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Protein

DNA annealing helicase and endonuclease ZRANB3

Gene

ZRANB3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.5 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi59 – 66ATPPROSITE-ProRule annotation8
Zinc fingeri621 – 650RanBP2-typePROSITE-ProRule annotationAdd BLAST30

GO - Molecular functioni

  • annealing helicase activity Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • endodeoxyribonuclease activity Source: UniProtKB
  • helicase activity Source: UniProtKB-KW
  • K63-linked polyubiquitin binding Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • cellular response to DNA damage stimulus Source: UniProtKB
  • DNA repair Source: UniProtKB
  • DNA rewinding Source: UniProtKB
  • negative regulation of DNA recombination Source: UniProtKB
  • replication fork processing Source: UniProtKB
  • replication fork protection Source: UniProtKB
  • response to UV Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Helicase, Hydrolase, Nuclease

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Names & Taxonomyi

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.-.-)
Gene namesi
Name:ZRANB3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:25249. ZRANB3.

Subcellular locationi

  • Nucleus
  • Chromosome

  • Note: Following DNA damage, recruited to sites of DNA damage and stalled replication forks by polyubiquitinated PCNA.

GO - Cellular componenti

  • nuclear replication fork Source: UniProtKB
  • nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi65K → R: Abolishes ATPase activity. Abolishes endonuclease activity; when associated with A-1021. 1 Publication1
Mutagenesisi157 – 158DE → AA: Abolishes fork regression activity. 1 Publication2
Mutagenesisi163K → D: Loss of DNA-dependent ATPase activity. 1 Publication1
Mutagenesisi519Q → A: Abolishes interaction with PCNA; when associated with A-522; 525-A-A-526 and A-1075. Abolishes interaction with PCNA; when associated with A-525. 3 Publications1
Mutagenesisi522I → A: Abolishes interaction with PCNA; when associated with A-519; 525-A-A-526 and A-1075. 1 Publication1
Mutagenesisi525 – 526FF → AA: Abolishes interaction with PCNA; when associated with A-519; A-522 and A-1075. 2 Publications2
Mutagenesisi525F → A: Abolishes interaction with PCNA; when associated with A-519. 1 Publication1
Mutagenesisi625W → A: Abolishes interaction with 'Lys-63'-linked polyubiquitin. 1 Publication1
Mutagenesisi631 – 632TY → AA: Abolishes interaction with 'Lys-63'-linked polyubiquitin. 2
Mutagenesisi631T → A: Impaired interaction with 'Lys-63'-linked polyubiquitin. 2 Publications1
Mutagenesisi632Y → A: Abolishes interaction with 'Lys-63'-linked polyubiquitin. 1 Publication1
Mutagenesisi634N → A: Abolishes interaction with 'Lys-63'-linked polyubiquitin. 1 Publication1
Mutagenesisi643M → A: Impaired interaction with polyubiquitin. 1 Publication1
Mutagenesisi762 – 764LDI → AAA: Loss of DNA-binding, DNA-dependent ATPase and nuclease activities. 1 Publication3
Mutagenesisi792 – 794WSS → AAA: Loss of DNA-dependent ATPase activity. 1 Publication3
Mutagenesisi1021H → A: Does not affect endonuclease. Abolishes endonuclease activity; when associated with R-65. 1 Publication1
Mutagenesisi1075F → A: Abolishes interaction with PCNA; when associated with A-519; A-522 and 525-A-A-526. 1 Publication1

Organism-specific databases

DisGeNETi84083.
OpenTargetsiENSG00000121988.
PharmGKBiPA134871612.

Polymorphism and mutation databases

BioMutaiZRANB3.
DMDMi74741477.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002781821 – 1079DNA annealing helicase and endonuclease ZRANB3Add BLAST1079

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei569PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ5FWF4.
MaxQBiQ5FWF4.
PaxDbiQ5FWF4.
PeptideAtlasiQ5FWF4.
PRIDEiQ5FWF4.

PTM databases

iPTMnetiQ5FWF4.
PhosphoSitePlusiQ5FWF4.

Expressioni

Gene expression databases

BgeeiENSG00000121988.
CleanExiHS_ZRANB3.
ExpressionAtlasiQ5FWF4. baseline and differential.
GenevisibleiQ5FWF4. HS.

Organism-specific databases

HPAiHPA035234.
HPA043073.
HPA043301.

Interactioni

Subunit structurei

Interacts (via PIP-box and RanBP2-type zinc finger) with PCNA (when PCNA is polyubiquitinated via 'Lys-63'-linked polyubiquitin).3 Publications

GO - Molecular functioni

  • K63-linked polyubiquitin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi123877. 9 interactors.
STRINGi9606.ENSP00000264159.

Structurei

3D structure databases

ProteinModelPortaliQ5FWF4.
SMRiQ5FWF4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini46 – 208Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST163
Domaini325 – 481Helicase C-terminalPROSITE-ProRule annotationAdd BLAST157
Domaini1011 – 1051HNHAdd BLAST41

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni46 – 481DNA annealing helicase activityAdd BLAST436
Regioni1011 – 1079Endonuclease activityAdd BLAST69

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi157 – 160DEAH box4
Motifi519 – 526PIP-box8
Motifi1074 – 1078APIM motif5

Domaini

The PIP-box mediates the interaction with PCNA, while the RanBP2-type zinc finger mediates binding to 'Lys-63'-linked polyubiquitin (PubMed:22704558, PubMed:22705370 and PubMed:22759634).3 Publications

Sequence similaritiesi

Belongs to the SNF2/RAD54 helicase family.Curated
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
Contains 1 HNH domain.Curated
Contains 1 RanBP2-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri621 – 650RanBP2-typePROSITE-ProRule annotationAdd BLAST30

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG1000. Eukaryota.
COG0553. LUCA.
GeneTreeiENSGT00860000133750.
HOGENOMiHOG000031233.
HOVERGENiHBG062387.
InParanoidiQ5FWF4.
OMAiCNLNAQE.
OrthoDBiEOG091G0A1B.
PhylomeDBiQ5FWF4.
TreeFamiTF354227.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR002711. HNH.
IPR003615. HNH_nuc.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
IPR001876. Znf_RanBP2.
[Graphical view]
PfamiPF00271. Helicase_C. 1 hit.
PF01844. HNH. 1 hit.
PF00176. SNF2_N. 1 hit.
PF00641. zf-RanBP. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00507. HNHc. 1 hit.
SM00547. ZnF_RBZ. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
SSF90209. SSF90209. 1 hit.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5FWF4-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPRVHNIKKS LTPHISCVTN ESDNLLDFLP DRLRAKLLPF QKDGIIFALK
60 70 80 90 100
RNGRCMVADE MGLGKTIQAI GITYFYKEEW PLLIVVPSSL RYPWTEEIEK
110 120 130 140 150
WIPELSPEEI NVIQNKTDVR RMSTSKVTVL GYGLLTADAK TLIDALNNQN
160 170 180 190 200
FKVVIVDESH YMKSRNATRS RILLPIVQKA RRAILLTGTP ALGRPEELFM
210 220 230 240 250
QIEALFPQKF GRWTDYAKRY CNAHIRYFGK RPQWDCRGAS NLNELHQLLS
260 270 280 290 300
DIMIRRLKTE VLTQLPPKVR QRIPFDLPSA AAKELNTSFE EWEKIMRTPN
310 320 330 340 350
SGAMETVMGL ITRMFKQTAI AKAGAVKDYI KMMLQNDSLK FLVFAHHLSM
360 370 380 390 400
LQACTEAVIE NKTRYIRIDG SVSSSERIHL VNQFQKDPDT RVAILSIQAA
410 420 430 440 450
GQGLTFTAAS HVVFAELYWD PGHIKQAEDR AHRIGQCSSV NIHYLIANGT
460 470 480 490 500
LDTLMWGMLN RKAQVTGSTL NGRKEKIQAE EGDKEKWDFL QFAEAWTPND
510 520 530 540 550
SSEELRKEAL FTHFEKEKQH DIRSFFVPQP KKRQLMTSCD ESKRFREENT
560 570 580 590 600
VVSSDPTKTA ARDIIDYESD VEPETKRLKL AASEDHCSPS EETPSQSKQI
610 620 630 640 650
RTPLVESVQE AKAQLTTPAF PVEGWQCSLC TYINNSELPY CEMCETPQGS
660 670 680 690 700
AVMQIDSLNH IQDKNEKDDS QKDTSKKVQT ISDCEKQALA QSEPGQLADS
710 720 730 740 750
KEETPKIEKE DGLTSQPGNE QWKSSDTLPV YDTLMFCASR NTDRIHIYTK
760 770 780 790 800
DGKQMSCNFI PLDIKLDLWE DLPASFQLKQ YRSLILRFVR EWSSLTAMKQ
810 820 830 840 850
RIIRKSGQLF CSPILALEEI TKQQTKQNCT KRYITKEDVA VASMDKVKNV
860 870 880 890 900
GGHVRLITKE SRPRDPFTKK LLEDGACVPF LNPYTVQADL TVKPSTSKGY
910 920 930 940 950
LQAVDNEGNP LCLRCQQPTC QTKQACKANS WDSRFCSLKC QEEFWIRSNN
960 970 980 990 1000
SYLRAKVFET EHGVCQLCNV NAQELFLRLR DAPKSQRKNL LYATWTSKLP
1010 1020 1030 1040 1050
LEQLNEMIRN PGEGHFWQVD HIKPVYGGGG QCSLDNLQTL CTVCHKERTA
1060 1070
RQAKERSQVR RQSLASKHGS DITRFLVKK
Length:1,079
Mass (Da):123,248
Last modified:July 5, 2005 - v2
Checksum:i7B65AB9568B15AAE
GO
Isoform 2 (identifier: Q5FWF4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-535: Missing.
     718-719: Missing.
     1077-1079: VKK → ETSKLHESHKVTGAEQGLQVSGLPDSAAPEGGAAHTNDQRRCQRMKQPLTEVQILSHSS

Note: No experimental confirmation available.
Show »
Length:598
Mass (Da):67,670
Checksum:i567D1E8DFC2E3D9E
GO
Isoform 3 (identifier: Q5FWF4-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     718-719: Missing.

Show »
Length:1,077
Mass (Da):123,077
Checksum:i6C4DC8DE47A66A80
GO
Isoform 4 (identifier: Q5FWF4-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-642: Missing.
     718-719: Missing.

Note: No experimental confirmation available.
Show »
Length:435
Mass (Da):49,723
Checksum:i6BFECF747A79E306
GO
Isoform 5 (identifier: Q5FWF4-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-60: Missing.
     403-428: GLTFTAASHVVFAELYWDPGHIKQAE → DLYDKVAWGKRTLVSGLFMECFCFVP
     429-1079: Missing.

Note: No experimental confirmation available.
Show »
Length:368
Mass (Da):42,179
Checksum:i5D491F23DDE285D4
GO

Sequence cautioni

The sequence AAX93066 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence BAG54763 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAG65387 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence EAX11631 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence EAX11633 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti366I → T in BAC04536 (PubMed:14702039).Curated1
Sequence conflicti700S → I in BAG65387 (PubMed:14702039).Curated1
Sequence conflicti847V → A in BAG54763 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_030671541E → K.Corresponds to variant rs935615dbSNPEnsembl.1
Natural variantiVAR_030672546R → Q.Corresponds to variant rs7608121dbSNPEnsembl.1
Natural variantiVAR_061237637E → V.Corresponds to variant rs59900519dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0441751 – 642Missing in isoform 4. 1 PublicationAdd BLAST642
Alternative sequenceiVSP_0231381 – 535Missing in isoform 2. 1 PublicationAdd BLAST535
Alternative sequenceiVSP_0441761 – 60Missing in isoform 5. 1 PublicationAdd BLAST60
Alternative sequenceiVSP_044177403 – 428GLTFT…IKQAE → DLYDKVAWGKRTLVSGLFME CFCFVP in isoform 5. 1 PublicationAdd BLAST26
Alternative sequenceiVSP_044178429 – 1079Missing in isoform 5. 1 PublicationAdd BLAST651
Alternative sequenceiVSP_023139718 – 719Missing in isoform 2, isoform 3 and isoform 4. 3 Publications2
Alternative sequenceiVSP_0231401077 – 1079VKK → ETSKLHESHKVTGAEQGLQV SGLPDSAAPEGGAAHTNDQR RCQRMKQPLTEVQILSHSS in isoform 2. 1 Publication3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL136824 mRNA. Translation: CAB66758.1.
AK095362 mRNA. Translation: BAC04536.1.
AK131303 mRNA. Translation: BAG54763.1. Different initiation.
AK304601 mRNA. Translation: BAG65387.1. Different initiation.
BX647838 mRNA. No translation available.
AC012450 Genomic DNA. No translation available.
AC016742 Genomic DNA. No translation available.
AC017031 Genomic DNA. Translation: AAX93066.1. Sequence problems.
AC020602 Genomic DNA. No translation available.
AC064850 Genomic DNA. No translation available.
CH471058 Genomic DNA. Translation: EAX11631.1. Sequence problems.
CH471058 Genomic DNA. Translation: EAX11633.1. Sequence problems.
BC064616 mRNA. Translation: AAH64616.1.
BC089429 mRNA. Translation: AAH89429.2.
CCDSiCCDS46419.1. [Q5FWF4-1]
CCDS67963.1. [Q5FWF4-3]
RefSeqiNP_001273497.1. NM_001286568.1. [Q5FWF4-3]
NP_115519.2. NM_032143.3. [Q5FWF4-1]
XP_005263866.1. XM_005263809.1. [Q5FWF4-1]
XP_006712851.1. XM_006712788.1. [Q5FWF4-1]
XP_011510260.1. XM_011511958.2. [Q5FWF4-1]
XP_011510262.1. XM_011511960.1. [Q5FWF4-1]
XP_011510265.1. XM_011511963.1. [Q5FWF4-3]
UniGeneiHs.658422.

Genome annotation databases

EnsembliENST00000264159; ENSP00000264159; ENSG00000121988. [Q5FWF4-1]
ENST00000401392; ENSP00000383979; ENSG00000121988. [Q5FWF4-3]
ENST00000619650; ENSP00000480120; ENSG00000121988. [Q5FWF4-2]
GeneIDi84083.
KEGGihsa:84083.
UCSCiuc002tul.5. human. [Q5FWF4-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL136824 mRNA. Translation: CAB66758.1.
AK095362 mRNA. Translation: BAC04536.1.
AK131303 mRNA. Translation: BAG54763.1. Different initiation.
AK304601 mRNA. Translation: BAG65387.1. Different initiation.
BX647838 mRNA. No translation available.
AC012450 Genomic DNA. No translation available.
AC016742 Genomic DNA. No translation available.
AC017031 Genomic DNA. Translation: AAX93066.1. Sequence problems.
AC020602 Genomic DNA. No translation available.
AC064850 Genomic DNA. No translation available.
CH471058 Genomic DNA. Translation: EAX11631.1. Sequence problems.
CH471058 Genomic DNA. Translation: EAX11633.1. Sequence problems.
BC064616 mRNA. Translation: AAH64616.1.
BC089429 mRNA. Translation: AAH89429.2.
CCDSiCCDS46419.1. [Q5FWF4-1]
CCDS67963.1. [Q5FWF4-3]
RefSeqiNP_001273497.1. NM_001286568.1. [Q5FWF4-3]
NP_115519.2. NM_032143.3. [Q5FWF4-1]
XP_005263866.1. XM_005263809.1. [Q5FWF4-1]
XP_006712851.1. XM_006712788.1. [Q5FWF4-1]
XP_011510260.1. XM_011511958.2. [Q5FWF4-1]
XP_011510262.1. XM_011511960.1. [Q5FWF4-1]
XP_011510265.1. XM_011511963.1. [Q5FWF4-3]
UniGeneiHs.658422.

3D structure databases

ProteinModelPortaliQ5FWF4.
SMRiQ5FWF4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123877. 9 interactors.
STRINGi9606.ENSP00000264159.

PTM databases

iPTMnetiQ5FWF4.
PhosphoSitePlusiQ5FWF4.

Polymorphism and mutation databases

BioMutaiZRANB3.
DMDMi74741477.

Proteomic databases

EPDiQ5FWF4.
MaxQBiQ5FWF4.
PaxDbiQ5FWF4.
PeptideAtlasiQ5FWF4.
PRIDEiQ5FWF4.

Protocols and materials databases

DNASUi84083.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264159; ENSP00000264159; ENSG00000121988. [Q5FWF4-1]
ENST00000401392; ENSP00000383979; ENSG00000121988. [Q5FWF4-3]
ENST00000619650; ENSP00000480120; ENSG00000121988. [Q5FWF4-2]
GeneIDi84083.
KEGGihsa:84083.
UCSCiuc002tul.5. human. [Q5FWF4-1]

Organism-specific databases

CTDi84083.
DisGeNETi84083.
GeneCardsiZRANB3.
HGNCiHGNC:25249. ZRANB3.
HPAiHPA035234.
HPA043073.
HPA043301.
MIMi615655. gene.
neXtProtiNX_Q5FWF4.
OpenTargetsiENSG00000121988.
PharmGKBiPA134871612.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1000. Eukaryota.
COG0553. LUCA.
GeneTreeiENSGT00860000133750.
HOGENOMiHOG000031233.
HOVERGENiHBG062387.
InParanoidiQ5FWF4.
OMAiCNLNAQE.
OrthoDBiEOG091G0A1B.
PhylomeDBiQ5FWF4.
TreeFamiTF354227.

Miscellaneous databases

ChiTaRSiZRANB3. human.
GenomeRNAii84083.
PROiQ5FWF4.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000121988.
CleanExiHS_ZRANB3.
ExpressionAtlasiQ5FWF4. baseline and differential.
GenevisibleiQ5FWF4. HS.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR002711. HNH.
IPR003615. HNH_nuc.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
IPR001876. Znf_RanBP2.
[Graphical view]
PfamiPF00271. Helicase_C. 1 hit.
PF01844. HNH. 1 hit.
PF00176. SNF2_N. 1 hit.
PF00641. zf-RanBP. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00507. HNHc. 1 hit.
SM00547. ZnF_RBZ. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
SSF90209. SSF90209. 1 hit.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiZRAB3_HUMAN
AccessioniPrimary (citable) accession number: Q5FWF4
Secondary accession number(s): B3KYA1
, B4E375, B5MDI3, D3DP76, E9PBP0, Q53SM1, Q6P2C4, Q8N1P4, Q9H0E8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: July 5, 2005
Last modified: November 30, 2016
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

In contrast to classical helicases that unwing DNA, annealing helicases rewind it.1 Publication

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.