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Q9H9Q4

- NHEJ1_HUMAN

UniProt

Q9H9Q4 - NHEJ1_HUMAN

Protein

Non-homologous end-joining factor 1

Gene

NHEJ1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    DNA repair protein involved in DNA nonhomologous end joining (NHEJ) required for double-strand break (DSB) repair and V(D)J recombination. May serve as a bridge between XRCC4 and the other NHEJ factors located at DNA ends, or may participate in reconfiguration of the end bound NHEJ factors to allow XRCC4 access to the DNA termini. It may act in concert with XRCC6/XRCC5 (Ku) to stimulate XRCC4-mediated joining of blunt ends and several types of mismatched ends that are noncomplementary or partially complementary.3 Publications

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. B cell differentiation Source: UniProtKB
    2. central nervous system development Source: UniProtKB
    3. DNA recombination Source: InterPro
    4. double-strand break repair via nonhomologous end joining Source: UniProtKB
    5. positive regulation of ligase activity Source: UniProtKB
    6. response to ionizing radiation Source: UniProtKB
    7. T cell differentiation Source: UniProtKB

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Non-homologous end-joining factor 1
    Alternative name(s):
    Protein cernunnos
    XRCC4-like factor
    Gene namesi
    Name:NHEJ1
    Synonyms:XLF
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:25737. NHEJ1.

    Subcellular locationi

    Nucleus 2 Publications

    GO - Cellular componenti

    1. nonhomologous end joining complex Source: UniProtKB
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Severe combined immunodeficiency due to NHEJ1 deficiency (NHEJ1-SCID) [MIM:611291]: SCID refers to a genetically and clinically heterogeneous group of rare congenital disorders characterized by impairment of both humoral and cell-mediated immunity, leukopenia and low or absent antibody levels. Patients with SCID present in infancy with recurrent, persistent infections by opportunistic organisms. The common characteristic of all types of SCID is absence of T-cell-mediated cellular immunity due to a defect in T-cell development. NHEJ1-SCID is characterized by a profound T- and B-lymphocytopenia associated with increased cellular sensitivity to ionizing radiation, microcephaly and growth retardation. Some patients may manifest SCID with sensitivity to ionizing radiation without microcephaly and mild growth retardation, probably due to hypomorphic NHEJ1 mutations.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti57 – 571R → G in NHEJ1-SCID; fails to translocate to the nucleus. 1 Publication
    VAR_025704
    Natural varianti123 – 1231C → R in NHEJ1-SCID. 1 Publication
    VAR_025705
    A chromosomal aberration involving NHEJ1 is found in a patient with polymicrogyria. Translocation t(2;7)(q35;p22).1 Publication

    Keywords - Diseasei

    Disease mutation, SCID

    Organism-specific databases

    MIMi611291. phenotype.
    Orphaneti208447. Bilateral generalized polymicrogyria.
    169079. Cernunnos-XLF deficiency.
    PharmGKBiPA144596401.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 299299Non-homologous end-joining factor 1PRO_0000228654Add
    BLAST

    Proteomic databases

    MaxQBiQ9H9Q4.
    PaxDbiQ9H9Q4.
    PRIDEiQ9H9Q4.

    PTM databases

    PhosphoSiteiQ9H9Q4.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.1 Publication

    Gene expression databases

    BgeeiQ9H9Q4.
    CleanExiHS_NHEJ1.
    GenevestigatoriQ9H9Q4.

    Organism-specific databases

    HPAiCAB012334.

    Interactioni

    Subunit structurei

    Exists mainly as a homodimer. Interacts with XRCC4 and the XRCC4-LIG4 complex. Binds DNA in a length-dependent manner.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LIG4P499174EBI-847807,EBI-847896
    XRCC4Q134268EBI-847807,EBI-717592

    Protein-protein interaction databases

    BioGridi122931. 4 interactions.
    DIPiDIP-37959N.
    IntActiQ9H9Q4. 4 interactions.
    MINTiMINT-5003574.
    STRINGi9606.ENSP00000349313.

    Structurei

    Secondary structure

    299
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1 – 99
    Beta strandi14 – 174
    Beta strandi19 – 3012
    Beta strandi33 – 397
    Beta strandi44 – 496
    Helixi51 – 6111
    Helixi69 – 8517
    Beta strandi94 – 1007
    Beta strandi103 – 11210
    Beta strandi115 – 12511
    Helixi128 – 1347
    Helixi136 – 16934
    Helixi186 – 19611
    Helixi198 – 2014
    Helixi208 – 2136
    Helixi215 – 22814

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2QM4X-ray2.30A/B/C/D1-233[»]
    2R9AX-ray2.50A/B1-224[»]
    3Q4FX-ray5.50A/B/E/F1-224[»]
    3RWRX-ray3.94D/E/H/I/L/M/O/Q/S/T/W/X1-224[»]
    3SR2X-ray3.97C/D/G/H1-224[»]
    3W03X-ray8.49A/B1-233[»]
    ProteinModelPortaliQ9H9Q4.
    SMRiQ9H9Q4. Positions 1-230.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9H9Q4.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 135135Globular headAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili128 – 170431 PublicationAdd
    BLAST

    Domaini

    The coiled-coil region mediates homodimerization.

    Sequence similaritiesi

    Belongs to the XLF family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG47408.
    HOGENOMiHOG000089974.
    HOVERGENiHBG080703.
    KOiK10980.
    OMAiYWNFHCI.
    OrthoDBiEOG7Z0JXT.
    PhylomeDBiQ9H9Q4.
    TreeFamiTF328567.

    Family and domain databases

    Gene3Di2.170.210.10. 1 hit.
    InterProiIPR015381. XLF/Cernunnos.
    IPR009089. XRCC4_N.
    [Graphical view]
    PfamiPF09302. XLF. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9H9Q4-1) [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

    MEELEQGLLM QPWAWLQLAE NSLLAKVFIT KQGYALLVSD LQQVWHEQVD    50
    TSVVSQRAKE LNKRLTAPPA AFLCHLDNLL RPLLKDAAHP SEATFSCDCV 100
    ADALILRVRS ELSGLPFYWN FHCMLASPSL VSQHLIRPLM GMSLALQCQV 150
    RELATLLHMK DLEIQDYQES GATLIRDRLK TEPFEENSFL EQFMIEKLPE 200
    ACSIGDGKPF VMNLQDLYMA VTTQEVQVGQ KHQGAGDPHT SNSASLQGID 250
    SQCVNQPEQL VSSAPTLSAP EKESTGTSGP LQRPQLSKVK RKKPRGLFS 299
    Length:299
    Mass (Da):33,337
    Last modified:March 1, 2001 - v1
    Checksum:iBC5C68076A5E7A96
    GO
    Isoform 2 (identifier: Q9H9Q4-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         276-299: GTSGPLQRPQLSKVKRKKPRGLFS → ALCRDLSCQRSRGRSQGVSSVNLLWPQLLRMDLENSFQASP

    Note: No experimental confirmation available.

    Show »
    Length:316
    Mass (Da):35,291
    Checksum:i11CAF1C6543580CE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti256 – 2561Q → R in CAG33572. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti14 – 141A → T.
    Corresponds to variant rs34689457 [ dbSNP | Ensembl ].
    VAR_038790
    Natural varianti57 – 571R → G in NHEJ1-SCID; fails to translocate to the nucleus. 1 Publication
    VAR_025704
    Natural varianti89 – 891H → R.
    Corresponds to variant rs1056296 [ dbSNP | Ensembl ].
    VAR_038791
    Natural varianti123 – 1231C → R in NHEJ1-SCID. 1 Publication
    VAR_025705
    Natural varianti256 – 2561Q → L.
    Corresponds to variant rs35270667 [ dbSNP | Ensembl ].
    VAR_038792

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei276 – 29924GTSGP…RGLFS → ALCRDLSCQRSRGRSQGVSS VNLLWPQLLRMDLENSFQAS P in isoform 2. 1 PublicationVSP_017689Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ972687 mRNA. Translation: CAI99410.1.
    AK022672 mRNA. Translation: BAB14168.1.
    CR457291 mRNA. Translation: CAG33572.1.
    AC020575 Genomic DNA. No translation available.
    AC068946 Genomic DNA. No translation available.
    AC097468 Genomic DNA. Translation: AAX88921.1.
    BC008210 mRNA. Translation: AAH08210.2.
    BC012732 mRNA. Translation: AAH12732.1.
    BC030986 mRNA. Translation: AAH30986.1.
    CCDSiCCDS2432.1. [Q9H9Q4-1]
    RefSeqiNP_079058.1. NM_024782.2. [Q9H9Q4-1]
    UniGeneiHs.225988.

    Genome annotation databases

    EnsembliENST00000356853; ENSP00000349313; ENSG00000187736. [Q9H9Q4-1]
    ENST00000409720; ENSP00000387290; ENSG00000187736. [Q9H9Q4-2]
    GeneIDi79840.
    KEGGihsa:79840.
    UCSCiuc002vjp.4. human. [Q9H9Q4-1]

    Polymorphism databases

    DMDMi74734059.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Web resourcesi

    NHEJ1base

    NHEJ1 mutation db

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ972687 mRNA. Translation: CAI99410.1 .
    AK022672 mRNA. Translation: BAB14168.1 .
    CR457291 mRNA. Translation: CAG33572.1 .
    AC020575 Genomic DNA. No translation available.
    AC068946 Genomic DNA. No translation available.
    AC097468 Genomic DNA. Translation: AAX88921.1 .
    BC008210 mRNA. Translation: AAH08210.2 .
    BC012732 mRNA. Translation: AAH12732.1 .
    BC030986 mRNA. Translation: AAH30986.1 .
    CCDSi CCDS2432.1. [Q9H9Q4-1 ]
    RefSeqi NP_079058.1. NM_024782.2. [Q9H9Q4-1 ]
    UniGenei Hs.225988.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2QM4 X-ray 2.30 A/B/C/D 1-233 [» ]
    2R9A X-ray 2.50 A/B 1-224 [» ]
    3Q4F X-ray 5.50 A/B/E/F 1-224 [» ]
    3RWR X-ray 3.94 D/E/H/I/L/M/O/Q/S/T/W/X 1-224 [» ]
    3SR2 X-ray 3.97 C/D/G/H 1-224 [» ]
    3W03 X-ray 8.49 A/B 1-233 [» ]
    ProteinModelPortali Q9H9Q4.
    SMRi Q9H9Q4. Positions 1-230.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122931. 4 interactions.
    DIPi DIP-37959N.
    IntActi Q9H9Q4. 4 interactions.
    MINTi MINT-5003574.
    STRINGi 9606.ENSP00000349313.

    PTM databases

    PhosphoSitei Q9H9Q4.

    Polymorphism databases

    DMDMi 74734059.

    Proteomic databases

    MaxQBi Q9H9Q4.
    PaxDbi Q9H9Q4.
    PRIDEi Q9H9Q4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000356853 ; ENSP00000349313 ; ENSG00000187736 . [Q9H9Q4-1 ]
    ENST00000409720 ; ENSP00000387290 ; ENSG00000187736 . [Q9H9Q4-2 ]
    GeneIDi 79840.
    KEGGi hsa:79840.
    UCSCi uc002vjp.4. human. [Q9H9Q4-1 ]

    Organism-specific databases

    CTDi 79840.
    GeneCardsi GC02M219941.
    HGNCi HGNC:25737. NHEJ1.
    HPAi CAB012334.
    MIMi 611290. gene.
    611291. phenotype.
    neXtProti NX_Q9H9Q4.
    Orphaneti 208447. Bilateral generalized polymicrogyria.
    169079. Cernunnos-XLF deficiency.
    PharmGKBi PA144596401.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG47408.
    HOGENOMi HOG000089974.
    HOVERGENi HBG080703.
    KOi K10980.
    OMAi YWNFHCI.
    OrthoDBi EOG7Z0JXT.
    PhylomeDBi Q9H9Q4.
    TreeFami TF328567.

    Miscellaneous databases

    EvolutionaryTracei Q9H9Q4.
    GeneWikii XLF_(protein).
    GenomeRNAii 79840.
    NextBioi 69516.
    PROi Q9H9Q4.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9H9Q4.
    CleanExi HS_NHEJ1.
    Genevestigatori Q9H9Q4.

    Family and domain databases

    Gene3Di 2.170.210.10. 1 hit.
    InterProi IPR015381. XLF/Cernunnos.
    IPR009089. XRCC4_N.
    [Graphical view ]
    Pfami PF09302. XLF. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cernunnos, a novel nonhomologous end-joining factor, is mutated in human immunodeficiency with microcephaly."
      Buck D., Malivert L., de Chasseval R., Barraud A., Fondaneche M.-C., Sanal O., Plebani A., Stephan J.-L., Hufnagel M., le Deist F., Fischer A., Durandy A., de Villartay J.-P., Revy P.
      Cell 124:287-299(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANTS NHEJ1-SCID GLY-57 AND ARG-123.
      Tissue: Thymus.
    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] (ISOFORM 1).
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 177-299 (ISOFORM 2).
      Tissue: Bone marrow and Skin.
    6. Cited for: DISEASE.
    7. "XLF interacts with the XRCC4-DNA ligase IV complex to promote DNA nonhomologous end-joining."
      Ahnesorg P., Smith P., Jackson S.P.
      Cell 124:301-313(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH XRCC4, INVOLVEMENT IN NHEJ1-SCID.
    8. "Cernunnos interacts with the XRCC4 x DNA-ligase IV complex and is homologous to the yeast nonhomologous end-joining factor Nej1."
      Callebaut I., Malivert L., Fischer A., Mornon J.P., Revy P., de Villartay J.P.
      J. Biol. Chem. 281:13857-13860(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH XRCC4-LIG4 COMPLEX.
    9. Cited for: CHROMOSOMAL TRANSLOCATION.
    10. "Length-dependent binding of human XLF to DNA and stimulation of XRCC4.DNA ligase IV activity."
      Lu H., Pannicke U., Schwarz K., Lieber M.R.
      J. Biol. Chem. 282:11155-11162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH XRCC4-LIG4 COMPLEX, DNA-BINDING, CHARACTERIZATION OF VARIANT NHEJ1-SCID GLY-57.
    11. "Cernunnos/XLF promotes the ligation of mismatched and noncohesive DNA ends."
      Tsai C.J., Kim S.A., Chu G.
      Proc. Natl. Acad. Sci. U.S.A. 104:7851-7856(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "Crystal structure of human XLF/Cernunnos reveals unexpected differences from XRCC4 with implications for NHEJ."
      Li Y., Chirgadze D.Y., Bolanos-Garcia V.M., Sibanda B.L., Davies O.R., Ahnesorg P., Jackson S.P., Blundell T.L.
      EMBO J. 27:290-300(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-233, COILED-COIL REGION, SUBUNIT.

    Entry informationi

    Entry nameiNHEJ1_HUMAN
    AccessioniPrimary (citable) accession number: Q9H9Q4
    Secondary accession number(s): B8ZZA4
    , Q4ZFW7, Q6IA64, Q96JS9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 21, 2006
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 106 of the entry and version 1 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

    Was named 'Cernunnos' after the enigmatic Celtic god of hunting, the underworld and fertility.

    Keywords - Technical termi

    3D-structure, Complete proteome, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

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