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Q7LG56

- RIR2B_HUMAN

UniProt

Q7LG56 - RIR2B_HUMAN

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Protein

Ribonucleoside-diphosphate reductase subunit M2 B

Gene

RRM2B

Organism
Homo sapiens (Human)
Status
Reviewed - 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.3 Publications

Catalytic activityi

2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.1 PublicationPROSITE-ProRule annotation

Cofactori

Fe cation1 PublicationNote: Binds 2 iron ions per subunit.1 Publication

Pathwayi

Sites

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

GO - Molecular functioni

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

GO - Biological processi

  1. deoxyribonucleoside diphosphate metabolic process Source: InterPro
  2. deoxyribonucleoside triphosphate metabolic process Source: Ensembl
  3. deoxyribonucleotide biosynthetic process Source: Ensembl
  4. DNA repair Source: UniProtKB-KW
  5. kidney development Source: Ensembl
  6. mitochondrial DNA replication Source: Ensembl
  7. negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator Source: Ensembl
  8. nucleobase-containing small molecule interconversion Source: Reactome
  9. nucleobase-containing small molecule metabolic process Source: Reactome
  10. renal system process Source: Ensembl
  11. response to oxidative stress Source: Ensembl
  12. small molecule metabolic process Source: Reactome
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

BRENDAi1.17.4.1. 2681.
ReactomeiREACT_21330. 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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:17296. RRM2B.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. extracellular vesicular exosome Source: UniProt
  3. nucleoplasm Source: Reactome
  4. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti64 – 641W → R in MTDPS8A. 1 Publication
VAR_046217
Natural varianti85 – 851Missing in MTDPS8A. 1 Publication
VAR_046218
Natural varianti194 – 1941E → G in MTDPS8A. 1 Publication
VAR_046219
Natural varianti194 – 1941E → K in MTDPS8A. 1 Publication
VAR_046220
Natural varianti224 – 2241I → S in MTDPS8A; without tubulopathy. 1 Publication
VAR_046221
Natural varianti236 – 2361C → F in MTDPS8A. 1 Publication
VAR_046222
Natural varianti282 – 2821M → I in MTDPS8A; without tubulopathy. 1 Publication
Corresponds to variant rs182614164 [ dbSNP | Ensembl ].
VAR_046223
Natural varianti317 – 3171L → V in MTDPS8A; without tubulopathy. 1 Publication
VAR_046224
Mitochondrial DNA depletion syndrome 8B (MTDPS8B) [MIM:612075]: A disease due to mitochondrial dysfunction and characterized by ophthalmoplegia, ptosis, gastrointestinal dysmotility, cachexia, peripheral neuropathy.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti110 – 1101R → H in MTDPS8B. 1 Publication
VAR_065122
Natural varianti121 – 1211R → H in MTDPS8B. 1 Publication
VAR_065123
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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

Keywords - Diseasei

Disease mutation, Neuropathy, Progressive external ophthalmoplegia

Organism-specific databases

MIMi612075. phenotype.
613077. phenotype.
Orphaneti329336. 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.
PharmGKBiPA34866.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 351351Ribonucleoside-diphosphate reductase subunit M2 BPRO_0000228150Add
BLAST

Proteomic databases

MaxQBiQ7LG56.
PaxDbiQ7LG56.
PRIDEiQ7LG56.

PTM databases

PhosphoSiteiQ7LG56.

Expressioni

Tissue specificityi

Widely expressed at a high level in skeletal muscle and at a weak level in thymus. Expressed in epithelial dysplasias and squamous cell carcinoma.1 Publication

Inductioni

In response to DNA damage in a wild-type p53/TP53-dependent manner.1 Publication

Gene expression databases

BgeeiQ7LG56.
ExpressionAtlasiQ7LG56. baseline and differential.
GenevestigatoriQ7LG56.

Organism-specific databases

HPAiCAB006854.
HPA028812.

Interactioni

Subunit structurei

Heterotetramer with large (RRM1) subunit. Interacts with p53/TP53. Interacts with RRM1 in response to DNA damage.5 Publications

Protein-protein interaction databases

BioGridi119071. 10 interactions.
DIPiDIP-24264N.
DIP-48627N.

Structurei

Secondary structure

1
351
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi29 – 313Combined sources
Turni33 – 353Combined sources
Helixi37 – 393Combined sources
Beta strandi42 – 443Combined sources
Helixi50 – 6112Combined sources
Helixi66 – 683Combined sources
Helixi74 – 785Combined sources
Helixi83 – 10927Combined sources
Helixi111 – 1144Combined sources
Helixi118 – 14528Combined sources
Helixi149 – 1568Combined sources
Helixi158 – 1614Combined sources
Helixi163 – 17715Combined sources
Beta strandi179 – 1813Combined sources
Helixi183 – 19513Combined sources
Turni196 – 1983Combined sources
Helixi199 – 21012Combined sources
Helixi215 – 24026Combined sources
Helixi248 – 26720Combined sources
Helixi272 – 2754Combined sources
Helixi279 – 29618Combined sources
Helixi310 – 3123Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VUXX-ray2.80A/B20-322[»]
3HF1X-ray2.60A/B1-351[»]
4DJNX-ray2.20A/B13-322[»]
ProteinModelPortaliQ7LG56.
SMRiQ7LG56. Positions 28-314.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7LG56.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0208.
GeneTreeiENSGT00390000013305.
HOVERGENiHBG001647.
InParanoidiQ7LG56.
KOiK10808.
OMAiNTSHEIA.
OrthoDBiEOG7VMP5N.
PhylomeDBiQ7LG56.
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]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q7LG56-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MGDPERPEAA GLDQDERSSS DTNESEIKSN EEPLLRKSSR RFVIFPIQYP
60 70 80 90 100
DIWKMYKQAQ ASFWTAEEVD LSKDLPHWNK LKADEKYFIS HILAFFAASD
110 120 130 140 150
GIVNENLVER FSQEVQVPEA RCFYGFQILI ENVHSEMYSL LIDTYIRDPK
160 170 180 190 200
KREFLFNAIE TMPYVKKKAD WALRWIADRK STFGERVVAF AAVEGVFFSG
210 220 230 240 250
SFAAIFWLKK RGLMPGLTFS NELISRDEGL HCDFACLMFQ YLVNKPSEER
260 270 280 290 300
VREIIVDAVK IEQEFLTEAL PVGLIGMNCI LMKQYIEFVA DRLLVELGFS
310 320 330 340 350
KVFQAENPFD FMENISLEGK TNFFEKRVSE YQRFAVMAET TDNVFTLDAD

F
Length:351
Mass (Da):40,737
Last modified:July 5, 2004 - v1
Checksum:i6D008687EEF40994
GO
Isoform 2 (identifier: Q7LG56-2) [UniParc]FASTAAdd to Basket

Also known as: Long form

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

Show »
Length:299
Mass (Da):34,529
Checksum:i4705C44389EB689B
GO
Isoform 3 (identifier: Q7LG56-3) [UniParc]FASTAAdd to Basket

Also known as: Short form gamma

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

Show »
Length:139
Mass (Da):15,963
Checksum:iE80F65CB030E89B5
GO
Isoform 4 (identifier: Q7LG56-4) [UniParc]FASTAAdd to Basket

Also known as: Short form beta

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

Show »
Length:66
Mass (Da):7,602
Checksum:iD432147F4FC35499
GO
Isoform 5 (identifier: Q7LG56-5) [UniParc]FASTAAdd to Basket

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.

Show »
Length:43
Mass (Da):4,852
Checksum:i29373C73112CBE75
GO
Isoform 6 (identifier: Q7LG56-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: MGDPERPEAAGLDQDE → MLLLRLPPHR...KDDAWRPQAG

Note: No experimental confirmation available.

Show »
Length:423
Mass (Da):48,787
Checksum:i0D2B8471AE362D44
GO

Sequence cautioni

The sequence BAG65196.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence EAW91842.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti277 – 2771M → V in BAA92005. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti64 – 641W → R in MTDPS8A. 1 Publication
VAR_046217
Natural varianti85 – 851Missing in MTDPS8A. 1 Publication
VAR_046218
Natural varianti110 – 1101R → H in MTDPS8B. 1 Publication
VAR_065122
Natural varianti115 – 1151V → L in colorectal adenocarcinomas cell line; loss of ribonucleotide reductase activity. 1 Publication
VAR_025699
Natural varianti121 – 1211R → H in MTDPS8B. 1 Publication
VAR_065123
Natural varianti194 – 1941E → G in MTDPS8A. 1 Publication
VAR_046219
Natural varianti194 – 1941E → K in MTDPS8A. 1 Publication
VAR_046220
Natural varianti224 – 2241I → S in MTDPS8A; without tubulopathy. 1 Publication
VAR_046221
Natural varianti236 – 2361C → F in MTDPS8A. 1 Publication
VAR_046222
Natural varianti282 – 2821M → I in MTDPS8A; without tubulopathy. 1 Publication
Corresponds to variant rs182614164 [ dbSNP | Ensembl ].
VAR_046223
Natural varianti317 – 3171L → V in MTDPS8A; without tubulopathy. 1 Publication
VAR_046224

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1616MGDPE…LDQDE → MLLLRLPPHRSHASPLDCKL QDRCRKCYSPRSGQACPPAL AAAWLRRCERRGGRPRGGRR KELTLGLRPARCSAPGPAKD DAWRPQAG in isoform 6. 1 PublicationVSP_053585Add
BLAST
Alternative sequencei17 – 301285Missing in isoform 4. 1 PublicationVSP_017668Add
BLAST
Alternative sequencei17 – 228212Missing in isoform 3. 1 PublicationVSP_017669Add
BLAST
Alternative sequencei17 – 6852Missing in isoform 2. 1 PublicationVSP_017670Add
BLAST
Alternative sequencei42 – 432FV → SF in isoform 5. 1 PublicationVSP_017671
Alternative sequencei44 – 351308Missing in isoform 5. 1 PublicationVSP_017672Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34932.1. [Q7LG56-1]
CCDS55267.1. [Q7LG56-2]
PIRiT46249.
RefSeqiNP_001165948.1. NM_001172477.1. [Q7LG56-6]
NP_001165949.1. NM_001172478.1. [Q7LG56-2]
NP_056528.2. NM_015713.4. [Q7LG56-1]
UniGeneiHs.512592.

Genome annotation databases

EnsembliENST00000251810; ENSP00000251810; ENSG00000048392. [Q7LG56-1]
ENST00000395912; ENSP00000379248; ENSG00000048392. [Q7LG56-2]
ENST00000519317; ENSP00000430641; ENSG00000048392. [Q7LG56-3]
ENST00000519962; ENSP00000429140; ENSG00000048392. [Q7LG56-4]
ENST00000522394; ENSP00000429578; ENSG00000048392. [Q7LG56-5]
ENST00000621845; ENSP00000484318; ENSG00000048392.
GeneIDi50484.
KEGGihsa:50484.
UCSCiuc003ykn.3. human. [Q7LG56-1]
uc010mbv.2. human. [Q7LG56-2]
uc010mbw.1. human. [Q7LG56-3]

Polymorphism databases

DMDMi74727333.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS34932.1. [Q7LG56-1 ]
CCDS55267.1. [Q7LG56-2 ]
PIRi T46249.
RefSeqi NP_001165948.1. NM_001172477.1. [Q7LG56-6 ]
NP_001165949.1. NM_001172478.1. [Q7LG56-2 ]
NP_056528.2. NM_015713.4. [Q7LG56-1 ]
UniGenei Hs.512592.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali Q7LG56.
SMRi Q7LG56. Positions 28-314.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119071. 10 interactions.
DIPi DIP-24264N.
DIP-48627N.

Chemistry

BindingDBi Q7LG56.
ChEMBLi CHEMBL2095215.
DrugBanki DB00242. Cladribine.

PTM databases

PhosphoSitei Q7LG56.

Polymorphism databases

DMDMi 74727333.

Proteomic databases

MaxQBi Q7LG56.
PaxDbi Q7LG56.
PRIDEi Q7LG56.

Protocols and materials databases

DNASUi 50484.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000251810 ; ENSP00000251810 ; ENSG00000048392 . [Q7LG56-1 ]
ENST00000395912 ; ENSP00000379248 ; ENSG00000048392 . [Q7LG56-2 ]
ENST00000519317 ; ENSP00000430641 ; ENSG00000048392 . [Q7LG56-3 ]
ENST00000519962 ; ENSP00000429140 ; ENSG00000048392 . [Q7LG56-4 ]
ENST00000522394 ; ENSP00000429578 ; ENSG00000048392 . [Q7LG56-5 ]
ENST00000621845 ; ENSP00000484318 ; ENSG00000048392 .
GeneIDi 50484.
KEGGi hsa:50484.
UCSCi uc003ykn.3. human. [Q7LG56-1 ]
uc010mbv.2. human. [Q7LG56-2 ]
uc010mbw.1. human. [Q7LG56-3 ]

Organism-specific databases

CTDi 50484.
GeneCardsi GC08M103216.
HGNCi HGNC:17296. RRM2B.
HPAi CAB006854.
HPA028812.
MIMi 604712. gene.
612075. phenotype.
613077. phenotype.
neXtProti NX_Q7LG56.
Orphaneti 329336. 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.
PharmGKBi PA34866.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0208.
GeneTreei ENSGT00390000013305.
HOVERGENi HBG001647.
InParanoidi Q7LG56.
KOi K10808.
OMAi NTSHEIA.
OrthoDBi EOG7VMP5N.
PhylomeDBi Q7LG56.
TreeFami TF300465.

Enzyme and pathway databases

UniPathwayi UPA00326 .
BRENDAi 1.17.4.1. 2681.
Reactomei REACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.

Miscellaneous databases

ChiTaRSi RRM2B. human.
EvolutionaryTracei Q7LG56.
GeneWikii RRM2B.
GenomeRNAii 50484.
NextBioi 53036.
PROi Q7LG56.
SOURCEi Search...

Gene expression databases

Bgeei Q7LG56.
ExpressionAtlasi Q7LG56. baseline and differential.
Genevestigatori Q7LG56.

Family and domain databases

Gene3Di 1.10.620.20. 1 hit.
InterProi IPR009078. Ferritin-like_SF.
IPR012348. RNR-rel.
IPR000358. RNR_small.
[Graphical view ]
PANTHERi PTHR23409. PTHR23409. 1 hit.
Pfami PF00268. Ribonuc_red_sm. 1 hit.
[Graphical view ]
SUPFAMi SSF47240. SSF47240. 1 hit.
PROSITEi PS00368. RIBORED_SMALL. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-351 (ISOFORM 6).
    Tissue: Placenta and Trachea.
  4. 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.
    , 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. 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. 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. 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.

Entry informationi

Entry nameiRIR2B_HUMAN
AccessioniPrimary (citable) accession number: Q7LG56
Secondary accession number(s): B4E2N4
, Q17R22, Q75PQ6, Q75PQ7, Q75PY8, Q75PY9, Q86YE3, Q9NPD6, Q9NTD8, Q9NUW3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: July 5, 2004
Last modified: November 26, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

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