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Protein

DNA helicase B

Gene

HELB

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

Functioni

Unwinds duplex DNA with 5'-3' polarity. Has single-strand DNA-dependent ATPase and DNA helicase activities. Prefers ATP and dATP as substrates. During S phase, may facilitate cellular recovery from replication stress.2 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Enzyme regulationi

Inhibited by salt concentration greater than 100 mM. Uses either magnesium or manganese ions to support helicase activity. Binds strongly to single-stranded DNA in the absence of ATP but dissociates readily in the presence of 1 mM ATP.1 Publication

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent 5'-3' DNA helicase activity Source: UniProtKB
  • single-stranded DNA-dependent ATP-dependent DNA helicase activity Source: UniProtKB

GO - Biological processi

  • DNA-dependent DNA replication Source: GO_Central
  • DNA duplex unwinding Source: GOC
  • DNA replication Source: UniProtKB
  • DNA replication, synthesis of RNA primer Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
DNA helicase B (EC:3.6.4.12)
Short name:
hDHB
Gene namesi
Name:HELB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:17196. HELB.

Subcellular locationi


    Note: Preferentially during S phase, recruited to chromatin following DNA damage induced by UV irradiation, or camptothecin or hydroxyurea treatment.

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi481 – 4811K → A: No ATPase activity. 1 Publication
Mutagenesisi499 – 4991E → A: Loss of RPA1-binding; when associated with A-506 and A-510. 1 Publication
Mutagenesisi506 – 5061D → A: Loss of RPA1-binding; when associated with A-499 and A-510. 1 Publication
Mutagenesisi510 – 5101D → A: Loss of RPA1-binding; when associated with A-499 and A-506. 1 Publication
Mutagenesisi591 – 5911E → Q: No ATPase activity. 1 Publication

Organism-specific databases

PharmGKBiPA134987279.

Polymorphism and mutation databases

BioMutaiHELB.
DMDMi190359604.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10871087DNA helicase BPRO_0000338992Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei967 – 9671PhosphoserineBy similarity
Modified residuei971 – 9711PhosphoserineBy similarity
Modified residuei1027 – 10271Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8NG08.
PaxDbiQ8NG08.
PRIDEiQ8NG08.

PTM databases

PhosphoSiteiQ8NG08.

Expressioni

Tissue specificityi

Highly expressed in testis and thymus and weakly in liver, spleen, kidney and brain.1 Publication

Gene expression databases

BgeeiQ8NG08.
CleanExiHS_HELB.
ExpressionAtlasiQ8NG08. baseline and differential.
GenevisibleiQ8NG08. HS.

Interactioni

Subunit structurei

Binds to RPA1; this interaction promotes HELB recruitment to chromatin following DNA damage. Interacts with at least two subunits of pol-prim.2 Publications

Protein-protein interaction databases

BioGridi124978. 5 interactions.
IntActiQ8NG08. 4 interactions.
STRINGi9606.ENSP00000247815.

Structurei

3D structure databases

ProteinModelPortaliQ8NG08.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiCOG0507.
GeneTreeiENSGT00390000006913.
HOGENOMiHOG000043085.
HOVERGENiHBG097647.
InParanoidiQ8NG08.
KOiK15254.
OMAiAVTRGRC.
OrthoDBiEOG7GBG16.
PhylomeDBiQ8NG08.
TreeFamiTF336223.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR027044. Helb.
IPR027417. P-loop_NTPase.
IPR027785. UvrD_like_helicase_C.
[Graphical view]
PANTHERiPTHR18934:SF97. PTHR18934:SF97. 1 hit.
PfamiPF13538. UvrD_C_2. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 6 hits.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8NG08-1) [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
MARSSPYLRQ LQGPLLPPRD LVEEDDDYLN DDVEEDEESV FIDAEELCSG
60 70 80 90 100
GVKAGSLPGC LRVSICDENT QETCKVFGRF PITGAWWRVK VQVKPVVGSR
110 120 130 140 150
SYQYQVQGFP SYFLQSDMSP PNQKHICALF LKECEVSSDD VNKFLTWVKE
160 170 180 190 200
VSNYKNLNFE NLRETLRTFH KETGRKDQKQ PTQNGQEELF LDNEMSLPLE
210 220 230 240 250
NTIPFRNVMT ALQFPKIMEF LPVLLPRHFK WIIGSGSKEM LKEIEEILGT
260 270 280 290 300
HPWKLGFSKI TYREWKLLRC EASWIAFCQC ESLLQLMTDL EKNALIMYSR
310 320 330 340 350
LKQICREDGH TYVEVNDLTL TLSNHMSFHA ASESLKFLKD IGVVTYEKSC
360 370 380 390 400
VFPYDLYHAE RAIAFSICDL MKKPPWHLCV DVEKVLASIH TTKPENSSDD
410 420 430 440 450
ALNESKPDEV RLENPVDVVD TQDNGDHIWT NGENEINAEI SEVQLDQDQV
460 470 480 490 500
EVPLDRDQVA ALEMICSNPV TVISGKGGCG KTTIVSRLFK HIEQLEEREV
510 520 530 540 550
KKACEDFEQD QNASEEWITF TEQSQLEADK AIEVLLTAPT GKAAGLLRQK
560 570 580 590 600
TGLHAYTLCQ VNYSFYSWTQ TMMTTNKPWK FSSVRVLVVD EGSLVSVGIF
610 620 630 640 650
KSVLNLLCEH SKLSKLIILG DIRQLPSIEP GNLLKDLFET LKSRNCAIEL
660 670 680 690 700
KTNHRAESQL IVDNATRISR RQFPKFDAEL NISDNPTLPI SIQDKTFIFV
710 720 730 740 750
RLPEEDASSQ SSKTNHHSCL YSAVKTLLQE NNLQNAKTSQ FIAFRRQDCD
760 770 780 790 800
LINDCCCKHY TGHLTKDHQS RLVFGIGDKI CCTRNAYLSD LLPENISGSQ
810 820 830 840 850
QNNDLDASSE DFSGTLPDFA KNKRDFESNV RLCNGEIFFI TNDVTDVTFG
860 870 880 890 900
KRRSLTINNM AGLEVTVDFK KLMKYCRIKH AWARTIHTFQ GSEEQTVVYV
910 920 930 940 950
VGKAGRQHWQ HVYTAVTRGR CRVYVIAEES QLRNAIMKNS FPRKTRLKHF
960 970 980 990 1000
LQSKLSSSGA PPADFPSPRK SSGDSGGPST PSASPLPVVT DHAMTNDVTW
1010 1020 1030 1040 1050
SEASSPDERT LTFAERWQLS SPDGVDTDDD LPKSRASKRT CGVNDDESPS
1060 1070 1080
KIFMVGESPQ VSSRLQNLRL NNLIPRQLFK PTDNQET
Length:1,087
Mass (Da):123,252
Last modified:June 10, 2008 - v2
Checksum:i05220F3186CE722B
GO
Isoform 2 (identifier: Q8NG08-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     562-574: NYSFYSWTQTMMT → TLDSYPVLNLVTC
     575-1087: Missing.

Note: No experimental confirmation available.
Show »
Length:574
Mass (Da):65,443
Checksum:i5628E8F75508B446
GO

Sequence cautioni

The sequence BAB15754.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti366 – 3661S → P in BAF83583 (PubMed:14702039).Curated
Sequence conflicti849 – 8491F → S in BAF83583 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti172 – 1721E → K.
Corresponds to variant rs35605829 [ dbSNP | Ensembl ].
VAR_043855
Natural varianti191 – 1911L → P.1 Publication
Corresponds to variant rs4430553 [ dbSNP | Ensembl ].
VAR_043856
Natural varianti267 – 2671L → F.
Corresponds to variant rs35138454 [ dbSNP | Ensembl ].
VAR_043857
Natural varianti575 – 5751T → A.
Corresponds to variant rs58589183 [ dbSNP | Ensembl ].
VAR_061665
Natural varianti966 – 9661P → L.1 Publication
Corresponds to variant rs1185244 [ dbSNP | Ensembl ].
VAR_043858
Natural varianti980 – 9801T → I.1 Publication
Corresponds to variant rs1168312 [ dbSNP | Ensembl ].
VAR_043859

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei562 – 57413NYSFY…QTMMT → TLDSYPVLNLVTC in isoform 2. 1 PublicationVSP_034086Add
BLAST
Alternative sequencei575 – 1087513Missing in isoform 2. 1 PublicationVSP_034087Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF319995 mRNA. Translation: AAM73554.1.
AK024464 mRNA. Translation: BAB15754.1. Different initiation.
AK290894 mRNA. Translation: BAF83583.1.
CCDSiCCDS8976.1. [Q8NG08-1]
RefSeqiNP_387467.2. NM_033647.3. [Q8NG08-1]
XP_005269291.1. XM_005269234.1. [Q8NG08-1]
UniGeneiHs.505941.

Genome annotation databases

EnsembliENST00000247815; ENSP00000247815; ENSG00000127311. [Q8NG08-1]
ENST00000440906; ENSP00000396955; ENSG00000127311. [Q8NG08-2]
ENST00000545134; ENSP00000443287; ENSG00000127311. [Q8NG08-1]
GeneIDi92797.
KEGGihsa:92797.
UCSCiuc001sti.3. human. [Q8NG08-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF319995 mRNA. Translation: AAM73554.1.
AK024464 mRNA. Translation: BAB15754.1. Different initiation.
AK290894 mRNA. Translation: BAF83583.1.
CCDSiCCDS8976.1. [Q8NG08-1]
RefSeqiNP_387467.2. NM_033647.3. [Q8NG08-1]
XP_005269291.1. XM_005269234.1. [Q8NG08-1]
UniGeneiHs.505941.

3D structure databases

ProteinModelPortaliQ8NG08.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124978. 5 interactions.
IntActiQ8NG08. 4 interactions.
STRINGi9606.ENSP00000247815.

PTM databases

PhosphoSiteiQ8NG08.

Polymorphism and mutation databases

BioMutaiHELB.
DMDMi190359604.

Proteomic databases

MaxQBiQ8NG08.
PaxDbiQ8NG08.
PRIDEiQ8NG08.

Protocols and materials databases

DNASUi92797.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000247815; ENSP00000247815; ENSG00000127311. [Q8NG08-1]
ENST00000440906; ENSP00000396955; ENSG00000127311. [Q8NG08-2]
ENST00000545134; ENSP00000443287; ENSG00000127311. [Q8NG08-1]
GeneIDi92797.
KEGGihsa:92797.
UCSCiuc001sti.3. human. [Q8NG08-1]

Organism-specific databases

CTDi92797.
GeneCardsiGC12P066696.
H-InvDBHIX0036722.
HGNCiHGNC:17196. HELB.
MIMi614539. gene.
neXtProtiNX_Q8NG08.
PharmGKBiPA134987279.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0507.
GeneTreeiENSGT00390000006913.
HOGENOMiHOG000043085.
HOVERGENiHBG097647.
InParanoidiQ8NG08.
KOiK15254.
OMAiAVTRGRC.
OrthoDBiEOG7GBG16.
PhylomeDBiQ8NG08.
TreeFamiTF336223.

Miscellaneous databases

GenomeRNAii92797.
NextBioi77879.
PROiQ8NG08.
SOURCEiSearch...

Gene expression databases

BgeeiQ8NG08.
CleanExiHS_HELB.
ExpressionAtlasiQ8NG08. baseline and differential.
GenevisibleiQ8NG08. HS.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR027044. Helb.
IPR027417. P-loop_NTPase.
IPR027785. UvrD_like_helicase_C.
[Graphical view]
PANTHERiPTHR18934:SF97. PTHR18934:SF97. 1 hit.
PfamiPF13538. UvrD_C_2. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 6 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A dominant-negative mutant of human DNA helicase B blocks the onset of chromosomal DNA replication."
    Taneja P., Gu J., Peng R., Carrick R., Uchiumi F., Ott R.D., Gustafson E., Podust V.N., Fanning E.
    J. Biol. Chem. 277:40853-40861(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION, ENZYME REGULATION, INTERACTION WITH RPA1 AND POL-PRIM COMPLEX, MUTAGENESIS OF LYS-481 AND GLU-591.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANTS PRO-191; LEU-966 AND ILE-980.
    Tissue: Spleen.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  4. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1027, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  6. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Human DNA helicase B (HDHB) binds to replication protein A and facilitates cellular recovery from replication stress."
    Guler G.D., Liu H., Vaithiyalingam S., Arnett D.R., Kremmer E., Chazin W.J., Fanning E.
    J. Biol. Chem. 287:6469-6481(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RPA1, MUTAGENESIS OF GLU-499; ASP-506 AND ASP-510.

Entry informationi

Entry nameiHELB_HUMAN
AccessioniPrimary (citable) accession number: Q8NG08
Secondary accession number(s): A8K4C9, Q4G0T2, Q9H7L5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: June 10, 2008
Last modified: June 24, 2015
This is version 84 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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

External Data

Dasty 3

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 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.