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P31350

- RIR2_HUMAN

UniProt

P31350 - RIR2_HUMAN

Protein

Ribonucleoside-diphosphate reductase subunit M2

Gene

RRM2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 1 (01 Jul 1993)
      Previous versions | rss
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    Functioni

    Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Inhibits Wnt signaling.

    Catalytic activityi

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

    Cofactori

    Binds 2 iron ions per subunit.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi138 – 1381Iron 1PROSITE-ProRule annotation
    Metal bindingi169 – 1691Iron 1PROSITE-ProRule annotation
    Metal bindingi169 – 1691Iron 2By similarity
    Metal bindingi172 – 1721Iron 1PROSITE-ProRule annotation
    Active sitei176 – 1761PROSITE-ProRule annotation
    Metal bindingi232 – 2321Iron 2By similarity
    Metal bindingi266 – 2661Iron 2By similarity
    Metal bindingi269 – 2691Iron 2By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. deoxyribonucleoside diphosphate metabolic process Source: InterPro
    2. deoxyribonucleotide biosynthetic process Source: UniProtKB
    3. DNA replication Source: UniProtKB-UniPathway
    4. G1/S transition of mitotic cell cycle Source: Reactome
    5. mitotic cell cycle Source: Reactome
    6. nucleobase-containing small molecule interconversion Source: Reactome
    7. nucleobase-containing small molecule metabolic process Source: Reactome
    8. protein heterotetramerization Source: Ensembl
    9. regulation of transcription involved in G1/S transition of mitotic cell cycle Source: Reactome
    10. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    DNA replication

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS10398-MONOMER.
    ReactomeiREACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.
    REACT_471. E2F mediated regulation of DNA replication.
    REACT_683. G1/S-Specific Transcription.
    UniPathwayiUPA00326.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribonucleoside-diphosphate reductase subunit M2 (EC:1.17.4.1)
    Alternative name(s):
    Ribonucleotide reductase small chain
    Ribonucleotide reductase small subunit
    Gene namesi
    Name:RRM2
    Synonyms:RR2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:10452. RRM2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. nucleoplasm Source: Reactome
    4. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi20 – 201S → A: Enhances inhibitory effect on Wnt signaling.
    Mutagenesisi20 – 201S → E: Prevents inhibitory effect on Wnt signaling.

    Organism-specific databases

    PharmGKBiPA299.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 389389Ribonucleoside-diphosphate reductase subunit M2PRO_0000190447Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei20 – 201Phosphoserine8 Publications
    Modified residuei33 – 331Phosphothreonine2 Publications

    Post-translational modificationi

    Phosphorylation on Ser-20 relieves the inhibitory effect on Wnt signaling.8 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP31350.
    PaxDbiP31350.
    PRIDEiP31350.

    PTM databases

    PhosphoSiteiP31350.

    Miscellaneous databases

    PMAP-CutDBP31350.

    Expressioni

    Gene expression databases

    ArrayExpressiP31350.
    BgeeiP31350.
    CleanExiHS_RRM2.
    GenevestigatoriP31350.

    Organism-specific databases

    HPAiHPA056994.

    Interactioni

    Subunit structurei

    Heterodimer of a large and a small subunit.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CCNFP4100212EBI-2339245,EBI-1207574
    FZR1Q9UM112EBI-2339245,EBI-724997
    RRM1P239213EBI-2339245,EBI-717006

    Protein-protein interaction databases

    BioGridi112155. 13 interactions.
    DIPiDIP-24232N.
    IntActiP31350. 7 interactions.
    STRINGi9606.ENSP00000302955.

    Structurei

    Secondary structure

    1
    389
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni71 – 733
    Turni77 – 804
    Helixi88 – 9912
    Helixi104 – 1063
    Helixi110 – 1123
    Helixi113 – 1186
    Helixi121 – 14727
    Helixi149 – 1524
    Helixi156 – 18328
    Helixi187 – 1948
    Helixi196 – 1994
    Helixi201 – 2033
    Helixi204 – 21512
    Beta strandi217 – 2193
    Helixi221 – 23313
    Turni234 – 2363
    Helixi237 – 24812
    Helixi253 – 27826
    Helixi286 – 30520
    Helixi310 – 3134
    Helixi317 – 33519

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2UW2X-ray2.80A60-389[»]
    3OLJX-ray2.10A/B/C/D66-350[»]
    3VPMX-ray2.70A/B66-350[»]
    3VPNX-ray2.25A/B66-350[»]
    3VPOX-ray2.30A/B66-350[»]
    ProteinModelPortaliP31350.
    SMRiP31350. Positions 66-350.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP31350.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0208.
    HOGENOMiHOG000255975.
    HOVERGENiHBG001647.
    InParanoidiP31350.
    KOiK10808.
    OMAiGVMNSTK.
    OrthoDBiEOG7VMP5N.
    PhylomeDBiP31350.
    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 (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P31350-1) [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

    MLSLRVPLAP ITDPQQLQLS PLKGLSLVDK ENTPPALSGT RVLASKTARR    50
    IFQEPTEPKT KAAAPGVEDE PLLRENPRRF VIFPIEYHDI WQMYKKAEAS 100
    FWTAEEVDLS KDIQHWESLK PEERYFISHV LAFFAASDGI VNENLVERFS 150
    QEVQITEARC FYGFQIAMEN IHSEMYSLLI DTYIKDPKER EFLFNAIETM 200
    PCVKKKADWA LRWIGDKEAT YGERVVAFAA VEGIFFSGSF ASIFWLKKRG 250
    LMPGLTFSNE LISRDEGLHC DFACLMFKHL VHKPSEERVR EIIINAVRIE 300
    QEFLTEALPV KLIGMNCTLM KQYIEFVADR LMLELGFSKV FRVENPFDFM 350
    ENISLEGKTN FFEKRVGEYQ RMGVMSSPTE NSFTLDADF 389
    Length:389
    Mass (Da):44,878
    Last modified:July 1, 1993 - v1
    Checksum:i10E6F5F84D34DA94
    GO
    Isoform 2 (identifier: P31350-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MGRVGGMAQPMGRAGAPKPMGRAGSARRGRFKGCWSEGSPVHPVPAVLSWLLALLRCASTM

    Note: No experimental confirmation available.Curated

    Show »
    Length:449
    Mass (Da):51,093
    Checksum:iDFEA2E41A26BD80E
    GO

    Sequence cautioni

    The sequence DA477511 differs from that shown. Reason: Frameshift at position 87.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Isoform 2 (identifier: P31350-2)
    Sequence conflicti28 – 281R → H in DA477511. (PubMed:14702039)Curated
    Sequence conflicti59 – 591S → A in DA477511. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MGRVGGMAQPMGRAGAPKPM GRAGSARRGRFKGCWSEGSP VHPVPAVLSWLLALLRCAST M in isoform 2. 1 PublicationVSP_044917

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59618 mRNA. Translation: CAA42181.1.
    S40301 mRNA. Translation: AAA09577.1.
    AY032750 Genomic DNA. Translation: AAK51163.1.
    AK313719 mRNA. Translation: BAG36462.1.
    DA477511 mRNA. No translation available.
    AC104794 Genomic DNA. Translation: AAX93099.1.
    AC118058 Genomic DNA. No translation available.
    BC001886 mRNA. Translation: AAH01886.1.
    BC030154 mRNA. Translation: AAH30154.1.
    CCDSiCCDS1669.1. [P31350-1]
    CCDS54334.1. [P31350-2]
    PIRiS25854.
    RefSeqiNP_001025.1. NM_001034.3. [P31350-1]
    NP_001159403.1. NM_001165931.1. [P31350-2]
    UniGeneiHs.226390.

    Genome annotation databases

    EnsembliENST00000304567; ENSP00000302955; ENSG00000171848. [P31350-1]
    ENST00000360566; ENSP00000353770; ENSG00000171848. [P31350-2]
    GeneIDi6241.
    KEGGihsa:6241.
    UCSCiuc021vdr.1. human. [P31350-1]

    Polymorphism databases

    DMDMi400979.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Ribonucleotide reductase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59618 mRNA. Translation: CAA42181.1 .
    S40301 mRNA. Translation: AAA09577.1 .
    AY032750 Genomic DNA. Translation: AAK51163.1 .
    AK313719 mRNA. Translation: BAG36462.1 .
    DA477511 mRNA. No translation available.
    AC104794 Genomic DNA. Translation: AAX93099.1 .
    AC118058 Genomic DNA. No translation available.
    BC001886 mRNA. Translation: AAH01886.1 .
    BC030154 mRNA. Translation: AAH30154.1 .
    CCDSi CCDS1669.1. [P31350-1 ]
    CCDS54334.1. [P31350-2 ]
    PIRi S25854.
    RefSeqi NP_001025.1. NM_001034.3. [P31350-1 ]
    NP_001159403.1. NM_001165931.1. [P31350-2 ]
    UniGenei Hs.226390.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2UW2 X-ray 2.80 A 60-389 [» ]
    3OLJ X-ray 2.10 A/B/C/D 66-350 [» ]
    3VPM X-ray 2.70 A/B 66-350 [» ]
    3VPN X-ray 2.25 A/B 66-350 [» ]
    3VPO X-ray 2.30 A/B 66-350 [» ]
    ProteinModelPortali P31350.
    SMRi P31350. Positions 66-350.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112155. 13 interactions.
    DIPi DIP-24232N.
    IntActi P31350. 7 interactions.
    STRINGi 9606.ENSP00000302955.

    Chemistry

    BindingDBi P31350.
    ChEMBLi CHEMBL2095215.
    GuidetoPHARMACOLOGYi 2631.

    PTM databases

    PhosphoSitei P31350.

    Polymorphism databases

    DMDMi 400979.

    Proteomic databases

    MaxQBi P31350.
    PaxDbi P31350.
    PRIDEi P31350.

    Protocols and materials databases

    DNASUi 6241.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000304567 ; ENSP00000302955 ; ENSG00000171848 . [P31350-1 ]
    ENST00000360566 ; ENSP00000353770 ; ENSG00000171848 . [P31350-2 ]
    GeneIDi 6241.
    KEGGi hsa:6241.
    UCSCi uc021vdr.1. human. [P31350-1 ]

    Organism-specific databases

    CTDi 6241.
    GeneCardsi GC02P010262.
    HGNCi HGNC:10452. RRM2.
    HPAi HPA056994.
    MIMi 180390. gene.
    neXtProti NX_P31350.
    PharmGKBi PA299.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0208.
    HOGENOMi HOG000255975.
    HOVERGENi HBG001647.
    InParanoidi P31350.
    KOi K10808.
    OMAi GVMNSTK.
    OrthoDBi EOG7VMP5N.
    PhylomeDBi P31350.
    TreeFami TF300465.

    Enzyme and pathway databases

    UniPathwayi UPA00326 .
    BioCyci MetaCyc:HS10398-MONOMER.
    Reactomei REACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.
    REACT_471. E2F mediated regulation of DNA replication.
    REACT_683. G1/S-Specific Transcription.

    Miscellaneous databases

    EvolutionaryTracei P31350.
    GeneWikii RRM2.
    GenomeRNAii 6241.
    NextBioi 24237.
    PMAP-CutDB P31350.
    PROi P31350.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P31350.
    Bgeei P31350.
    CleanExi HS_RRM2.
    Genevestigatori P31350.

    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. "Sequence analysis of the large and small subunits of human ribonucleotide reductase."
      Pavloff N., Rivard D., Masson S., Shen S.-H., Mes-Masson A.-M.
      DNA Seq. 2:227-234(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Mammary carcinoma.
    2. "Characterization of the human ribonucleotide reductase M2 subunit gene; genomic structure and promoter analyses."
      Zhou B., Yen Y.
      Cytogenet. Cell Genet. 95:52-59(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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 1-94 (ISOFORM 2).
      Tissue: Neonatal skin.
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Muscle and Skin.
    6. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
      Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
      Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20 AND THR-33, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20 AND THR-33, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRIR2_HUMAN
    AccessioniPrimary (citable) accession number: P31350
    Secondary accession number(s): B2R9B5, J3KP43, Q5WRU7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 156 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

    Miscellaneous

    Two distinct regulatory sites have been defined: the specificity site, which controls substrate specificity, and the activity site which regulates overall catalytic activity. A substrate-binding catalytic site, located on M1, is formed only in the presence of the second subunit M2.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3