POLK_HUMAN - dbPTM
POLK_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID POLK_HUMAN
UniProt AC Q9UBT6
Protein Name DNA polymerase kappa
Gene Name POLK
Organism Homo sapiens (Human).
Sequence Length 870
Subcellular Localization Nucleus . Detected throughout the nucleus and at replication foci (PubMed:12414988). Recruited to DNA damage sites in response to ultraviolet irradiation: N6-methyladenosine (m6A)-containing mRNAs accumulate in the vicinity of DNA damage sites and th
Protein Description DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Depending on the context, it inserts the correct base, but causes frequent base transitions, transversions and frameshifts. Lacks 3'-5' proofreading exonuclease activity. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity..
Protein Sequence MDSTKEKCDSYKDDLLLRMGLNDNKAGMEGLDKEKINKIIMEATKGSRFYGNELKKEKQVNQRIENMMQQKAQITSQQLRKAQLQVDRFAMELEQSRNLSNTIVHIDMDAFYAAVEMRDNPELKDKPIAVGSMSMLSTSNYHARRFGVRAAMPGFIAKRLCPQLIIVPPNFDKYRAVSKEVKEILADYDPNFMAMSLDEAYLNITKHLEERQNWPEDKRRYFIKMGSSVENDNPGKEVNKLSEHERSISPLLFEESPSDVQPPGDPFQVNFEEQNNPQILQNSVVFGTSAQEVVKEIRFRIEQKTTLTASAGIAPNTMLAKVCSDKNKPNGQYQILPNRQAVMDFIKDLPIRKVSGIGKVTEKMLKALGIITCTELYQQRALLSLLFSETSWHYFLHISLGLGSTHLTRDGERKSMSVERTFSEINKAEEQYSLCQELCSELAQDLQKERLKGRTVTIKLKNVNFEVKTRASTVSSVVSTAEEIFAIAKELLKTEIDADFPHPLRLRLMGVRISSFPNEEDRKHQQRSIIGFLQAGNQALSATECTLEKTDKDKFVKPLEMSHKKSFFDKKRSERKWSHQDTFKCEAVNKQSFQTSQPFQVLKKKMNENLEISENSDDCQILTCPVCFRAQGCISLEALNKHVDECLDGPSISENFKMFSCSHVSATKVNKKENVPASSLCEKQDYEAHPKIKEISSVDCIALVDTIDNSSKAESIDALSNKHSKEECSSLPSKSFNIEHCHQNSSSTVSLENEDVGSFRQEYRQPYLCEVKTGQALVCPVCNVEQKTSDLTLFNVHVDVCLNKSFIQELRKDKFNPVNQPKESSRSTGSSSGVQKAVTRTKRPGLMTKYSTSKKIKPNNPKHTLDIFFK
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
12UbiquitinationKEKCDSYKDDLLLRM
HHHHHHHHHHHHHHC		49.03-
25SumoylationRMGLNDNKAGMEGLD
HCCCCCCCCCCCCCC		49.53-
25AcetylationRMGLNDNKAGMEGLD
HCCCCCCCCCCCCCC		49.537308179
25SumoylationRMGLNDNKAGMEGLD
HCCCCCCCCCCCCCC		49.53-
25UbiquitinationRMGLNDNKAGMEGLD
HCCCCCCCCCCCCCC		49.53-
38UbiquitinationLDKEKINKIIMEATK
CCHHHHHHHHHHHHC		36.76-
44PhosphorylationNKIIMEATKGSRFYG
HHHHHHHHCCCCCCC		23.72-
45UbiquitinationKIIMEATKGSRFYGN
HHHHHHHCCCCCCCH		63.03-
55SumoylationRFYGNELKKEKQVNQ
CCCCHHHHHHHHHHH		53.35-
55SumoylationRFYGNELKKEKQVNQ
CCCCHHHHHHHHHHH		53.35-
55UbiquitinationRFYGNELKKEKQVNQ
CCCCHHHHHHHHHHH		53.35-
56UbiquitinationFYGNELKKEKQVNQR
CCCHHHHHHHHHHHH		80.78-
58UbiquitinationGNELKKEKQVNQRIE
CHHHHHHHHHHHHHH		69.31-
71UbiquitinationIENMMQQKAQITSQQ
HHHHHHHHHHHCHHH		25.93-
75PhosphorylationMQQKAQITSQQLRKA
HHHHHHHCHHHHHHH		14.3827174698
76PhosphorylationQQKAQITSQQLRKAQ
HHHHHHCHHHHHHHH		19.9827174698
158UbiquitinationAMPGFIAKRLCPQLI
CCCHHHHHHHCCCEE		40.88-
173UbiquitinationIVPPNFDKYRAVSKE
EECCCHHHHHHHHHH		32.28-
179UbiquitinationDKYRAVSKEVKEILA
HHHHHHHHHHHHHHH		60.99-
218UbiquitinationRQNWPEDKRRYFIKM
HCCCCHHHHHHHHCC		36.79-
224SumoylationDKRRYFIKMGSSVEN
HHHHHHHCCCCCCCC		27.58-
224SumoylationDKRRYFIKMGSSVEN
HHHHHHHCCCCCCCC		27.58-
224UbiquitinationDKRRYFIKMGSSVEN
HHHHHHHCCCCCCCC		27.58-
236UbiquitinationVENDNPGKEVNKLSE
CCCCCCCCHHHHHCC		60.80-
240UbiquitinationNPGKEVNKLSEHERS
CCCCHHHHHCCCCCC		59.57-
247PhosphorylationKLSEHERSISPLLFE
HHCCCCCCCCHHEEC		25.1626074081
249PhosphorylationSEHERSISPLLFEES
CCCCCCCCHHEECCC		15.6726074081
317PhosphorylationSAGIAPNTMLAKVCS
CCCCCCCCCHHHHHC		16.7124719451
326UbiquitinationLAKVCSDKNKPNGQY
HHHHHCCCCCCCCCE		51.05-
328UbiquitinationKVCSDKNKPNGQYQI
HHHCCCCCCCCCEEE		45.67-
347UbiquitinationQAVMDFIKDLPIRKV
HHHHHHHHCCCCCCC		53.88-
353UbiquitinationIKDLPIRKVSGIGKV
HHCCCCCCCCCCCHH		41.28-
359UbiquitinationRKVSGIGKVTEKMLK
CCCCCCCHHHHHHHH		44.02-
371UbiquitinationMLKALGIITCTELYQ
HHHHCCCCCHHHHHH		2.16-
372PhosphorylationLKALGIITCTELYQQ
HHHCCCCCHHHHHHH		16.0822817900
378UbiquitinationITCTELYQQRALLSL
CCHHHHHHHHHHHHH		38.62-
415PhosphorylationTRDGERKSMSVERTF
CCCCCCCCEEEEHHH		23.6330624053
417PhosphorylationDGERKSMSVERTFSE
CCCCCCEEEEHHHHH		28.1124719451
423PhosphorylationMSVERTFSEINKAEE
EEEEHHHHHHHHHHH		36.6324247654
427UbiquitinationRTFSEINKAEEQYSL
HHHHHHHHHHHHHHH		63.94-
433UbiquitinationNKAEEQYSLCQELCS
HHHHHHHHHHHHHHH		23.51-
448UbiquitinationELAQDLQKERLKGRT
HHHHHHHHHHHCCCE		52.69-
461UbiquitinationRTVTIKLKNVNFEVK
CEEEEEECCCCEEEE		54.57-
468UbiquitinationKNVNFEVKTRASTVS
CCCCEEEEECCCCHH		25.70-
479PhosphorylationSTVSSVVSTAEEIFA
CCHHHHHHCHHHHHH		21.53-
486UbiquitinationSTAEEIFAIAKELLK
HCHHHHHHHHHHHHC		13.39-
493UbiquitinationAIAKELLKTEIDADF
HHHHHHHCCCCCCCC		57.65-
494UbiquitinationIAKELLKTEIDADFP
HHHHHHCCCCCCCCC		37.84-
513UbiquitinationLRLMGVRISSFPNEE
HHEEEEEECCCCCHH		3.62-
514UbiquitinationRLMGVRISSFPNEED
HEEEEEECCCCCHHH		18.50-
523UbiquitinationFPNEEDRKHQQRSII
CCCHHHHHHHHHHHH		59.07-
528PhosphorylationDRKHQQRSIIGFLQA
HHHHHHHHHHHHHHH		17.77-
541PhosphorylationQAGNQALSATECTLE
HHHHHEECCEECCEE		35.84-
551UbiquitinationECTLEKTDKDKFVKP
ECCEECCCHHCCCCC		69.12-
557SumoylationTDKDKFVKPLEMSHK
CCHHCCCCCCCCCCC		47.20-
557SumoylationTDKDKFVKPLEMSHK
CCHHCCCCCCCCCCC		47.20-
557UbiquitinationTDKDKFVKPLEMSHK
CCHHCCCCCCCCCCC		47.20-
564UbiquitinationKPLEMSHKKSFFDKK
CCCCCCCCHHHCCCC		42.69-
576UbiquitinationDKKRSERKWSHQDTF
CCCCCCCCCCHHCCC		49.34-
578PhosphorylationKRSERKWSHQDTFKC
CCCCCCCCHHCCCCC		17.8228555341
584SumoylationWSHQDTFKCEAVNKQ
CCHHCCCCCEECCCH		33.00-
584SumoylationWSHQDTFKCEAVNKQ
CCHHCCCCCEECCCH		33.00-
584UbiquitinationWSHQDTFKCEAVNKQ
CCHHCCCCCEECCCH		33.00-
590UbiquitinationFKCEAVNKQSFQTSQ
CCCEECCCHHCCCCC		40.49-
592PhosphorylationCEAVNKQSFQTSQPF
CEECCCHHCCCCCCH		22.41-
593UbiquitinationEAVNKQSFQTSQPFQ
EECCCHHCCCCCCHH		9.46-
603UbiquitinationSQPFQVLKKKMNENL
CCCHHHHHHHHHCCC		52.03-
603UbiquitinationSQPFQVLKKKMNENL
CCCHHHHHHHHHCCC		52.03-
604UbiquitinationQPFQVLKKKMNENLE
CCHHHHHHHHHCCCC		53.76-
605UbiquitinationPFQVLKKKMNENLEI
CHHHHHHHHHCCCCC		45.42-
632UbiquitinationPVCFRAQGCISLEAL
CHHHCCCCCEEHHHH		15.11-
635PhosphorylationFRAQGCISLEALNKH
HCCCCCEEHHHHHHC		25.0028555341
641UbiquitinationISLEALNKHVDECLD
EEHHHHHHCHHHHHC		45.94-
644UbiquitinationEALNKHVDECLDGPS
HHHHHCHHHHHCCCC		40.38-
679PhosphorylationKENVPASSLCEKQDY
CCCCCHHHHCHHCCC		38.86-
682UbiquitinationVPASSLCEKQDYEAH
CCHHHHCHHCCCCCC		60.07-
683UbiquitinationPASSLCEKQDYEAHP
CHHHHCHHCCCCCCC		47.69-
686PhosphorylationSLCEKQDYEAHPKIK
HHCHHCCCCCCCCHH		16.72-
691AcetylationQDYEAHPKIKEISSV
CCCCCCCCHHHCCCC		57.4518603845
691UbiquitinationQDYEAHPKIKEISSV
CCCCCCCCHHHCCCC		57.45-
693UbiquitinationYEAHPKIKEISSVDC
CCCCCCHHHCCCCCE		55.94-
712UbiquitinationDTIDNSSKAESIDAL
ECCCCCCCHHHHHHH		56.87-
715PhosphorylationDNSSKAESIDALSNK
CCCCCHHHHHHHHCC		30.5427251275
720PhosphorylationAESIDALSNKHSKEE
HHHHHHHHCCCCHHH		45.6227251275
722UbiquitinationSIDALSNKHSKEECS
HHHHHHCCCCHHHHH		45.97-
724UbiquitinationDALSNKHSKEECSSL
HHHHCCCCHHHHHCC		43.29-
724PhosphorylationDALSNKHSKEECSSL
HHHHCCCCHHHHHCC		43.2927251275
725UbiquitinationALSNKHSKEECSSLP
HHHCCCCHHHHHCCC		58.20-
729PhosphorylationKHSKEECSSLPSKSF
CCCHHHHHCCCCCCC		37.8827251275
730PhosphorylationHSKEECSSLPSKSFN
CCHHHHHCCCCCCCC		56.8327251275
732UbiquitinationKEECSSLPSKSFNIE
HHHHHCCCCCCCCCE		41.48-
733PhosphorylationEECSSLPSKSFNIEH
HHHHCCCCCCCCCEE		46.3424719451
734UbiquitinationECSSLPSKSFNIEHC
HHHCCCCCCCCCEEC		58.06-
746UbiquitinationEHCHQNSSSTVSLEN
EECCCCCCCCEEECC		37.26-
772UbiquitinationQPYLCEVKTGQALVC
CCEEEEEECCCEEEE		25.33-
814SumoylationIQELRKDKFNPVNQP
HHHHHHCCCCCCCCC		50.50-
814SumoylationIQELRKDKFNPVNQP
HHHHHHCCCCCCCCC		50.50-
814UbiquitinationIQELRKDKFNPVNQP
HHHHHHCCCCCCCCC		50.50-
822UbiquitinationFNPVNQPKESSRSTG
CCCCCCCCCCCCCCC		61.54-
824PhosphorylationPVNQPKESSRSTGSS
CCCCCCCCCCCCCCC		36.8622817900
825PhosphorylationVNQPKESSRSTGSSS
CCCCCCCCCCCCCCH		31.2022817900
827PhosphorylationQPKESSRSTGSSSGV
CCCCCCCCCCCCHHH		38.7817322306
828PhosphorylationPKESSRSTGSSSGVQ
CCCCCCCCCCCHHHH		39.72-
830PhosphorylationESSRSTGSSSGVQKA
CCCCCCCCCHHHHHH		22.7822817900
831PhosphorylationSSRSTGSSSGVQKAV
CCCCCCCCHHHHHHH		32.2422817900
836UbiquitinationGSSSGVQKAVTRTKR
CCCHHHHHHHHCCCC		42.28-
839PhosphorylationSGVQKAVTRTKRPGL
HHHHHHHHCCCCCCC		37.16-
848PhosphorylationTKRPGLMTKYSTSKK
CCCCCCCCEECCCCC		31.69-
849UbiquitinationKRPGLMTKYSTSKKI
CCCCCCCEECCCCCC		24.20-
850PhosphorylationRPGLMTKYSTSKKIK
CCCCCCEECCCCCCC		14.1729083192
851PhosphorylationPGLMTKYSTSKKIKP
CCCCCEECCCCCCCC		27.9729083192
852PhosphorylationGLMTKYSTSKKIKPN
CCCCEECCCCCCCCC		41.2829083192
853PhosphorylationLMTKYSTSKKIKPNN
CCCEECCCCCCCCCC		26.4729083192
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 POLK_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of POLK_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 POLK_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAD18_HUMANRAD18physical
16611994
XRCC1_HUMANXRCC1physical
20227374
DPOD1_HUMANPOLD1physical
20227374
RFA1_HUMANRPA1physical
20227374
PCNA_HUMANPCNAphysical
20227374
PCNA_HUMANPCNAphysical
22157819
RAD18_HUMANRAD18physical
21396873
SHPRH_MOUSEShprhphysical
21396873
REV1_HUMANREV1physical
15189446
MSH2_HUMANMSH2physical
24038355
MCM4_HUMANMCM4physical
24038355
XPO7_HUMANXPO7physical
24038355
MCM6_HUMANMCM6physical
24038355
MSH6_HUMANMSH6physical
24038355
H33_HUMANH3F3Aphysical
26496610
RAD51_HUMANRAD51physical
26496610
RBM4_HUMANRBM4physical
26496610
STAT6_HUMANSTAT6physical
26496610
TIA1_HUMANTIA1physical
26496610
UB2V2_HUMANUBE2V2physical
26496610
PIAS1_HUMANPIAS1physical
26496610
NOLC1_HUMANNOLC1physical
26496610
SRA1_HUMANSRA1physical
26496610
CD2B2_HUMANCD2BP2physical
26496610
APOL2_HUMANAPOL2physical
26496610
RPAP1_HUMANRPAP1physical
26496610
KCTD5_HUMANKCTD5physical
26496610
PLXA3_HUMANPLXNA3physical
26496610
BHE41_HUMANBHLHE41physical
26496610
TUT7_HUMANZCCHC6physical
26496610
FIP1_HUMANFIP1L1physical
26496610
C99L2_HUMANCD99L2physical
26496610
KLF16_HUMANKLF16physical
26496610
PCGF5_HUMANPCGF5physical
26496610
MAK16_HUMANMAK16physical
26496610
SYNP2_HUMANSYNPO2physical
26496610
SBSN_HUMANSBSNphysical
26496610
WRN_HUMANWRNphysical
25294835
PCNA_HUMANPCNAphysical
26903512
REV1_HUMANREV1physical
26903512
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 POLK_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-372, AND MASSSPECTROMETRY.

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