Reviewed, UniProtKB/Swiss-Prot Q6PEE3 (RIR2B_MOUSE)

Names and origin

Protein names

Recommended name:
    Ribonucleoside-diphosphate reductase subunit M2 B
    EC=1.17.4.1
Alternative name(s):
    TP53-inducible ribonucleotide reductase M2 B
    p53-inducible ribonucleotide reductase small subunit 2-like protein
      Short name=p53R2

Gene names

Name:	Rrm2b
Synonyms:	P53r2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	351 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Plays a pivotal role in cell survival by repairing damaged DNA in a p53/TP53-dependent manner. Supplies deoxyribonucleotides for DNA repair in cells arrested at G1 or G2. Contains an iron-tyrosyl free radical center required for catalysis. Forms an active ribonucleotide reductase (RNR) complex with RRM1 which is expressed both in resting and proliferating cells in response to DNA damage. Ref.3 Ref.4
Catalytic activity	2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.
Cofactor	Binds 2 iron ions per subunit By similarity.
Pathway	Genetic information processing; DNA replication.
Subunit structure	Heterotetramer with large (RRM1) subunit. Interacts with p53/TP53. Interacts with RRM1 in response to DNA damage By similarity. Ref.3
Subcellular location	Cytoplasm By similarity. Nucleus By similarity. Note: Translocates from cytoplasm to nucleus in response to DNA damage By similarity.
Disruption phenotype	Mice develop normally until they are weaned but from then on exhibit growth retardation and early mortality. Pathological examination indicates that multiple organs fail and that they die from severe renal failure by the age of 14 weeks. Ref.4
Sequence similarities	Belongs to the ribonucleoside diphosphate reductase small chain family.

Ontologies

Keywords
Biological process	DNA damage DNA repair DNA replication
Cellular component	Cytoplasm Nucleus
Ligand	Iron Metal-binding
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	DNA repair Ref.4 Inferred from mutant phenotype. Source: MGI deoxyribonucleoside diphosphate metabolic process Inferred from electronic annotation. Source: InterPro deoxyribonucleoside triphosphate metabolic process Ref.4 Inferred from mutant phenotype. Source: MGI deoxyribonucleotide biosynthetic process Ref.3 Inferred from direct assay. Source: MGI induction of apoptosis Ref.4 Inferred from mutant phenotype. Source: MGI kidney development Ref.4 Inferred from mutant phenotype. Source: MGI mitochondrial DNA replication Inferred from mutant phenotype. Source: MGI oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW renal system process Ref.4 Inferred from mutant phenotype. Source: MGI response to oxidative stress Ref.4 Inferred from mutant phenotype. Source: MGI
Cellular component	mitochondrion Inferred by curator. Source: MGI nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW ribonucleoside-diphosphate reductase activity Ref.3 Inferred from direct assay. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 351	351	Ribonucleoside-diphosphate reductase subunit M2 B		PRO_0000228152
Sites
	Active site	138	1	By similarity
	Metal binding	100	1	Iron 1 By similarity
	Metal binding	131	1	Iron 1 By similarity
	Metal binding	131	1	Iron 2 By similarity
	Metal binding	134	1	Iron 1 By similarity
	Metal binding	194	1	Iron 2 By similarity
	Metal binding	228	1	Iron 2 By similarity
	Metal binding	231	1	Iron 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6PEE3-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 4E1259233C9CC8A9	FASTA	351	40,804
	10 20 30 40 50 60 MGDPERPEAA RPEKGEQLCS ETEENVVRSN EEPLLRKSSR RFVIFPIQYP DIWRMYKQAQ 70 80 90 100 110 120 ASFWTAEEVD LSKDLPHWNK LKSDEKYFIS HILAFFAASD GIVNENLVER FSQEVQVPEA 130 140 150 160 170 180 RCFYGFQILI ENVHSEMYSL LIDTYIRDPK KREFLFNAIE TMPYVKKKAD WALRWIADRK 190 200 210 220 230 240 STFGERVVAF AAVEGIFFSG SFAAIFWLKK RGLMPGLTFS NELISRDEGL HCDFACLMFQ 250 260 270 280 290 300 YLVNKPSEDR VREIIADAVQ IEQEFLTEAL PVGLIGMNCV LMKQYIEFVA DRLLGELGFS 310 320 330 340 350 KIFQAENPFD FMENISLEGK TNFFEKRVSE YQRFAVMAET TDNVFTLDAD F

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." 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. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Thymus.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain.
[3]	"Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells." Guittet O., Haakansson P., Voevodskaya N., Fridd S., Graeslund A., Arakawa H., Nakamura Y., Thelander L. J. Biol. Chem. 276:40647-40651(2001) [PubMed: 11517226] [Abstract] Cited for: FUNCTION, SUBUNIT.
[4]	"Impaired function of p53R2 in Rrm2b-null mice causes severe renal failure through attenuation of dNTP pools." Kimura T., Takeda S., Sagiya Y., Gotoh M., Nakamura Y., Arakawa H. Nat. Genet. 34:440-445(2003) [PubMed: 12858174] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK138731 mRNA. Translation: BAE23760.1. BC058103 mRNA. Translation: AAH58103.1.
IPI	IPI00399462.
RefSeq	NP_955770.1.
UniGene	Mm.24738
3D structure databases
SMR	Q6PEE3. Positions 30-312.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6PEE3.
PTM databases
PhosphoSite	Q6PEE3.
Proteomic databases
PRIDE	Q6PEE3.
Genome annotation databases
Ensembl	ENSMUST00000022901; ENSMUSP00000022901; ENSMUSG00000022292; Mus musculus. [Genome view]
GeneID	382985.
KEGG	mmu:382985.
NMPDR	fig|10090.3.peg.29827.
UCSC	uc007vnl.1. mouse.
Organism-specific databases
CTD	382985.
MGI	MGI:2155865. Rrm2b.
Phylogenomic databases
eggNOG	roNOG14627.
HOGENOM	HBG418082.
HOVERGEN	Q6PEE3.
InParanoid	Q6PEE3.
OMA	LLMELGF.
OrthoDB	EOG9Q5C7S.
PhylomeDB	Q6PEE3.
Enzyme and pathway databases
BRENDA	1.17.4.1. 244.
Gene expression databases
ArrayExpress	Q6PEE3.
Bgee	Q6PEE3.
CleanEx	MM_RRM2B.
Genevestigator	Q6PEE3.
GermOnline	ENSMUSG00000022292. Mus musculus.
Family and domain databases
InterPro	IPR009078. Ferritin/RR-like. IPR012348. Ribncl_red_rel. IPR000358. Ribonucl_redctse. [Graphical view]
Gene3D	G3DSA:1.10.620.20. Ribncl_red_rel. 1 hit.
PANTHER	PTHR23409. Ribonucl_redctse. 1 hit.
Pfam	PF00268. Ribonuc_red_sm. 1 hit. [Graphical view]
PROSITE	PS00368. RIBORED_SMALL. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	403612.
SOURCE	Search...

Entry information

Entry name

RIR2B_MOUSE

Accession

Primary (citable) accession number: Q6PEE3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 21, 2006
Last sequence update:	July 5, 2004
Last modified:	January 19, 2010
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)