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CYREN_CRIGR
ID   CYREN_CRIGR             Reviewed;         154 AA.
AC   Q09HN1;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 37.
DE   RecName: Full=Cell cycle regulator of non-homologous end joining {ECO:0000250|UniProtKB:Q9BWK5};
DE            Short=Cell cycle regulator of NHEJ {ECO:0000250|UniProtKB:Q9BWK5};
DE   AltName: Full=Modulator of retrovirus infection {ECO:0000303|PubMed:17043244};
GN   Name=CYREN {ECO:0000250|UniProtKB:Q9BWK5};
GN   Synonyms=MRI {ECO:0000303|PubMed:17043244};
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Lung;
RX   PubMed=17043244; DOI=10.1073/pnas.0602674103;
RA   Agarwal S., Harada J., Schreifels J., Lech P., Nikolai B., Yamaguchi T.,
RA   Chanda S.K., Somia N.V.;
RT   "Isolation, characterization, and genetic complementation of a cellular
RT   mutant resistant to retroviral infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15933-15938(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 (By similarity). Acts as a regulator of DNA repair pathway choice
CC       by specifically inhibiting classical NHEJ during the S and G2 phases,
CC       thereby promoting error-free repair by homologous recombination during
CC       cell cycle phases when sister chromatids are present. Preferentially
CC       protects single-stranded overhangs at break sites by inhibiting
CC       classical NHEJ, thereby creating a local environment that favors
CC       homologous recombination. Acts via interaction with XRCC5/Ku80 and
CC       XRCC6/Ku70 (By similarity). In contrast, acts as an activator of NHEJ
CC       during G1 phase of the cell cycle: promotes classical NHEJ in G1 phase
CC       cells via multivalent interactions that increase the affinity of DNA
CC       damage response proteins for DSB-associated chromatin. Also involved in
CC       immunoglobulin V(D)J recombination (By similarity). May act as a
CC       regulator of proteasome (PubMed:17043244). In case of infection by a
CC       retrovirus, may regulate the proteasome during the uncoating phase of
CC       retrovirus (PubMed:17043244). {ECO:0000250|UniProtKB:Q8BHZ5,
CC       ECO:0000250|UniProtKB:Q9BWK5, ECO:0000269|PubMed:17043244}.
CC   -!- SUBUNIT: Interacts (via KBM motif) with XRCC5/Ku80 and XRCC6/Ku70
CC       heterodimer. Interacts (via XLF motif) with TRIM28/KAP1, ATM, MRE11,
CC       NBN and RAD50. {ECO:0000250|UniProtKB:Q8BHZ5}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17043244}. Nucleus
CC       {ECO:0000250|UniProtKB:Q9BWK5}. Chromosome
CC       {ECO:0000250|UniProtKB:Q8BHZ5}. Note=Nuclear localization may depend
CC       upon interaction with XRCC5/Ku80 and XRCC6/Ku70 heterodimer (By
CC       similarity). Localizes to DNA damage sites (By similarity).
CC       {ECO:0000250|UniProtKB:Q8BHZ5, ECO:0000250|UniProtKB:Q9BWK5}.
CC   -!- DOMAIN: The KBM (Ku-binding motif) mediates interaction with XRCC5/Ku80
CC       and XRCC6/Ku70 and recruitment to DNA damage sites.
CC       {ECO:0000250|UniProtKB:Q8BHZ5}.
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}.
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DR   EMBL; DQ899952; ABI64109.1; -; mRNA.
DR   RefSeq; NP_001233721.1; NM_001246792.1.
DR   AlphaFoldDB; Q09HN1; -.
DR   STRING; 10029.NP_001233721.1; -.
DR   GeneID; 100689364; -.
DR   KEGG; cge:100689364; -.
DR   CTD; 78996; -.
DR   eggNOG; ENOG502SEX2; Eukaryota.
DR   OrthoDB; 1349796at2759; -.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS: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; ISS: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; ISS:UniProtKB.
DR   InterPro; IPR028278; MRI.
DR   PANTHER; PTHR14566; PTHR14566; 1.
DR   Pfam; PF15325; MRI; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Chromosome; Cytoplasm; DNA damage; DNA repair; Nucleus.
FT   CHAIN           1..154
FT                   /note="Cell cycle regulator of non-homologous end joining"
FT                   /id="PRO_0000320947"
FT   REGION          77..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1..21
FT                   /note="KBM"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BWK5"
FT   MOTIF           144..154
FT                   /note="XLM"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BWK5"
FT   COMPBIAS        97..111
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BWK5"
SQ   SEQUENCE   154 AA;  16850 MW;  9C65BDFB9C27BF5D CRC64;
     METLKSENKK RVLPSWMTAP VDEKRELSVK TPKRKKIAAG QVGLATRAPV MKTVYCMNEA
     EMVDVALGIL IEGRKQEEPT LVAPDKPQPS PPYSASPHTS SPGSSSEKED SGNRWPALGL
     SPSHGPEAAD SPCSRSPEEE EEDALKYVRE IFFS
 
 
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