CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013606
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA annealing helicase and endonuclease ZRANB3 
Protein Synonyms/Alias
 Annealing helicase 2; AH2; Zinc finger Ran-binding domain-containing protein 3; DNA annealing helicase ZRANB3; Endonuclease ZRANB3 
Gene Name
 ZRANB3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
36LPDRLRAKLLPFQKDubiquitination[1]
42AKLLPFQKDGIIFALubiquitination[1]
50DGIIFALKRNGRCMVubiquitination[1]
116EINVIQNKTDVRRMSubiquitination[1]
163VDESHYMKSRNATRSubiquitination[1]
179ILLPIVQKARRAILLubiquitination[1]
218GRWTDYAKRYCNAHIubiquitination[1]
230AHIRYFGKRPQWDCRubiquitination[1]
283DLPSAAAKELNTSFEubiquitination[1]
327IAKAGAVKDYIKMMLubiquitination[1]
386HLVNQFQKDPDTRVAubiquitination[1]
518FTHFEKEKQHDIRSFubiquitination[1]
543MTSCDESKRFREENTubiquitination[1]
558VVSSDPTKTAARDIIubiquitination[1]
579EPETKRLKLAASEDHubiquitination[1]
598EETPSQSKQIRTPLVubiquitination[1]
677SQKDTSKKVQTISDCubiquitination[1]
750DRIHIYTKDGKQMSCubiquitination[1]
779LPASFQLKQYRSLILubiquitination[2]
805MKQRIIRKSGQLFCSubiquitination[1]
822LALEEITKQQTKQNCubiquitination[1]
836CTKRYITKEDVAVASubiquitination[1]
923QQPTCQTKQACKANSubiquitination[1]
927CQTKQACKANSWDSRubiquitination[1]
956NNSYLRAKVFETEHGubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983] 
Functional 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. Recruited to the sites of stalled DNA replication by polyubiquitinated PCNA and acts as a structure-specific endonuclease that cleaves the replication fork D-loop intermediate, generating an accessible 3'-OH group in the template of the leading strand, which is amenable to extension by DNA polymerase. In addition to endonuclease activity, also catalyzes the fork regression via annealing helicase activity in order to prevent disintegration of the replication fork and the formation of double-strand breaks. 
Sequence Annotation
 DOMAIN 46 208 Helicase ATP-binding.
 DOMAIN 325 481 Helicase C-terminal.
 DOMAIN 1011 1051 HNH.
 NP_BIND 59 66 ATP (By similarity).
 ZN_FING 621 650 RanBP2-type.
 REGION 46 481 DNA annealing helicase activity.
 REGION 1011 1079 Endonuclease activity.
 MOTIF 157 160 DEAH box.
 MOTIF 519 526 PIP-box.
 MOTIF 1074 1078 APIM motif.
 CROSSLNK 322 322 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Alternative splicing; ATP-binding; Chromosome; Complete proteome; DNA damage; DNA repair; Endonuclease; Helicase; Hydrolase; Isopeptide bond; Metal-binding; Multifunctional enzyme; Nuclease; Nucleotide-binding; Nucleus; Polymorphism; Reference proteome; Ubl conjugation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1079 AA 
Protein Sequence
MPRVHNIKKS LTPHISCVTN ESDNLLDFLP DRLRAKLLPF QKDGIIFALK RNGRCMVADE 60
MGLGKTIQAI GITYFYKEEW PLLIVVPSSL RYPWTEEIEK WIPELSPEEI NVIQNKTDVR 120
RMSTSKVTVL GYGLLTADAK TLIDALNNQN FKVVIVDESH YMKSRNATRS RILLPIVQKA 180
RRAILLTGTP ALGRPEELFM QIEALFPQKF GRWTDYAKRY CNAHIRYFGK RPQWDCRGAS 240
NLNELHQLLS DIMIRRLKTE VLTQLPPKVR QRIPFDLPSA AAKELNTSFE EWEKIMRTPN 300
SGAMETVMGL ITRMFKQTAI AKAGAVKDYI KMMLQNDSLK FLVFAHHLSM LQACTEAVIE 360
NKTRYIRIDG SVSSSERIHL VNQFQKDPDT RVAILSIQAA GQGLTFTAAS HVVFAELYWD 420
PGHIKQAEDR AHRIGQCSSV NIHYLIANGT LDTLMWGMLN RKAQVTGSTL NGRKEKIQAE 480
EGDKEKWDFL QFAEAWTPND SSEELRKEAL FTHFEKEKQH DIRSFFVPQP KKRQLMTSCD 540
ESKRFREENT VVSSDPTKTA ARDIIDYESD VEPETKRLKL AASEDHCSPS EETPSQSKQI 600
RTPLVESVQE AKAQLTTPAF PVEGWQCSLC TYINNSELPY CEMCETPQGS AVMQIDSLNH 660
IQDKNEKDDS QKDTSKKVQT ISDCEKQALA QSEPGQLADS KEETPKIEKE DGLTSQPGNE 720
QWKSSDTLPV YDTLMFCASR NTDRIHIYTK DGKQMSCNFI PLDIKLDLWE DLPASFQLKQ 780
YRSLILRFVR EWSSLTAMKQ RIIRKSGQLF CSPILALEEI TKQQTKQNCT KRYITKEDVA 840
VASMDKVKNV GGHVRLITKE SRPRDPFTKK LLEDGACVPF LNPYTVQADL TVKPSTSKGY 900
LQAVDNEGNP LCLRCQQPTC QTKQACKANS WDSRFCSLKC QEEFWIRSNN SYLRAKVFET 960
EHGVCQLCNV NAQELFLRLR DAPKSQRKNL LYATWTSKLP LEQLNEMIRN PGEGHFWQVD 1020
HIKPVYGGGG QCSLDNLQTL CTVCHKERTA RQAKERSQVR RQSLASKHGS DITRFLVKK 1079 
Gene Ontology
 GO:0043596; C:nuclear replication fork; IDA:UniProtKB.
 GO:0036310; F:annealing helicase activity; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0004520; F:endodeoxyribonuclease activity; IDA:UniProtKB.
 GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
 GO:0070530; F:K63-linked polyubiquitin binding; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006281; P:DNA repair; IDA:UniProtKB.
 GO:0036292; P:DNA rewinding; IDA:UniProtKB.
 GO:0045910; P:negative regulation of DNA recombination; IDA:UniProtKB.
 GO:0031297; P:replication fork processing; IDA:UniProtKB.
 GO:0048478; P:replication fork protection; IDA:UniProtKB.
 GO:0009411; P:response to UV; IDA:UniProtKB. 
Interpro
 IPR014001; Helicase_ATP-bd.
 IPR001650; Helicase_C.
 IPR002711; HNH.
 IPR003615; HNH_nuc.
 IPR027417; P-loop_NTPase.
 IPR000330; SNF2_N.
 IPR001876; Znf_RanBP2. 
Pfam
 PF00271; Helicase_C
 PF01844; HNH
 PF00176; SNF2_N
 PF00641; zf-RanBP 
SMART
 SM00487; DEXDc
 SM00490; HELICc
 SM00507; HNHc
 SM00547; ZnF_RBZ 
PROSITE
 PS51192; HELICASE_ATP_BIND_1
 PS51194; HELICASE_CTER
 PS01358; ZF_RANBP2_1
 PS50199; ZF_RANBP2_2 
PRINTS