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Q8NG08

- HELB_HUMAN

UniProt

Q8NG08 - HELB_HUMAN

Protein

DNA helicase B

Gene

HELB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 2 (10 Jun 2008)
      Previous versions | rss
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    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

    GO - Biological processi

    1. DNA duplex unwinding Source: GOC
    2. DNA replication Source: UniProtKB
    3. DNA replication, synthesis of RNA primer Source: UniProtKB

    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.

    Subcellular locationi


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

    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 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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    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.

    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:
    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 76 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