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Q7LG56 (RIR2B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length351 AA.
Sequence statusComplete.
Protein existenceEvidence 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.9 Ref.10

Catalytic activity

2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin. Ref.13

Cofactor

Binds 2 iron ions per subunit. Ref.16

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.9 Ref.11 Ref.13

Subcellular location

Cytoplasm. Nucleus. Note: Translocates from cytoplasm to nucleus in response to DNA damage. Ref.10 Ref.11

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.12

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.18 Ref.19

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.20

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.14

Sequence similarities

Belongs to the ribonucleoside diphosphate reductase small chain family.

Sequence caution

The sequence BAG65196.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence EAW91842.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
DNA replication
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Neuropathy
Progressive external ophthalmoplegia
   LigandIron
Metal-binding
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA 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: Ensembl

deoxyribonucleotide biosynthetic process

Inferred from electronic annotation. Source: Ensembl

kidney development

Inferred from electronic annotation. Source: Ensembl

mitochondrial DNA replication

Inferred from electronic annotation. Source: Ensembl

negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator

Inferred from electronic annotation. Source: Ensembl

nucleobase-containing small molecule interconversion

Traceable author statement. Source: Reactome

nucleobase-containing small molecule metabolic process

Traceable author statement. Source: Reactome

renal system process

Inferred from electronic annotation. Source: Ensembl

response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 6 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.
Isoform 6 (identifier: Q7LG56-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: MGDPERPEAAGLDQDE → MLLLRLPPHR...KDDAWRPQAG
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 351351Ribonucleoside-diphosphate reductase subunit M2 B
PRO_0000228150

Sites

Active site1381 By similarity
Metal binding1001Iron 1
Metal binding1311Iron 1
Metal binding1311Iron 2
Metal binding1341Iron 1
Metal binding1941Iron 2
Metal binding2281Iron 2
Metal binding2311Iron 2

Natural variations

Alternative sequence1 – 1616MGDPE…LDQDE → MLLLRLPPHRSHASPLDCKL QDRCRKCYSPRSGQACPPAL AAAWLRRCERRGGRPRGGRR KELTLGLRPARCSAPGPAKD DAWRPQAG in isoform 6.
VSP_053585
Alternative sequence17 – 301285Missing in isoform 4.
VSP_017668
Alternative sequence17 – 228212Missing in isoform 3.
VSP_017669
Alternative sequence17 – 6852Missing in isoform 2.
VSP_017670
Alternative sequence42 – 432FV → SF in isoform 5.
VSP_017671
Alternative sequence44 – 351308Missing in isoform 5.
VSP_017672
Natural variant641W → R in MTDPS8A. Ref.18
VAR_046217
Natural variant851Missing in MTDPS8A. Ref.18
VAR_046218
Natural variant1101R → H in MTDPS8B. Ref.20
VAR_065122
Natural variant1151V → L in colorectal adenocarcinomas cell line; loss of ribonucleotide reductase activity. Ref.10
VAR_025699
Natural variant1211R → H in MTDPS8B. Ref.20
VAR_065123
Natural variant1941E → G in MTDPS8A. Ref.18
VAR_046219
Natural variant1941E → K in MTDPS8A. Ref.18
VAR_046220
Natural variant2241I → S in MTDPS8A; without tubulopathy. Ref.19
VAR_046221
Natural variant2361C → F in MTDPS8A. Ref.18
VAR_046222
Natural variant2821M → I in MTDPS8A; without tubulopathy. Ref.19
Corresponds to variant rs182614164 [ dbSNP | Ensembl ].
VAR_046223
Natural variant3171L → V in MTDPS8A; without tubulopathy. Ref.19
VAR_046224

Experimental info

Sequence conflict2771M → V in BAA92005. Ref.3

Secondary structure

........................................... 351
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 6D008687EEF40994

FASTA35140,737
        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 

« Hide

Isoform 2 (Long form) [UniParc].

Checksum: 4705C44389EB689B
Show »

FASTA29934,529
Isoform 3 (Short form gamma) [UniParc].

Checksum: E80F65CB030E89B5
Show »

FASTA13915,963
Isoform 4 (Short form beta) [UniParc].

Checksum: D432147F4FC35499
Show »

FASTA667,602
Isoform 5 (Short form) [UniParc].

Checksum: 29373C73112CBE75
Show »

FASTA434,852
Isoform 6 [UniParc].

Checksum: 0D2B8471AE362D44
Show »

FASTA42348,787

References

« Hide '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. expand/collapse author list , 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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-351 (ISOFORM 6).
Tissue: Placenta and Trachea.
[4]"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.
[5]"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. expand/collapse author list , 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].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]NIEHS SNPs program
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]"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.
[9]"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.
[10]"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.
[11]"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.
[12]"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.
[13]"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.
[14]"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.
[15]"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].
[16]"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.
[17]"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.
[18]"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.
[19]"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.
[20]"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

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.
AK304354 mRNA. Translation: BAG65196.1. Different initiation.
DC308409 mRNA. No translation available.
AL137348 mRNA. Translation: CAB70703.2.
DQ027001 Genomic DNA. Translation: AAY29059.1.
AP001328 Genomic DNA. No translation available.
AP002907 Genomic DNA. No translation available.
CH471060 Genomic DNA. Translation: EAW91842.1. Sequence problems.
BC042468 mRNA. Translation: AAH42468.1.
BC108261 mRNA. Translation: AAI08262.1.
BC117496 mRNA. Translation: AAI17497.1.
BC130628 mRNA. Translation: AAI30629.1.
CCDSCCDS34932.1. [Q7LG56-1]
CCDS55267.1. [Q7LG56-2]
PIRT46249.
RefSeqNP_001165948.1. NM_001172477.1. [Q7LG56-6]
NP_001165949.1. NM_001172478.1. [Q7LG56-2]
NP_056528.2. NM_015713.4. [Q7LG56-1]
UniGeneHs.512592.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2VUXX-ray2.80A/B20-322[»]
3HF1X-ray2.60A/B1-351[»]
4DJNX-ray2.20A/B13-322[»]
ProteinModelPortalQ7LG56.
SMRQ7LG56. Positions 28-314.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119071. 7 interactions.
DIPDIP-24264N.
DIP-48627N.

Chemistry

BindingDBQ7LG56.
ChEMBLCHEMBL2095215.

PTM databases

PhosphoSiteQ7LG56.

Polymorphism databases

DMDM74727333.

Proteomic databases

MaxQBQ7LG56.
PaxDbQ7LG56.
PRIDEQ7LG56.

Protocols and materials databases

DNASU50484.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000251810; ENSP00000251810; ENSG00000048392. [Q7LG56-1]
ENST00000395912; ENSP00000379248; ENSG00000048392. [Q7LG56-2]
ENST00000519317; ENSP00000430641; ENSG00000048392. [Q7LG56-3]
ENST00000519962; ENSP00000429140; ENSG00000048392. [Q7LG56-4]
ENST00000522394; ENSP00000429578; ENSG00000048392. [Q7LG56-5]
GeneID50484.
KEGGhsa:50484.
UCSCuc003ykn.3. human. [Q7LG56-1]
uc010mbv.2. human. [Q7LG56-2]
uc010mbw.1. human. [Q7LG56-3]

Organism-specific databases

CTD50484.
GeneCardsGC08M103216.
HGNCHGNC:17296. RRM2B.
HPACAB006854.
HPA028812.
MIM604712. gene.
612075. phenotype.
613077. phenotype.
neXtProtNX_Q7LG56.
Orphanet329336. Adult-onset chronic progressive external ophthalmoplegia with mitochondrial myopathy.
254892. Autosomal dominant progressive external ophthalmoplegia.
480. Kearns-Sayre syndrome.
255235. Mitochondrial DNA depletion syndrome, encephalomyopathic form with renal tubulopathy.
298. Mitochondrial neurogastrointestinal encephalomyopathy.
PharmGKBPA34866.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0208.
HOVERGENHBG001647.
InParanoidQ7LG56.
KOK10808.
OMANTSHEIA.
OrthoDBEOG7VMP5N.
PhylomeDBQ7LG56.
TreeFamTF300465.

Enzyme and pathway databases

BRENDA1.17.4.1. 2681.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00326.

Gene expression databases

ArrayExpressQ7LG56.
BgeeQ7LG56.
GenevestigatorQ7LG56.

Family and domain databases

Gene3D1.10.620.20. 1 hit.
InterProIPR009078. Ferritin-like_SF.
IPR012348. RNR-rel.
IPR000358. RNR_small.
[Graphical view]
PANTHERPTHR23409. PTHR23409. 1 hit.
PfamPF00268. Ribonuc_red_sm. 1 hit.
[Graphical view]
SUPFAMSSF47240. SSF47240. 1 hit.
PROSITEPS00368. RIBORED_SMALL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRRM2B. human.
EvolutionaryTraceQ7LG56.
GeneWikiRRM2B.
GenomeRNAi50484.
NextBio53036.
PROQ7LG56.
SOURCESearch...

Entry information

Entry nameRIR2B_HUMAN
AccessionPrimary (citable) accession number: Q7LG56
Secondary accession number(s): B4E2N4 expand/collapse secondary AC list , 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: July 9, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM