCCCCHHHHHCC		28.46-
1036PhosphorylationCNDRSAEYERGVLKE
CCCCCHHHHHCCCCC		15.61-
1157PhosphorylationLDGSSKISERRDMVA
CCCCCCHHHHHHHHH		28.8722817900
1455PhosphorylationGKGRSRKSTAGSAAA
CCCCCCCCHHHHHHH		23.52-
1490PhosphorylationYNVSKGISASSPLQT
CCCCCCCCCCCCCCC		30.6626643407
1492PhosphorylationVSKGISASSPLQTSI
CCCCCCCCCCCCCCC		26.2126643407
1493PhosphorylationSKGISASSPLQTSIV
CCCCCCCCCCCCCCC		29.3726643407
1497PhosphorylationSASSPLQTSIVRPAG
CCCCCCCCCCCCCCC		28.2726643407
1498PhosphorylationASSPLQTSIVRPAGL
CCCCCCCCCCCCCCC		13.2126643407
1511PhosphorylationGLADFGPSSASSPLS
CCCCCCCCCCCCCCC		38.6326643407
1512PhosphorylationLADFGPSSASSPLSS
CCCCCCCCCCCCCCC		34.9926643407
1514PhosphorylationDFGPSSASSPLSSPL
CCCCCCCCCCCCCCC		34.1426643407
1515PhosphorylationFGPSSASSPLSSPLN
CCCCCCCCCCCCCCC		29.5826643407
1518PhosphorylationSSASSPLSSPLNKGN
CCCCCCCCCCCCCCC		33.0426643407
1519PhosphorylationSASSPLSSPLNKGNN
CCCCCCCCCCCCCCC		40.8826643407
1530PhosphorylationKGNNIPGTPKSLHMT
CCCCCCCCCCCHHHC		23.3722006019
1553PhosphorylationIRKQGKGTNPSGGR-
HHHCCCCCCCCCCC-		47.6517693683
1556PhosphorylationQGKGTNPSGGR----
CCCCCCCCCCC----		56.8228059163
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_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of INO80_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of INO80_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of INO80_MOUSE

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Related Literatures of Post-Translational Modification

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