CYREN_HUMAN
ID CYREN_HUMAN Reviewed; 157 AA.
AC Q9BWK5; A0A024R780; A0A087WWQ8; Q6NWZ4; Q6ZNR5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Cell cycle regulator of non-homologous end joining {ECO:0000303|PubMed:28959974};
DE Short=Cell cycle regulator of NHEJ {ECO:0000303|PubMed:28959974};
DE AltName: Full=Modulator of retrovirus infection homolog {ECO:0000250|UniProtKB:Q09HN1};
GN Name=CYREN {ECO:0000312|HGNC:HGNC:22432};
GN Synonyms=C7orf49 {ECO:0000312|HGNC:HGNC:22432},
GN MRI {ECO:0000250|UniProtKB:Q09HN1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Mammary gland, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 54-69 (ISOFORM 4), FUNCTION, INTERACTION WITH XRCC5 AND
RP XRCC6, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RX PubMed=24610814; DOI=10.1074/jbc.c113.533968;
RA Slavoff S.A., Heo J., Budnik B.A., Hanakahi L.A., Saghatelian A.;
RT "A human short open reading frame (sORF)-encoded polypeptide that
RT stimulates DNA end joining.";
RL J. Biol. Chem. 289:10950-10957(2014).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP DOMAIN, INTERACTION WITH XRCC5 AND XRCC6, AND MUTAGENESIS OF TRP-16.
RX PubMed=27063109; DOI=10.1038/ncomms11242;
RA Grundy G.J., Rulten S.L., Arribas-Bosacoma R., Davidson K., Kozik Z.,
RA Oliver A.W., Pearl L.H., Caldecott K.W.;
RT "The Ku-binding motif is a conserved module for recruitment and stimulation
RT of non-homologous end-joining proteins.";
RL Nat. Commun. 7:11242-11242(2016).
RN [9]
RP FUNCTION, INTERACTION WITH XRCC5 AND XRCC6, DOMAIN, AND MUTAGENESIS OF
RP ARG-11; PRO-14 AND TRP-16.
RX PubMed=28959974; DOI=10.1038/nature24023;
RA Arnoult N., Correia A., Ma J., Merlo A., Garcia-Gomez S., Maric M.,
RA Tognetti M., Benner C.W., Boulton S.J., Saghatelian A., Karlseder J.;
RT "Regulation of DNA repair pathway choice in S and G2 phases by the NHEJ
RT inhibitor CYREN.";
RL Nature 549:548-552(2017).
RN [10]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-82.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Cell-cycle-specific regulator of classical non-homologous end
CC joining (NHEJ) of DNA double-strand break (DSB) repair, which can act
CC both as an activator or inhibitor of NHEJ, depending on the cell cycle
CC phase (PubMed:24610814, PubMed:28959974). Acts as a regulator of DNA
CC repair pathway choice by specifically inhibiting classical NHEJ during
CC the S and G2 phases, thereby promoting error-free repair by homologous
CC recombination during cell cycle phases when sister chromatids are
CC present (PubMed:28959974). Preferentially protects single-stranded
CC overhangs at break sites by inhibiting classical NHEJ, thereby creating
CC a local environment that favors homologous recombination
CC (PubMed:28959974). Acts via interaction with XRCC5/Ku80 and XRCC6/Ku70
CC (PubMed:28959974). In contrast, acts as an activator of NHEJ during G1
CC phase of the cell cycle: promotes classical NHEJ in G1 phase cells via
CC multivalent interactions that increase the affinity of DNA damage
CC response proteins for DSB-associated chromatin. Also involved in
CC immunoglobulin V(D)J recombination (By similarity). May also act as an
CC indirect regulator of proteasome (By similarity).
CC {ECO:0000250|UniProtKB:Q09HN1, ECO:0000250|UniProtKB:Q8BHZ5,
CC ECO:0000269|PubMed:24610814, ECO:0000269|PubMed:28959974}.
CC -!- SUBUNIT: [Isoform 1]: Interacts (via KBM motif) with XRCC5/Ku80 and
CC XRCC6/Ku70 heterodimer (PubMed:24610814, PubMed:27063109,
CC PubMed:28959974). Interacts (via XLF motif) with TRIM28/KAP1, ATM,
CC MRE11, NBN and RAD50 (By similarity). {ECO:0000250|UniProtKB:Q8BHZ5,
CC ECO:0000269|PubMed:24610814, ECO:0000269|PubMed:27063109,
CC ECO:0000269|PubMed:28959974}.
CC -!- SUBUNIT: [Isoform 3]: Does not interact with XRCC5/Ku80 and XRCC6/Ku70
CC heterodimer (PubMed:24610814). {ECO:0000269|PubMed:24610814}.
CC -!- SUBUNIT: [Isoform 4]: Interacts (via KBM motif) with XRCC5/Ku80 and
CC XRCC6/Ku70 heterodimer (PubMed:24610814, PubMed:28959974).
CC {ECO:0000269|PubMed:24610814, ECO:0000269|PubMed:28959974}.
CC -!- INTERACTION:
CC Q9BWK5; Q5T890: ERCC6L2; NbExp=3; IntAct=EBI-8787584, EBI-3951765;
CC Q9BWK5; Q9UL63: MKLN1; NbExp=3; IntAct=EBI-8787584, EBI-1048053;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm
CC {ECO:0000269|PubMed:24610814}. Nucleus {ECO:0000269|PubMed:24610814}.
CC Chromosome {ECO:0000269|PubMed:27063109}. Note=Nuclear localization may
CC depend upon interaction with XRCC5/Ku80 and XRCC6/Ku70 heterodimer
CC (PubMed:24610814). Localizes to DNA damage sites (PubMed:27063109).
CC {ECO:0000269|PubMed:24610814, ECO:0000269|PubMed:27063109}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm
CC {ECO:0000269|PubMed:24610814}. Note=Some nuclear localization may be
CC due to passive diffusion. {ECO:0000269|PubMed:24610814}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm
CC {ECO:0000269|PubMed:24610814}. Nucleus {ECO:0000269|PubMed:24610814}.
CC Note=Nuclear localization may depend upon interaction with XRCC5/Ku80
CC and XRCC6/Ku70 heterodimer and increases upon etoposide treatment.
CC {ECO:0000269|PubMed:24610814}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=CYREN-1 {ECO:0000303|PubMed:28959974}, MRI-1
CC {ECO:0000303|PubMed:24610814};
CC IsoId=Q9BWK5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BWK5-2; Sequence=VSP_031768;
CC Name=3; Synonyms=CYREN-3 {ECO:0000303|PubMed:28959974}, MRI-3
CC {ECO:0000303|PubMed:24610814};
CC IsoId=Q9BWK5-3; Sequence=VSP_031767;
CC Name=4; Synonyms=CYREN-2 {ECO:0000303|PubMed:28959974}, MRI-2
CC {ECO:0000303|PubMed:24610814};
CC IsoId=Q9BWK5-4; Sequence=VSP_058524, VSP_058525;
CC -!- DOMAIN: The KBM (Ku-binding motif) mediates interaction with XRCC5/Ku80
CC and XRCC6/Ku70 and recruitment to DNA damage sites.
CC {ECO:0000269|PubMed:27063109, ECO:0000269|PubMed:28959974}.
CC -!- DOMAIN: The XLM (XLF-like motif) mediates interaction with DNA damage
CC response proteins TRIM28/KAP1, ATM and members of the MRN complex
CC (MRE11, NBN and RAD50). {ECO:0000250|UniProtKB:Q8BHZ5}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH00168.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK026103; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK130795; BAC85431.1; -; mRNA.
DR EMBL; AC083862; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236950; EAL24064.1; -; Genomic_DNA.
DR EMBL; CH471070; EAW83840.1; -; Genomic_DNA.
DR EMBL; CH471070; EAW83841.1; -; Genomic_DNA.
DR EMBL; BC000168; AAH00168.1; ALT_INIT; mRNA.
DR EMBL; BC067350; AAH67350.1; -; mRNA.
DR CCDS; CCDS5838.2; -. [Q9BWK5-1]
DR CCDS; CCDS59082.1; -. [Q9BWK5-3]
DR CCDS; CCDS75663.1; -. [Q9BWK5-4]
DR RefSeq; NP_001230678.1; NM_001243749.1. [Q9BWK5-4]
DR RefSeq; NP_001230680.1; NM_001243751.1. [Q9BWK5-4]
DR RefSeq; NP_001230681.1; NM_001243752.1. [Q9BWK5-4]
DR RefSeq; NP_001230682.1; NM_001243753.1. [Q9BWK5-4]
DR RefSeq; NP_001230683.1; NM_001243754.1. [Q9BWK5-3]
DR RefSeq; NP_001230684.1; NM_001243755.1. [Q9BWK5-3]
DR RefSeq; NP_001292558.1; NM_001305629.1.
DR RefSeq; NP_076938.2; NM_024033.3. [Q9BWK5-1]
DR RefSeq; XP_016868078.1; XM_017012589.1.
DR RefSeq; XP_016868079.1; XM_017012590.1.
DR RefSeq; XP_016868080.1; XM_017012591.1. [Q9BWK5-1]
DR RefSeq; XP_016868082.1; XM_017012593.1. [Q9BWK5-3]
DR RefSeq; XP_016868083.1; XM_017012594.1. [Q9BWK5-3]
DR RefSeq; XP_016868084.1; XM_017012595.1. [Q9BWK5-4]
DR PDB; 6TYU; X-ray; 1.47 A; B=6-21.
DR PDBsum; 6TYU; -.
DR AlphaFoldDB; Q9BWK5; -.
DR SMR; Q9BWK5; -.
DR BioGRID; 122467; 13.
DR IntAct; Q9BWK5; 5.
DR STRING; 9606.ENSP00000376823; -.
DR iPTMnet; Q9BWK5; -.
DR PhosphoSitePlus; Q9BWK5; -.
DR BioMuta; C7orf49; -.
DR DMDM; 182676205; -.
DR EPD; Q9BWK5; -.
DR jPOST; Q9BWK5; -.
DR MassIVE; Q9BWK5; -.
DR MaxQB; Q9BWK5; -.
DR PaxDb; Q9BWK5; -.
DR PeptideAtlas; Q9BWK5; -.
DR PRIDE; Q9BWK5; -.
DR ProteomicsDB; 79284; -. [Q9BWK5-1]
DR ProteomicsDB; 79285; -. [Q9BWK5-2]
DR ProteomicsDB; 79286; -. [Q9BWK5-3]
DR Antibodypedia; 18116; 54 antibodies from 17 providers.
DR DNASU; 78996; -.
DR Ensembl; ENST00000393114.8; ENSP00000376823.3; ENSG00000122783.17. [Q9BWK5-1]
DR Ensembl; ENST00000424142.5; ENSP00000400024.1; ENSG00000122783.17. [Q9BWK5-3]
DR Ensembl; ENST00000483029.2; ENSP00000473365.1; ENSG00000122783.17. [Q9BWK5-3]
DR Ensembl; ENST00000617987.1; ENSP00000480430.1; ENSG00000122783.17. [Q9BWK5-4]
DR Ensembl; ENST00000620897.4; ENSP00000481014.1; ENSG00000122783.17. [Q9BWK5-3]
DR GeneID; 78996; -.
DR KEGG; hsa:78996; -.
DR MANE-Select; ENST00000393114.8; ENSP00000376823.3; NM_024033.4; NP_076938.2.
DR UCSC; uc003vsl.4; human. [Q9BWK5-1]
DR UCSC; uc022amb.2; human.
DR CTD; 78996; -.
DR DisGeNET; 78996; -.
DR GeneCards; CYREN; -.
DR HGNC; HGNC:22432; CYREN.
DR HPA; ENSG00000122783; Low tissue specificity.
DR MIM; 616980; gene.
DR neXtProt; NX_Q9BWK5; -.
DR OpenTargets; ENSG00000122783; -.
DR PharmGKB; PA162380533; -.
DR VEuPathDB; HostDB:ENSG00000122783; -.
DR eggNOG; ENOG502SEX2; Eukaryota.
DR GeneTree; ENSGT00390000013192; -.
DR HOGENOM; CLU_126072_0_0_1; -.
DR InParanoid; Q9BWK5; -.
DR OMA; AKAPKRM; -.
DR OrthoDB; 1634776at2759; -.
DR PhylomeDB; Q9BWK5; -.
DR TreeFam; TF336925; -.
DR PathwayCommons; Q9BWK5; -.
DR SignaLink; Q9BWK5; -.
DR BioGRID-ORCS; 78996; 14 hits in 1059 CRISPR screens.
DR ChiTaRS; C7orf49; human.
DR GenomeRNAi; 78996; -.
DR Pharos; Q9BWK5; Tbio.
DR PRO; PR:Q9BWK5; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9BWK5; protein.
DR Bgee; ENSG00000122783; Expressed in gastrocnemius and 187 other tissues.
DR ExpressionAtlas; Q9BWK5; baseline and differential.
DR Genevisible; Q9BWK5; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IDA:UniProtKB.
DR GO; GO:0033152; P:immunoglobulin V(D)J recombination; ISS:UniProtKB.
DR GO; GO:2001033; P:negative regulation of double-strand break repair via nonhomologous end joining; IDA:UniProtKB.
DR InterPro; IPR028278; MRI.
DR PANTHER; PTHR14566; PTHR14566; 1.
DR Pfam; PF15325; MRI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chromosome; Cytoplasm;
KW Direct protein sequencing; DNA damage; DNA repair; Nucleus;
KW Reference proteome.
FT CHAIN 1..157
FT /note="Cell cycle regulator of non-homologous end joining"
FT /id="PRO_0000320948"
FT REGION 77..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1..21
FT /note="KBM"
FT /evidence="ECO:0000269|PubMed:27063109,
FT ECO:0000269|PubMed:28959974"
FT MOTIF 147..157
FT /note="XLM"
FT /evidence="ECO:0000303|PubMed:27063109"
FT COMPBIAS 95..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VAR_SEQ 1..55
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031767"
FT VAR_SEQ 1..45
FT /note="METLQSETKTRVLPSWLTAQVATKNVAPMKAPKRMRMAAVPVAAA -> MRL
FT ESLCHLCLACLFF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_031768"
FT VAR_SEQ 47..69
FT /note="LPATRTVYCMNEAEIVDVALGIL -> CDSSGQKTPANLTPCDKDCVLHE
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_058524"
FT VAR_SEQ 70..157
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_058525"
FT VARIANT 82
FT /note="P -> L (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs776124276)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_039320"
FT MUTAGEN 11
FT /note="R->A: Abolishes interaction with XRCC5/Ku80 and
FT XRCC6/Ku70 and ability to inhibit classical non-homologous
FT end joining (NHEJ)."
FT /evidence="ECO:0000269|PubMed:28959974"
FT MUTAGEN 14
FT /note="P->A: Abolishes interaction with XRCC5/Ku80 and
FT XRCC6/Ku70 and ability to inhibit classical non-homologous
FT end joining (NHEJ)."
FT /evidence="ECO:0000269|PubMed:28959974"
FT MUTAGEN 16
FT /note="W->A: Abolishes interaction with XRCC5/Ku80 and
FT XRCC6/Ku70 and ability to inhibit classical non-homologous
FT end joining (NHEJ)."
FT /evidence="ECO:0000269|PubMed:27063109,
FT ECO:0000269|PubMed:28959974"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:6TYU"
SQ SEQUENCE 157 AA; 16829 MW; EA52CB3CCD231B74 CRC64;
METLQSETKT RVLPSWLTAQ VATKNVAPMK APKRMRMAAV PVAAARLPAT RTVYCMNEAE
IVDVALGILI ESRKQEKACE QPALAGADNP EHSPPCSVSP HTSSGSSSEE EDSGKQALAP
GLSPSQRPGG SSSACSRSPE EEEEEDVLKY VREIFFS
