Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Ribonucleoside-diphosphate reductase subunit M2 B (EC 1.17.4.1) (TP53-inducible ribonucleotide reductase M2 B) (p53-inducible ribonucleotide reductase small subunit 2-like protein) (p53R2)

 RIR2B_MOUSE             Reviewed;         351 AA.
Q6PEE3;
21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
23-MAY-2018, entry version 128.
RecName: Full=Ribonucleoside-diphosphate reductase subunit M2 B;
EC=1.17.4.1;
AltName: Full=TP53-inducible ribonucleotide reductase M2 B;
AltName: Full=p53-inducible ribonucleotide reductase small subunit 2-like protein;
Short=p53R2;
Name=Rrm2b; Synonyms=P53r2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
FUNCTION, AND SUBUNIT.
PubMed=11517226; DOI=10.1074/jbc.M106088200;
Guittet O., Haakansson P., Voevodskaya N., Fridd S., Graeslund A.,
Arakawa H., Nakamura Y., Thelander L.;
"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.";
J. Biol. Chem. 276:40647-40651(2001).
[4]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=12858174; DOI=10.1038/ng1212;
Kimura T., Takeda S., Sagiya Y., Gotoh M., Nakamura Y., Arakawa H.;
"Impaired function of p53R2 in Rrm2b-null mice causes severe renal
failure through attenuation of dNTP pools.";
Nat. Genet. 34:440-445(2003).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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. {ECO:0000269|PubMed:11517226,
ECO:0000269|PubMed:12858174}.
-!- CATALYTIC ACTIVITY: 2'-deoxyribonucleoside diphosphate +
thioredoxin disulfide + H(2)O = ribonucleoside diphosphate +
thioredoxin. {ECO:0000255|PROSITE-ProRule:PRU10014}.
-!- COFACTOR:
Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
Note=Binds 2 iron ions per subunit. {ECO:0000250};
-!- PATHWAY: Genetic information processing; DNA replication.
-!- SUBUNIT: Heterotetramer with large (RRM1) subunit. Interacts with
p53/TP53. Interacts with RRM1 in response to DNA damage (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}. Note=Translocates from cytoplasm to nucleus in
response to DNA damage. {ECO:0000250}.
-!- 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.
{ECO:0000269|PubMed:12858174}.
-!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase
small chain family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AK138731; BAE23760.1; -; mRNA.
EMBL; BC058103; AAH58103.1; -; mRNA.
CCDS; CCDS27437.1; -.
RefSeq; NP_955770.1; NM_199476.1.
UniGene; Mm.24738; -.
ProteinModelPortal; Q6PEE3; -.
SMR; Q6PEE3; -.
STRING; 10090.ENSMUSP00000022901; -.
iPTMnet; Q6PEE3; -.
PhosphoSitePlus; Q6PEE3; -.
EPD; Q6PEE3; -.
MaxQB; Q6PEE3; -.
PaxDb; Q6PEE3; -.
PRIDE; Q6PEE3; -.
Ensembl; ENSMUST00000022901; ENSMUSP00000022901; ENSMUSG00000022292.
GeneID; 382985; -.
KEGG; mmu:382985; -.
UCSC; uc007vnl.1; mouse.
CTD; 50484; -.
MGI; MGI:2155865; Rrm2b.
eggNOG; KOG1567; Eukaryota.
eggNOG; COG0208; LUCA.
GeneTree; ENSGT00390000013305; -.
HOGENOM; HOG000255975; -.
HOVERGEN; HBG001647; -.
InParanoid; Q6PEE3; -.
KO; K10808; -.
OMA; SEEKYFI; -.
OrthoDB; EOG091G0AZQ; -.
PhylomeDB; Q6PEE3; -.
TreeFam; TF300465; -.
Reactome; R-MMU-499943; Interconversion of nucleotide di- and triphosphates.
UniPathway; UPA00326; -.
PRO; PR:Q6PEE3; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000022292; -.
CleanEx; MM_RRM2B; -.
ExpressionAtlas; Q6PEE3; baseline and differential.
Genevisible; Q6PEE3; MM.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IC:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IDA:MGI.
GO; GO:0009200; P:deoxyribonucleoside triphosphate metabolic process; IMP:MGI.
GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IDA:MGI.
GO; GO:0006281; P:DNA repair; IMP:MGI.
GO; GO:0001822; P:kidney development; IMP:MGI.
GO; GO:0006264; P:mitochondrial DNA replication; IMP:MGI.
GO; GO:1902254; P:negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator; IMP:MGI.
GO; GO:0003014; P:renal system process; IMP:MGI.
GO; GO:0014075; P:response to amine; IEA:Ensembl.
GO; GO:0006979; P:response to oxidative stress; IMP:MGI.
CDD; cd01049; RNRR2; 1.
Gene3D; 1.10.620.20; -; 1.
InterPro; IPR009078; Ferritin-like_SF.
InterPro; IPR012348; RNR-like.
InterPro; IPR033909; RNR_small.
InterPro; IPR030475; RNR_small_AS.
InterPro; IPR000358; RNR_small_fam.
PANTHER; PTHR23409; PTHR23409; 1.
Pfam; PF00268; Ribonuc_red_sm; 1.
PIRSF; PIRSF000355; NrdB; 1.
SUPFAM; SSF47240; SSF47240; 1.
PROSITE; PS00368; RIBORED_SMALL; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; DNA damage; DNA repair; DNA replication;
Iron; Metal-binding; Nucleus; Oxidoreductase; Reference proteome.
CHAIN 1 351 Ribonucleoside-diphosphate reductase
subunit M2 B.
/FTId=PRO_0000228152.
ACT_SITE 138 138 {ECO:0000255|PROSITE-ProRule:PRU10014}.
METAL 100 100 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU10014}.
METAL 131 131 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU10014}.
METAL 131 131 Iron 2. {ECO:0000250}.
METAL 134 134 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU10014}.
METAL 194 194 Iron 2. {ECO:0000250}.
METAL 228 228 Iron 2. {ECO:0000250}.
METAL 231 231 Iron 2. {ECO:0000250}.
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


Related products :

Catalog number Product name Quantity
EIAAB34889 Homo sapiens,Human,p53-inducible ribonucleotide reductase small subunit 2-like protein,p53R2,P53R2,Ribonucleoside-diphosphate reductase subunit M2 B,RRM2B,TP53-inducible ribonucleotide reductase M2 B
EIAAB34890 Mouse,Mus musculus,p53-inducible ribonucleotide reductase small subunit 2-like protein,p53R2,P53r2,Ribonucleoside-diphosphate reductase subunit M2 B,Rrm2b,TP53-inducible ribonucleotide reductase M2 B
18-661-15107 Ribonucleoside-diphosphate reductase M2 subunit B - EC 1.17.4.1; TP53-inducible ribonucleotide reductase M2 B; p53-inducible ribonucleotide reductase small subunit 2-like protein; p53R2 Polyclonal 0.1 mg
20-783-72861 MOUSE ANTI HUMAN RIBONUCLEOTIDE REDUCTASE - EC 1.17.4.1; TP53-inducible ribonucleotide reductase M2 B; p53-inducible ribonucleotide reductase small subunit 2-like protein; p53R2 Monoclonal 0.1 mg
EIAAB34887 Homo sapiens,Human,Ribonucleoside-diphosphate reductase subunit M2,Ribonucleotide reductase small chain,Ribonucleotide reductase small subunit,RR2,RRM2
EIAAB34888 Mouse,Mus musculus,Ribonucleoside-diphosphate reductase subunit M2,Ribonucleotide reductase small chain,Ribonucleotide reductase small subunit,Rrm2
EIAAB34886 Rat,Rattus norvegicus,Ribonucleoside-diphosphate reductase subunit M2,Ribonucleotide reductase small chain,Ribonucleotide reductase small subunit,Rrm2
15-288-22152A Ribonucleoside-diphosphate reductase M2 subunit - EC 1.17.4.1; Ribonucleotide reductase small subunit; Ribonucleotide reductase small chain Polyclonal 0.05 mg
15-288-22152A Ribonucleoside-diphosphate reductase M2 subunit - EC 1.17.4.1; Ribonucleotide reductase small subunit; Ribonucleotide reductase small chain Polyclonal 0.1 mg
10-288-22152F Ribonucleoside-diphosphate reductase M2 subunit - EC 1.17.4.1; Ribonucleotide reductase small subunit; Ribonucleotide reductase small chain 0.1 mg
10-288-22152F Ribonucleoside-diphosphate reductase M2 subunit - EC 1.17.4.1; Ribonucleotide reductase small subunit; Ribonucleotide reductase small chain 0.05 mg
E0190h ELISA kit Homo sapiens,Human,Ribonucleoside-diphosphate reductase large subunit,Ribonucleoside-diphosphate reductase subunit M1,Ribonucleotide reductase large subunit,RR1,RRM1 96T
E0190h ELISA Homo sapiens,Human,Ribonucleoside-diphosphate reductase large subunit,Ribonucleoside-diphosphate reductase subunit M1,Ribonucleotide reductase large subunit,RR1,RRM1 96T
U0190h CLIA Homo sapiens,Human,Ribonucleoside-diphosphate reductase large subunit,Ribonucleoside-diphosphate reductase subunit M1,Ribonucleotide reductase large subunit,RR1,RRM1 96T
E0190m ELISA Mouse,Mus musculus,Ribonucleoside-diphosphate reductase large subunit,Ribonucleoside-diphosphate reductase subunit M1,Ribonucleotide reductase large subunit,Rrm1 96T
E0190m ELISA kit Mouse,Mus musculus,Ribonucleoside-diphosphate reductase large subunit,Ribonucleoside-diphosphate reductase subunit M1,Ribonucleotide reductase large subunit,Rrm1 96T
U0190m CLIA Mouse,Mus musculus,Ribonucleoside-diphosphate reductase large subunit,Ribonucleoside-diphosphate reductase subunit M1,Ribonucleotide reductase large subunit,Rrm1 96T
GWB-E50D10 Ribonucleotide Reductase M2 B (TP53 Inducible) (RRM2B P53R2) Rabbit anti-Human Polyclonal (aa2-17) Antibody
BMAT4726/500 p53_Inducible Ribonucleotide Reductase Small Subunit 2 Homologue (p53R2), N_terminal, Rabbit anti_Human, Mouse, Rat; WB 500 µg.
BMAT4726/100 p53_Inducible Ribonucleotide Reductase Small Subunit 2 Homologue (p53R2), N_terminal, Rabbit anti_Human, Mouse, Rat; WB 100 µg.
GWB-E50D10 Ribonucleotide Reductase M2 B (TP53 Inducible) (RRM2B_P53R2) Rabbit anti-Human Polyclonal (aa2-17) Antibody
RRM2B RRM2B Gene ribonucleotide reductase M2 B (TP53 inducible)
CSB-EL020520MO Mouse ribonucleotide reductase M2 B (TP53 inducible) (RRM2B) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL020520HU Human ribonucleotide reductase M2 B (TP53 inducible) (RRM2B) ELISA kit, Species Human, Sample Type serum, plasma 96T
BM033 Ribonucleotide Reductase (M1 subunit) 0.1 mg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur