REV1_HUMAN - dbPTM
REV1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID REV1_HUMAN
UniProt AC Q9UBZ9
Protein Name DNA repair protein REV1
Gene Name REV1
Organism Homo sapiens (Human).
Sequence Length 1251
Subcellular Localization Nucleus .
Protein Description Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents..
Protein Sequence MRRGGWRKRAENDGWETWGGYMAAKVQKLEEQFRSDAAMQKDGTSSTIFSGVAIYVNGYTDPSAEELRKLMMLHGGQYHVYYSRSKTTHIIATNLPNAKIKELKGEKVIRPEWIVESIKAGRLLSYIPYQLYTKQSSVQKGLSFNPVCRPEDPLPGPSNIAKQLNNRVNHIVKKIETENEVKVNGMNSWNEEDENNDFSFVDLEQTSPGRKQNGIPHPRGSTAIFNGHTPSSNGALKTQDCLVPMVNSVASRLSPAFSQEEDKAEKSSTDFRDCTLQQLQQSTRNTDALRNPHRTNSFSLSPLHSNTKINGAHHSTVQGPSSTKSTSSVSTFSKAAPSVPSKPSDCNFISNFYSHSRLHHISMWKCELTEFVNTLQRQSNGIFPGREKLKKMKTGRSALVVTDTGDMSVLNSPRHQSCIMHVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGTGRAPLRPGANPQLEWQYYQNKILKGKAADIPDSSLWENPDSAQANGIDSVLSRAEIASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILAETKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKIMVRKPGAPVETAKFGGHGICDNIARTVTLDQATDNAKIIGKAMLNMFHTMKLNISDMRGVGIHVNQLVPTNLNPSTCPSRPSVQSSHFPSGSYSVRDVFQVQKAKKSTEEEHKEVFRAAVDLEISSASRTCTFLPPFPAHLPTSPDTNKAESSGKWNGLHTPVSVQSRLNLSIEVPSPSQLDQSVLEALPPDLREQVEQVCAVQQAESHGDKKKEPVNGCNTGILPQPVGTVLLQIPEPQESNSDAGINLIALPAFSQVDPEVFAALPAELQRELKAAYDQRQRQGENSTHQQSASASVPKNPLLHLKAAVKEKKRNKKKKTIGSPKRIQSPLNNKLLNSPAKTLPGACGSPQKLIDGFLKHEGPPAEKPLEELSASTSGVPGLSSLQSDPAGCVRPPAPNLAGAVEFNDVKTLLREWITTISDPMEEDILQVVKYCTDLIEEKDLEKLDLVIKYMKRLMQQSVESVWNMAFDFILDNVQVVLQQTYGSTLKVT
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
28UbiquitinationYMAAKVQKLEEQFRS
HHHHHHHHHHHHHHH		61.93-
99SumoylationATNLPNAKIKELKGE
EECCCCCCHHHHCCC		62.03-
99SumoylationATNLPNAKIKELKGE
EECCCCCCHHHHCCC		62.03-
107UbiquitinationIKELKGEKVIRPEWI
HHHHCCCCCCCCHHH		52.19-
119UbiquitinationEWIVESIKAGRLLSY
HHHHHHHHHHHHHHH		54.81-
134UbiquitinationIPYQLYTKQSSVQKG
CCCEEEECCCCCCCC		34.33-
140UbiquitinationTKQSSVQKGLSFNPV
ECCCCCCCCCCCCCC		60.71-
177PhosphorylationHIVKKIETENEVKVN
HHHHHCCCCCCEEEC		47.8129052541
199PhosphorylationEDENNDFSFVDLEQT
CCCCCCCCEEEHHHC		27.5028348404
206PhosphorylationSFVDLEQTSPGRKQN
CEEEHHHCCCCCCCC		27.7528348404
207PhosphorylationFVDLEQTSPGRKQNG
EEEHHHCCCCCCCCC		25.6728348404
254PhosphorylationNSVASRLSPAFSQEE
HHHHHHHCCCCCHHH		17.0523312004
295PhosphorylationALRNPHRTNSFSLSP
HHHCCCCCCCCCCCC		31.9828450419
297PhosphorylationRNPHRTNSFSLSPLH
HCCCCCCCCCCCCCC		18.6628450419
299PhosphorylationPHRTNSFSLSPLHSN
CCCCCCCCCCCCCCC		27.9728450419
301PhosphorylationRTNSFSLSPLHSNTK
CCCCCCCCCCCCCCC		24.9826055452
305PhosphorylationFSLSPLHSNTKINGA
CCCCCCCCCCCCCCC		54.6129449344
307PhosphorylationLSPLHSNTKINGAHH
CCCCCCCCCCCCCCC		35.9923312004
442UbiquitinationNRPDLKGKPVAVTSN
CCCCCCCCCEEEECC		34.43-
473UbiquitinationEWQYYQNKILKGKAA
CHHHHHHHHHCCCCC		33.61-
541PhosphorylationPNLQAVPYDFHAYKE
CCCCCCCCCHHHHHH		25.33-
546PhosphorylationVPYDFHAYKEVAQTL
CCCCHHHHHHHHHHH		10.10-
607PhosphorylationDQTKCAASVGIGSNI
CCCCHHHHCCCCHHH		11.44-
625UbiquitinationRMATRKAKPDGQYHL
HHHCCCCCCCCCCCC		46.83-
673PhosphorylationKTCGDLQYMTMAKLQ
CCCCCHHHHHHHHHH		11.2330242111
675PhosphorylationCGDLQYMTMAKLQKE
CCCHHHHHHHHHHHH		14.7230242111
678UbiquitinationLQYMTMAKLQKEFGP
HHHHHHHHHHHHHCC		40.40-
687PhosphorylationQKEFGPKTGQMLYRF
HHHHCCCHHHHHHHH		35.46-
692PhosphorylationPKTGQMLYRFCRGLD
CCHHHHHHHHHCCCC		9.0526074081
770UbiquitinationGAPVETAKFGGHGIC
CCCCCCCCCCCCCCC		52.54-
812PhosphorylationHTMKLNISDMRGVGI
HHCCCCHHHHCCCCE		25.04-
885PhosphorylationDLEISSASRTCTFLP
HHEECCCCCCEEECC		30.0326074081
887PhosphorylationEISSASRTCTFLPPF
EECCCCCCEEECCCC		17.2526074081
889PhosphorylationSSASRTCTFLPPFPA
CCCCCCEEECCCCCC		27.8226074081
900PhosphorylationPFPAHLPTSPDTNKA
CCCCCCCCCCCCCCC		60.2926074081
901PhosphorylationFPAHLPTSPDTNKAE
CCCCCCCCCCCCCCC		20.8826074081
904PhosphorylationHLPTSPDTNKAESSG
CCCCCCCCCCCCCCC		41.8426074081
1033UbiquitinationAELQRELKAAYDQRQ
HHHHHHHHHHHHHHH		26.64-
1047PhosphorylationQRQGENSTHQQSASA
HHHCCCCCCCHHCCC		34.9722468782
1076AcetylationKEKKRNKKKKTIGSP
HHHHHHCCCCCCCCC		64.1519413330
1077AcetylationEKKRNKKKKTIGSPK
HHHHHCCCCCCCCCH		57.6819413330
1079PhosphorylationKRNKKKKTIGSPKRI
HHHCCCCCCCCCHHC		39.1823312004
1082PhosphorylationKKKKTIGSPKRIQSP
CCCCCCCCCHHCCCH		24.3323312004
1088PhosphorylationGSPKRIQSPLNNKLL
CCCHHCCCHHHCCCC		29.0530266825
1097PhosphorylationLNNKLLNSPAKTLPG
HHCCCCCCCCCCCCC		26.6330266825
1101PhosphorylationLLNSPAKTLPGACGS
CCCCCCCCCCCCCCC		40.0526552605
1108PhosphorylationTLPGACGSPQKLIDG
CCCCCCCCHHHHHHH		24.8430266825
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 ligaseCDC20Q12834
PMID:23287467
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of REV1_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 REV1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MD2L2_HUMANMAD2L2physical
11485998
PDIP2_HUMANPOLDIP2physical
20554254
HS90A_HUMANHSP90AA1physical
21690293
HS90B_HUMANHSP90AB1physical
21690293
POLK_HUMANPOLKphysical
15189446
MD2L2_HUMANMAD2L2physical
15189446
REV3L_HUMANREV3Lphysical
21926160
MD2L2_HUMANMAD2L2physical
20164194
REV3L_HUMANREV3Lphysical
20164194
POLH_HUMANPOLHphysical
22691049
MD2L2_HUMANMAD2L2physical
12529368
POLH_HUMANPOLHphysical
15380106
POLK_HUMANPOLKphysical
15380106
MD2L2_HUMANMAD2L2physical
15380106
POLK_HUMANPOLKphysical
19170759
POLI_HUMANPOLIphysical
19170759
POLH_HUMANPOLHphysical
19170759
REV1_HUMANREV1physical
19170759
CDC27_HUMANCDC27physical
23287467
MD2L2_HUMANMAD2L2physical
22828282
POLH_HUMANPOLHphysical
22828282
MD2L2_HUMANMAD2L2physical
22859296
PCNA_HUMANPCNAphysical
23761444
BRCA1_HUMANBRCA1physical
23901102
MSH2_HUMANMSH2physical
24038355
DPOD3_HUMANPOLD3physical
23254330
PIAS4_HUMANPIAS4physical
25614517
P53_HUMANTP53physical
25614517
PCNA_HUMANPCNAphysical
25614517
MD2L2_MOUSEMad2l2physical
25614517
FHL2_HUMANFHL2physical
10906324
DPOD3_HUMANPOLD3physical
26982350
POLK_HUMANPOLKphysical
26982350
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 REV1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1082 AND SER-1108, ANDMASS SPECTROMETRY.

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