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Q3KNJ2

- NHEJ1_MOUSE

UniProt

Q3KNJ2 - NHEJ1_MOUSE

Protein

Non-homologous end-joining factor 1

Gene

Nhej1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 1 (08 Nov 2005)
      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.1 Publication

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. B cell differentiation Source: UniProtKB
    2. DNA recombination Source: InterPro
    3. double-strand break repair via nonhomologous end joining Source: UniProtKB
    4. response to ionizing radiation Source: UniProtKB
    5. 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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:1922820. Nhej1.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Embryonic stem cells are highly sensitive to ionizing radiation and have intrinsic DNA double-strand break repair defects.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 295295Non-homologous end-joining factor 1PRO_0000228655Add
    BLAST

    Proteomic databases

    MaxQBiQ3KNJ2.
    PRIDEiQ3KNJ2.

    PTM databases

    PhosphoSiteiQ3KNJ2.

    Expressioni

    Gene expression databases

    BgeeiQ3KNJ2.
    CleanExiMM_NHEJ1.
    GenevestigatoriQ3KNJ2.

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliQ3KNJ2.
    SMRiQ3KNJ2. Positions 1-227.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

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

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili128 – 17043By similarityAdd
    BLAST

    Domaini

    The coiled-coil region mediates homodimerization.By similarity

    Sequence similaritiesi

    Belongs to the XLF family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG47408.
    HOVERGENiHBG080703.
    KOiK10980.
    PhylomeDBiQ3KNJ2.

    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: Q3KNJ2-1) [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

    MEELEQDLLL QPWAWLQLAE NSLLAKVSIT KHGYALLISD LQQVWHEQVD    50
    TSVVSQRAKE LNKRLTAPPA ALLCHLDEAL RPLFKDSAHP SKATFSCDRG 100
    EEGLILRVQS ELSGLPFSWH FHCIPASSSL VSQHLIHPLM GVSLALQSHV 150
    RELAALLRMK DLEIQAYQES GAVLSRSRLK TEPFEENSFL EQFMAEKLPE 200
    ACAVGDGKPF AMSLQSLYVA VTKQQIQARQ AHKDSGETQA SSSTSPRGTD 250
    NQPEEPVSLS STLSEPEYEP VAASGPMHRA RLVKSKRKKP RGLFS 295
    Length:295
    Mass (Da):32,739
    Last modified:November 8, 2005 - v1
    Checksum:i679D548AC627696D
    GO
    Isoform 2 (identifier: Q3KNJ2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         131-196: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:229
    Mass (Da):25,233
    Checksum:iAE78F572827EBE7C
    GO

    Sequence cautioni

    The sequence BAB24611.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti260 – 2601S → P in AAH06063. (PubMed:15489334)Curated
    Sequence conflicti281 – 2811R → Q in AAH06063. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei131 – 19666Missing in isoform 2. 1 PublicationVSP_017690Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK006481 mRNA. Translation: BAB24611.1. Different initiation.
    BC006063 mRNA. Translation: AAH06063.1.
    BC107252 mRNA. Translation: AAI07253.1.
    BC107253 mRNA. Translation: AAI07254.1.
    BC132359 mRNA. Translation: AAI32360.1.
    BC132361 mRNA. Translation: AAI32362.1.
    RefSeqiNP_083618.3. NM_029342.4. [Q3KNJ2-1]
    UniGeneiMm.442409.

    Genome annotation databases

    GeneIDi75570.
    KEGGimmu:75570.
    UCSCiuc029qpd.1. mouse. [Q3KNJ2-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK006481 mRNA. Translation: BAB24611.1 . Different initiation.
    BC006063 mRNA. Translation: AAH06063.1 .
    BC107252 mRNA. Translation: AAI07253.1 .
    BC107253 mRNA. Translation: AAI07254.1 .
    BC132359 mRNA. Translation: AAI32360.1 .
    BC132361 mRNA. Translation: AAI32362.1 .
    RefSeqi NP_083618.3. NM_029342.4. [Q3KNJ2-1 ]
    UniGenei Mm.442409.

    3D structure databases

    ProteinModelPortali Q3KNJ2.
    SMRi Q3KNJ2. Positions 1-227.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q3KNJ2.

    Proteomic databases

    MaxQBi Q3KNJ2.
    PRIDEi Q3KNJ2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 75570.
    KEGGi mmu:75570.
    UCSCi uc029qpd.1. mouse. [Q3KNJ2-1 ]

    Organism-specific databases

    CTDi 79840.
    MGIi MGI:1922820. Nhej1.

    Phylogenomic databases

    eggNOGi NOG47408.
    HOVERGENi HBG080703.
    KOi K10980.
    PhylomeDBi Q3KNJ2.

    Miscellaneous databases

    NextBioi 343394.
    PROi Q3KNJ2.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q3KNJ2.
    CleanExi MM_NHEJ1.
    Genevestigatori Q3KNJ2.

    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. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Strain: C57BL/6J.
      Tissue: Testis.
    2. "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).
      Strain: Czech II.
      Tissue: Brain and Mammary tumor.
    3. "Defective DNA repair and increased genomic instability in Cernunnos-XLF-deficient murine ES cells."
      Zha S., Alt F.W., Cheng H.-L., Brush J.W., Li G.
      Proc. Natl. Acad. Sci. U.S.A. 104:4518-4523(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiNHEJ1_MOUSE
    AccessioniPrimary (citable) accession number: Q3KNJ2
    Secondary accession number(s): A2RT39, Q99JK0, Q9D9U0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 21, 2006
    Last sequence update: November 8, 2005
    Last modified: October 1, 2014
    This is version 75 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3