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

 NHEJ1_MOUSE             Reviewed;         295 AA.
Q3KNJ2; A2RT39; Q99JK0; Q9D9U0;
21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
08-NOV-2005, sequence version 1.
23-FEB-2022, entry version 107.
RecName: Full=Non-homologous end-joining factor 1 {ECO:0000305};
AltName: Full=Protein cernunnos {ECO:0000303|PubMed:17360556};
AltName: Full=XRCC4-like factor {ECO:0000303|PubMed:17360556};
Name=Nhej1 {ECO:0000312|MGI:MGI:1922820};
Synonyms=Xlf {ECO:0000303|PubMed:17360556};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=Czech II; TISSUE=Brain, and Mammary tumor;
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).
[3]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17360556; DOI=10.1073/pnas.0611734104;
Zha S., Alt F.W., Cheng H.-L., Brush J.W., Li G.;
"Defective DNA repair and increased genomic instability in Cernunnos-XLF-
deficient murine ES cells.";
Proc. Natl. Acad. Sci. U.S.A. 104:4518-4523(2007).
[4]
DISRUPTION PHENOTYPE.
PubMed=18775323; DOI=10.1016/j.molcel.2008.07.017;
Li G., Alt F.W., Cheng H.L., Brush J.W., Goff P.H., Murphy M.M., Franco S.,
Zhang Y., Zha S.;
"Lymphocyte-specific compensation for XLF/cernunnos end-joining functions
in V(D)J recombination.";
Mol. Cell 31:631-640(2008).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and expression.";
Cell 143:1174-1189(2010).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=27601299; DOI=10.1016/j.celrep.2016.08.069;
Lescale C., Lenden Hasse H., Blackford A.N., Balmus G., Bianchi J.J.,
Yu W., Bacoccina L., Jarade A., Clouin C., Sivapalan R.,
Reina-San-Martin B., Jackson S.P., Deriano L.;
"Specific roles of XRCC4 paralogs PAXX and XLF during V(D)J
recombination.";
Cell Rep. 16:2967-2979(2016).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=27798842; DOI=10.1101/gad.290510.116;
Balmus G., Barros A.C., Wijnhoven P.W., Lescale C., Hasse H.L.,
Boroviak K., le Sage C., Doe B., Speak A.O., Galli A., Jacobsen M.,
Deriano L., Adams D.J., Blackford A.N., Jackson S.P.;
"Synthetic lethality between PAXX and XLF in mammalian development.";
Genes Dev. 30:2152-2157(2016).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=27601633; DOI=10.1073/pnas.1611882113;
Kumar V., Alt F.W., Frock R.L.;
"PAXX and XLF DNA repair factors are functionally redundant in joining DNA
breaks in a G1-arrested progenitor B-cell line.";
Proc. Natl. Acad. Sci. U.S.A. 113:10619-10624(2016).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=27830975; DOI=10.1080/15384101.2016.1253640;
Hung P.J., Chen B.R., George R., Liberman C., Morales A.J., Colon-Ortiz P.,
Tyler J.K., Sleckman B.P., Bredemeyer A.L.;
"Deficiency of XLF and PAXX prevents DNA double-strand break repair by non-
homologous end joining in lymphocytes.";
Cell Cycle 16:286-295(2017).
[10]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=28051062; DOI=10.1038/ncomms13816;
Liu X., Shao Z., Jiang W., Lee B.J., Zha S.;
"PAXX promotes KU accumulation at DNA breaks and is essential for end-
joining in XLF-deficient mice.";
Nat. Commun. 8:13816-13816(2017).
[11]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=29077092; DOI=10.1038/cdd.2017.184;
Abramowski V., Etienne O., Elsaid R., Yang J., Berland A., Kermasson L.,
Roch B., Musilli S., Moussu J.P., Lipson-Ruffert K., Revy P., Cumano A.,
Boussin F.D., de Villartay J.P.;
"PAXX and Xlf interplay revealed by impaired CNS development and
immunodeficiency of double KO mice.";
Cell Death Differ. 25:444-452(2018).
[12]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=30017584; DOI=10.1016/j.molcel.2018.06.018;
Hung P.J., Johnson B., Chen B.R., Byrum A.K., Bredemeyer A.L.,
Yewdell W.T., Johnson T.E., Lee B.J., Deivasigamani S., Hindi I.,
Amatya P., Gross M.L., Paull T.T., Pisapia D.J., Chaudhuri J.,
Petrini J.J.H., Mosammaparast N., Amarasinghe G.K., Zha S., Tyler J.K.,
Sleckman B.P.;
"MRI is a DNA damage response adaptor during classical non-homologous end
joining.";
Mol. Cell 71:332-342(2018).
-!- FUNCTION: DNA repair protein involved in DNA non-homologous end joining
(NHEJ); required for double-strand break (DSB) repair and V(D)J
recombination (PubMed:17360556, PubMed:27601299, PubMed:27798842,
PubMed:27601633, PubMed:27830975, PubMed:28051062, PubMed:29077092,
PubMed:30017584). Plays a key role in NHEJ by promoting the ligation of
various mismatched and non-cohesive ends (PubMed:17360556). Interacts
with POLL (DNA polymerase lambda); promoting POLL recruitment to
double-strand breaks (DSBs) and stimulation of the end-filling activity
of POLL (By similarity). May act in concert with XRCC5-XRCC6 (Ku) to
stimulate XRCC4-mediated joining of blunt ends and several types of
mismatched ends that are non-complementary or partially complementary
(PubMed:17360556). Associates with XRCC4 to form alternating helical
filaments that bridge DNA and act like a bandage, holding together the
broken DNA until it is repaired (By similarity). The XRCC4-NHEJ1/XLF
subcomplex binds to the DNA fragments of a DSB in a highly diffusive
manner and robustly bridges two independent DNA molecules, holding the
broken DNA fragments in close proximity to one other (By similarity).
The mobility of the bridges ensures that the ends remain accessible for
further processing by other repair factors (By similarity). Binds DNA
in a length-dependent manner (By similarity).
{ECO:0000250|UniProtKB:Q9H9Q4, ECO:0000269|PubMed:17360556,
ECO:0000269|PubMed:27601299, ECO:0000269|PubMed:27601633,
ECO:0000269|PubMed:27798842, ECO:0000269|PubMed:27830975,
ECO:0000269|PubMed:28051062, ECO:0000269|PubMed:29077092,
ECO:0000269|PubMed:30017584}.
-!- SUBUNIT: Homodimer; mainly exists as a homodimer when not associated
with XRCC4. Interacts with XRCC4; the interaction is direct and is
mediated via a head-to-head interaction between N-terminal head
regions. Component of the core long-range non-homologous end joining
(NHEJ) complex (also named DNA-PK complex) composed of PRKDC, LIG4,
XRCC4, XRCC6/Ku70, XRCC5/Ku86 and NHEJ1/XLF. Additional component of
the NHEJ complex includes PAXX. Following autophosphorylation, PRKDC
dissociates from DNA, leading to formation of the short-range NHEJ
complex, composed of LIG4, XRCC4, XRCC6/Ku70, XRCC5/Ku86 and NHEJ1/XLF.
Interacts with POLL (DNA polymerase lambda); promoting POLL recruitment
to double-strand breaks (DSBs) and stimulation of the end-filling
activity of POLL. {ECO:0000250|UniProtKB:Q9H9Q4}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H9Q4}.
Chromosome {ECO:0000250|UniProtKB:Q9H9Q4}. Note=Localizes to site of
double-strand breaks; recruitment is dependent on XRCC5-XRCC6 (Ku)
heterodimer. {ECO:0000250|UniProtKB:Q9H9Q4}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q3KNJ2-1; Sequence=Displayed;
Name=2;
IsoId=Q3KNJ2-2; Sequence=VSP_017690;
-!- DOMAIN: The coiled-coil region mediates homodimerization.
{ECO:0000250|UniProtKB:Q9H9Q4}.
-!- DOMAIN: The Leu-lock (Leu-115) site inserts into a hydrophobic pocket
in XRCC4. {ECO:0000250|UniProtKB:Q9H9Q4}.
-!- PTM: Phosphorylated by PRKDC at the C-terminus in response to DNA
damage. Phosphorylation by PRKDC at the C-terminus of XRCC4 and
NHEJ1/XLF are highly redundant and regulate ability of the XRCC4-
NHEJ1/XLF subcomplex to bridge DNA. Phosphorylation does not prevent
interaction with XRCC4 but disrupts ability to bridge DNA and promotes
detachment from DNA. {ECO:0000250|UniProtKB:Q9H9Q4}.
-!- DISRUPTION PHENOTYPE: Embryonic stem cells are highly sensitive to
ionizing radiation and have intrinsic DNA double-strand break repair
defects (PubMed:17360556). In contrast, knockout mice only have a
relatively mild phenotype with no growth defects, neuronal cell death
or overt immunodeficiency (PubMed:18775323). Mature lymphocyte numbers
are slightly decreased, and pro-B lines, while ionizing radiation-
sensitive, perform V(D)J recombination at nearly wild-type levels
(PubMed:18775323). Mice lacking both Paxx and Nhej1/Xlf show embryonic
lethality caused by severe defects in classical non-homologous end
joining (NHEJ) (PubMed:27601299, PubMed:27798842, PubMed:27601633,
PubMed:27830975, PubMed:28051062, PubMed:29077092). Mice lacking both
Cyren and Nhej1/Xlf show embryonic lethality caused by severe defects
in classical non-homologous end joining (NHEJ) (PubMed:30017584).
{ECO:0000269|PubMed:17360556, ECO:0000269|PubMed:18775323,
ECO:0000269|PubMed:27601299, ECO:0000269|PubMed:27601633,
ECO:0000269|PubMed:27798842, ECO:0000269|PubMed:27830975,
ECO:0000269|PubMed:28051062, ECO:0000269|PubMed:29077092,
ECO:0000269|PubMed:30017584}.
-!- SIMILARITY: Belongs to the XRCC4-XLF family. XLF subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB24611.1; Type=Erroneous initiation; Evidence={ECO:0000305};
---------------------------------------------------------------------------
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EMBL; AK006481; BAB24611.1; ALT_INIT; mRNA.
EMBL; BC006063; AAH06063.1; -; mRNA.
EMBL; BC107252; AAI07253.1; -; mRNA.
EMBL; BC107253; AAI07254.1; -; mRNA.
EMBL; BC132359; AAI32360.1; -; mRNA.
EMBL; BC132361; AAI32362.1; -; mRNA.
RefSeq; NP_083618.3; NM_029342.4. [Q3KNJ2-1]
SMR; Q3KNJ2; -.
IntAct; Q3KNJ2; 1.
MINT; Q3KNJ2; -.
STRING; 10090.ENSMUSP00000116797; -.
iPTMnet; Q3KNJ2; -.
PhosphoSitePlus; Q3KNJ2; -.
EPD; Q3KNJ2; -.
MaxQB; Q3KNJ2; -.
PaxDb; Q3KNJ2; -.
PeptideAtlas; Q3KNJ2; -.
PRIDE; Q3KNJ2; -.
ProteomicsDB; 293652; -. [Q3KNJ2-1]
ProteomicsDB; 293653; -. [Q3KNJ2-2]
Ensembl; ENSMUST00000152855; ENSMUSP00000116797; ENSMUSG00000026162. [Q3KNJ2-1]
GeneID; 75570; -.
KEGG; mmu:75570; -.
UCSC; uc029qpd.1; mouse. [Q3KNJ2-1]
CTD; 79840; -.
MGI; MGI:1922820; Nhej1.
eggNOG; ENOG502S0R3; Eukaryota.
GeneTree; ENSGT00390000009940; -.
InParanoid; Q3KNJ2; -.
OMA; QCHGREL; -.
OrthoDB; 1397591at2759; -.
PhylomeDB; Q3KNJ2; -.
Reactome; R-MMU-5693571; Nonhomologous End-Joining (NHEJ).
BioGRID-ORCS; 75570; 17 hits in 80 CRISPR screens.
ChiTaRS; Nhej1; mouse.
PRO; PR:Q3KNJ2; -.
Proteomes; UP000000589; Chromosome 1.
RNAct; Q3KNJ2; protein.
GO; GO:0032807; C:DNA ligase IV complex; IBA:GO_Central.
GO; GO:0001650; C:fibrillar center; ISO:MGI.
GO; GO:0070419; C:nonhomologous end joining complex; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
GO; GO:0045027; F:DNA end binding; ISS:UniProtKB.
GO; GO:0070182; F:DNA polymerase binding; ISO:MGI.
GO; GO:0030183; P:B cell differentiation; ISS:UniProtKB.
GO; GO:0051103; P:DNA ligation involved in DNA repair; ISO:MGI.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:UniProtKB.
GO; GO:0033152; P:immunoglobulin V(D)J recombination; ISS:UniProtKB.
GO; GO:0010212; P:response to ionizing radiation; ISS:UniProtKB.
GO; GO:0030217; P:T cell differentiation; ISS:UniProtKB.
Gene3D; 2.170.210.10; -; 1.
InterPro; IPR015381; XLF_N.
InterPro; IPR038051; XRCC4-like_N_sf.
Pfam; PF09302; XLF; 1.
1: Evidence at protein level;
Alternative splicing; Chromosome; Coiled coil; DNA damage; DNA repair;
DNA-binding; Nucleus; Phosphoprotein; Reference proteome.
CHAIN 1..295
/note="Non-homologous end-joining factor 1"
/id="PRO_0000228655"
REGION 1..135
/note="Globular head"
/evidence="ECO:0000250|UniProtKB:Q9H9Q4"
REGION 228..295
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COILED 128..170
/evidence="ECO:0000250|UniProtKB:Q9H9Q4"
MOTIF 285..295
/note="XLM"
/evidence="ECO:0000250|UniProtKB:Q9H9Q4"
COMPBIAS 228..267
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 280..295
/note="Basic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
SITE 115
/note="Leu-lock"
/evidence="ECO:0000250|UniProtKB:Q9H9Q4"
MOD_RES 132
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q9H9Q4"
MOD_RES 245
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:21183079"
MOD_RES 262
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:Q9H9Q4"
VAR_SEQ 131..196
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:16141072"
/id="VSP_017690"
CONFLICT 260
/note="S -> P (in Ref. 2; AAH06063)"
/evidence="ECO:0000305"
CONFLICT 281
/note="R -> Q (in Ref. 2; AAH06063)"
/evidence="ECO:0000305"
SEQUENCE 295 AA; 32739 MW; 679D548AC627696D CRC64;
MEELEQDLLL QPWAWLQLAE NSLLAKVSIT KHGYALLISD LQQVWHEQVD TSVVSQRAKE
LNKRLTAPPA ALLCHLDEAL RPLFKDSAHP SKATFSCDRG EEGLILRVQS ELSGLPFSWH
FHCIPASSSL VSQHLIHPLM GVSLALQSHV RELAALLRMK DLEIQAYQES GAVLSRSRLK
TEPFEENSFL EQFMAEKLPE ACAVGDGKPF AMSLQSLYVA VTKQQIQARQ AHKDSGETQA
SSSTSPRGTD NQPEEPVSLS STLSEPEYEP VAASGPMHRA RLVKSKRKKP RGLFS


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Related Genes :
[NHEJ1 XLF] Non-homologous end-joining factor 1 (Protein cernunnos) (XRCC4-like factor)
[Nhej1 Xlf] Non-homologous end-joining factor 1 (Protein cernunnos) (XRCC4-like factor)
[XRCC4] DNA repair protein XRCC4 (hXRCC4) (X-ray repair cross-complementing protein 4) [Cleaved into: Protein XRCC4, C-terminus (XRCC4/C)]
[Nhej1 Xlf] Non-homologous end-joining factor 1 (Protein cernunnos) (XRCC4-like factor)
[Xrcc4] DNA repair protein XRCC4 (X-ray repair cross-complementing protein 4) [Cleaved into: Protein XRCC4, C-terminus (XRCC4/C)]
[PAXX C9orf142 XLS] Protein PAXX (Paralog of XRCC4 and XLF) (XRCC4-like small protein)
[Paxx] Protein PAXX (Paralog of XRCC4 and XLF)
[PRKDC HYRC HYRC1] DNA-dependent protein kinase catalytic subunit (DNA-PK catalytic subunit) (DNA-PKcs) (EC 2.7.11.1) (DNPK1) (p460)
[XRCC6 G22P1] X-ray repair cross-complementing protein 6 (EC 3.6.4.-) (EC 4.2.99.-) (5'-deoxyribose-5-phosphate lyase Ku70) (5'-dRP lyase Ku70) (70 kDa subunit of Ku antigen) (ATP-dependent DNA helicase 2 subunit 1) (ATP-dependent DNA helicase II 70 kDa subunit) (CTC box-binding factor 75 kDa subunit) (CTC75) (CTCBF) (DNA repair protein XRCC6) (Lupus Ku autoantigen protein p70) (Ku70) (Thyroid-lupus autoantigen) (TLAA) (X-ray repair complementing defective repair in Chinese hamster cells 6)
[APLF C2orf13 PALF XIP1] Aprataxin and PNK-like factor (EC 3.1.-.-) (Apurinic-apyrimidinic endonuclease APLF) (PNK and APTX-like FHA domain-containing protein) (XRCC1-interacting protein 1)
[ligD PA2138] Multifunctional non-homologous end joining protein LigD (NHEJ DNA polymerase) [Includes: 3'-phosphoesterase (3'-ribonuclease/3'-phosphatase); DNA ligase D (LigD) (EC 6.5.1.1) (Polydeoxyribonucleotide synthase [ATP]); DNA repair polymerase (Pol) (Polymerase/primase)]
[ligD MSMEG_5570 MSMEI_5419] Multifunctional non-homologous end joining protein LigD (NHEJ DNA polymerase) [Includes: DNA repair polymerase (Pol) (Polymerase/primase); 3'-phosphoesterase (3'-ribonuclease/3'-phosphatase) (PE); DNA ligase (Lig) (EC 6.5.1.1) (Polydeoxyribonucleotide synthase [ATP])]
[ligD Rv0938 MTCY08D9.01c MTCY10D7.36c] Multifunctional non-homologous end joining DNA repair protein LigD (NHEJ DNA repair protein D) (Mt-Lig) (NHEJ DNA polymerase) [Includes: DNA repair polymerase (Pol) (Polymerase/primase); 3'-phosphoesterase (3'-ribonuclease/3'-phosphatase) (PE); DNA ligase (Lig) (EC 6.5.1.1) (Polydeoxyribonucleotide synthase [ATP])]
[Aplf] Aprataxin and PNK-like factor (EC 3.1.-.-) (Apurinic-apyrimidinic endonuclease APLF)
[CYREN C7orf49 MRI] Cell cycle regulator of non-homologous end joining (Cell cycle regulator of NHEJ) (Modulator of retrovirus infection homolog)
[Cyren Mri] Cell cycle regulator of non-homologous end joining (Cell cycle regulator of NHEJ) (Modulator of retrovirus infection homolog)
[XRCC4 At3g23100 MXC7.14] DNA repair protein XRCC4
[mku Rv0937c] Non-homologous end joining protein Ku (Mt-Ku)
[ligD BQ2027_MB0963] Multifunctional non-homologous end joining protein LigD (NHEJ DNA polymerase) [Includes: DNA repair polymerase (Pol) (Polymerase/primase); 3'-phosphoesterase (3'-ribonuclease/3'-phosphatase) (PE); DNA ligase (Lig) (EC 6.5.1.1) (Polydeoxyribonucleotide synthase [ATP])]
[FBXW7 FBW7 FBX30 SEL10] F-box/WD repeat-containing protein 7 (Archipelago homolog) (hAgo) (F-box and WD-40 domain-containing protein 7) (F-box protein FBX30) (SEL-10) (hCdc4)
[FGF13 FHF2] Fibroblast growth factor 13 (FGF-13) (Fibroblast growth factor homologous factor 2) (FHF-2)
[AIFM2 AMID PRG3] Ferroptosis suppressor protein 1 (FSP1) (EC 1.6.5.-) (Apoptosis-inducing factor homologous mitochondrion-associated inducer of death) (AMID) (p53-responsive gene 3 protein)
[CD59 MIC11 MIN1 MIN2 MIN3 MSK21] CD59 glycoprotein (1F5 antigen) (20 kDa homologous restriction factor) (HRF-20) (HRF20) (MAC-inhibitory protein) (MAC-IP) (MEM43 antigen) (Membrane attack complex inhibition factor) (MACIF) (Membrane inhibitor of reactive lysis) (MIRL) (Protectin) (CD antigen CD59)
[Fbxw7 Fbw7 Fbwd6 Fbxw6] F-box/WD repeat-containing protein 7 (F-box and WD-40 domain-containing protein 7) (F-box protein FBW7) (F-box protein Fbxw6) (F-box-WD40 repeat protein 6) (SEL-10)
[LIG4] DNA ligase 4 (EC 6.5.1.1) (DNA ligase IV) (Polydeoxyribonucleotide synthase [ATP] 4)
[MYC2 BHLH6 EN38 JAI1 JIN1 RAP1 RD22BP1 ZBF1 At1g32640 F6N18.4] Transcription factor MYC2 (AtMYC2) (Basic helix-loop-helix protein 6) (AtbHLH6) (bHLH 6) (Protein JASMONATE INSENSITIVE 1) (R-homologous Arabidopsis protein 1) (RAP-1) (Transcription factor EN 38) (Z-box binding factor 1 protein) (bHLH transcription factor bHLH006) (rd22BP1)
[EIF4E2 EIF4EL3] Eukaryotic translation initiation factor 4E type 2 (eIF-4E type 2) (eIF4E type 2) (Eukaryotic translation initiation factor 4E homologous protein) (Eukaryotic translation initiation factor 4E-like 3) (eIF4E-like protein 4E-LP) (mRNA cap-binding protein 4EHP) (h4EHP) (mRNA cap-binding protein type 3)
[APLF] Aprataxin and PNK-like factor (EC 3.1.1.-) (Apurinic-apyrimidinic endonuclease APLF)
[FBXW7 FBW7] F-box/WD repeat-containing protein 7 (F-box and WD-40 domain-containing protein 7)
[Fbxw7] F-box/WD repeat-containing protein 7

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