Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 52 (07 Oct 2020)
Sequence version 3 (03 Oct 2012)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

DNA annealing helicase and endonuclease ZRANB3

Gene

ZRANB3

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Protein inferred from homologyi <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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 (By similarity).By similarity

Miscellaneous

In contrast to classical helicases that unwing DNA, annealing helicases rewind it.By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi59 – 66ATPPROSITE-ProRule annotation8
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri617 – 647RanBP2-typePROSITE-ProRule annotationAdd BLAST31

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionEndonuclease, Helicase, Hydrolase, Multifunctional enzyme, Nuclease
Biological processDNA damage, DNA repair
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
DNA annealing helicase and endonuclease ZRANB3
Alternative name(s):
Annealing helicase 2
Short name:
AH2
Zinc finger Ran-binding domain-containing protein 3
Including the following 2 domains:
DNA annealing helicase ZRANB3 (EC:3.6.4.-)
Endonuclease ZRANB3 (EC:3.1.-.-)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ZRANB3
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiBos taurus (Bovine)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9913 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaArtiodactylaRuminantiaPecoraBovidaeBovinaeBos
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000321980 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unassembled WGS sequence
  • UP000009136 Componenti: Unplaced

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Nucleus

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004194891 – 1074DNA annealing helicase and endonuclease ZRANB3Add BLAST1074

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei566PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
E1BB03

PRoteomics IDEntifications database

More...
PRIDEi
E1BB03

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts (via PIP-box and RanBP2-type zinc finger) with PCNA (when PCNA is polyubiquitinated via 'Lys-63'-linked polyubiquitin).

By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9913.ENSBTAP00000038188

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
E1BB03

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini46 – 208Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST163
Domaini325 – 481Helicase C-terminalPROSITE-ProRule annotationAdd BLAST157
Domaini1006 – 1046HNHAdd BLAST41

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni46 – 481DNA annealing helicase activityBy similarityAdd BLAST436
Regioni1006 – 1074Endonuclease activityBy similarityAdd BLAST69

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi157 – 160DEAH box4
Motifi519 – 526PIP-box8
Motifi1069 – 1073APIM motif5

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The PIP-box mediates the interaction with PCNA, while the RanBP2-type zinc finger mediates binding to 'Lys-63'-linked polyubiquitin.By similarity

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the SNF2/RAD54 helicase family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri617 – 647RanBP2-typePROSITE-ProRule annotationAdd BLAST31

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1000, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
E1BB03

Database of Orthologous Groups

More...
OrthoDBi
1082831at2759

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00085, HNHc, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.10810, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR014001, Helicase_ATP-bd
IPR001650, Helicase_C
IPR002711, HNH
IPR003615, HNH_nuc
IPR027417, P-loop_NTPase
IPR038718, SNF2-like_sf
IPR000330, SNF2_N
IPR001876, Znf_RanBP2
IPR036443, Znf_RanBP2_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00271, Helicase_C, 1 hit
PF01844, HNH, 1 hit
PF00176, SNF2_N, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00487, DEXDc, 1 hit
SM00490, HELICc, 1 hit
SM00507, HNHc, 1 hit
SM00547, ZnF_RBZ, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540, SSF52540, 2 hits
SSF90209, SSF90209, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51192, HELICASE_ATP_BIND_1, 1 hit
PS51194, HELICASE_CTER, 1 hit
PS01358, ZF_RANBP2_1, 1 hit
PS50199, ZF_RANBP2_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

E1BB03-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSRGHNIKKS LTPQISCSTS ESYKQLDFLP DKLRAKLLPF QKDGITFALR
60 70 80 90 100
RDGRCMVADE MGLGKTVQAI GIAYFYKEEW PLLIVVPSSL RYPWTEEIEK
110 120 130 140 150
WIPELSPEEI NVIQNKTDVG RISTSKVTVL GYGLLTTDAE TLIDALNNQN
160 170 180 190 200
FKVVIVDESH YMKSRSATRS RILLPIVQKA KRAILLTGTP ALGRPEELFM
210 220 230 240 250
QIEALFPQKF GTWTEYAKRY CNAHVRYFGR RSQWDCRGAS NLNELHQLLS
260 270 280 290 300
DIMIRRLKTE VLTQLPPKIR QRIPFDLPSA AAKELNSSFE EWEKLMRDPY
310 320 330 340 350
SGATETVMGL ITRMFKQTAI AKAGAVKDYI KMMLQNDSLK FLVFAHHLSM
360 370 380 390 400
LQACTEAVIE NKTRYIRIDG SVPSSERIHL VNQFQKDPET RVAILSIQAA
410 420 430 440 450
GQGLTFTAAT HVVFAELYWD PGHIKQAEDR AHRIGQCSSV NIHYLIANGT
460 470 480 490 500
LDTLMWGMLN RKAQVTGSTL NGRKEKLQAE EGDKEKWDFL QFAEAWTPNE
510 520 530 540 550
RSEELRDEML FTHFEKEKQR DIRSFFLPNA KKRQLETSCD ESRVSQEKNT
560 570 580 590 600
IVPADPVKTA TRGDESDLEP EAKKLKSVAI DDPCRPPEEQ PCRPGQAEAL
610 620 630 640 650
LTFGICKAKA QATTPAFCGE GWQCAFCTYI NNSVLPYCEM CENPRGGAVP
660 670 680 690 700
QIDSLNQTQN KNKNEKDDSQ DTSKKIQTSS DGEKQVLAHS TPEPLAKSKE
710 720 730 740 750
EISTTESEDR LTPQPGDEQL KNWPVYDTLM FCASKNTDRI HVYTKDGNQM
760 770 780 790 800
NCNFIPLDIK LDLWEDLPAS FQLKQNRSLI LRFVREWSSL TAMKQKIIKK
810 820 830 840 850
SGQLFRSPVL ALEEIAKQQT KQNSTKRYIT KEDVAAASMD KVKNDGGHVR
860 870 880 890 900
LITKGPKPGD PSTKEFLEGG ECVPFLNPCT AQGDLILKAS TSKGYLQAVD
910 920 930 940 950
NEGNPLCLRC QQPTCQTKQE RKADAWDSRF CSLKCQEEFW IRSNNSYLRA
960 970 980 990 1000
KVFEIEHGVC QLCNLNAQEL FLRLRDAPKS QRKSLLDATW TSKLPLEQLN
1010 1020 1030 1040 1050
EMIRSPGEGH FWQVDHIKPV SGGGGQCSLD NLQTLCTVCH RERTAQQAKE
1060 1070
RSQVRRQSLA SNHGSDITRF LVKK
Length:1,074
Mass (Da):121,768
Last modified:October 3, 2012 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i28D0ABC8FC9C986F
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
DAAA02005001 Genomic DNA No translation available.
DAAA02005002 Genomic DNA No translation available.

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DAAA02005001 Genomic DNA No translation available.
DAAA02005002 Genomic DNA No translation available.

3D structure databases

SMRiE1BB03
ModBaseiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000038188

Proteomic databases

PaxDbiE1BB03
PRIDEiE1BB03

Phylogenomic databases

eggNOGiKOG1000, Eukaryota
InParanoidiE1BB03
OrthoDBi1082831at2759

Family and domain databases

CDDicd00085, HNHc, 1 hit
Gene3Di3.40.50.10810, 1 hit
InterProiView protein in InterPro
IPR014001, Helicase_ATP-bd
IPR001650, Helicase_C
IPR002711, HNH
IPR003615, HNH_nuc
IPR027417, P-loop_NTPase
IPR038718, SNF2-like_sf
IPR000330, SNF2_N
IPR001876, Znf_RanBP2
IPR036443, Znf_RanBP2_sf
PfamiView protein in Pfam
PF00271, Helicase_C, 1 hit
PF01844, HNH, 1 hit
PF00176, SNF2_N, 1 hit
SMARTiView protein in SMART
SM00487, DEXDc, 1 hit
SM00490, HELICc, 1 hit
SM00507, HNHc, 1 hit
SM00547, ZnF_RBZ, 1 hit
SUPFAMiSSF52540, SSF52540, 2 hits
SSF90209, SSF90209, 1 hit
PROSITEiView protein in PROSITE
PS51192, HELICASE_ATP_BIND_1, 1 hit
PS51194, HELICASE_CTER, 1 hit
PS01358, ZF_RANBP2_1, 1 hit
PS50199, ZF_RANBP2_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiZRAB3_BOVIN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: E1BB03
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 3, 2012
Last sequence update: October 3, 2012
Last modified: October 7, 2020
This is version 52 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again