POLH_HUMAN - dbPTM
POLH_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID POLH_HUMAN
UniProt AC Q9Y253
Protein Name DNA polymerase eta
Gene Name POLH
Organism Homo sapiens (Human).
Sequence Length 713
Subcellular Localization Nucleus . Accumulates at replication forks after DNA damage (PubMed:12606586). After UV irradiation, recruited to DNA damage sites within 1 hour, to a maximum of about 80%
this recruitment may not be not restricted to cells active in DNA replication
Protein Description DNA polymerase specifically involved in the DNA repair by translesion synthesis (TLS). [PubMed: 10385124]
Protein Sequence MATGQDRVVALVDMDCFFVQVEQRQNPHLRNKPCAVVQYKSWKGGGIIAVSYEARAFGVTRSMWADDAKKLCPDLLLAQVRESRGKANLTKYREASVEVMEIMSRFAVIERASIDEAYVDLTSAVQERLQKLQGQPISADLLPSTYIEGLPQGPTTAEETVQKEGMRKQGLFQWLDSLQIDNLTSPDLQLTVGAVIVEEMRAAIERETGFQCSAGISHNKVLAKLACGLNKPNRQTLVSHGSVPQLFSQMPIRKIRSLGGKLGASVIEILGIEYMGELTQFTESQLQSHFGEKNGSWLYAMCRGIEHDPVKPRQLPKTIGCSKNFPGKTALATREQVQWWLLQLAQELEERLTKDRNDNDRVATQLVVSIRVQGDKRLSSLRRCCALTRYDAHKMSHDAFTVIKNCNTSGIQTEWSPPLTMLFLCATKFSASAPSSSTDITSFLSSDPSSLPKVPVTSSEAKTQGSGPAVTATKKATTSLESFFQKAAERQKVKEASLSSLTAPTQAPMSNSPSKPSLPFQTSQSTGTEPFFKQKSLLLKQKQLNNSSVSSPQQNPWSNCKALPNSLPTEYPGCVPVCEGVSKLEESSKATPAEMDLAHNSQSMHASSASKSVLEVTQKATPNPSLLAAEDQVPCEKCGSLVPVWDMPEHMDYHFALELQKSFLQPHSSNPQVVSAVSHQGKRNPKSPLACTNKRPRPEGMQTLESFFKPLTH
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
32UbiquitinationQNPHLRNKPCAVVQY
CCCCCCCCCEEEEEE		34.73-
70UbiquitinationMWADDAKKLCPDLLL
HHHHHHHHHCHHHHH		57.98-
86AcetylationQVRESRGKANLTKYR
HHHHHCCCCCCHHHH		32.7518525633
90PhosphorylationSRGKANLTKYREASV
HCCCCCCHHHHHHHH		26.3227174698
91UbiquitinationRGKANLTKYREASVE
CCCCCCHHHHHHHHH		45.54-
92PhosphorylationGKANLTKYREASVEV
CCCCCHHHHHHHHHH		14.4027174698
96PhosphorylationLTKYREASVEVMEIM
CHHHHHHHHHHHHHH		17.6627174698
104PhosphorylationVEVMEIMSRFAVIER
HHHHHHHHHHHHHHH		29.8824043423
118PhosphorylationRASIDEAYVDLTSAV
HCCCCHHHHHHHHHH		7.7625332170
122PhosphorylationDEAYVDLTSAVQERL
CHHHHHHHHHHHHHH		15.3525332170
123PhosphorylationEAYVDLTSAVQERLQ
HHHHHHHHHHHHHHH		33.4725332170
131 (in isoform 2)Ubiquitination-47.5821906983
131 (in isoform 1)Ubiquitination-47.5821890473
131UbiquitinationAVQERLQKLQGQPIS
HHHHHHHHHCCCCCC		47.5821906983
163SumoylationTAEETVQKEGMRKQG
CHHHHHHHHHHHHCC		52.48-
213PhosphorylationRETGFQCSAGISHNK
HHHCCCCCCCCCCHH		20.8122210691
224AcetylationSHNKVLAKLACGLNK
CCHHHHHHHHCCCCC		32.2419810443
224UbiquitinationSHNKVLAKLACGLNK
CCHHHHHHHHCCCCC		32.24-
231UbiquitinationKLACGLNKPNRQTLV
HHHCCCCCCCCCHHH		49.03-
242PhosphorylationQTLVSHGSVPQLFSQ
CHHHCCCCHHHHHHC		25.79-
311UbiquitinationGIEHDPVKPRQLPKT
CCCCCCCCHHCCCCC		39.61-
317AcetylationVKPRQLPKTIGCSKN
CCHHCCCCCCCCCCC		62.4612656637
323UbiquitinationPKTIGCSKNFPGKTA
CCCCCCCCCCCCCCC		67.68-
369PhosphorylationVATQLVVSIRVQGDK
HEEEEEEEEEECCCH		9.37-
376UbiquitinationSIRVQGDKRLSSLRR
EEEECCCHHHHHHHH		63.16-
379PhosphorylationVQGDKRLSSLRRCCA
ECCCHHHHHHHHHHH		31.2122167270
380PhosphorylationQGDKRLSSLRRCCAL
CCCHHHHHHHHHHHH		30.4122167270
396PhosphorylationRYDAHKMSHDAFTVI
HHHHHHCCCCCEEEE		24.0227251275
401PhosphorylationKMSHDAFTVIKNCNT
HCCCCCEEEECCCCC		24.0427251275
408PhosphorylationTVIKNCNTSGIQTEW
EEECCCCCCCCCCCC		30.4527251275
409PhosphorylationVIKNCNTSGIQTEWS
EECCCCCCCCCCCCC		21.6527251275
413 (in isoform 2)Phosphorylation-37.1828842319
413PhosphorylationCNTSGIQTEWSPPLT
CCCCCCCCCCCCCCH		37.1827251275
416PhosphorylationSGIQTEWSPPLTMLF
CCCCCCCCCCCHHHH		15.4827251275
427PhosphorylationTMLFLCATKFSASAP
HHHHHHHHHCCCCCC		31.4627251275
453UbiquitinationSDPSSLPKVPVTSSE
CCCCCCCCCCCCCHH		65.55-
457O-linked_GlycosylationSLPKVPVTSSEAKTQ
CCCCCCCCCHHHCCC		22.0630059200
462UbiquitinationPVTSSEAKTQGSGPA
CCCCHHHCCCCCCCC		37.0121906983
462 (in isoform 1)Ubiquitination-37.0121890473
486UbiquitinationSLESFFQKAAERQKV
HHHHHHHHHHHHHHH		44.39-
510PhosphorylationAPTQAPMSNSPSKPS
CCCCCCCCCCCCCCC		32.8525159151
512PhosphorylationTQAPMSNSPSKPSLP
CCCCCCCCCCCCCCC		24.2027050516
514PhosphorylationAPMSNSPSKPSLPFQ
CCCCCCCCCCCCCCC		57.9525159151
517PhosphorylationSNSPSKPSLPFQTSQ
CCCCCCCCCCCCCCC		53.0328348404
522PhosphorylationKPSLPFQTSQSTGTE
CCCCCCCCCCCCCCC		29.1628348404
523PhosphorylationPSLPFQTSQSTGTEP
CCCCCCCCCCCCCCC		16.0228348404
547PhosphorylationKQKQLNNSSVSSPQQ
HHHHHCCCCCCCCCC		30.9225627689
548PhosphorylationQKQLNNSSVSSPQQN
HHHHCCCCCCCCCCC		28.3025627689
550PhosphorylationQLNNSSVSSPQQNPW
HHCCCCCCCCCCCCC		37.9425627689
551PhosphorylationLNNSSVSSPQQNPWS
HCCCCCCCCCCCCCC		25.2725627689
566PhosphorylationNCKALPNSLPTEYPG
CCCCCCCCCCCCCCC		33.5126714015
569PhosphorylationALPNSLPTEYPGCVP
CCCCCCCCCCCCCEE		54.1426714015
587PhosphorylationGVSKLEESSKATPAE
CHHHHHHHCCCCHHH		27.9718946034
601PhosphorylationEMDLAHNSQSMHASS
HHHHHHHHCHHCCHH		17.4821242293
603PhosphorylationDLAHNSQSMHASSAS
HHHHHHCHHCCHHHC		16.6226714015
617PhosphorylationSKSVLEVTQKATPNP
CHHHHHHHHCCCCCH		18.2518946034
619UbiquitinationSVLEVTQKATPNPSL
HHHHHHHCCCCCHHH		44.88-
682UbiquitinationSAVSHQGKRNPKSPL
HCEECCCCCCCCCCC		42.2921890473
682 (in isoform 1)Ubiquitination-42.2921890473
686UbiquitinationHQGKRNPKSPLACTN
CCCCCCCCCCCCCCC		69.1520159558
687PhosphorylationQGKRNPKSPLACTNK
CCCCCCCCCCCCCCC		26.8025849741
694UbiquitinationSPLACTNKRPRPEGM
CCCCCCCCCCCCCHH		45.7020159558
709UbiquitinationQTLESFFKPLTH---
HHHHHHHCCCCC---		36.7920159558
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
601SPhosphorylationKinaseATRQ13535
PSP
687SPhosphorylationKinaseCDK2P24941
PSP
-KUbiquitinationE3 ubiquitin ligaseRCHY1Q96PM5
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseDTLQ9NZJ0
PMID:29208956
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of POLH_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 POLH_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PCNA_HUMANPCNAphysical
11585903
REV1_HUMANREV1physical
16824193
RAD18_HUMANRAD18physical
16824193
TBA1B_HUMANTUBA1Bphysical
16824193
TBB5_HUMANTUBBphysical
16824193
UBE2B_HUMANUBE2Bphysical
16824193
PCNA_HUMANPCNAphysical
20159558
RAD18_HUMANRAD18physical
15359278
REV1_HUMANREV1physical
21690293
UBC_HUMANUBCphysical
16763556
PCNA_HUMANPCNAphysical
16763556
REV1_HUMANREV1physical
15189446
REV1_HUMANREV1physical
22691049
HS90A_HUMANHSP90AA1physical
20129057
ZN363_HUMANRCHY1physical
20008555
MDM2_HUMANMDM2physical
22056306
SPRTN_HUMANSPRTNphysical
22902628
MLH1_HUMANMLH1physical
19703417
PCNA_HUMANPCNAphysical
22989887
PCNA_HUMANPCNAphysical
23042605
A4_HUMANAPPphysical
21832049
PCNA_HUMANPCNAphysical
23761444
BRCA1_HUMANBRCA1physical
23901102
FACD2_HUMANFANCD2physical
23388460
PCNA_HUMANPCNAphysical
23388460
PCNA_HUMANPCNAphysical
20129057
TRAIP_HUMANTRAIPphysical
24553286
PALB2_HUMANPALB2physical
24485656
BRCA2_HUMANBRCA2physical
24485656
UBP7_HUMANUSP7physical
25435364
CENPF_HUMANCENPFphysical
26496610
PLD1_HUMANPLD1physical
26496610
DHX16_HUMANDHX16physical
26496610
PACN3_HUMANPACSIN3physical
26496610
SIR7_HUMANSIRT7physical
26496610
GTPB2_HUMANGTPBP2physical
26496610
KNL1_HUMANCASC5physical
26496610
FRYL_HUMANFRYLphysical
26496610
PCNA_HUMANPCNAphysical
24474685
PCNA_HUMANPCNAphysical
27770570
PCNA_HUMANPCNAphysical
26988343
POTEI_HUMANPOTEIphysical
28514442
ACTBL_HUMANACTBL2physical
28514442
ACTB_HUMANACTBphysical
28514442
TBA4A_HUMANTUBA4Aphysical
28514442
AHNK_HUMANAHNAKphysical
28514442
Drug and Disease Associations
Kegg Disease
OMIM Disease
278750Xeroderma pigmentosum variant type (XPV)
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of POLH_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-379 AND SER-380, ANDMASS SPECTROMETRY.
"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-379, 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-379 AND SER-380, ANDMASS SPECTROMETRY.

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