ARP8_HUMAN - dbPTM
ARP8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARP8_HUMAN
UniProt AC Q9H981
Protein Name Actin-related protein 8
Gene Name ACTR8
Organism Homo sapiens (Human).
Sequence Length 624
Subcellular Localization Nucleus . Chromosome . Specifically localizes to mitotic chromosomes.
Protein Description Plays an important role in the functional organization of mitotic chromosomes. Exhibits low basal ATPase activity, and unable to polymerize.; Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. Required for the recruitment of INO80 (and probably the INO80 complex) to sites of DNA damage. Strongly prefer nucleosomes and H3-H4 tetramers over H2A-H2B dimers, suggesting it may act as a nucleosome recognition module within the complex..
Protein Sequence MTQAEKGDTENGKEKGGEKEKEQRGVKRPIVPALVPESLQEQIQSNFIIVIHPGSTTLRIGRATDTLPASIPHVIARRHKQQGQPLYKDSWLLREGLNKPESNEQRQNGLKMVDQAIWSKKMSNGTRRIPVSPEQARSYNKQMRPAILDHCSGNKWTNTSHHPEYLVGEEALYVNPLDCYNIHWPIRRGQLNIHPGPGGSLTAVLADIEVIWSHAIQKYLEIPLKDLKYYRCILLIPDIYNKQHVKELVNMILMKMGFSGIVVHQESVCATYGSGLSSTCIVDVGDQKTSVCCVEDGVSHRNTRLCLAYGGSDVSRCFYWLMQRAGFPYRECQLTNKMDCLLLQHLKETFCHLDQDISGLQDHEFQIRHPDSPALLYQFRLGDEKLQAPMALFYPATFGIVGQKMTTLQHRSQGDPEDPHDEHYLLATQSKQEQSAKATADRKSASKPIGFEGDLRGQSSDLPERLHSQEVDLGSAQGDGLMAGNDSEEALTALMSRKTAISLFEGKALGLDKAILHSIDCCSSDDTKKKMYSSILVVGGGLMFHKAQEFLQHRILNKMPPSFRRIIENVDVITRPKDMDPRLIAWKGGAVLACLDTTQELWIYQREWQRFGVRMLRERAAFVW
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
1Acetylation-------MTQAEKGD
-------CCCCCCCC		5.9022814378
13UbiquitinationKGDTENGKEKGGEKE
CCCCCCCCCCCCHHH		68.7624816145
88UbiquitinationQQGQPLYKDSWLLRE
HCCCCCCCHHHHHHC		53.6329967540
99UbiquitinationLLREGLNKPESNEQR
HHHCCCCCCCCHHHH		56.03-
114UbiquitinationQNGLKMVDQAIWSKK
HHHHHHHHHHHHHHH		28.7923000965
117UbiquitinationLKMVDQAIWSKKMSN
HHHHHHHHHHHHCCC		3.3823000965
119PhosphorylationMVDQAIWSKKMSNGT
HHHHHHHHHHCCCCC		19.1150563373
120AcetylationVDQAIWSKKMSNGTR
HHHHHHHHHCCCCCE		37.1826051181
132PhosphorylationGTRRIPVSPEQARSY
CCEECCCCHHHHHHC		19.8429255136
138PhosphorylationVSPEQARSYNKQMRP
CCHHHHHHCCCCCCH		35.7526074081
139PhosphorylationSPEQARSYNKQMRPA
CHHHHHHCCCCCCHH		22.3326074081
173PhosphorylationLVGEEALYVNPLDCY
HCCCCEEEECCCCCC		12.7746158875
180PhosphorylationYVNPLDCYNIHWPIR
EECCCCCCCCCCCCC		19.4746158881
219PhosphorylationWSHAIQKYLEIPLKD
HHHHHHHHHCCCHHH		8.0046158887
225UbiquitinationKYLEIPLKDLKYYRC
HHHCCCHHHCCCEEE		56.5123000965
228UbiquitinationEIPLKDLKYYRCILL
CCCHHHCCCEEEEEE		50.8223000965
303PhosphorylationDGVSHRNTRLCLAYG
CCCCCCCCEEEEEEC		25.6020068231
309PhosphorylationNTRLCLAYGGSDVSR
CCEEEEEECCCHHHH		14.7420068231
312PhosphorylationLCLAYGGSDVSRCFY
EEEEECCCHHHHHHH		30.4020068231
315PhosphorylationAYGGSDVSRCFYWLM
EECCCHHHHHHHHHH		28.4620068231
320UbiquitinationDVSRCFYWLMQRAGF
HHHHHHHHHHHHCCC		2.5122817900
329PhosphorylationMQRAGFPYRECQLTN
HHHCCCCHHHCHHCC		19.4574103121
337UbiquitinationRECQLTNKMDCLLLQ
HHCHHCCHHHHHHHH		30.77-
404UbiquitinationTFGIVGQKMTTLQHR
CCEECCCHHCCCCCC		32.08-
406PhosphorylationGIVGQKMTTLQHRSQ
EECCCHHCCCCCCCC		31.2421949786
407PhosphorylationIVGQKMTTLQHRSQG
ECCCHHCCCCCCCCC		22.4121949786
412PhosphorylationMTTLQHRSQGDPEDP
HCCCCCCCCCCCCCC		36.0725159151
424PhosphorylationEDPHDEHYLLATQSK
CCCCCCHHHEECCCH		11.0229978859
428PhosphorylationDEHYLLATQSKQEQS
CCHHHEECCCHHHHH		33.0929978859
430PhosphorylationHYLLATQSKQEQSAK
HHHEECCCHHHHHHH		31.7729978859
431UbiquitinationYLLATQSKQEQSAKA
HHEECCCHHHHHHHH		48.3021906983
435PhosphorylationTQSKQEQSAKATADR
CCCHHHHHHHHHCCC		30.8623917254
443UbiquitinationAKATADRKSASKPIG
HHHHCCCHHCCCCCC		51.4229967540
444PhosphorylationKATADRKSASKPIGF
HHHCCCHHCCCCCCC		38.3725159151
446PhosphorylationTADRKSASKPIGFEG
HCCCHHCCCCCCCCC		46.1663745599
447AcetylationADRKSASKPIGFEGD
CCCHHCCCCCCCCCC		40.1323954790
447UbiquitinationADRKSASKPIGFEGD
CCCHHCCCCCCCCCC		40.1329967540
459PhosphorylationEGDLRGQSSDLPERL
CCCCCCCCCCCCHHH		28.7522210691
460PhosphorylationGDLRGQSSDLPERLH
CCCCCCCCCCCHHHH		34.9722210691
466UbiquitinationSSDLPERLHSQEVDL
CCCCCHHHHCCCCCC		4.3123000965
468PhosphorylationDLPERLHSQEVDLGS
CCCHHHHCCCCCCCC		32.4020740481
475PhosphorylationSQEVDLGSAQGDGLM
CCCCCCCCCCCCCCC		25.3927080861
498UbiquitinationLTALMSRKTAISLFE
HHHHHCCHHHHHHHC		34.6932142685
507UbiquitinationAISLFEGKALGLDKA
HHHHHCCHHHCCCHH		32.9929967540
507MethylationAISLFEGKALGLDKA
HHHHHCCHHHCCCHH		32.99-
507"N6,N6-dimethyllysine"AISLFEGKALGLDKA
HHHHHCCHHHCCCHH		32.99-
513UbiquitinationGKALGLDKAILHSID
CHHHCCCHHHHHHCC		42.2329967540
513AcetylationGKALGLDKAILHSID
CHHHCCCHHHHHHCC		42.2326051181
558UbiquitinationLQHRILNKMPPSFRR
HHHHHHHHCCHHHHH		49.71-
562PhosphorylationILNKMPPSFRRIIEN
HHHHCCHHHHHHHHC		26.0536012747
577UbiquitinationVDVITRPKDMDPRLI
CCEECCCCCCCCCCE		63.4923000965
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 ARP8_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARP8_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 ARP8_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IN80E_HUMANINO80Ephysical
17721549
RUVB1_HUMANRUVBL1physical
17721549
RUVB2_HUMANRUVBL2physical
17721549
ACL6A_HUMANACTL6Aphysical
17721549
IN80C_HUMANINO80Cphysical
17721549
TYY1_HUMANYY1physical
17721549
INO80_HUMANINO80physical
17721549
NFRKB_HUMANNFRKBphysical
17721549
TFPT_HUMANTFPTphysical
17721549
ARP5_HUMANACTR5physical
17721549
IN80B_HUMANINO80Bphysical
17721549
UCHL5_HUMANUCHL5physical
17721549
IN80D_HUMANINO80Dphysical
17721549
MCRS1_HUMANMCRS1physical
17721549
INO80_HUMANINO80physical
22939629
ARP5_HUMANACTR5physical
18163988
H4_YEASTHHF1physical
22977180
H2A1_YEASTHTA1physical
22977180
H2B1_YEASTHTB1physical
22977180
ARP8_HUMANACTR8physical
22977180
DCA10_HUMANDCAF10physical
26186194
NFRKB_HUMANNFRKBphysical
26344197
RUVB1_HUMANRUVBL1physical
28514442
RUVB2_HUMANRUVBL2physical
28514442
DCA10_HUMANDCAF10physical
28514442
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 ARP8_HUMAN

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Related Literatures of Post-Translational Modification
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-412, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, AND MASSSPECTROMETRY.

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