INO80_HUMAN - dbPTM
INO80_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID INO80_HUMAN
UniProt AC Q9ULG1
Protein Name Chromatin-remodeling ATPase INO80 {ECO:0000305}
Gene Name INO80
Organism Homo sapiens (Human).
Sequence Length 1556
Subcellular Localization Cytoplasm . Nucleus . Cytoplasm, cytoskeleton, spindle . Chromosome . Localizes to the cytoplasm in quiescent cell (PubMed:20237820). Associates with spindle microtubules during mitosis (PubMed:20237820). Colocalizes with PCNA at replication forks du
Protein Description ATPase component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and DNA repair. [PubMed: 16230350]
Protein Sequence MASELGARDDGGCTELAKPLYLQYLERALRLDHFLRQTSAIFNRNISSDDSEDGLDDSNPLLPQSGDPLIQVKEEPPNSLLGETSGAGSSGMLNTYSLNGVLQSESKCDKGNLYNFSKLKKSRKWLKSILLSDESSEADSQSEDDDEEELNLSREELHNMLRLHKYKKLHQNKYSKDKELQQYQYYSAGLLSTYDPFYEQQRHLLGPKKKKFKEEKKLKAKLKKVKKKRRRDEELSSEESPRRHHHQTKVFAKFSHDAPPPGTKKKHLSIEQLNARRRKVWLSIVKKELPKANKQKASARNLFLTNSRKLAHQCMKEVRRAALQAQKNCKETLPRARRLTKEMLLYWKKYEKVEKEHRKRAEKEALEQRKLDEEMREAKRQQRKLNFLITQTELYAHFMSRKRDMGHDGIQEEILRKLEDSSTQRQIDIGGGVVVNITQEDYDSNHFKAQALKNAENAYHIHQARTRSFDEDAKESRAAALRAANKSGTGFGESYSLANPSIRAGEDIPQPTIFNGKLKGYQLKGMNWLANLYEQGINGILADEMGLGKTVQSIALLAHLAERENIWGPFLIISPASTLNNWHQEFTRFVPKFKVLPYWGNPHDRKVIRRFWSQKTLYTQDAPFHVVITSYQLVVQDVKYFQRVKWQYMVLDEAQALKSSSSVRWKILLQFQCRNRLLLTGTPIQNTMAELWALLHFIMPTLFDSHEEFNEWFSKDIESHAENKSAIDENQLSRLHMILKPFMLRRIKKDVENELSDKIEILMYCQLTSRQKLLYQALKNKISIEDLLQSSMGSTQQAQNTTSSLMNLVMQFRKVCNHPELFERQETWSPFHISLKPYHISKFIYRHGQIRVFNHSRDRWLRVLSPFAPDYIQRSLFHRKGINEESCFSFLRFIDISPAEMANLMLQGLLARWLALFLSLKASYRLHQLRSWGAPEGESHQRYLRNKDFLLGVNFPLSFPNLCSCPLLKSLVFSSHCKAVSGYSDQVVHQRRSATSSLRRCLLTELPSFLCVASPRVTAVPLDSYCNDRSAEYERRVLKEGGSLAAKQCLLNGAPELAADWLNRRSQFFPEPAGGLWSIRPQNGWSFIRIPGKESLITDSGKLYALDVLLTRLKSQGHRVLIYSQMTRMIDLLEEYMVYRKHTYMRLDGSSKISERRDMVADFQNRNDIFVFLLSTRAGGLGINLTAADTVIFYDSDWNPTVDQQAMDRAHRLGQTKQVTVYRLICKGTIEERILQRAKEKSEIQRMVISGGNFKPDTLKPKEVVSLLLDDEELEKKLRLRQEEKRQQEETNRVKERKRKREKYAEKKKKEDELDGKRRKEGVNLVIPFVPSADNSNLSADGDDSFISVDSAMPSPFSEISISSELHTGSIPLDESSSDMLVIVDDPASSAPQSRATNSPASITGSVSDTVNGISIQEMPAAGRGHSARSRGRPKGSGSTAKGAGKGRSRKSTAGSAAAMAGAKAGAAAASAAAYAAYGYNVSKGISASSPLQTSLVRPAGLADFGPSSASSPLSSPLSKGNNVPGNPKNLHMTSSLAPDSLVRKQGKGTNPSGGR
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-----MASELGARDD
-----CCCCCCCCCC		45.2530001349
18AcetylationGGCTELAKPLYLQYL
CCHHHHHHHHHHHHH		48.4526051181
47PhosphorylationAIFNRNISSDDSEDG
HHHCCCCCCCCCCCC		31.1230278072
48PhosphorylationIFNRNISSDDSEDGL
HHCCCCCCCCCCCCC		41.4630278072
51PhosphorylationRNISSDDSEDGLDDS
CCCCCCCCCCCCCCC		42.4530278072
58PhosphorylationSEDGLDDSNPLLPQS
CCCCCCCCCCCCCCC		39.7622199227
65PhosphorylationSNPLLPQSGDPLIQV
CCCCCCCCCCCCEEE		43.1320873877
118AcetylationGNLYNFSKLKKSRKW
CCCCCHHHHHHHHHH		61.2519608861
140PhosphorylationDESSEADSQSEDDDE
CCCCCCCCCCCCCCH		42.53-
142PhosphorylationSSEADSQSEDDDEEE
CCCCCCCCCCCCHHH		47.12-
236PhosphorylationRRRDEELSSEESPRR
HHHHHHCCCCCCCCH		38.7029255136
237PhosphorylationRRDEELSSEESPRRH
HHHHHCCCCCCCCHH		58.9929255136
240PhosphorylationEELSSEESPRRHHHQ
HHCCCCCCCCHHCCC		21.4729255136
253AcetylationHQTKVFAKFSHDAPP
CCHHHHEEECCCCCC		35.6225953088
255PhosphorylationTKVFAKFSHDAPPPG
HHHHEEECCCCCCCC		21.54-
264AcetylationDAPPPGTKKKHLSIE
CCCCCCCCCCCCCHH		66.787964343
287AcetylationVWLSIVKKELPKANK
HHHHHHHHHCCHHHH		54.307492141
291AcetylationIVKKELPKANKQKAS
HHHHHCCHHHHHHHH		76.777492151
294AcetylationKELPKANKQKASARN
HHCCHHHHHHHHHHH		59.027492161
392PhosphorylationLNFLITQTELYAHFM
HHHHEEHHHHHHHHH		21.2128331001
395PhosphorylationLITQTELYAHFMSRK
HEEHHHHHHHHHHCC		7.5628331001
423PhosphorylationRKLEDSSTQRQIDIG
HHHCCCCCCEEEEEC		31.5526546556
466PhosphorylationYHIHQARTRSFDEDA
HHHHHHHCCCCCHHH		33.4128857561
468PhosphorylationIHQARTRSFDEDAKE
HHHHHCCCCCHHHHH		36.1129496963
474UbiquitinationRSFDEDAKESRAAAL
CCCCHHHHHHHHHHH		69.42-
476PhosphorylationFDEDAKESRAAALRA
CCHHHHHHHHHHHHH		26.8923312004
486UbiquitinationAALRAANKSGTGFGE
HHHHHHHHCCCCCCC		45.60-
486AcetylationAALRAANKSGTGFGE
HHHHHHHHCCCCCCC		45.6026051181
487PhosphorylationALRAANKSGTGFGES
HHHHHHHCCCCCCCC		41.2028555341
489PhosphorylationRAANKSGTGFGESYS
HHHHHCCCCCCCCCC		36.1128555341
494PhosphorylationSGTGFGESYSLANPS
CCCCCCCCCCCCCCC		22.02-
495PhosphorylationGTGFGESYSLANPSI
CCCCCCCCCCCCCCC		11.9127642862
648PhosphorylationFQRVKWQYMVLDEAQ
HHHCCEEEEECCHHH		6.5129759185
659PhosphorylationDEAQALKSSSSVRWK
CHHHHHHCCCCCHHH		35.9829759185
660PhosphorylationEAQALKSSSSVRWKI
HHHHHHCCCCCHHHH		25.6629759185
661PhosphorylationAQALKSSSSVRWKIL
HHHHHCCCCCHHHHH		39.6929759185
662PhosphorylationQALKSSSSVRWKILL
HHHHCCCCCHHHHHH		20.0429759185
724UbiquitinationIESHAENKSAIDENQ
HHHHHHCCCCCCHHH		32.54-
725PhosphorylationESHAENKSAIDENQL
HHHHHCCCCCCHHHH		41.8825002506
740AcetylationSRLHMILKPFMLRRI
HHHHHHHHHHHHHHH		25.8625953088
779UbiquitinationKLLYQALKNKISIED
HHHHHHHHCCCCHHH		60.24-
790PhosphorylationSIEDLLQSSMGSTQQ
CHHHHHHHCCCCCHH		23.43-
834PhosphorylationTWSPFHISLKPYHIS
CCCCEEEEECHHHHH		23.0524719451
880UbiquitinationQRSLFHRKGINEESC
HHHHHHCCCCCHHHH		56.42-
993PhosphorylationQVVHQRRSATSSLRR
HHHHHHHHHCHHHHH		37.7824719451
995PhosphorylationVHQRRSATSSLRRCL
HHHHHHHCHHHHHHH		21.7924719451
996PhosphorylationHQRRSATSSLRRCLL
HHHHHHCHHHHHHHH		27.3924719451
1043O-linked_GlycosylationRVLKEGGSLAAKQCL
HHHHHCCCHHHHHHH		26.2030379171
1098PhosphorylationPGKESLITDSGKLYA
CCCCEEECCCCCCHH		29.4321214269
1100PhosphorylationKESLITDSGKLYALD
CCEEECCCCCCHHHH		29.2221214269
1104PhosphorylationITDSGKLYALDVLLT
ECCCCCCHHHHHHHH		14.4921214269
1123PhosphorylationQGHRVLIYSQMTRMI
CCCEEEEEECHHHHH		6.68-
1124PhosphorylationGHRVLIYSQMTRMID
CCEEEEEECHHHHHH		13.39-
1127PhosphorylationVLIYSQMTRMIDLLE
EEEEECHHHHHHHHH		14.95-
1136PhosphorylationMIDLLEEYMVYRKHT
HHHHHHHHHHHCCCC		5.1922817900
1139PhosphorylationLLEEYMVYRKHTYMR
HHHHHHHHCCCCEEE		9.4522817900
1143PhosphorylationYMVYRKHTYMRLDGS
HHHHCCCCEEECCCC		23.2730108239
1144PhosphorylationMVYRKHTYMRLDGSS
HHHCCCCEEECCCCC		4.6730108239
1150PhosphorylationTYMRLDGSSKISERR
CEEECCCCCCHHHCH		28.2930108239
1151PhosphorylationYMRLDGSSKISERRD
EEECCCCCCHHHCHH		39.2730108239
1154PhosphorylationLDGSSKISERRDMVA
CCCCCCHHHCHHHHH		28.87-
1217UbiquitinationAHRLGQTKQVTVYRL
HHHHCCCCEEEHEEH		34.58-
1250PhosphorylationEIQRMVISGGNFKPD
HHCHHHHCCCCCCCC		29.2720860994
1258PhosphorylationGGNFKPDTLKPKEVV
CCCCCCCCCCHHHHH		45.2520860994
1304PhosphorylationRKRKREKYAEKKKKE
HHHHHHHHHHHHHHH		18.42-
1317UbiquitinationKEDELDGKRRKEGVN
HHHHCCCCCCCCCCC		49.01-
1399PhosphorylationPQSRATNSPASITGS
CCCCCCCCCCCCCCC		19.9326074081
1402PhosphorylationRATNSPASITGSVSD
CCCCCCCCCCCCCCC		24.8626074081
1424MethylationQEMPAAGRGHSARSR
EECCCCCCCCCCCCC		34.62115389305
1429MethylationAGRGHSARSRGRPKG
CCCCCCCCCCCCCCC		29.87115389313
1452PhosphorylationGKGRSRKSTAGSAAA
CCCCCCCCHHHHHHH		23.5223403867
1453PhosphorylationKGRSRKSTAGSAAAM
CCCCCCCHHHHHHHH		37.7623403867
1456PhosphorylationSRKSTAGSAAAMAGA
CCCCHHHHHHHHHHH		16.5722210691
1478PhosphorylationSAAAYAAYGYNVSKG
HHHHHHHHCCCCCCC		16.39-
1487PhosphorylationYNVSKGISASSPLQT
CCCCCCCCCCCCCCC		30.6619691289
1489PhosphorylationVSKGISASSPLQTSL
CCCCCCCCCCCCCCC		26.2121712546
1490PhosphorylationSKGISASSPLQTSLV
CCCCCCCCCCCCCCC		29.3721712546
1494PhosphorylationSASSPLQTSLVRPAG
CCCCCCCCCCCCCCC		31.5428450419
1495PhosphorylationASSPLQTSLVRPAGL
CCCCCCCCCCCCCCC		16.3528450419
1508PhosphorylationGLADFGPSSASSPLS
CCCCCCCCCCCCCCC		38.6326657352
1509PhosphorylationLADFGPSSASSPLSS
CCCCCCCCCCCCCCC		34.9929255136
1511PhosphorylationDFGPSSASSPLSSPL
CCCCCCCCCCCCCCC		34.1429255136
1512PhosphorylationFGPSSASSPLSSPLS
CCCCCCCCCCCCCCC		29.5829255136
1515PhosphorylationSSASSPLSSPLSKGN
CCCCCCCCCCCCCCC		33.0429255136
1516PhosphorylationSASSPLSSPLSKGNN
CCCCCCCCCCCCCCC		37.2329255136
1519PhosphorylationSPLSSPLSKGNNVPG
CCCCCCCCCCCCCCC		41.7329255136
1541PhosphorylationTSSLAPDSLVRKQGK
CCCCCCHHHHHCCCC		27.9228555341
1550PhosphorylationVRKQGKGTNPSGGR-
HHCCCCCCCCCCCC-		47.6517693683
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of INO80_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACTN4_HUMANACTN4physical
20197409
ARP5_HUMANACTR5physical
20197409
ACTB_HUMANACTBphysical
20197409
RUVB1_HUMANRUVBL1physical
21303910
RUVB2_HUMANRUVBL2physical
21303910
ARP5_HUMANACTR5physical
21303910
IN80C_HUMANINO80Cphysical
21303910
IN80B_HUMANINO80Bphysical
21303910
TYY1_HUMANYY1physical
21303910
ACL6A_HUMANACTL6Aphysical
21303910
ARP8_HUMANACTR8physical
21303910
MCRS1_HUMANMCRS1physical
21303910
UCHL5_HUMANUCHL5physical
21303910
IN80D_HUMANINO80Dphysical
21303910
IN80E_HUMANINO80Ephysical
21303910
NFRKB_HUMANNFRKBphysical
21303910
TFPT_HUMANTFPTphysical
21303910
TYY1_HUMANYY1physical
18026119
TBA1B_HUMANTUBA1Bphysical
20237820
TBA1A_HUMANTUBA1Aphysical
22133677
RUVB1_HUMANRUVBL1physical
22939629
NFRKB_HUMANNFRKBphysical
22939629
MBD3_HUMANMBD3physical
22939629
RPA1_HUMANPOLR1Aphysical
22939629
ARP5_HUMANACTR5physical
20855601
DDB1_HUMANDDB1physical
20855601
BAP1_HUMANBAP1physical
25283999
H2A2C_HUMANHIST2H2ACphysical
25283999
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of INO80_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-118, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1490; SER-1512 ANDSER-1516, AND MASS SPECTROMETRY.
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction.";
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
Mol. Cell. Proteomics 6:1952-1967(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1550, AND MASSSPECTROMETRY.

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