ID   RIR2B_MOUSE             Reviewed;         351 AA.
AC   Q6PEE3;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   04-NOV-2026, entry version 169.
DE   RecName: Full=Ribonucleoside-diphosphate reductase subunit M2 B {ECO:0000305};
DE            EC=1.17.4.1 {ECO:0000269|PubMed:11517226, ECO:0000269|PubMed:12858174};
DE   AltName: Full=TP53-inducible ribonucleotide reductase M2 B;
DE   AltName: Full=p53-inducible ribonucleotide reductase small subunit 2-like protein;
DE            Short=p53R2;
GN   Name=Rrm2b {ECO:0000312|MGI:MGI:2155865}; Synonyms=P53r2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   [3]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=11517226; DOI=10.1074/jbc.m106088200;
RA   Guittet O., Haakansson P., Voevodskaya N., Fridd S., Graeslund A.,
RA   Arakawa H., Nakamura Y., Thelander L.;
RT   "Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro
RT   with the R1 protein, which is expressed both in resting cells in response
RT   to DNA damage and in proliferating cells.";
RL   J. Biol. Chem. 276:40647-40651(2001).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=12858174; DOI=10.1038/ng1212;
RA   Kimura T., Takeda S., Sagiya Y., Gotoh M., Nakamura Y., Arakawa H.;
RT   "Impaired function of p53R2 in Rrm2b-null mice causes severe renal failure
RT   through attenuation of dNTP pools.";
RL   Nat. Genet. 34:440-445(2003).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Part of the ribonucleotide reductase (RNR) complex composed
CC       of a catalytic large alpha subunit (RRM1/RR1) and a small beta subunit
CC       (RRM2B/RR2B) required for DNA synthesis (By similarity). The active
CC       form is an alpha2beta2 heterotetramer in which the RR1-containing
CC       subunits (alpha2) catalyze reduction of ribonucleotides to
CC       deoxyribonucleotides, while the RRM2B-containing subunits (beta2)
CC       provide the diferric-tyrosyl radical cofactor required for catalysis
CC       and radical transfer (PubMed:11517226, PubMed:12858174).
CC       Mechanistically, RRM2B-containing subunits (beta2) initiates a long-
CC       distance radical transfer (RT) to the RRM1 subunits (alpha2) by
CC       generating a transient active site thiyl radical in alpha2 that
CC       catalyzes ribonucleotides reduction and, reverse radical transfer from
CC       alpha2 to beta2 regenerates the tyrosyl-radical in beta2 on every
CC       turnover (By similarity). Supplies deoxyribonucleotides for DNA repair
CC       in cells arrested at G1 or G2 in a p53/TP53-dependent manner (By
CC       similarity). {ECO:0000250|UniProtKB:P23921,
CC       ECO:0000250|UniProtKB:Q7LG56, ECO:0000269|PubMed:11517226,
CC       ECO:0000269|PubMed:12858174}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + [thioredoxin]-
CC         disulfide + H2O = a ribonucleoside 5'-diphosphate + [thioredoxin]-
CC         dithiol; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC         COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1;
CC         Evidence={ECO:0000269|PubMed:11517226, ECO:0000269|PubMed:12858174};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:23254;
CC         Evidence={ECO:0000269|PubMed:11517226, ECO:0000269|PubMed:12858174};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dCDP + [thioredoxin]-disulfide + H2O = CDP + [thioredoxin]-
CC         dithiol; Xref=Rhea:RHEA:28038, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC         COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:58069, ChEBI:CHEBI:58593;
CC         Evidence={ECO:0000269|PubMed:11517226, ECO:0000269|PubMed:12858174};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28040;
CC         Evidence={ECO:0000269|PubMed:11517226, ECO:0000269|PubMed:12858174};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dUDP + [thioredoxin]-disulfide + H2O = [thioredoxin]-dithiol +
CC         UDP; Xref=Rhea:RHEA:28026, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC         COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:60471;
CC         Evidence={ECO:0000250|UniProtKB:Q7LG56};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28028;
CC         Evidence={ECO:0000250|UniProtKB:Q7LG56};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dADP + [thioredoxin]-disulfide + H2O = [thioredoxin]-dithiol +
CC         ADP; Xref=Rhea:RHEA:28034, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC         COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:57667, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:P23921};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28036;
CC         Evidence={ECO:0000250|UniProtKB:P23921};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dGDP + [thioredoxin]-disulfide + H2O = [thioredoxin]-dithiol +
CC         GDP; Xref=Rhea:RHEA:28030, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC         COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:58189, ChEBI:CHEBI:58595;
CC         Evidence={ECO:0000250|UniProtKB:P23921};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28032;
CC         Evidence={ECO:0000250|UniProtKB:P23921};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000250|UniProtKB:Q7LG56};
CC       Note=Binds 2 iron ions per subunit. Contains a dinuclear iron center,
CC       which in its diferrous form spontaneously reacts with O2, forming a
CC       micro-oxo-bridged diferric cluster and a stable tyrosyl radical.
CC       {ECO:0000250|UniProtKB:Q7LG56};
CC   -!- ACTIVITY REGULATION: Allosterically regulated by nucleotide effectors
CC       binding to the specificity site (S site) and the activity site (A site)
CC       on the catalytic large subunit RRM1. Binding of ATP, dATP, TTP or dGTP
CC       to the specificity site promotes RRM1 dimerization (alpha2) and
CC       assembly of the catalytic holoenzyme with a RRM2B dimer (beta2).
CC       Binding of ATP or dATP to the activity site promotes formation of
CC       hexamers (alpha6). dATP stabilizes hexamers by strengthening
CC       association between cone domains, thereby preventing association
CC       between beta2 and alpha2 dimers and leading to inactivation. In
CC       contrast, ATP destabilizes hexamers by weakening association between
CC       cone domains, thus promoting insertion of beta2 dimers into the central
CC       opening to form an active complex with alpha2 dimer.
CC       {ECO:0000250|UniProtKB:P23921}.
CC   -!- SUBUNIT: Part of the ribonucleotide reductase (RNR) complex that is
CC       composed of a catalytic large alpha subunit (RRM1/RR1) and a small beta
CC       subunit RRM2B/RR2B. Interacts with p53/TP53; this interaction decreases
CC       in response to DNA damage. Forms a complex with RRM1 and AHCYL1; this
CC       interaction is dATP-dependent, stabilizes dATP in the A-site of the
CC       catalytic subunit (RRM1) of the ribonucleotide reductase (RR)
CC       holoenzyme complex and enhances dATP inhibition of RR holoenzyme
CC       complex's ribonucleotides reductase activity.
CC       {ECO:0000250|UniProtKB:Q7LG56}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7LG56}. Nucleus
CC       {ECO:0000250|UniProtKB:Q7LG56}. Note=Translocates from cytoplasm to
CC       nucleus in response to DNA damage. {ECO:0000250|UniProtKB:Q7LG56}.
CC   -!- DISRUPTION PHENOTYPE: Mice develop normally until they are weaned but
CC       from then on exhibit growth retardation and early mortality.
CC       Pathological examination indicates that multiple organs fail and that
CC       they die from severe renal failure by the age of 14 weeks.
CC       {ECO:0000269|PubMed:12858174}.
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC       chain family. {ECO:0000305}.
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DR   EMBL; AK138731; BAE23760.1; -; mRNA.
DR   EMBL; BC058103; AAH58103.1; -; mRNA.
DR   CCDS; CCDS27437.1; -.
DR   RefSeq; NP_955770.1; NM_199476.2.
DR   AlphaFoldDB; Q6PEE3; -.
DR   SMR; Q6PEE3; -.
DR   BioGRID; 238573; 2.
DR   ComplexPortal; CPX-371; Ribonucleoside-diphosphate reductase RR1 complex, RRM2B variant.
DR   FunCoup; Q6PEE3; 3126.
DR   STRING; 10090.ENSMUSP00000022901; -.
DR   iPTMnet; Q6PEE3; -.
DR   PhosphoSitePlus; Q6PEE3; -.
DR   PaxDb; 10090-ENSMUSP00000022901; -.
DR   ProteomicsDB; 253247; -.
DR   Antibodypedia; 3483; 388 antibodies from 41 providers.
DR   DNASU; 382985; -.
DR   Ensembl; ENSMPUT00000015275; ENSMPUP00000015038; ENSMPUG00000015147.
DR   Ensembl; ENSMUST00000022901.16; ENSMUSP00000022901.10; ENSMUSG00000022292.17.
DR   GeneID; 382985; -.
DR   KEGG; mmu:382985; -.
DR   UCSC; uc007vnl.1; mouse.
DR   AGR; MGI:2155865; -.
DR   CTD; 50484; -.
DR   MGI; MGI:2155865; Rrm2b.
DR   VEuPathDB; HostDB:ENSMUSG00000022292; -.
DR   eggNOG; KOG1567; Eukaryota.
DR   GeneTree; ENSGT00390000013305; -.
DR   HOGENOM; CLU_035339_2_0_1; -.
DR   InParanoid; Q6PEE3; -.
DR   OMA; ACILFAH; -.
DR   OrthoDB; 10248373at2759; -.
DR   PhylomeDB; Q6PEE3; -.
DR   Reactome; R-MMU-499943; Interconversion of nucleotide di- and triphosphates.
DR   BioGRID-ORCS; 382985; 1 hit in 113 CRISPR screens.
DR   PRO; PR:Q6PEE3; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q6PEE3; protein.
DR   Bgee; ENSMUSG00000022292; Expressed in animal zygote and 269 other cell types or tissues.
DR   ExpressionAtlas; Q6PEE3; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IC:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; ISS:ComplexPortal.
DR   GO; GO:0042802; F:identical protein binding; ISO:GO_Central.
DR   GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IDA:MGI.
DR   GO; GO:0009265; P:2'-deoxyribonucleotide biosynthetic process; ISO:GO_Central.
DR   GO; GO:0009200; P:deoxyribonucleoside triphosphate metabolic process; IMP:MGI.
DR   GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IDA:MGI.
DR   GO; GO:0006281; P:DNA repair; IMP:MGI.
DR   GO; GO:0000731; P:DNA synthesis involved in DNA repair; ISS:UniProtKB.
DR   GO; GO:0001822; P:kidney development; IMP:MGI.
DR   GO; GO:0006264; P:mitochondrial DNA replication; IMP:ComplexPortal.
DR   GO; GO:1902254; P:negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator; IMP:MGI.
DR   GO; GO:0070318; P:positive regulation of G0 to G1 transition; IDA:ComplexPortal.
DR   GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; ISO:GO_Central.
DR   GO; GO:0003014; P:renal system process; IMP:MGI.
DR   GO; GO:0014075; P:response to amine; IEA:Ensembl.
DR   GO; GO:0006979; P:response to oxidative stress; IMP:MGI.
DR   GO; GO:0009185; P:ribonucleoside diphosphate metabolic process; ISO:GO_Central.
DR   CDD; cd01049; RNRR2; 1.
DR   FunFam; 1.10.620.20:FF:000004; Ribonucleoside-diphosphate reductase subunit M2 B; 1.
DR   Gene3D; 1.10.620.20; Ribonucleotide Reductase, subunit A; 1.
DR   InterPro; IPR009078; Ferritin-like_SF.
DR   InterPro; IPR012348; RNR-like.
DR   InterPro; IPR033909; RNR_small.
DR   InterPro; IPR030475; RNR_small_AS.
DR   InterPro; IPR000358; RNR_small_fam.
DR   PANTHER; PTHR23409; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SMALL CHAIN; 1.
DR   PANTHER; PTHR23409:SF19; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SUBUNIT M2 B; 1.
DR   Pfam; PF00268; Ribonuc_red_sm; 1.
DR   PIRSF; PIRSF000355; NrdB; 1.
DR   SUPFAM; SSF47240; Ferritin-like; 1.
DR   PROSITE; PS00368; RIBORED_SMALL; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Deoxyribonucleotide synthesis; DNA damage; DNA repair; Iron;
KW   Metal-binding; Nucleus; Oxidoreductase; Reference proteome.
FT   CHAIN           1..351
FT                   /note="Ribonucleoside-diphosphate reductase subunit M2 B"
FT                   /id="PRO_0000228152"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT   BINDING         100
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P11157"
FT   BINDING         131
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P11157"
FT   BINDING         131
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q7LG56"
FT   BINDING         134
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P11157"
FT   BINDING         194
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q7LG56"
FT   BINDING         228
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P11157"
FT   BINDING         228
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q7LG56"
FT   BINDING         231
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q7LG56"
SQ   SEQUENCE   351 AA;  40804 MW;  4E1259233C9CC8A9 CRC64;
     MGDPERPEAA RPEKGEQLCS ETEENVVRSN EEPLLRKSSR RFVIFPIQYP DIWRMYKQAQ
     ASFWTAEEVD LSKDLPHWNK LKSDEKYFIS HILAFFAASD GIVNENLVER FSQEVQVPEA
     RCFYGFQILI ENVHSEMYSL LIDTYIRDPK KREFLFNAIE TMPYVKKKAD WALRWIADRK
     STFGERVVAF AAVEGIFFSG SFAAIFWLKK RGLMPGLTFS NELISRDEGL HCDFACLMFQ
     YLVNKPSEDR VREIIADAVQ IEQEFLTEAL PVGLIGMNCV LMKQYIEFVA DRLLGELGFS
     KIFQAENPFD FMENISLEGK TNFFEKRVSE YQRFAVMAET TDNVFTLDAD F
//