Q7LG56 (RIR2B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

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.1 Ref.8 Ref.9
Catalytic activity	2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin. Ref.12
Cofactor	Binds 2 iron ions per subunit. Ref.15
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. Ref.8 Ref.10 Ref.12
Subcellular location	Cytoplasm. Nucleus. Note: Translocates from cytoplasm to nucleus in response to DNA damage. Ref.9 Ref.10
Tissue specificity	Widely expressed at a high level in skeletal muscle and at a weak level in thymus. Expressed in epithelial dysplasias and squamous cell carcinoma. Ref.11
Induction	In response to DNA damage in a wild-type p53/TP53-dependent manner. Ref.1
Involvement in disease	Mitochondrial DNA depletion syndrome 8A (MTDPS8A) [MIM:612075]: A disorder due to mitochondrial dysfunction characterized by various combinations of neonatal hypotonia, neurological deterioration, respiratory distress, lactic acidosis, and renal tubulopathy. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.17 Ref.18 Mitochondrial DNA depletion syndrome 8B (MTDPS8B) [MIM:612075]: A disease due to mitochondrial dysfunction and characterized by ophthalmoplegia, ptosis, gastrointestinal dysmotility, cachexia, peripheral neuropathy. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.19 Progressive external ophthalmoplegia with mitochondrial DNA deletions autosomal dominant 5 (PEOA5) [MIM:613077]: A disorder characterized by progressive weakness of ocular muscles and levator muscle of the upper eyelid. In a minority of cases, it is associated with skeletal myopathy, which predominantly involves axial or proximal muscles and which causes abnormal fatigability and even permanent muscle weakness. Ragged-red fibers and atrophy are found on muscle biopsy. A large proportion of chronic ophthalmoplegias are associated with other symptoms, leading to a multisystemic pattern of this disease. Additional symptoms are variable, and may include cataracts, hearing loss, sensory axonal neuropathy, ataxia, depression, hypogonadism, and parkinsonism. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13
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
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Neuropathy Progressive external ophthalmoplegia
Ligand	Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW deoxyribonucleoside diphosphate metabolic process Inferred from electronic annotation. Source: InterPro deoxyribonucleoside triphosphate metabolic process Inferred from electronic annotation. Source: Compara deoxyribonucleotide biosynthetic process Inferred from electronic annotation. Source: Compara kidney development Inferred from electronic annotation. Source: Compara mitochondrial DNA replication Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara nucleobase-containing small molecule interconversion Traceable author statement. Source: Reactome renal system process Inferred from electronic annotation. Source: Compara response to oxidative stress Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA nucleoplasm Traceable author statement. Source: Reactome ribonucleoside-diphosphate reductase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Inferred from electronic annotation. Source: EC transition metal ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q7LG56-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q7LG56-2)

Also known as: Long form;

The sequence of this isoform differs from the canonical sequence as follows:
     17-68: Missing.

Isoform 3 (identifier: Q7LG56-3)

Also known as: Short form gamma;

The sequence of this isoform differs from the canonical sequence as follows:
     17-228: Missing.

Isoform 4 (identifier: Q7LG56-4)

Also known as: Short form beta;

The sequence of this isoform differs from the canonical sequence as follows:
     17-301: Missing.

Isoform 5 (identifier: Q7LG56-5)

Also known as: Short form;

The sequence of this isoform differs from the canonical sequence as follows:
     42-43: FV → SF
     44-351: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

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_0000228150

Sites

Active site

138

1

By similarity

Metal binding

100

1

Iron 1

Metal binding

131

1

Iron 1

Metal binding

131

1

Iron 2

Metal binding

134

1

Iron 1

Metal binding

194

1

Iron 2

Metal binding

228

1

Iron 2

Metal binding

231

1

Iron 2

Natural variations

Alternative sequence

17 – 301

285

Missing in isoform 4.

VSP_017668

Alternative sequence

17 – 228

212

Missing in isoform 3.

VSP_017669

Alternative sequence

17 – 68

52

Missing in isoform 2.

VSP_017670

Alternative sequence

42 – 43

2

FV → SF in isoform 5.

VSP_017671

Alternative sequence

44 – 351

308

Missing in isoform 5.

VSP_017672

Natural variant

64

1

W → R in MTDPS8A. Ref.17

VAR_046217

Natural variant

85

1

Missing in MTDPS8A. Ref.17

VAR_046218

Natural variant

110

1

R → H in MTDPS8B. Ref.19

VAR_065122

Natural variant

115

1

V → L in colorectal adenocarcinomas cell line; loss of ribonucleotide reductase activity. Ref.9

VAR_025699

Natural variant

121

1

R → H in MTDPS8B. Ref.19

VAR_065123

Natural variant

194

1

E → G in MTDPS8A. Ref.17

VAR_046219

Natural variant

194

1

E → K in MTDPS8A. Ref.17

VAR_046220

Natural variant

224

1

I → S in MTDPS8A; without tubulopathy. Ref.18

VAR_046221

Natural variant

236

1

C → F in MTDPS8A. Ref.17

VAR_046222

Natural variant

282

1

M → I in MTDPS8A; without tubulopathy. Ref.18

VAR_046223

Natural variant

317

1

L → V in MTDPS8A; without tubulopathy. Ref.18

VAR_046224

Experimental info

Sequence conflict

277

1

M → V in BAA92005. Ref.3

Secondary structure

1

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351

Helix Strand Turn

Details...

Helix

29 – 31

3

Turn

33 – 35

3

Helix

37 – 39

3

Beta strand

42 – 44

3

Helix

50 – 61

12

Helix

66 – 68

3

Helix

74 – 78

5

Helix

83 – 109

27

Helix

111 – 114

4

Helix

118 – 145

28

Helix

149 – 156

8

Helix

158 – 161

4

Helix

163 – 177

15

Beta strand

179 – 181

3

Helix

183 – 195

13

Turn

196 – 198

3

Helix

199 – 210

12

Helix

215 – 240

26

Helix

248 – 267

20

Helix

272 – 275

4

Helix

279 – 296

18

Helix

310 – 312

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 6D008687EEF40994	FASTA	351	40,737
	10 20 30 40 50 60 MGDPERPEAA GLDQDERSSS DTNESEIKSN EEPLLRKSSR RFVIFPIQYP DIWKMYKQAQ 70 80 90 100 110 120 ASFWTAEEVD LSKDLPHWNK LKADEKYFIS HILAFFAASD GIVNENLVER FSQEVQVPEA 130 140 150 160 170 180 RCFYGFQILI ENVHSEMYSL LIDTYIRDPK KREFLFNAIE TMPYVKKKAD WALRWIADRK 190 200 210 220 230 240 STFGERVVAF AAVEGVFFSG SFAAIFWLKK RGLMPGLTFS NELISRDEGL HCDFACLMFQ 250 260 270 280 290 300 YLVNKPSEER VREIIVDAVK IEQEFLTEAL PVGLIGMNCI LMKQYIEFVA DRLLVELGFS 310 320 330 340 350 KVFQAENPFD FMENISLEGK TNFFEKRVSE YQRFAVMAET TDNVFTLDAD F
	Isoform 2 (Long form) [UniParc]. Checksum: 4705C44389EB689B	FASTA	299	34,529
	10 20 30 40 50 60 MGDPERPEAA GLDQDEVDLS KDLPHWNKLK ADEKYFISHI LAFFAASDGI VNENLVERFS 70 80 90 100 110 120 QEVQVPEARC FYGFQILIEN VHSEMYSLLI DTYIRDPKKR EFLFNAIETM PYVKKKADWA 130 140 150 160 170 180 LRWIADRKST FGERVVAFAA VEGVFFSGSF AAIFWLKKRG LMPGLTFSNE LISRDEGLHC 190 200 210 220 230 240 DFACLMFQYL VNKPSEERVR EIIVDAVKIE QEFLTEALPV GLIGMNCILM KQYIEFVADR 250 260 270 280 290 LLVELGFSKV FQAENPFDFM ENISLEGKTN FFEKRVSEYQ RFAVMAETTD NVFTLDADF
	Isoform 3 (Short form gamma) [UniParc]. Checksum: E80F65CB030E89B5	FASTA	139	15,963
	10 20 30 40 50 60 MGDPERPEAA GLDQDEGLHC DFACLMFQYL VNKPSEERVR EIIVDAVKIE QEFLTEALPV 70 80 90 100 110 120 GLIGMNCILM KQYIEFVADR LLVELGFSKV FQAENPFDFM ENISLEGKTN FFEKRVSEYQ 130 RFAVMAETTD NVFTLDADF
	Isoform 4 (Short form beta) [UniParc]. Checksum: D432147F4FC35499	FASTA	66	7,602
	10 20 30 40 50 60 MGDPERPEAA GLDQDEVFQA ENPFDFMENI SLEGKTNFFE KRVSEYQRFA VMAETTDNVF TLDADF
	Isoform 5 (Short form) [UniParc]. Checksum: 29373C73112CBE75	FASTA	43	4,852
	10 20 30 40 MGDPERPEAA GLDQDERSSS DTNESEIKSN EEPLLRKSSR RSF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage." Tanaka H., Arakawa H., Yamaguchi T., Shiraishi K., Fukuda S., Matsui K., Takei Y., Nakamura Y. Nature 404:42-49(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), FUNCTION, INDUCTION.
[2]	"Homo sapiens p53-inducible ribonucleotide reductase small subunit 2 splicing variants." Ugai H., Yokoyama K.K. Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5).
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Placenta.
[4]	"DNA sequence and analysis of human chromosome 8." Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S. Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Amygdala.
[6]	NIEHS SNPs program Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]	"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] (ISOFORM 1). Tissue: Brain and Eye.
[8]	"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.
[9]	"p53R2-dependent pathway for DNA synthesis in a p53-regulated cell cycle checkpoint." Yamaguchi T., Matsuda K., Sagiya Y., Iwadate M., Fujino M.A., Nakamura Y., Arakawa H. Cancer Res. 61:8256-8262(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, VARIANT LEU-115.
[10]	"Wild-type p53 regulates human ribonucleotide reductase by protein-protein interaction with p53R2 as well as hRRM2 subunits." Xue L., Zhou B., Liu X., Qiu W., Jin Z., Yen Y. Cancer Res. 63:980-986(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH TP53 AND RRM1.
[11]	"The human ribonucleotide reductase subunit hRRM2 complements p53R2 in response to UV-induced DNA repair in cells with mutant p53." Zhou B., Liu X., Mo X., Xue L., Darwish D., Qiu W., Shih J., Hwu E.B., Luh F., Yen Y. Cancer Res. 63:6583-6594(2003) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[12]	"Characterization of enzymatic properties of human ribonucleotide reductase holoenzyme reconstituted in vitro from hRRM1, hRRM2, and p53R2 subunits." Qiu W., Zhou B., Darwish D., Shao J., Yen Y. Biochem. Biophys. Res. Commun. 340:428-434(2006) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, SUBUNIT.
[13]	"A heterozygous truncating mutation in RRM2B causes autosomal-dominant progressive external ophthalmoplegia with multiple mtDNA deletions." Tyynismaa H., Ylikallio E., Patel M., Molnar M.J., Haller R.G., Suomalainen A. Am. J. Hum. Genet. 85:290-295(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN PEOA5.
[14]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]	"2.6 A X-ray crystal structure of human p53R2, a p53-inducible ribonucleotide reductase." Smith P., Zhou B., Ho N., Yuan Y.C., Su L., Tsai S.C., Yen Y. Biochemistry 48:11134-11141(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH IRON IONS, COFACTOR.
[16]	"Human ribonucleotide reductase, subunit M2 B." Structural genomics consortium (SGC) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 20-322 IN COMPLEX WITH IRON IONS.
[17]	"Mutation of RRM2B, encoding p53-controlled ribonucleotide reductase (p53R2), causes severe mitochondrial DNA depletion." Bourdon A., Minai L., Serre V., Jais J.-P., Sarzi E., Aubert S., Chretien D., de Lonlay P., Paquis-Flucklinger V., Arakawa H., Nakamura Y., Munnich A., Roetig A. Nat. Genet. 39:776-780(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MTDPS8A ARG-64; GLU-85 DEL; GLY-194; LYS-194 AND PHE-236.
[18]	"Mitochondrial DNA depletion syndrome due to mutations in the RRM2B gene." Bornstein B., Area E., Flanigan K.M., Ganesh J., Jayakar P., Swoboda K.J., Coku J., Naini A., Shanske S., Tanji K., Hirano M., DiMauro S. Neuromuscul. Disord. 18:453-459(2008) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MTDPS8A SER-224; ILE-282 AND VAL-317.
[19]	"Mitochondrial neurogastrointestinal encephalopathy due to mutations in RRM2B." Shaibani A., Shchelochkov O.A., Zhang S., Katsonis P., Lichtarge O., Wong L.J., Shinawi M. Arch. Neurol. 66:1028-1032(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MTDPS8B HIS-110 AND HIS-121.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB036063 mRNA. Translation: BAA92434.1.
AB036532 Genomic DNA. Translation: BAA92493.1.
AB163437 mRNA. Translation: BAD11774.1.
AB163438 mRNA. Translation: BAD11775.1.
AB166669 mRNA. Translation: BAD12265.1.
AB166670 mRNA. Translation: BAD12266.1.
AB166671 mRNA. Translation: BAD12267.1.
AK001965 mRNA. Translation: BAA92005.1.
AL137348 mRNA. Translation: CAB70703.2.
DQ027001 Genomic DNA. Translation: AAY29059.1.
AP001328 Genomic DNA. No translation available.
AP002907 Genomic DNA. No translation available.
BC042468 mRNA. Translation: AAH42468.1.
BC108261 mRNA. Translation: AAI08262.1.
BC117496 mRNA. Translation: AAI17497.1.
BC130628 mRNA. Translation: AAI30629.1.

IPI

IPI00100213.
IPI00438859.
IPI00438860.
IPI00735900.
IPI00741117.

PIR

T46249.

RefSeq

NP_001165948.1. NM_001172477.1.
NP_001165949.1. NM_001172478.1.
NP_056528.2. NM_015713.4.

UniGene

Hs.512592.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2VUX	X-ray	2.80	A/B	20-322	[»]
3HF1	X-ray	2.60	A/B	1-351	[»]
4DJN	X-ray	2.20	A/B	13-322	[»]

ProteinModelPortal

Q7LG56.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-24264N.
DIP-48627N.

PTM databases

PhosphoSite

Q7LG56.

Polymorphism databases

DMDM

74727333.

Proteomic databases

PaxDb

Q7LG56.

PRIDE

Q7LG56.

Protocols and materials databases

DNASU

50484.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000251810; ENSP00000251810; ENSG00000048392.
ENST00000395912; ENSP00000379248; ENSG00000048392.
ENST00000519317; ENSP00000430641; ENSG00000048392.
ENST00000519962; ENSP00000429140; ENSG00000048392.
ENST00000522394; ENSP00000429578; ENSG00000048392.

GeneID

50484.

KEGG

hsa:50484.

UCSC

uc003ykn.3. human.
uc010mbv.2. human.
uc010mbw.1. human.

Organism-specific databases

CTD

50484.

GeneCards

GC08M103216.

HGNC

HGNC:17296. RRM2B.

HPA

CAB006854.
HPA028812.

MIM

604712. gene.
612075. phenotype.
613077. phenotype.

neXtProt

NX_Q7LG56.

PharmGKB

PA34866.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0208.

HOVERGEN

HBG001647.

InParanoid

Q7LG56.

KO

K10808.

OrthoDB

EOG4BCDN7.

Enzyme and pathway databases

BRENDA

1.17.4.1. 2681.

Reactome

REACT_111217. Metabolism.

UniPathway

UPA00326.

Gene expression databases

ArrayExpress

Q7LG56.

Bgee

Q7LG56.

Genevestigator

Q7LG56.

GermOnline

ENSG00000048392. Homo sapiens.

Family and domain databases

Gene3D

1.10.620.20. 1 hit.

InterPro

IPR009078. Ferritin-like_SF.
IPR012348. RNR-rel.
IPR000358. RNR_small.
[Graphical view]

PANTHER

PTHR23409. PTHR23409. 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

BindingDB

Q7LG56.

ChEMBL

CHEMBL1896.

ChiTaRS

RRM2B. human.

EvolutionaryTrace

Q7LG56.

GenomeRNAi

50484.

NextBio

53036.

SOURCE

Search...

Entry information

Entry name

RIR2B_HUMAN

Accession

Primary (citable) accession number: Q7LG56
Secondary accession number(s): Q17R22 , Q75PQ6, Q75PQ7, Q75PY8, Q75PY9, Q86YE3, Q9NPD6, Q9NTD8, Q9NUW3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 21, 2006
Last sequence update:	July 5, 2004
Last modified:	May 1, 2013
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.