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Protein

Ribonucleoside-diphosphate reductase subunit M2 B

Gene

Rrm2b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.PROSITE-ProRule annotation

Cofactori

Fe cationBy similarityNote: Binds 2 iron ions per subunit.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi100 – 1001Iron 1PROSITE-ProRule annotation
Metal bindingi131 – 1311Iron 1PROSITE-ProRule annotation
Metal bindingi131 – 1311Iron 2By similarity
Metal bindingi134 – 1341Iron 1PROSITE-ProRule annotation
Active sitei138 – 1381PROSITE-ProRule annotation
Metal bindingi194 – 1941Iron 2By similarity
Metal bindingi228 – 2281Iron 2By similarity
Metal bindingi231 – 2311Iron 2By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Source: MGI

GO - Biological processi

  1. deoxyribonucleoside diphosphate metabolic process Source: InterPro
  2. deoxyribonucleoside triphosphate metabolic process Source: MGI
  3. deoxyribonucleotide biosynthetic process Source: MGI
  4. DNA repair Source: MGI
  5. kidney development Source: MGI
  6. mitochondrial DNA replication Source: MGI
  7. negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator Source: MGI
  8. renal system process Source: MGI
  9. response to oxidative stress Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

DNA damage, DNA repair, DNA replication

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_238368. Synthesis and interconversion of nucleotide di- and triphosphates.
UniPathwayiUPA00326.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Rrm2b
Synonyms:P53r2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:2155865. Rrm2b.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity
Note: Translocates from cytoplasm to nucleus in response to DNA damage.By similarity

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. extracellular vesicular exosome Source: MGI
  3. mitochondrion Source: MGI
  4. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 351351Ribonucleoside-diphosphate reductase subunit M2 BPRO_0000228152Add
BLAST

Proteomic databases

MaxQBiQ6PEE3.
PaxDbiQ6PEE3.
PRIDEiQ6PEE3.

PTM databases

PhosphoSiteiQ6PEE3.

Expressioni

Gene expression databases

BgeeiQ6PEE3.
CleanExiMM_RRM2B.
ExpressionAtlasiQ6PEE3. baseline and differential.
GenevestigatoriQ6PEE3.

Interactioni

Subunit structurei

Heterotetramer with large (RRM1) subunit. Interacts with p53/TP53. Interacts with RRM1 in response to DNA damage (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000022901.

Structurei

3D structure databases

ProteinModelPortaliQ6PEE3.
SMRiQ6PEE3. Positions 28-314.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0208.
GeneTreeiENSGT00390000013305.
HOGENOMiHOG000255975.
HOVERGENiHBG001647.
InParanoidiQ6PEE3.
KOiK10808.
OMAiHWNKLKA.
OrthoDBiEOG7VMP5N.
PhylomeDBiQ6PEE3.
TreeFamiTF300465.

Family and domain databases

Gene3Di1.10.620.20. 1 hit.
InterProiIPR009078. Ferritin-like_SF.
IPR012348. RNR-rel.
IPR000358. RNR_small.
[Graphical view]
PANTHERiPTHR23409. PTHR23409. 1 hit.
PfamiPF00268. Ribonuc_red_sm. 1 hit.
[Graphical view]
SUPFAMiSSF47240. SSF47240. 1 hit.
PROSITEiPS00368. RIBORED_SMALL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6PEE3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGDPERPEAA RPEKGEQLCS ETEENVVRSN EEPLLRKSSR RFVIFPIQYP
60 70 80 90 100
DIWRMYKQAQ ASFWTAEEVD LSKDLPHWNK LKSDEKYFIS HILAFFAASD
110 120 130 140 150
GIVNENLVER FSQEVQVPEA RCFYGFQILI ENVHSEMYSL LIDTYIRDPK
160 170 180 190 200
KREFLFNAIE TMPYVKKKAD WALRWIADRK STFGERVVAF AAVEGIFFSG
210 220 230 240 250
SFAAIFWLKK RGLMPGLTFS NELISRDEGL HCDFACLMFQ YLVNKPSEDR
260 270 280 290 300
VREIIADAVQ IEQEFLTEAL PVGLIGMNCV LMKQYIEFVA DRLLGELGFS
310 320 330 340 350
KIFQAENPFD FMENISLEGK TNFFEKRVSE YQRFAVMAET TDNVFTLDAD

F
Length:351
Mass (Da):40,804
Last modified:July 5, 2004 - v1
Checksum:i4E1259233C9CC8A9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK138731 mRNA. Translation: BAE23760.1.
BC058103 mRNA. Translation: AAH58103.1.
CCDSiCCDS27437.1.
RefSeqiNP_955770.1. NM_199476.1.
UniGeneiMm.24738.

Genome annotation databases

EnsembliENSMUST00000022901; ENSMUSP00000022901; ENSMUSG00000022292.
GeneIDi382985.
KEGGimmu:382985.
UCSCiuc007vnl.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK138731 mRNA. Translation: BAE23760.1.
BC058103 mRNA. Translation: AAH58103.1.
CCDSiCCDS27437.1.
RefSeqiNP_955770.1. NM_199476.1.
UniGeneiMm.24738.

3D structure databases

ProteinModelPortaliQ6PEE3.
SMRiQ6PEE3. Positions 28-314.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000022901.

PTM databases

PhosphoSiteiQ6PEE3.

Proteomic databases

MaxQBiQ6PEE3.
PaxDbiQ6PEE3.
PRIDEiQ6PEE3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022901; ENSMUSP00000022901; ENSMUSG00000022292.
GeneIDi382985.
KEGGimmu:382985.
UCSCiuc007vnl.1. mouse.

Organism-specific databases

CTDi50484.
MGIiMGI:2155865. Rrm2b.

Phylogenomic databases

eggNOGiCOG0208.
GeneTreeiENSGT00390000013305.
HOGENOMiHOG000255975.
HOVERGENiHBG001647.
InParanoidiQ6PEE3.
KOiK10808.
OMAiHWNKLKA.
OrthoDBiEOG7VMP5N.
PhylomeDBiQ6PEE3.
TreeFamiTF300465.

Enzyme and pathway databases

UniPathwayiUPA00326.
ReactomeiREACT_238368. Synthesis and interconversion of nucleotide di- and triphosphates.

Miscellaneous databases

NextBioi403612.
PROiQ6PEE3.
SOURCEiSearch...

Gene expression databases

BgeeiQ6PEE3.
CleanExiMM_RRM2B.
ExpressionAtlasiQ6PEE3. baseline and differential.
GenevestigatoriQ6PEE3.

Family and domain databases

Gene3Di1.10.620.20. 1 hit.
InterProiIPR009078. Ferritin-like_SF.
IPR012348. RNR-rel.
IPR000358. RNR_small.
[Graphical view]
PANTHERiPTHR23409. PTHR23409. 1 hit.
PfamiPF00268. Ribonuc_red_sm. 1 hit.
[Graphical view]
SUPFAMiSSF47240. SSF47240. 1 hit.
PROSITEiPS00368. RIBORED_SMALL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiRIR2B_MOUSE
AccessioniPrimary (citable) accession number: Q6PEE3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: July 5, 2004
Last modified: February 4, 2015
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.