ZRAB3_HUMAN - dbPTM
ZRAB3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZRAB3_HUMAN
UniProt AC Q5FWF4
Protein Name DNA annealing helicase and endonuclease ZRANB3 {ECO:0000305}
Gene Name ZRANB3 {ECO:0000303|PubMed:22759634, ECO:0000312|HGNC:HGNC:25249}
Organism Homo sapiens (Human).
Sequence Length 1079
Subcellular Localization Nucleus . Chromosome . Following DNA damage, recruited to sites of DNA damage and stalled replication forks by polyubiquitinated PCNA (PubMed:22704558, PubMed:22705370, PubMed:22759634).
Protein Description DNA annealing helicase and endonuclease required to maintain genome stability at stalled or collapsed replication forks by facilitating fork restart and limiting inappropriate recombination that could occur during template switching events. [PubMed: 21078962]
Protein Sequence MPRVHNIKKSLTPHISCVTNESDNLLDFLPDRLRAKLLPFQKDGIIFALKRNGRCMVADEMGLGKTIQAIGITYFYKEEWPLLIVVPSSLRYPWTEEIEKWIPELSPEEINVIQNKTDVRRMSTSKVTVLGYGLLTADAKTLIDALNNQNFKVVIVDESHYMKSRNATRSRILLPIVQKARRAILLTGTPALGRPEELFMQIEALFPQKFGRWTDYAKRYCNAHIRYFGKRPQWDCRGASNLNELHQLLSDIMIRRLKTEVLTQLPPKVRQRIPFDLPSAAAKELNTSFEEWEKIMRTPNSGAMETVMGLITRMFKQTAIAKAGAVKDYIKMMLQNDSLKFLVFAHHLSMLQACTEAVIENKTRYIRIDGSVSSSERIHLVNQFQKDPDTRVAILSIQAAGQGLTFTAASHVVFAELYWDPGHIKQAEDRAHRIGQCSSVNIHYLIANGTLDTLMWGMLNRKAQVTGSTLNGRKEKIQAEEGDKEKWDFLQFAEAWTPNDSSEELRKEALFTHFEKEKQHDIRSFFVPQPKKRQLMTSCDESKRFREENTVVSSDPTKTAARDIIDYESDVEPETKRLKLAASEDHCSPSEETPSQSKQIRTPLVESVQEAKAQLTTPAFPVEGWQCSLCTYINNSELPYCEMCETPQGSAVMQIDSLNHIQDKNEKDDSQKDTSKKVQTISDCEKQALAQSEPGQLADSKEETPKIEKEDGLTSQPGNEQWKSSDTLPVYDTLMFCASRNTDRIHIYTKDGKQMSCNFIPLDIKLDLWEDLPASFQLKQYRSLILRFVREWSSLTAMKQRIIRKSGQLFCSPILALEEITKQQTKQNCTKRYITKEDVAVASMDKVKNVGGHVRLITKESRPRDPFTKKLLEDGACVPFLNPYTVQADLTVKPSTSKGYLQAVDNEGNPLCLRCQQPTCQTKQACKANSWDSRFCSLKCQEEFWIRSNNSYLRAKVFETEHGVCQLCNVNAQELFLRLRDAPKSQRKNLLYATWTSKLPLEQLNEMIRNPGEGHFWQVDHIKPVYGGGGQCSLDNLQTLCTVCHKERTARQAKERSQVRRQSLASKHGSDITRFLVKK
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
36UbiquitinationLPDRLRAKLLPFQKD
CCHHHHHHHCCCCCC		44.09-
42UbiquitinationAKLLPFQKDGIIFAL
HHHCCCCCCCEEEEE		59.30-
50UbiquitinationDGIIFALKRNGRCMV
CCEEEEEEECCEEEE		40.15-
116UbiquitinationEINVIQNKTDVRRMS
HCEEECCCCCHHCCC		29.71-
163UbiquitinationVDESHYMKSRNATRS
ECCHHHHHCCCCCCC		38.81-
179UbiquitinationILLPIVQKARRAILL
HHHHHHHHHHHHHHH		32.73-
189PhosphorylationRAILLTGTPALGRPE
HHHHHCCCCCCCCHH		10.51-
218MethylationGRWTDYAKRYCNAHI
CCHHHHHHHHHHHHH		37.36115978033
218UbiquitinationGRWTDYAKRYCNAHI
CCHHHHHHHHHHHHH		37.36-
230UbiquitinationAHIRYFGKRPQWDCR
HHHHHCCCCCCCCCC		51.51-
283UbiquitinationDLPSAAAKELNTSFE
CCCHHHHHHHCCCHH		58.99-
306PhosphorylationPNSGAMETVMGLITR
CCCCHHHHHHHHHHH		11.6030243723
312PhosphorylationETVMGLITRMFKQTA
HHHHHHHHHHHHHHH		22.5630243723
322AcetylationFKQTAIAKAGAVKDY
HHHHHHHHHHHHHHH		41.0425953088
322UbiquitinationFKQTAIAKAGAVKDY
HHHHHHHHHHHHHHH		41.04-
327UbiquitinationIAKAGAVKDYIKMML
HHHHHHHHHHHHHHH		44.26-
365PhosphorylationVIENKTRYIRIDGSV
HHHCCCCEEEEECCC		10.3622461510
371PhosphorylationRYIRIDGSVSSSERI
CEEEEECCCCHHHHH		18.3224719451
374PhosphorylationRIDGSVSSSERIHLV
EEECCCCHHHHHEHH		33.7822461510
375PhosphorylationIDGSVSSSERIHLVN
EECCCCHHHHHEHHH		24.3224719451
386UbiquitinationHLVNQFQKDPDTRVA
EHHHHHHCCCCCCEE		72.94-
390PhosphorylationQFQKDPDTRVAILSI
HHHCCCCCCEEEEEE		32.2224719451
439PhosphorylationHRIGQCSSVNIHYLI
HHHCCCCCCEEEEEE		27.1522210691
444PhosphorylationCSSVNIHYLIANGTL
CCCCEEEEEECCCCH		8.9422210691
468PhosphorylationRKAQVTGSTLNGRKE
CCCCCCCCCCCCHHH		21.9824275569
507UbiquitinationDSSEELRKEALFTHF
CCCHHHHHHHHHHHH		61.02-
518UbiquitinationFTHFEKEKQHDIRSF
HHHHHHHHHCCCHHH		65.09-
543UbiquitinationMTSCDESKRFREENT
HHCCCHHHHHHHHCC		54.21-
558UbiquitinationVVSSDPTKTAARDII
CCCCCCCHHHHHHHH		41.37-
567PhosphorylationAARDIIDYESDVEPE
HHHHHHCCCCCCCCC		13.6123403867
569PhosphorylationRDIIDYESDVEPETK
HHHHCCCCCCCCCHH		40.5025159151
575PhosphorylationESDVEPETKRLKLAA
CCCCCCCHHHHHHHH		31.9823403867
579UbiquitinationEPETKRLKLAASEDH
CCCHHHHHHHHCCCC		39.86-
583PhosphorylationKRLKLAASEDHCSPS
HHHHHHHCCCCCCCC		37.6428450419
588PhosphorylationAASEDHCSPSEETPS
HHCCCCCCCCCCCCC		28.2125849741
590PhosphorylationSEDHCSPSEETPSQS
CCCCCCCCCCCCCCC		31.6028450419
593PhosphorylationHCSPSEETPSQSKQI
CCCCCCCCCCCCCCC		24.9628450419
598UbiquitinationEETPSQSKQIRTPLV
CCCCCCCCCCCCHHH		41.95-
677UbiquitinationSQKDTSKKVQTISDC
CCHHHHHHCEEHHHH		39.07-
686UbiquitinationQTISDCEKQALAQSE
EEHHHHHHHHHHHCC		47.40-
750AcetylationDRIHIYTKDGKQMSC
CEEEEEECCCCEEEC		47.7324889803
750UbiquitinationDRIHIYTKDGKQMSC
CEEEEEECCCCEEEC		47.73-
753AcetylationHIYTKDGKQMSCNFI
EEEECCCCEEECEEE		53.6224889811
779UbiquitinationLPASFQLKQYRSLIL
CCHHHHHHHHHHHHH		34.20-
805UbiquitinationMKQRIIRKSGQLFCS
HHHHHHHHCCCCCHH		48.83-
822AcetylationLALEEITKQQTKQNC
HHHHHHHHHHHHCCC		46.1819829025
822UbiquitinationLALEEITKQQTKQNC
HHHHHHHHHHHHCCC		46.18-
826AcetylationEITKQQTKQNCTKRY
HHHHHHHHCCCCCCC		34.8619829033
836UbiquitinationCTKRYITKEDVAVAS
CCCCCCCHHHEEEEC		42.21-
884PhosphorylationCVPFLNPYTVQADLT
CEECCCCCEEEEEEE		20.6119835603
885PhosphorylationVPFLNPYTVQADLTV
EECCCCCEEEEEEEE		13.8519835603
923UbiquitinationQQPTCQTKQACKANS
CCCCCCCHHHHHCCC		15.26-
927UbiquitinationCQTKQACKANSWDSR
CCCHHHHHCCCCCHH		54.33-
948PhosphorylationQEEFWIRSNNSYLRA
CEEEEECCCCCEEEE		31.0928152594
951PhosphorylationFWIRSNNSYLRAKVF
EEECCCCCEEEEEEE		29.7828152594
952PhosphorylationWIRSNNSYLRAKVFE
EECCCCCEEEEEEEE		11.4328152594
956UbiquitinationNNSYLRAKVFETEHG
CCCEEEEEEEECCCC		40.81-
1023UbiquitinationFWQVDHIKPVYGGGG
CEEEEECCCCCCCCC		25.63-
1057PhosphorylationARQAKERSQVRRQSL
HHHHHHHHHHHHHHH		33.8326074081
1063PhosphorylationRSQVRRQSLASKHGS
HHHHHHHHHHHHCCC		24.8826074081
1066PhosphorylationVRRQSLASKHGSDIT
HHHHHHHHHCCCCHH		30.4023882029
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 ZRAB3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZRAB3_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 ZRAB3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZRAB3_HUMAN !!
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 ZRAB3_HUMAN

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Related Literatures of Post-Translational Modification

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