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Q7LG56

- RIR2B_HUMAN

UniProt

Q7LG56 - RIR2B_HUMAN

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
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    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

    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

    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

    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

    ArrayExpressiQ7LG56.
    BgeeiQ7LG56.
    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. 7 interactions.
    DIPiDIP-24264N.
    DIP-48627N.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MGDPERPEAA GLDQDERSSS DTNESEIKSN EEPLLRKSSR RFVIFPIQYP    50
    DIWKMYKQAQ ASFWTAEEVD LSKDLPHWNK LKADEKYFIS HILAFFAASD 100
    GIVNENLVER FSQEVQVPEA RCFYGFQILI ENVHSEMYSL LIDTYIRDPK 150
    KREFLFNAIE TMPYVKKKAD WALRWIADRK STFGERVVAF AAVEGVFFSG 200
    SFAAIFWLKK RGLMPGLTFS NELISRDEGL HCDFACLMFQ YLVNKPSEER 250
    VREIIVDAVK IEQEFLTEAL PVGLIGMNCI LMKQYIEFVA DRLLVELGFS 300
    KVFQAENPFD FMENISLEGK TNFFEKRVSE YQRFAVMAET TDNVFTLDAD 350
    F 351
    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.
    The sequence EAW91842.1 differs from that shown. Reason: Erroneous gene model prediction.

    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:
    EMBL
    GenBank
    DDBJ
    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]
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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. 7 interactions.
    DIPi DIP-24264N.
    DIP-48627N.

    Chemistry

    BindingDBi Q7LG56.
    ChEMBLi CHEMBL2095215.

    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 ]
    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.
    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

    ArrayExpressi Q7LG56.
    Bgeei Q7LG56.
    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

    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: October 1, 2014
    This is version 118 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

    Dasty 3