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Non-homologous end-joining factor 1 (Protein cernunnos) (XRCC4-like factor)

 NHEJ1_HUMAN             Reviewed;         299 AA.
Q9H9Q4; B8ZZA4; Q4ZFW7; Q6IA64; Q96JS9;
21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
28-MAR-2018, entry version 135.
RecName: Full=Non-homologous end-joining factor 1;
AltName: Full=Protein cernunnos;
AltName: Full=XRCC4-like factor;
Name=NHEJ1; Synonyms=XLF;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, AND VARIANTS NHEJ1-SCID GLY-57 AND
ARG-123.
TISSUE=Thymus;
PubMed=16439204; DOI=10.1016/j.cell.2005.12.030;
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.;
"Cernunnos, a novel nonhomologous end-joining factor, is mutated in
human immunodeficiency with microcephaly.";
Cell 124:287-299(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
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.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 177-299 (ISOFORM 2).
TISSUE=Bone marrow, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
DISEASE.
PubMed=12604777; DOI=10.1073/pnas.0437964100;
Dai Y., Kysela B., Hanakahi L.A., Manolis K., Riballo E., Stumm M.,
Harville T.O., West S.C., Oettinger M.A., Jeggo P.A.;
"Nonhomologous end joining and V(D)J recombination require an
additional factor.";
Proc. Natl. Acad. Sci. U.S.A. 100:2462-2467(2003).
[7]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH XRCC4, AND
INVOLVEMENT IN NHEJ1-SCID.
PubMed=16439205; DOI=10.1016/j.cell.2005.12.031;
Ahnesorg P., Smith P., Jackson S.P.;
"XLF interacts with the XRCC4-DNA ligase IV complex to promote DNA
nonhomologous end-joining.";
Cell 124:301-313(2006).
[8]
INTERACTION WITH XRCC4-LIG4 COMPLEX.
PubMed=16571728; DOI=10.1074/jbc.C500473200;
Callebaut I., Malivert L., Fischer A., Mornon J.P., Revy P.,
de Villartay J.P.;
"Cernunnos interacts with the XRCC4 x DNA-ligase IV complex and is
homologous to the yeast nonhomologous end-joining factor Nej1.";
J. Biol. Chem. 281:13857-13860(2006).
[9]
CHROMOSOMAL TRANSLOCATION.
PubMed=17191205; DOI=10.1002/humu.20450;
Cantagrel V., Lossi A.M., Lisgo S., Missirian C., Borges A.,
Philip N., Fernandez C., Cardoso C., Figarella-Branger D., Moncla A.,
Lindsay S., Dobyns W.B., Villard L.;
"Truncation of NHEJ1 in a patient with polymicrogyria.";
Hum. Mutat. 28:356-364(2007).
[10]
INTERACTION WITH XRCC4-LIG4 COMPLEX, DNA-BINDING, AND CHARACTERIZATION
OF VARIANT NHEJ1-SCID GLY-57.
PubMed=17317666; DOI=10.1074/jbc.M609904200;
Lu H., Pannicke U., Schwarz K., Lieber M.R.;
"Length-dependent binding of human XLF to DNA and stimulation of
XRCC4.DNA ligase IV activity.";
J. Biol. Chem. 282:11155-11162(2007).
[11]
FUNCTION.
PubMed=17470781; DOI=10.1073/pnas.0702620104;
Tsai C.J., Kim S.A., Chu G.;
"Cernunnos/XLF promotes the ligation of mismatched and noncohesive DNA
ends.";
Proc. Natl. Acad. Sci. U.S.A. 104:7851-7856(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
SUBUNIT.
PubMed=25941166; DOI=10.1038/cdd.2015.22;
Craxton A., Somers J., Munnur D., Jukes-Jones R., Cain K.,
Malewicz M.;
"XLS (c9orf142) is a new component of mammalian DNA double-stranded
break repair.";
Cell Death Differ. 22:890-897(2015).
[14]
SUBUNIT.
PubMed=25670504; DOI=10.1038/ncomms7233;
Xing M., Yang M., Huo W., Feng F., Wei L., Jiang W., Ning S., Yan Z.,
Li W., Wang Q., Hou M., Dong C., Guo R., Gao G., Ji J., Zha S.,
Lan L., Liang H., Xu D.;
"Interactome analysis identifies a new paralogue of XRCC4 in non-
homologous end joining DNA repair pathway.";
Nat. Commun. 6:6233-6233(2015).
[15]
SUBUNIT.
PubMed=25574025; DOI=10.1126/science.1261971;
Ochi T., Blackford A.N., Coates J., Jhujh S., Mehmood S., Tamura N.,
Travers J., Wu Q., Draviam V.M., Robinson C.V., Blundell T.L.,
Jackson S.P.;
"DNA repair. PAXX, a paralog of XRCC4 and XLF, interacts with Ku to
promote DNA double-strand break repair.";
Science 347:185-188(2015).
[16]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-233, COILED-COIL REGION,
AND SUBUNIT.
PubMed=18046455; DOI=10.1038/sj.emboj.7601942;
Li Y., Chirgadze D.Y., Bolanos-Garcia V.M., Sibanda B.L., Davies O.R.,
Ahnesorg P., Jackson S.P., Blundell T.L.;
"Crystal structure of human XLF/Cernunnos reveals unexpected
differences from XRCC4 with implications for NHEJ.";
EMBO J. 27:290-300(2008).
-!- FUNCTION: 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 (PubMed:16439204, PubMed:16439205, PubMed:17470781).
Binds DNA in a length-dependent manner (PubMed:17317666).
{ECO:0000269|PubMed:16439204, ECO:0000269|PubMed:16439205,
ECO:0000269|PubMed:17317666, ECO:0000269|PubMed:17470781}.
-!- SUBUNIT: Exists mainly as a homodimer. Associates with the non-
homologous end joining (NHEJ) complex which is at least composed
of the core proteins XRCC5/Ku80, XRCC6/Ku70, PRKDC/DNA-PKcs, LIG4
and XRCC4. {ECO:0000269|PubMed:16439205,
ECO:0000269|PubMed:16571728, ECO:0000269|PubMed:17317666,
ECO:0000269|PubMed:18046455, ECO:0000269|PubMed:25574025,
ECO:0000269|PubMed:25670504, ECO:0000269|PubMed:25941166}.
-!- INTERACTION:
P49917:LIG4; NbExp=4; IntAct=EBI-847807, EBI-847896;
Q13426:XRCC4; NbExp=8; IntAct=EBI-847807, EBI-717592;
Q13426-2:XRCC4; NbExp=3; IntAct=EBI-15891382, EBI-15891375;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16439204,
ECO:0000269|PubMed:16439205}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9H9Q4-1; Sequence=Displayed;
Name=2;
IsoId=Q9H9Q4-2; Sequence=VSP_017689;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:16439204}.
-!- DOMAIN: The coiled-coil region mediates homodimerization.
-!- DISEASE: 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.
{ECO:0000269|PubMed:16439204, ECO:0000269|PubMed:16439205,
ECO:0000269|PubMed:17317666}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Note=A chromosomal aberration involving NHEJ1 is found in
a patient with polymicrogyria. Translocation t(2;7)(q35;p22).
{ECO:0000269|PubMed:12604777}.
-!- MISCELLANEOUS: Was named 'Cernunnos' after the enigmatic Celtic
god of hunting, the underworld and fertility.
-!- SIMILARITY: Belongs to the XLF family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NHEJ1base; Note=NHEJ1 mutation db;
URL="http://structure.bmc.lu.se/idbase/NHEJ1base/";
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EMBL; AJ972687; CAI99410.1; -; mRNA.
EMBL; AK022672; BAB14168.1; -; mRNA.
EMBL; CR457291; CAG33572.1; -; mRNA.
EMBL; AC020575; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC068946; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC097468; AAX88921.1; -; Genomic_DNA.
EMBL; BC008210; AAH08210.2; -; mRNA.
EMBL; BC012732; AAH12732.1; -; mRNA.
EMBL; BC030986; AAH30986.1; -; mRNA.
CCDS; CCDS2432.1; -. [Q9H9Q4-1]
RefSeq; NP_079058.1; NM_024782.2. [Q9H9Q4-1]
UniGene; Hs.225988; -.
PDB; 2QM4; X-ray; 2.30 A; A/B/C/D=1-233.
PDB; 2R9A; X-ray; 2.50 A; A/B=1-224.
PDB; 3Q4F; X-ray; 5.50 A; A/B/E/F=1-224.
PDB; 3RWR; X-ray; 3.94 A; D/E/H/I/L/M/O/Q/S/T/W/X=1-224.
PDB; 3SR2; X-ray; 3.97 A; C/D/G/H=1-224.
PDB; 3W03; X-ray; 8.49 A; A/B=1-233.
PDBsum; 2QM4; -.
PDBsum; 2R9A; -.
PDBsum; 3Q4F; -.
PDBsum; 3RWR; -.
PDBsum; 3SR2; -.
PDBsum; 3W03; -.
ProteinModelPortal; Q9H9Q4; -.
SMR; Q9H9Q4; -.
BioGrid; 122931; 7.
CORUM; Q9H9Q4; -.
DIP; DIP-37959N; -.
IntAct; Q9H9Q4; 7.
MINT; Q9H9Q4; -.
STRING; 9606.ENSP00000349313; -.
iPTMnet; Q9H9Q4; -.
PhosphoSitePlus; Q9H9Q4; -.
BioMuta; NHEJ1; -.
DMDM; 74734059; -.
EPD; Q9H9Q4; -.
MaxQB; Q9H9Q4; -.
PaxDb; Q9H9Q4; -.
PeptideAtlas; Q9H9Q4; -.
PRIDE; Q9H9Q4; -.
Ensembl; ENST00000356853; ENSP00000349313; ENSG00000187736. [Q9H9Q4-1]
Ensembl; ENST00000409720; ENSP00000387290; ENSG00000187736. [Q9H9Q4-2]
GeneID; 79840; -.
KEGG; hsa:79840; -.
UCSC; uc002vjp.5; human. [Q9H9Q4-1]
CTD; 79840; -.
DisGeNET; 79840; -.
EuPathDB; HostDB:ENSG00000187736.12; -.
GeneCards; NHEJ1; -.
HGNC; HGNC:25737; NHEJ1.
HPA; CAB012334; -.
HPA; HPA043869; -.
MalaCards; NHEJ1; -.
MIM; 611290; gene.
MIM; 611291; phenotype.
neXtProt; NX_Q9H9Q4; -.
OpenTargets; ENSG00000187736; -.
Orphanet; 208447; Bilateral generalized polymicrogyria.
Orphanet; 169079; Cernunnos-XLF deficiency.
PharmGKB; PA144596401; -.
eggNOG; ENOG410IT7Y; Eukaryota.
eggNOG; ENOG411291V; LUCA.
GeneTree; ENSGT00390000009940; -.
HOGENOM; HOG000089974; -.
HOVERGEN; HBG080703; -.
InParanoid; Q9H9Q4; -.
KO; K10980; -.
OMA; YWNFHCI; -.
OrthoDB; EOG091G1269; -.
PhylomeDB; Q9H9Q4; -.
TreeFam; TF328567; -.
Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ).
SIGNOR; Q9H9Q4; -.
ChiTaRS; NHEJ1; human.
EvolutionaryTrace; Q9H9Q4; -.
GeneWiki; XLF_(protein); -.
GenomeRNAi; 79840; -.
PRO; PR:Q9H9Q4; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000187736; -.
CleanEx; HS_NHEJ1; -.
ExpressionAtlas; Q9H9Q4; baseline and differential.
Genevisible; Q9H9Q4; HS.
GO; GO:0032807; C:DNA ligase IV complex; IBA:GO_Central.
GO; GO:0001650; C:fibrillar center; IDA:HPA.
GO; GO:0070419; C:nonhomologous end joining complex; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0045027; F:DNA end binding; IBA:GO_Central.
GO; GO:0030183; P:B cell differentiation; IMP:UniProtKB.
GO; GO:0007417; P:central nervous system development; NAS:UniProtKB.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:UniProtKB.
GO; GO:0051351; P:positive regulation of ligase activity; NAS:UniProtKB.
GO; GO:0010212; P:response to ionizing radiation; IDA:UniProtKB.
GO; GO:0030217; P:T cell differentiation; IMP:UniProtKB.
InterPro; IPR015381; XLF_fam.
Pfam; PF09302; XLF; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chromosomal rearrangement;
Coiled coil; Complete proteome; Disease mutation; DNA damage;
DNA repair; DNA-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; SCID.
CHAIN 1 299 Non-homologous end-joining factor 1.
/FTId=PRO_0000228654.
REGION 1 135 Globular head.
COILED 128 170 {ECO:0000269|PubMed:18046455}.
MOD_RES 245 245 Phosphoserine.
{ECO:0000250|UniProtKB:Q3KNJ2}.
MOD_RES 287 287 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 276 299 GTSGPLQRPQLSKVKRKKPRGLFS -> ALCRDLSCQRSRG
RSQGVSSVNLLWPQLLRMDLENSFQASP (in isoform
2). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_017689.
VARIANT 14 14 A -> T (in dbSNP:rs34689457).
/FTId=VAR_038790.
VARIANT 57 57 R -> G (in NHEJ1-SCID; fails to
translocate to the nucleus;
dbSNP:rs118204451).
{ECO:0000269|PubMed:16439204,
ECO:0000269|PubMed:17317666}.
/FTId=VAR_025704.
VARIANT 89 89 H -> R (in dbSNP:rs1056296).
/FTId=VAR_038791.
VARIANT 123 123 C -> R (in NHEJ1-SCID;
dbSNP:rs118204452).
{ECO:0000269|PubMed:16439204}.
/FTId=VAR_025705.
VARIANT 256 256 Q -> L (in dbSNP:rs35270667).
/FTId=VAR_038792.
CONFLICT 256 256 Q -> R (in Ref. 3; CAG33572).
{ECO:0000305}.
HELIX 1 9 {ECO:0000244|PDB:2QM4}.
STRAND 14 17 {ECO:0000244|PDB:2QM4}.
STRAND 19 30 {ECO:0000244|PDB:2QM4}.
STRAND 33 39 {ECO:0000244|PDB:2QM4}.
STRAND 44 49 {ECO:0000244|PDB:2QM4}.
HELIX 51 61 {ECO:0000244|PDB:2QM4}.
HELIX 69 85 {ECO:0000244|PDB:2QM4}.
STRAND 94 100 {ECO:0000244|PDB:2QM4}.
STRAND 103 112 {ECO:0000244|PDB:2QM4}.
STRAND 115 125 {ECO:0000244|PDB:2QM4}.
HELIX 128 134 {ECO:0000244|PDB:2QM4}.
HELIX 136 169 {ECO:0000244|PDB:2QM4}.
HELIX 186 196 {ECO:0000244|PDB:2QM4}.
HELIX 198 201 {ECO:0000244|PDB:2QM4}.
HELIX 208 213 {ECO:0000244|PDB:2QM4}.
HELIX 215 228 {ECO:0000244|PDB:2QM4}.
SEQUENCE 299 AA; 33337 MW; BC5C68076A5E7A96 CRC64;
MEELEQGLLM QPWAWLQLAE NSLLAKVFIT KQGYALLVSD LQQVWHEQVD TSVVSQRAKE
LNKRLTAPPA AFLCHLDNLL RPLLKDAAHP SEATFSCDCV ADALILRVRS ELSGLPFYWN
FHCMLASPSL VSQHLIRPLM GMSLALQCQV RELATLLHMK DLEIQDYQES GATLIRDRLK
TEPFEENSFL EQFMIEKLPE ACSIGDGKPF VMNLQDLYMA VTTQEVQVGQ KHQGAGDPHT
SNSASLQGID SQCVNQPEQL VSSAPTLSAP EKESTGTSGP LQRPQLSKVK RKKPRGLFS


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EIAAB27146 Homo sapiens,Human,NHEJ1,Non-homologous end-joining factor 1,Protein cernunnos,XLF,XRCC4-like factor
CSB-EL015787RA Rat Non-homologous end-joining factor 1(NHEJ1) ELISA kit 96T
CSB-EL015787MO Mouse Non-homologous end-joining factor 1(NHEJ1) ELISA kit 96T
CSB-EL015787HU Human Non-homologous end-joining factor 1(NHEJ1) ELISA kit 96T
CSB-EL015787RA Rat Non-homologous end-joining factor 1(NHEJ1) ELISA kit SpeciesRat 96T
CSB-EL015787MO Mouse Non-homologous end-joining factor 1(NHEJ1) ELISA kit SpeciesMouse 96T
NHEJ1_RAT ELISA Kit FOR Non-homologous end-joining factor 1; organism: Rat; gene name: Nhej1 96T
CSB-EL015787HU Human Non-homologous end-joining factor 1(NHEJ1) ELISA kit SpeciesHuman 96T
NHEJ1_MOUSE ELISA Kit FOR Non-homologous end-joining factor 1; organism: Mouse; gene name: Nhej1 96T
18-003-42098 Ets domain transcription factor - ESE3 transcription factor; EHF protein; DJ875K15.1.2 (Ets homologous factor (Ets-domain transcription factor. ESE-3B (Isoform 2))); ETS-family transcription factor EH 0.1 mg Protein A
orb19337 XRCC4-like factor antibody Polyclonal Goat polyclonal to XRCC4-like factor 100
EIAAB12649 EHF,Epithelium-specific Ets transcription factor 3,ESE3,ESE-3,ESE3B,ESEJ,ETS domain-containing transcription factor,ETS homologous factor,hEHF,Homo sapiens,Human
EIAAB12651 Bos taurus,Bovine,EHF,ETS domain-containing transcription factor,ETS homologous factor
EIAAB12650 Ehf,ETS domain-containing transcription factor,ETS homologous factor,Mouse,Mus musculus
U2116h CLIA 1F5 antigen,20 kDa homologous restriction factor,CD59,CD59 glycoprotein,Homo sapiens,HRF20,HRF-20,Human,MACIF,MAC-inhibitory protein,MAC-IP,MEM43 antigen,Membrane attack complex inhibition factor 96T
EHMT1 EHF Gene ets homologous factor
RPR-436 Recombinant Human Ets Homologous Factor 2
RPR-193 Recombinant Human Nonhomologous End-Joining Factor 1 2
GWB-AA7090 Anti- EHF (ets homologous factor) Antibody
GWB-4DA524 Anti- EHF (ets homologous factor) Antibody
pro-1436 Recombinant Human Ets Homologous Factor 10
E13568r Bovine ELISA Kit FOR ETS homologous factor 96T
pro-1436 Recombinant Human Ets Homologous Factor 2


 

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