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Q8NG08

- HELB_HUMAN

UniProt

Q8NG08 - HELB_HUMAN

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Protein
DNA helicase B
Gene
HELB
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. ATP binding Source: UniProtKB-KW
  2. ATP-dependent 5'-3' DNA helicase activity Source: UniProtKB
  3. single-stranded DNA-dependent ATP-dependent DNA helicase activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. DNA duplex unwinding Source: GOC
  2. DNA replication Source: UniProtKB
  3. 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: Chromosome 12

Organism-specific databases

HGNCiHGNC:17196. HELB.

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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10871087DNA helicase B
PRO_0000338992Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei967 – 9671Phosphoserine By similarity
Modified residuei971 – 9711Phosphoserine By 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

ArrayExpressiQ8NG08.
BgeeiQ8NG08.
CleanExiHS_HELB.
GenevestigatoriQ8NG08.

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. 4 interactions.
IntActiQ8NG08. 1 interaction.
STRINGi9606.ENSP00000247815.

Structurei

3D structure databases

ProteinModelPortaliQ8NG08.

Family & Domainsi

Phylogenomic databases

eggNOGiCOG0507.
HOGENOMiHOG000043085.
HOVERGENiHBG097647.
InParanoidiQ8NG08.
KOiK15254.
OMAiGRQHWQH.
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. Align

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

MARSSPYLRQ LQGPLLPPRD LVEEDDDYLN DDVEEDEESV FIDAEELCSG     50
GVKAGSLPGC LRVSICDENT QETCKVFGRF PITGAWWRVK VQVKPVVGSR 100
SYQYQVQGFP SYFLQSDMSP PNQKHICALF LKECEVSSDD VNKFLTWVKE 150
VSNYKNLNFE NLRETLRTFH KETGRKDQKQ PTQNGQEELF LDNEMSLPLE 200
NTIPFRNVMT ALQFPKIMEF LPVLLPRHFK WIIGSGSKEM LKEIEEILGT 250
HPWKLGFSKI TYREWKLLRC EASWIAFCQC ESLLQLMTDL EKNALIMYSR 300
LKQICREDGH TYVEVNDLTL TLSNHMSFHA ASESLKFLKD IGVVTYEKSC 350
VFPYDLYHAE RAIAFSICDL MKKPPWHLCV DVEKVLASIH TTKPENSSDD 400
ALNESKPDEV RLENPVDVVD TQDNGDHIWT NGENEINAEI SEVQLDQDQV 450
EVPLDRDQVA ALEMICSNPV TVISGKGGCG KTTIVSRLFK HIEQLEEREV 500
KKACEDFEQD QNASEEWITF TEQSQLEADK AIEVLLTAPT GKAAGLLRQK 550
TGLHAYTLCQ VNYSFYSWTQ TMMTTNKPWK FSSVRVLVVD EGSLVSVGIF 600
KSVLNLLCEH SKLSKLIILG DIRQLPSIEP GNLLKDLFET LKSRNCAIEL 650
KTNHRAESQL IVDNATRISR RQFPKFDAEL NISDNPTLPI SIQDKTFIFV 700
RLPEEDASSQ SSKTNHHSCL YSAVKTLLQE NNLQNAKTSQ FIAFRRQDCD 750
LINDCCCKHY TGHLTKDHQS RLVFGIGDKI CCTRNAYLSD LLPENISGSQ 800
QNNDLDASSE DFSGTLPDFA KNKRDFESNV RLCNGEIFFI TNDVTDVTFG 850
KRRSLTINNM AGLEVTVDFK KLMKYCRIKH AWARTIHTFQ GSEEQTVVYV 900
VGKAGRQHWQ HVYTAVTRGR CRVYVIAEES QLRNAIMKNS FPRKTRLKHF 950
LQSKLSSSGA PPADFPSPRK SSGDSGGPST PSASPLPVVT DHAMTNDVTW 1000
SEASSPDERT LTFAERWQLS SPDGVDTDDD LPKSRASKRT CGVNDDESPS 1050
KIFMVGESPQ VSSRLQNLRL NNLIPRQLFK PTDNQET 1087
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.

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.
VSP_034086Add
BLAST
Alternative sequencei575 – 1087513Missing in isoform 2.
VSP_034087Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti366 – 3661S → P in BAF83583. 1 Publication
Sequence conflicti849 – 8491F → S in BAF83583. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]

Polymorphism databases

DMDMi190359604.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF319995 mRNA. Translation: AAM73554.1 .
AK024464 mRNA. Translation: BAB15754.1 . Different initiation.
AK290894 mRNA. Translation: BAF83583.1 .
CCDSi CCDS8976.1. [Q8NG08-1 ]
RefSeqi NP_387467.2. NM_033647.3. [Q8NG08-1 ]
XP_005269291.1. XM_005269234.1. [Q8NG08-1 ]
UniGenei Hs.505941.

3D structure databases

ProteinModelPortali Q8NG08.
ModBasei Search...

Protein-protein interaction databases

BioGridi 124978. 4 interactions.
IntActi Q8NG08. 1 interaction.
STRINGi 9606.ENSP00000247815.

PTM databases

PhosphoSitei Q8NG08.

Polymorphism databases

DMDMi 190359604.

Proteomic databases

MaxQBi Q8NG08.
PaxDbi Q8NG08.
PRIDEi Q8NG08.

Protocols and materials databases

DNASUi 92797.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000247815 ; ENSP00000247815 ; ENSG00000127311 . [Q8NG08-1 ]
ENST00000440906 ; ENSP00000396955 ; ENSG00000127311 . [Q8NG08-2 ]
ENST00000545134 ; ENSP00000443287 ; ENSG00000127311 . [Q8NG08-1 ]
GeneIDi 92797.
KEGGi hsa:92797.
UCSCi uc001sti.3. human. [Q8NG08-1 ]

Organism-specific databases

CTDi 92797.
GeneCardsi GC12P066696.
H-InvDB HIX0036722.
HGNCi HGNC:17196. HELB.
MIMi 614539. gene.
neXtProti NX_Q8NG08.
PharmGKBi PA134987279.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0507.
HOGENOMi HOG000043085.
HOVERGENi HBG097647.
InParanoidi Q8NG08.
KOi K15254.
OMAi GRQHWQH.
OrthoDBi EOG7GBG16.
PhylomeDBi Q8NG08.
TreeFami TF336223.

Miscellaneous databases

GenomeRNAii 92797.
NextBioi 77879.
PROi Q8NG08.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8NG08.
Bgeei Q8NG08.
CleanExi HS_HELB.
Genevestigatori Q8NG08.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR027044. Helb.
IPR027417. P-loop_NTPase.
IPR027785. UvrD_like_helicase_C.
[Graphical view ]
PANTHERi PTHR18934:SF97. PTHR18934:SF97. 1 hit.
Pfami PF13538. UvrD_C_2. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 6 hits.
ProtoNeti Search...

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: July 9, 2014
This is version 75 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

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