P11157 (RIR2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribonucleoside-diphosphate reductase subunit M2
EC=1.17.4.1

Alternative name(s):
Ribonucleotide reductase small chain
Ribonucleotide reductase small subunit

Gene names

Name:

Rrm2

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 › Mus

Protein attributes

Sequence length	390 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Inhibits Wnt signaling By similarity.
Catalytic activity	2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.
Cofactor	Binds 2 iron ions per subunit.
Pathway	Genetic information processing; DNA replication.
Subunit structure	Heterodimer of a large and a small subunit.
Subcellular location	Cytoplasm.
Post-translational modification	Phosphorylation on Ser-20 relieves the inhibitory effect on Wnt signaling By similarity.
Miscellaneous	Two distinct regulatory sites have been defined: the specificity site, which controls substrate specificity, and the activity site which regulates overall catalytic activity. A substrate-binding catalytic site, located on M1, is formed only in the presence of the second subunit M2.
Sequence similarities	Belongs to the ribonucleoside diphosphate reductase small chain family.

Ontologies

Keywords
Biological process	DNA replication
Cellular component	Cytoplasm
Ligand	Iron Metal-binding
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA replication Inferred from electronic annotation. Source: UniProtKB-KW deoxyribonucleoside diphosphate metabolic process Inferred from electronic annotation. Source: InterPro deoxyribonucleotide biosynthetic process Inferred from direct assay. Source: UniProtKB protein heterotetramerization Inferred from physical interaction. Source: UniProtKB
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Inferred from physical interaction. Source: MGI ribonucleoside-diphosphate reductase activity Inferred from direct assay. Source: UniProtKB transition metal ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 390

390

Ribonucleoside-diphosphate reductase subunit M2

PRO_0000190450

Sites

Active site

177

1

By similarity

Metal binding

139

1

Iron 1

Metal binding

170

1

Iron 1

Metal binding

170

1

Iron 2

Metal binding

173

1

Iron 1

Metal binding

233

1

Iron 2

Metal binding

267

1

Iron 1

Metal binding

267

1

Iron 2

Metal binding

270

1

Iron 2

Amino acid modifications

Modified residue

20

1

Phosphoserine Ref.5

Modified residue

33

1

Phosphothreonine By similarity

Secondary structure

1

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390

Helix Strand Turn

Details...

Helix

67 – 70

4

Turn

72 – 74

3

Beta strand

83 – 85

3

Helix

89 – 100

12

Helix

105 – 107

3

Helix

113 – 119

7

Helix

122 – 135

14

Helix

138 – 147

10

Helix

150 – 153

4

Helix

157 – 184

28

Helix

188 – 195

8

Turn

196 – 200

5

Helix

202 – 216

15

Beta strand

218 – 220

3

Helix

222 – 249

28

Helix

254 – 278

25

Helix

287 – 306

20

Helix

311 – 314

4

Helix

318 – 335

18

Turn

349 – 351

3

Turn

386 – 388

3

Sequences

	Sequence		Length	Mass (Da)
	P11157 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: AC7ACC4FAF8A4A2F	FASTA	390	45,096
	10 20 30 40 50 60 MLSVRTPLAT IADQQQLQLS PLKRLTLADK ENTPPTLSST RVLASKAARR IFQDSAELES 70 80 90 100 110 120 KAPTNPSVED EPLLRENPRR FVVFPIEYHD IWQMYKKAEA SFWTAEEVDL SKDIQHWEAL 130 140 150 160 170 180 KPDERHFISH VLAFFAASDG IVNENLVERF SQEVQVTEAR CFYGFQIAME NIHSEMYSLL 190 200 210 220 230 240 IDTYIKDPKE REYLFNAIET MPCVKKKADW ALRWIGDKEA TYGERVVAFA AVEGIFFSGS 250 260 270 280 290 300 FASIFWLKKR GLMPGLTFSN ELISRDEGLH CDFACLMFKH LVHKPAEQRV REIITNAVRI 310 320 330 340 350 360 EQEFLTEALP VKLIGMNCTL MKQYIEFVAD RLMLELGFNK IFRVENPFDF MENISLEGKT 370 380 390 NFFEKRVGEY QRMGVMSNST ENSFTLDADF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of expressible cDNA clones encoding the M1 and M2 subunits of mouse ribonucleotide reductase." Thelander L., Berg P. Mol. Cell. Biol. 6:3433-3442(1986) [PubMed: 3025593] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Molecular cloning and expression of the functional gene encoding the M2 subunit of mouse ribonucleotide reductase: a new dominant marker gene." Thelander M., Thelander L. EMBO J. 8:2475-2479(1989) [PubMed: 2684652] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"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, DBA/2 and NOD. Tissue: Eye, Kidney, Liver and Thymus.
[4]	"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.
[5]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed: 19131326] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
[6]	"The three-dimensional structure of mammalian ribonucleotide reductase protein R2 reveals a more-accessible iron-radical site than Escherichia coli R2." Kauppi B., Nielsen B.B., Ramaswamy S., Larsen I.K., Thelander M., Thelander L., Eklund H. J. Mol. Biol. 262:706-720(1996) [PubMed: 8876648] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 65-352.
[7]	"Cobalt substitution of mouse R2 ribonucleotide reductase as a model for the reactive diferrous state. Spectroscopic and structural evidence for a ferromagnetically coupled dinuclear cobalt cluster." Strand K.R., Karlsen S., Andersson K.K. J. Biol. Chem. 277:34229-34238(2002) [PubMed: 12087093] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 65-352.
[8]	"NMR structure of an inhibitory R2 C-terminal peptide bound to mouse ribonucleotide reductase R1 subunit." Fisher A.L., Laub P.B., Cooperman B.S. Nat. Struct. Biol. 2:951-955(1995) [PubMed: 7583667] [Abstract] Cited for: STRUCTURE BY NMR OF 384-390.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M14223 mRNA. Translation: AAA40062.1.
X15666 Genomic DNA. Translation: CAA33707.1.
AK088907 mRNA. Translation: BAC40647.1.
AK142027 mRNA. Translation: BAE24918.1.
AK147111 mRNA. Translation: BAE27683.1.
AK161643 mRNA. Translation: BAE36508.1.
AK167078 mRNA. Translation: BAE39238.1.
AK167204 mRNA. Translation: BAE39331.1.
AK168205 mRNA. Translation: BAE40165.1.
AK168994 mRNA. Translation: BAE40793.1.
BC085136 mRNA. Translation: AAH85136.1.

IPI

IPI00112645.

PIR

S06735.

RefSeq

NP_033130.1. NM_009104.2.

UniGene

Mm.99.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AFT	NMR	-	A	384-390	[»]
1H0N	X-ray	2.40	A	1-390	[»]
1H0O	X-ray	2.20	A	1-390	[»]
1W68	X-ray	2.20	A	1-390	[»]
1W69	X-ray	2.20	A	1-390	[»]
1XSM	X-ray	2.30	A	1-390	[»]

ProteinModelPortal

P11157.

SMR

P11157. Positions 8-353.

DisProt

DP00462.

ModBase

Search...

Protein-protein interaction databases

IntAct

P11157. 1 interaction.

STRING

P11157.

PTM databases

PhosphoSite

P11157.

Proteomic databases

PRIDE

P11157.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000020980; ENSMUSP00000020980; ENSMUSG00000020649.

GeneID

20135.

KEGG

mmu:20135.

NMPDR

fig|10090.3.peg.26031.

UCSC

uc007ner.2. mouse.

Organism-specific databases

CTD

6241.

MGI

MGI:98181. Rrm2.

Phylogenomic databases

eggNOG

roNOG06367.

HOGENOM

HBG418082.

HOVERGEN

HBG001647.

InParanoid

P11157.

OMA

YIADWRL.

OrthoDB

EOG4BCDN7.

PhylomeDB

P11157.

Enzyme and pathway databases

BRENDA

1.17.4.1. 3474.

Gene expression databases

ArrayExpress

P11157.

Bgee

P11157.

CleanEx

MM_RRM2.

Genevestigator

P11157.

GermOnline

ENSMUSG00000020649. 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.

KO

K10808.

PANTHER

PTHR23409. Ribonucl_redctse. 1 hit.

Pfam

PF00268. Ribonuc_red_sm. 1 hit.
[Graphical view]

SUPFAM

SSF47240. Ferritin/RR_like. 1 hit.

PROSITE

PS00368. RIBORED_SMALL. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

297647.

SOURCE

Search...

Entry information

Entry name

RIR2_MOUSE

Accession

Primary (citable) accession number: P11157
Secondary accession number(s): Q3UI23, Q542E2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	November 16, 2011
This is version 124 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program