DPOLQ_HUMAN - dbPTM
DPOLQ_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DPOLQ_HUMAN
UniProt AC O75417
Protein Name DNA polymerase theta {ECO:0000303|PubMed:10395804, ECO:0000303|PubMed:14576298, ECO:0000312|HGNC:HGNC:9186}
Gene Name POLQ {ECO:0000303|PubMed:10395804, ECO:0000303|PubMed:14576298, ECO:0000312|HGNC:HGNC:9186}
Organism Homo sapiens (Human).
Sequence Length 2590
Subcellular Localization Nucleus . Chromosome . Enriched in chromatin in response to ultaviolet (UV) light (PubMed:25642963). Binds to chromatin during early G1 (PubMed:24989122).
Protein Description DNA polymerase that promotes microhomology-mediated end-joining (MMEJ), an alternative non-homologous end-joining (NHEJ) machinery triggered in response to double-strand breaks in DNA. [PubMed: 25642963]
Protein Sequence MNLLRRSGKRRRSESGSDSFSGSGGDSSASPQFLSGSVLSPPPGLGRCLKAAAAGECKPTVPDYERDKLLLANWGLPKAVLEKYHSFGVKKMFEWQAECLLLGQVLEGKNLVYSAPTSAGKTLVAELLILKRVLEMRKKALFILPFVSVAKEKKYYLQSLFQEVGIKVDGYMGSTSPSRHFSSLDIAVCTIERANGLINRLIEENKMDLLGMVVVDELHMLGDSHRGYLLELLLTKICYITRKSASCQADLASSLSNAVQIVGMSATLPNLELVASWLNAELYHTDFRPVPLLESVKVGNSIYDSSMKLVREFEPMLQVKGDEDHVVSLCYETICDNHSVLLFCPSKKWCEKLADIIAREFYNLHHQAEGLVKPSECPPVILEQKELLEVMDQLRRLPSGLDSVLQKTVPWGVAFHHAGLTFEERDIIEGAFRQGLIRVLAATSTLSSGVNLPARRVIIRTPIFGGRPLDILTYKQMVGRAGRKGVDTVGESILICKNSEKSKGIALLQGSLKPVRSCLQRREGEEVTGSMIRAILEIIVGGVASTSQDMHTYAACTFLAASMKEGKQGIQRNQESVQLGAIEACVMWLLENEFIQSTEASDGTEGKVYHPTHLGSATLSSSLSPADTLDIFADLQRAMKGFVLENDLHILYLVTPMFEDWTTIDWYRFFCLWEKLPTSMKRVAELVGVEEGFLARCVKGKVVARTERQHRQMAIHKRFFTSLVLLDLISEVPLREINQKYGCNRGQIQSLQQSAAVYAGMITVFSNRLGWHNMELLLSQFQKRLTFGIQRELCDLVRVSLLNAQRARVLYASGFHTVADLARANIVEVEVILKNAVPFKSARKAVDEEEEAVEERRNMRTIWVTGRKGLTEREAAALIVEEARMILQQDLVEMGVQWNPCALLHSSTCSLTHSESEVKEHTFISQTKSSYKKLTSKNKSNTIFSDSYIKHSPNIVQDLNKSREHTSSFNCNFQNGNQEHQTCSIFRARKRASLDINKEKPGASQNEGKTSDKKVVQTFSQKTKKAPLNFNSEKMSRSFRSWKRRKHLKRSRDSSPLKDSGACRIHLQGQTLSNPSLCEDPFTLDEKKTEFRNSGPFAKNVSLSGKEKDNKTSFPLQIKQNCSWNITLTNDNFVEHIVTGSQSKNVTCQATSVVSEKGRGVAVEAEKINEVLIQNGSKNQNVYMKHHDIHPINQYLRKQSHEQTSTITKQKNIIERQMPCEAVSSYINRDSNVTINCERIKLNTEENKPSHFQALGDDISRTVIPSEVLPSAGAFSKSEGQHENFLNISRLQEKTGTYTTNKTKNNHVSDLGLVLCDFEDSFYLDTQSEKIIQQMATENAKLGAKDTNLAAGIMQKSLVQQNSMNSFQKECHIPFPAEQHPLGATKIDHLDLKTVGTMKQSSDSHGVDILTPESPIFHSPILLEENGLFLKKNEVSVTDSQLNSFLQGYQTQETVKPVILLIPQKRTPTGVEGECLPVPETSLNMSDSLLFDSFSDDYLVKEQLPDMQMKEPLPSEVTSNHFSDSLCLQEDLIKKSNVNENQDTHQQLTCSNDESIIFSEMDSVQMVEALDNVDIFPVQEKNHTVVSPRALELSDPVLDEHHQGDQDGGDQDERAEKSKLTGTRQNHSFIWSGASFDLSPGLQRILDKVSSPLENEKLKSMTINFSSLNRKNTELNEEQEVISNLETKQVQGISFSSNNEVKSKIEMLENNANHDETSSLLPRKESNIVDDNGLIPPTPIPTSASKLTFPGILETPVNPWKTNNVLQPGESYLFGSPSDIKNHDLSPGSRNGFKDNSPISDTSFSLQLSQDGLQLTPASSSSESLSIIDVASDQNLFQTFIKEWRCKKRFSISLACEKIRSLTSSKTATIGSRFKQASSPQEIPIRDDGFPIKGCDDTLVVGLAVCWGGRDAYYFSLQKEQKHSEISASLVPPSLDPSLTLKDRMWYLQSCLRKESDKECSVVIYDFIQSYKILLLSCGISLEQSYEDPKVACWLLDPDSQEPTLHSIVTSFLPHELPLLEGMETSQGIQSLGLNAGSEHSGRYRASVESILIFNSMNQLNSLLQKENLQDVFRKVEMPSQYCLALLELNGIGFSTAECESQKHIMQAKLDAIETQAYQLAGHSFSFTSSDDIAEVLFLELKLPPNREMKNQGSKKTLGSTRRGIDNGRKLRLGRQFSTSKDVLNKLKALHPLPGLILEWRRITNAITKVVFPLQREKCLNPFLGMERIYPVSQSHTATGRITFTEPNIQNVPRDFEIKMPTLVGESPPSQAVGKGLLPMGRGKYKKGFSVNPRCQAQMEERAADRGMPFSISMRHAFVPFPGGSILAADYSQLELRILAHLSHDRRLIQVLNTGADVFRSIAAEWKMIEPESVGDDLRQQAKQICYGIIYGMGAKSLGEQMGIKENDAACYIDSFKSRYTGINQFMTETVKNCKRDGFVQTILGRRRYLPGIKDNNPYRKAHAERQAINTIVQGSAADIVKIATVNIQKQLETFHSTFKSHGHREGMLQSDQTGLSRKRKLQGMFCPIRGGFFILQLHDELLYEVAEEDVVQVAQIVKNEMESAVKLSVKLKVKVKIGASWGELKDFDV
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
13 (in isoform 2)Phosphorylation-34.0122617229
15PhosphorylationGKRRRSESGSDSFSG
CCCCCCCCCCCCCCC		44.86-
23PhosphorylationGSDSFSGSGGDSSAS
CCCCCCCCCCCCCCC		38.10-
30PhosphorylationSGGDSSASPQFLSGS
CCCCCCCCCCHHCCC		22.6028387310
35PhosphorylationSASPQFLSGSVLSPP
CCCCCHHCCCCCCCC		30.2528387310
37PhosphorylationSPQFLSGSVLSPPPG
CCCHHCCCCCCCCCC		19.2628387310
60PhosphorylationAAGECKPTVPDYERD
HCCCCCCCCCCHHHH		30.1126074081
64PhosphorylationCKPTVPDYERDKLLL
CCCCCCCHHHHHHHH		13.5423663014
84PhosphorylationPKAVLEKYHSFGVKK
CHHHHHHHHHCCCHH		8.04-
117PhosphorylationNLVYSAPTSAGKTLV
CEEEECCCHHCHHHH		30.81-
171PhosphorylationVGIKVDGYMGSTSPS
HCCEECCCCCCCCCC		8.21-
176PhosphorylationDGYMGSTSPSRHFSS
CCCCCCCCCCCCCCC		23.6817192257
308UbiquitinationSIYDSSMKLVREFEP
CHHHHHHHHHHHHHC		45.86-
421PhosphorylationAFHHAGLTFEERDII
HHHCCCCCCHHHHHH		28.2526074081
475UbiquitinationPLDILTYKQMVGRAG
EEEHHHHHHHHCCCC		27.04-
484UbiquitinationMVGRAGRKGVDTVGE
HHCCCCCCCCCCCCC		63.47-
497UbiquitinationGESILICKNSEKSKG
CCCEEEECCCCCCCC		57.42-
513UbiquitinationALLQGSLKPVRSCLQ
EEECCCCHHHHHHHH		43.07-
557PhosphorylationMHTYAACTFLAASMK
HHHHHHHHHHHHHHH		19.56-
750PhosphorylationCNRGQIQSLQQSAAV
CCHHHHHHHHHHHHH		29.76-
786PhosphorylationSQFQKRLTFGIQREL
HHHHHHHCHHHHHHH		24.6922210691
844UbiquitinationVPFKSARKAVDEEEE
CCHHHHHHCCCHHHH		53.10-
925PhosphorylationVKEHTFISQTKSSYK
HHHCEEEECCHHHHH		27.8325159151
928UbiquitinationHTFISQTKSSYKKLT
CEEEECCHHHHHHHC		29.75-
947PhosphorylationSNTIFSDSYIKHSPN
CCCCCCCHHHCCCCC		27.7921815630
950UbiquitinationIFSDSYIKHSPNIVQ
CCCCHHHCCCCCHHH		29.78-
952PhosphorylationSDSYIKHSPNIVQDL
CCHHHCCCCCHHHHC		18.0325159151
961UbiquitinationNIVQDLNKSREHTSS
CHHHHCHHCCCCCCC		59.18-
990AcetylationCSIFRARKRASLDIN
EHHHHCHHHHCCCCC		51.8619608861
993PhosphorylationFRARKRASLDINKEK
HHCHHHHCCCCCCCC		30.5228102081
998AcetylationRASLDINKEKPGASQ
HHCCCCCCCCCCCCC		73.177824939
1000AcetylationSLDINKEKPGASQNE
CCCCCCCCCCCCCCC		50.8118586509
1009AcetylationGASQNEGKTSDKKVV
CCCCCCCCCCCHHHH		38.3818586517
1018PhosphorylationSDKKVVQTFSQKTKK
CCHHHHHHHHHHCCC		17.40-
1020PhosphorylationKKVVQTFSQKTKKAP
HHHHHHHHHHCCCCC		33.87-
1034UbiquitinationPLNFNSEKMSRSFRS
CCCCCHHHHHHHHHH		41.83-
1054PhosphorylationHLKRSRDSSPLKDSG
HHHCCCCCCCCCCCC		32.5123312004
1055PhosphorylationLKRSRDSSPLKDSGA
HHCCCCCCCCCCCCC		38.2423312004
1060PhosphorylationDSSPLKDSGACRIHL
CCCCCCCCCCEEEEE		27.0623312004
1089O-linked_GlycosylationFTLDEKKTEFRNSGP
CCCCHHHHCCCCCCC		51.9630379171
1147PhosphorylationGSQSKNVTCQATSVV
CCCCCCEEEEEEEEE		14.3224719451
1155PhosphorylationCQATSVVSEKGRGVA
EEEEEEECCCCCCEE		31.2824719451
1248UbiquitinationKLNTEENKPSHFQAL
ECCCCCCCCCHHHHC		51.70-
1260PhosphorylationQALGDDISRTVIPSE
HHCCCCHHCCCCCHH		28.9718452278
1277UbiquitinationPSAGAFSKSEGQHEN
CCCCCCCCCCCCCCC		46.18-
1289PhosphorylationHENFLNISRLQEKTG
CCCCCCHHHHHHHCC		26.3521712546
1294UbiquitinationNISRLQEKTGTYTTN
CHHHHHHHCCCCCCC		39.02-
1295PhosphorylationISRLQEKTGTYTTNK
HHHHHHHCCCCCCCC		33.72-
1299PhosphorylationQEKTGTYTTNKTKNN
HHHCCCCCCCCCCCC		24.59-
1300PhosphorylationEKTGTYTTNKTKNNH
HHCCCCCCCCCCCCC		25.05-
1341UbiquitinationQMATENAKLGAKDTN
HHHHHCHHCCCCCCH		60.06-
1345UbiquitinationENAKLGAKDTNLAAG
HCHHCCCCCCHHHHH		64.39-
1347PhosphorylationAKLGAKDTNLAAGIM
HHCCCCCCHHHHHHH		31.27-
1357PhosphorylationAAGIMQKSLVQQNSM
HHHHHHHHHHHHHCC		19.5125849741
1363PhosphorylationKSLVQQNSMNSFQKE
HHHHHHHCCHHHHHH		18.2725849741
1366PhosphorylationVQQNSMNSFQKECHI
HHHHCCHHHHHHCCC		22.0325849741
1414PhosphorylationVDILTPESPIFHSPI
CCEECCCCCCCCCCE		25.2125159151
1584PhosphorylationPVQEKNHTVVSPRAL
ECCCCCCEEECCCCE		31.8128102081
1587PhosphorylationEKNHTVVSPRALELS
CCCCEEECCCCEECC		12.3425159151
1650PhosphorylationQRILDKVSSPLENEK
HHHHHHCCCCCCCHH		31.7929214152
1651PhosphorylationRILDKVSSPLENEKL
HHHHHCCCCCCCHHH		36.1725159151
1660O-linked_GlycosylationLENEKLKSMTINFSS
CCCHHHHHCEECHHH		31.4330379171
1660PhosphorylationLENEKLKSMTINFSS
CCCHHHHHCEECHHH		31.43-
1667PhosphorylationSMTINFSSLNRKNTE
HCEECHHHHCCCCCC		26.06-
1671UbiquitinationNFSSLNRKNTELNEE
CHHHHCCCCCCCCHH		68.12-
1683PhosphorylationNEEQEVISNLETKQV
CHHHHHHHHCCCCEE		40.30-
1687PhosphorylationEVISNLETKQVQGIS
HHHHHCCCCEECCEE		29.91-
1694PhosphorylationTKQVQGISFSSNNEV
CCEECCEECCCCHHH		26.3728555341
1745PhosphorylationTPIPTSASKLTFPGI
CCCCCCCCCCCCCCC		28.1521712546
1776PhosphorylationGESYLFGSPSDIKNH
CCEECCCCHHHHCCC		17.5625627689
1786PhosphorylationDIKNHDLSPGSRNGF
HHCCCCCCCCCCCCC		33.0223663014
1789PhosphorylationNHDLSPGSRNGFKDN
CCCCCCCCCCCCCCC		26.4229449344
1866UbiquitinationIRSLTSSKTATIGSR
HHHCCCCCCEECCHH		41.78-
1879PhosphorylationSRFKQASSPQEIPIR
HHHCCCCCCCCCCCC		33.3525627689
1938PhosphorylationVPPSLDPSLTLKDRM
CCCCCCCCCCHHHHH		33.3824719451
1940PhosphorylationPSLDPSLTLKDRMWY
CCCCCCCCHHHHHHH		35.78-
1947PhosphorylationTLKDRMWYLQSCLRK
CHHHHHHHHHHHHCC		5.8728060719
1961PhosphorylationKESDKECSVVIYDFI
CCCCCCCCCHHHHHH		22.1022468782
1965PhosphorylationKECSVVIYDFIQSYK
CCCCCHHHHHHHHHH		8.0027732954
1970PhosphorylationVIYDFIQSYKILLLS
HHHHHHHHHHHHHHH		24.4727732954
1971PhosphorylationIYDFIQSYKILLLSC
HHHHHHHHHHHHHHC		5.9127732954
1977PhosphorylationSYKILLLSCGISLEQ
HHHHHHHHCCCCHHH		15.4022468782
1981PhosphorylationLLLSCGISLEQSYED
HHHHCCCCHHHHCCC		15.9022468782
2056PhosphorylationESILIFNSMNQLNSL
HHHHHHCCHHHHHHH		14.3624719451
2154PhosphorylationREMKNQGSKKTLGST
HHHCCCCCCCCCCCC		22.6329083192
2157PhosphorylationKNQGSKKTLGSTRRG
CCCCCCCCCCCCCCC		39.8429083192
2160PhosphorylationGSKKTLGSTRRGIDN
CCCCCCCCCCCCCCC		23.1229083192
2161PhosphorylationSKKTLGSTRRGIDNG
CCCCCCCCCCCCCCC		23.6929083192
2179PhosphorylationRLGRQFSTSKDVLNK
CCCCCCCCCHHHHHH		40.87-
2262PhosphorylationDFEIKMPTLVGESPP
CEEECCCEECCCCCC		30.4928634298
2267PhosphorylationMPTLVGESPPSQAVG
CCEECCCCCCHHCCC		35.8625159151
2270PhosphorylationLVGESPPSQAVGKGL
ECCCCCCHHCCCCCC		33.8728634298
2311PhosphorylationADRGMPFSISMRHAF
HHCCCCCEEEEECCC		14.1020860994
2313PhosphorylationRGMPFSISMRHAFVP
CCCCCEEEEECCCCC		14.4720860994
2397PhosphorylationIYGMGAKSLGEQMGI
HHCCCHHHHHHHHCC		40.86-
2412PhosphorylationKENDAACYIDSFKSR
CCCCCEEEECCHHHH		11.75-
2417UbiquitinationACYIDSFKSRYTGIN
EEEECCHHHHCCCHH		37.67-
2430PhosphorylationINQFMTETVKNCKRD
HHHHHHHHHHHCCCC		27.84-
2432UbiquitinationQFMTETVKNCKRDGF
HHHHHHHHHCCCCCH		65.14-
2449PhosphorylationTILGRRRYLPGIKDN
HHCCCCCCCCCCCCC		18.5518083107
2471PhosphorylationAERQAINTIVQGSAA
HHHHHHHHHHHCCHH		19.20-
2497PhosphorylationKQLETFHSTFKSHGH
HHHHHHHHHHHHCCC		31.2024260401
2511PhosphorylationHREGMLQSDQTGLSR
CCCCCCCCCCCCCCH		27.94-
2544PhosphorylationQLHDELLYEVAEEDV
EECHHHHHHHCHHHH		22.4523879269
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
-KUbiquitinationE3 ubiquitin ligaseRCHY1Q96PM5
PMID:21791603
-KUbiquitinationE3 ubiquitin ligaseMDM2Q00987
PMID:22056306
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

Oops, there are no PPI records of DPOLQ_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
114480Breast cancer (BC)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DPOLQ_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-990, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1651, AND MASSSPECTROMETRY.

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