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Cell cycle regulator of non-homologous end joining (Cell cycle regulator of NHEJ) (Modulator of retrovirus infection homolog)

 CYREN_HUMAN             Reviewed;         157 AA.
Q9BWK5; A0A024R780; A0A087WWQ8; Q6NWZ4; Q6ZNR5;
26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
26-FEB-2008, sequence version 2.
12-AUG-2020, entry version 128.
RecName: Full=Cell cycle regulator of non-homologous end joining {ECO:0000303|PubMed:28959974};
Short=Cell cycle regulator of NHEJ {ECO:0000303|PubMed:28959974};
AltName: Full=Modulator of retrovirus infection homolog {ECO:0000250|UniProtKB:Q09HN1};
Name=CYREN {ECO:0000312|HGNC:HGNC:22432};
Synonyms=C7orf49 {ECO:0000312|HGNC:HGNC:22432},
MRI {ECO:0000250|UniProtKB:Q09HN1};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
TISSUE=Thymus;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Mammary gland, and Placenta;
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]
PROTEIN SEQUENCE OF 54-69 (ISOFORM 4), FUNCTION, INTERACTION WITH XRCC5 AND
XRCC6, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
PubMed=24610814; DOI=10.1074/jbc.c113.533968;
Slavoff S.A., Heo J., Budnik B.A., Hanakahi L.A., Saghatelian A.;
"A human short open reading frame (sORF)-encoded polypeptide that
stimulates DNA end joining.";
J. Biol. Chem. 289:10950-10957(2014).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-terminal
acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[8]
FUNCTION, INTERACTION WITH XRCC5 AND XRCC6, DOMAIN, AND MUTAGENESIS OF
ARG-11; PRO-14 AND TRP-16.
PubMed=28959974; DOI=10.1038/nature24023;
Arnoult N., Correia A., Ma J., Merlo A., Garcia-Gomez S., Maric M.,
Tognetti M., Benner C.W., Boulton S.J., Saghatelian A., Karlseder J.;
"Regulation of DNA repair pathway choice in S and G2 phases by the NHEJ
inhibitor CYREN.";
Nature 549:548-552(2017).
[9]
VARIANT [LARGE SCALE ANALYSIS] LEU-82.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
-!- FUNCTION: [Isoform 1]: Cell-cycle-specific inhibitor of classical non-
homologous end joining (NHEJ) of DNA double-strand break (DSB) repair
during the S and G2 phases (PubMed:28959974). Acts as a regulator of
DNA repair pathway choice by specifically inhibiting classical NHEJ
during the S and G2 phases, thereby promoting error-free repair by
homologous recombination during cell cycle phases when sister
chromatids are present (PubMed:28959974). Preferentially protects
single-stranded overhangs at break sites by inhibiting classical NHEJ,
thereby creating a local environment that favors homologous
recombination (PubMed:28959974). Acts via interaction with XRCC5/Ku80
and XRCC6/Ku70, interaction restricted during the S and G2 phases only
(PubMed:28959974). Molecular mechanisms governing classical NHEJ
inhibition via interaction with XRCC5/Ku80 and XRCC6/Ku70 are unknown
(PubMed:28959974). May act as a regulator of proteasome (By
similarity). {ECO:0000250|UniProtKB:Q09HN1,
ECO:0000269|PubMed:28959974}.
-!- FUNCTION: [Isoform 4]: Cell-cycle-specific inhibitor of classical non-
homologous end joining (NHEJ) of DNA double-strand break (DSB) repair
during the S and G2 phases (PubMed:24610814, PubMed:28959974). Acts as
a regulator of DNA repair pathway choice by specifically inhibiting
classical NHEJ during the S and G2 phases, thereby promoting error-free
repair by homologous recombination during cell cycle phases when sister
chromatids are present (PubMed:28959974). Preferentially protects
single-stranded overhangs at break sites by inhibiting classical NHEJ,
thereby creating a local environment that favors homologous
recombination (PubMed:28959974). Acts via interaction with XRCC5/Ku80
and XRCC6/Ku70, interaction restricted during the S and G2 phases only
(PubMed:28959974). Molecular mechanisms governing classical NHEJ
inhibition via interaction with XRCC5/Ku80 and XRCC6/Ku70 are unknown
(PubMed:28959974). {ECO:0000269|PubMed:24610814,
ECO:0000269|PubMed:28959974}.
-!- SUBUNIT: Isoform 1: Interacts (via KBM motif) with XRCC5/Ku80 and
XRCC6/Ku70 heterodimer; interaction is restricted during the S and G2
phases (PubMed:24610814, PubMed:28959974). Isoform 4: Interacts (via
KBM motif) with XRCC5/Ku80 and XRCC6/Ku70 heterodimer; interaction is
restricted during the S and G2 phases (PubMed:24610814,
PubMed:28959974). Isoform 3: Does not interact with XRCC5/Ku80 and
XRCC6/Ku70 heterodimer (PubMed:24610814). {ECO:0000269|PubMed:24610814,
ECO:0000269|PubMed:28959974}.
-!- INTERACTION:
Q9BWK5; H7BXQ9: ERCC6L2; NbExp=3; IntAct=EBI-8787584, EBI-10300946;
Q9BWK5; Q5T890: ERCC6L2; NbExp=3; IntAct=EBI-8787584, EBI-3951765;
Q9BWK5; Q9UL63: MKLN1; NbExp=3; IntAct=EBI-8787584, EBI-1048053;
-!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm
{ECO:0000269|PubMed:24610814}. Nucleus {ECO:0000269|PubMed:24610814}.
Note=Nuclear localization may depend upon interaction with XRCC5/Ku80
and XRCC6/Ku70 heterodimer. {ECO:0000269|PubMed:24610814}.
-!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm
{ECO:0000269|PubMed:24610814}. Note=Some nuclear localization may be
due to passive diffusion. {ECO:0000269|PubMed:24610814}.
-!- SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm
{ECO:0000269|PubMed:24610814}. Nucleus {ECO:0000269|PubMed:24610814}.
Note=Nuclear localization may depend upon interaction with XRCC5/Ku80
and XRCC6/Ku70 heterodimer and increases upon etoposide treatment.
{ECO:0000269|PubMed:24610814}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=CYREN-1 {ECO:0000303|PubMed:28959974}, MRI-1
{ECO:0000303|PubMed:24610814};
IsoId=Q9BWK5-1; Sequence=Displayed;
Name=2;
IsoId=Q9BWK5-2; Sequence=VSP_031768;
Name=3; Synonyms=CYREN-3 {ECO:0000303|PubMed:28959974}, MRI-3
{ECO:0000303|PubMed:24610814};
IsoId=Q9BWK5-3; Sequence=VSP_031767;
Name=4; Synonyms=CYREN-2 {ECO:0000303|PubMed:28959974}, MRI-2
{ECO:0000303|PubMed:24610814};
IsoId=Q9BWK5-4; Sequence=VSP_058524, VSP_058525;
-!- DOMAIN: The KBM (Ku-binding motif) mediates interaction with XRCC5/Ku80
and XRCC6/Ku70. {ECO:0000269|PubMed:28959974}.
-!- CAUTION: Was initially reported to stimulate non-homologous end joining
in vitro (PubMed:24610814). This result was not confirmed by another
group (PubMed:28959974). The difference was possibly due to the
consequences of oversaturating the reaction with recombinant protein in
vitro (PubMed:28959974). {ECO:0000269|PubMed:24610814,
ECO:0000269|PubMed:28959974}.
-!- SEQUENCE CAUTION:
Sequence=AAH00168.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
---------------------------------------------------------------------------
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EMBL; AK026103; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK130795; BAC85431.1; -; mRNA.
EMBL; AC083862; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH236950; EAL24064.1; -; Genomic_DNA.
EMBL; CH471070; EAW83840.1; -; Genomic_DNA.
EMBL; CH471070; EAW83841.1; -; Genomic_DNA.
EMBL; BC000168; AAH00168.1; ALT_INIT; mRNA.
EMBL; BC067350; AAH67350.1; -; mRNA.
CCDS; CCDS5838.2; -. [Q9BWK5-1]
CCDS; CCDS59082.1; -. [Q9BWK5-3]
CCDS; CCDS75663.1; -. [Q9BWK5-4]
RefSeq; NP_001230678.1; NM_001243749.1. [Q9BWK5-4]
RefSeq; NP_001230680.1; NM_001243751.1. [Q9BWK5-4]
RefSeq; NP_001230681.1; NM_001243752.1. [Q9BWK5-4]
RefSeq; NP_001230682.1; NM_001243753.1. [Q9BWK5-4]
RefSeq; NP_001230683.1; NM_001243754.1. [Q9BWK5-3]
RefSeq; NP_001230684.1; NM_001243755.1. [Q9BWK5-3]
RefSeq; NP_001292558.1; NM_001305629.1.
RefSeq; NP_076938.2; NM_024033.3. [Q9BWK5-1]
RefSeq; XP_016868078.1; XM_017012589.1.
RefSeq; XP_016868079.1; XM_017012590.1.
RefSeq; XP_016868080.1; XM_017012591.1. [Q9BWK5-1]
RefSeq; XP_016868082.1; XM_017012593.1. [Q9BWK5-3]
RefSeq; XP_016868083.1; XM_017012594.1. [Q9BWK5-3]
RefSeq; XP_016868084.1; XM_017012595.1. [Q9BWK5-4]
PDB; 6TYU; X-ray; 1.47 A; B=6-21.
PDBsum; 6TYU; -.
SMR; Q9BWK5; -.
BioGRID; 122467; 3.
IntAct; Q9BWK5; 6.
STRING; 9606.ENSP00000376823; -.
iPTMnet; Q9BWK5; -.
PhosphoSitePlus; Q9BWK5; -.
BioMuta; C7orf49; -.
DMDM; 182676205; -.
EPD; Q9BWK5; -.
jPOST; Q9BWK5; -.
MassIVE; Q9BWK5; -.
MaxQB; Q9BWK5; -.
PaxDb; Q9BWK5; -.
PeptideAtlas; Q9BWK5; -.
PRIDE; Q9BWK5; -.
ProteomicsDB; 79284; -. [Q9BWK5-1]
ProteomicsDB; 79285; -. [Q9BWK5-2]
ProteomicsDB; 79286; -. [Q9BWK5-3]
Antibodypedia; 18116; 46 antibodies.
Ensembl; ENST00000393114; ENSP00000376823; ENSG00000122783. [Q9BWK5-1]
Ensembl; ENST00000424142; ENSP00000400024; ENSG00000122783. [Q9BWK5-3]
Ensembl; ENST00000483029; ENSP00000473365; ENSG00000122783. [Q9BWK5-3]
Ensembl; ENST00000617987; ENSP00000480430; ENSG00000122783. [Q9BWK5-4]
Ensembl; ENST00000620897; ENSP00000481014; ENSG00000122783. [Q9BWK5-3]
GeneID; 78996; -.
KEGG; hsa:78996; -.
UCSC; uc003vsl.4; human. [Q9BWK5-1]
UCSC; uc022amb.2; human.
CTD; 78996; -.
DisGeNET; 78996; -.
EuPathDB; HostDB:ENSG00000122783.16; -.
GeneCards; CYREN; -.
HGNC; HGNC:22432; CYREN.
HPA; ENSG00000122783; Low tissue specificity.
MIM; 616980; gene.
neXtProt; NX_Q9BWK5; -.
OpenTargets; ENSG00000122783; -.
PharmGKB; PA162380533; -.
eggNOG; ENOG502SEX2; Eukaryota.
GeneTree; ENSGT00390000013192; -.
HOGENOM; CLU_126072_0_0_1; -.
InParanoid; Q9BWK5; -.
OMA; KACEQPA; -.
OrthoDB; 1634776at2759; -.
PhylomeDB; Q9BWK5; -.
TreeFam; TF336925; -.
PathwayCommons; Q9BWK5; -.
BioGRID-ORCS; 78996; 2 hits in 864 CRISPR screens.
ChiTaRS; C7orf49; human.
GenomeRNAi; 78996; -.
Pharos; Q9BWK5; Tdark.
PRO; PR:Q9BWK5; -.
Proteomes; UP000005640; Chromosome 7.
RNAct; Q9BWK5; protein.
Bgee; ENSG00000122783; Expressed in gastrocnemius and 224 other tissues.
ExpressionAtlas; Q9BWK5; baseline and differential.
Genevisible; Q9BWK5; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IDA:UniProtKB.
GO; GO:2001033; P:negative regulation of double-strand break repair via nonhomologous end joining; IDA:UniProtKB.
InterPro; IPR028278; MRI.
PANTHER; PTHR14566; PTHR14566; 1.
Pfam; PF15325; MRI; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cytoplasm;
Direct protein sequencing; DNA damage; DNA repair; Nucleus; Polymorphism;
Reference proteome.
CHAIN 1..157
/note="Cell cycle regulator of non-homologous end joining"
/id="PRO_0000320948"
MOTIF 1..21
/note="KBM"
/evidence="ECO:0000269|PubMed:28959974"
MOD_RES 1
/note="N-acetylmethionine"
/evidence="ECO:0000244|PubMed:22814378"
VAR_SEQ 1..55
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_031767"
VAR_SEQ 1..45
/note="METLQSETKTRVLPSWLTAQVATKNVAPMKAPKRMRMAAVPVAAA -> MRL
ESLCHLCLACLFF (in isoform 2)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_031768"
VAR_SEQ 47..69
/note="LPATRTVYCMNEAEIVDVALGIL -> CDSSGQKTPANLTPCDKDCVLHE
(in isoform 4)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_058524"
VAR_SEQ 70..157
/note="Missing (in isoform 4)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_058525"
VARIANT 82
/note="P -> L (in a colorectal cancer sample; somatic
mutation; dbSNP:rs776124276)"
/evidence="ECO:0000269|PubMed:16959974"
/id="VAR_039320"
MUTAGEN 11
/note="R->A: Abolishes interaction with XRCC5/Ku80 and
XRCC6/Ku70 and ability to inhibit classical non-homologous
end joining (NHEJ)."
/evidence="ECO:0000269|PubMed:28959974"
MUTAGEN 14
/note="P->A: Abolishes interaction with XRCC5/Ku80 and
XRCC6/Ku70 and ability to inhibit classical non-homologous
end joining (NHEJ)."
/evidence="ECO:0000269|PubMed:28959974"
MUTAGEN 16
/note="W->A: Abolishes interaction with XRCC5/Ku80 and
XRCC6/Ku70 and ability to inhibit classical non-homologous
end joining (NHEJ)."
/evidence="ECO:0000269|PubMed:28959974"
HELIX 15..18
/evidence="ECO:0000244|PDB:6TYU"
SEQUENCE 157 AA; 16829 MW; EA52CB3CCD231B74 CRC64;
METLQSETKT RVLPSWLTAQ VATKNVAPMK APKRMRMAAV PVAAARLPAT RTVYCMNEAE
IVDVALGILI ESRKQEKACE QPALAGADNP EHSPPCSVSP HTSSGSSSEE EDSGKQALAP
GLSPSQRPGG SSSACSRSPE EEEEEDVLKY VREIFFS


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Pathways :
WP840: G1 to S cell cycle control
WP414: Cell Cycle and Cell Division
WP1083: Cell cycle
WP45: G1 to S cell cycle control
WP959: G1 to S cell cycle control
WP1900: Regulation of mitotic cell cycle
WP1775: Cell Cycle Checkpoints
WP1200: Cell cycle
WP1792: Cell Cycle, Mitotic
WP413: G1 to S cell cycle control
WP1078: G1 to S cell cycle control
WP429: Cell cycle
WP445: G1 to S cell cycle control
WP31: Cell cycle
WP190: Cell cycle
WP348: G1 to S cell cycle control
WP1195: G1 to S cell cycle control
WP179: Cell cycle
WP844: Cell cycle
WP1393: Cell cycle
WP964: Cell cycle
WP1782: APC/C-mediated degradation of cell cycle proteins
WP1201: Non-homologous end joining
WP1793: Cell junction organization
WP584: test-cell-graphics

Related Genes :
[INTS13 ASUN C12orf11 GCT1] Integrator complex subunit 13 (Cell cycle regulator Mat89Bb homolog) (Germ cell tumor 1) (Protein asunder homolog) (Sarcoma antigen NY-SAR-95)
[Asun IntS13 Mat89Bb ovary2 CG6814] Protein asunder (Cell cycle regulator Mat89Bb) (Integrator complex subunit 13) (Maternal transcript 89Bb) (Set apart in position or space protein)
[CCAR1 CARP1 DIS] Cell division cycle and apoptosis regulator protein 1 (Cell cycle and apoptosis regulatory protein 1) (CARP-1) (Death inducer with SAP domain)
[NBN NBS NBS1 P95] Nibrin (Cell cycle regulatory protein p95) (Nijmegen breakage syndrome protein 1)
[RCC1 CHC1] Regulator of chromosome condensation (Cell cycle regulatory protein) (Chromosome condensation protein 1)
[Ccar1 Carp1] Cell division cycle and apoptosis regulator protein 1 (Cell cycle and apoptosis regulatory protein 1) (CARP-1)
[CDK13 CDC2L CDC2L5 CHED KIAA1791] Cyclin-dependent kinase 13 (EC 2.7.11.22) (EC 2.7.11.23) (CDC2-related protein kinase 5) (Cell division cycle 2-like protein kinase 5) (Cell division protein kinase 13) (hCDK13) (Cholinesterase-related cell division controller)
[RAD17 R24L] Cell cycle checkpoint protein RAD17 (hRad17) (RF-C/activator 1 homolog)
[CHEK1 CHK1] Serine/threonine-protein kinase Chk1 (EC 2.7.11.1) (CHK1 checkpoint homolog) (Cell cycle checkpoint kinase) (Checkpoint kinase-1)
[RAD1 REC1] Cell cycle checkpoint protein RAD1 (hRAD1) (EC 3.1.11.2) (DNA repair exonuclease rad1 homolog) (Rad1-like DNA damage checkpoint protein)
[TAF1 BA2R CCG1 CCGS TAF2A] Transcription initiation factor TFIID subunit 1 (EC 2.3.1.48) (EC 2.7.11.1) (Cell cycle gene 1 protein) (TBP-associated factor 250 kDa) (p250) (Transcription initiation factor TFIID 250 kDa subunit) (TAF(II)250) (TAFII-250) (TAFII250)
[CDC48 YDL126C] Cell division control protein 48 (EC 3.6.4.6) (Cell division cycle protein 48) (Transitional endoplasmic reticulum ATPase homolog)
[CDC36 DNA19 NOT2 YDL165W] General negative regulator of transcription subunit 2 (cell division cycle protein 36)
[IntS13 Asun Spata30] Integrator complex subunit 13 (Cell cycle regulator Mat89Bb homolog) (Protein asunder homolog) (Spermatogenesis-associated protein 30)
[RAD9A] Cell cycle checkpoint control protein RAD9A (hRAD9) (EC 3.1.11.2) (DNA repair exonuclease rad9 homolog A)
[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])]
[CDC39 NOT1 ROS1 YCR093W YCR1151 YCR93W] General negative regulator of transcription subunit 1 (Cell division cycle protein 39)
[Cdk11b Cdc2l1 Cdk11] Cyclin-dependent kinase 11B (Cell division cycle 2-like protein kinase 1) (Cell division protein kinase 11) (Cyclin-dependent kinase 11) (EC 2.7.11.22) (Galactosyltransferase-associated protein kinase p58/GTA) (PITSLRE serine/threonine-protein kinase CDC2L1)
[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])]
[TBRG4 CPR2 FASTKD4 KIAA0948] FAST kinase domain-containing protein 4 (Cell cycle progression restoration protein 2) (Cell cycle progression protein 2) (Protein TBRG4) (Transforming growth factor beta regulator 4)
[cdc-48.1 C06A1.1] Transitional endoplasmic reticulum ATPase homolog 1 (EC 3.6.4.6) (Cell division cycle-related protein 48.1) (p97/CDC48 homolog 1)
[cdc-48.2 C41C4.8] Transitional endoplasmic reticulum ATPase homolog 2 (EC 3.6.4.6) (Cell division cycle-related protein 48.2) (p97/CDC48 homolog 2)
[CDK9 CDC2L4 TAK] Cyclin-dependent kinase 9 (EC 2.7.11.22) (EC 2.7.11.23) (C-2K) (Cell division cycle 2-like protein kinase 4) (Cell division protein kinase 9) (Serine/threonine-protein kinase PITALRE) (Tat-associated kinase complex catalytic subunit)
[Rad9a Rad9] Cell cycle checkpoint control protein RAD9A (mRAD9) (EC 3.1.11.2) (DNA repair exonuclease rad9 homolog A) (Rad9-like protein)
[mat-3 apc-8 cdc-23 pod-4 vex-2 F10C5.1] Cell division cycle protein 23 homolog (Anaphase-promoting complex subunit 8) (APC8) (Metaphase-to-anaphase transition defect protein 3)
[NHEJ1 XLF] Non-homologous end-joining factor 1 (Protein cernunnos) (XRCC4-like factor)
[CDC73 C1orf28 HRPT2] Parafibromin (Cell division cycle protein 73 homolog) (Hyperparathyroidism 2 protein)
[CDK11B CDC2L1 CDK11 PITSLREA PK58] Cyclin-dependent kinase 11B (EC 2.7.11.22) (Cell division cycle 2-like protein kinase 1) (CLK-1) (Cell division protein kinase 11B) (Galactosyltransferase-associated protein kinase p58/GTA) (PITSLRE serine/threonine-protein kinase CDC2L1) (p58 CLK-1)
[CDK11A CDC2L2 CDC2L3 PITSLREB] Cyclin-dependent kinase 11A (EC 2.7.11.22) (Cell division cycle 2-like protein kinase 2) (Cell division protein kinase 11A) (Galactosyltransferase-associated protein kinase p58/GTA) (PITSLRE serine/threonine-protein kinase CDC2L2)
[CDCA8 PESCRG3] Borealin (Cell division cycle-associated protein 8) (Dasra-B) (hDasra-B) (Pluripotent embryonic stem cell-related gene 3 protein)

Bibliography :
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