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P23921

- RIR1_HUMAN

UniProt

P23921 - RIR1_HUMAN

Protein

Ribonucleoside-diphosphate reductase large subunit

Gene

RRM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 1 (01 Mar 1992)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

    2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.1 Publication

    Enzyme regulationi

    Under complex allosteric control mediated by deoxynucleoside triphosphates and ATP binding to separate specificity and activation sites on the M1 subunit. The type of nucleotide bound at the specificity site determines substrate preference. It seems probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP reduction and dTTP favors GDP reduction. Stimulated by ATP and inhibited by dATP binding to the activity site.2 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei5 – 51Allosteric activatorBy similarity
    Binding sitei53 – 531Allosteric activatorBy similarity
    Binding sitei88 – 881Allosteric activatorBy similarity
    Binding sitei202 – 2021SubstrateBy similarity
    Sitei218 – 2181Important for hydrogen atom transferBy similarity
    Sitei226 – 2261Allosteric effector binding, determines substrate specificity
    Binding sitei247 – 2471Substrate; via amide nitrogenBy similarity
    Sitei256 – 2561Allosteric effector binding, determines substrate specificity
    Active sitei427 – 4271Proton acceptorBy similarity
    Active sitei429 – 4291Cysteine radical intermediateBy similarity
    Active sitei431 – 4311Proton acceptorBy similarity
    Sitei444 – 4441Important for hydrogen atom transferBy similarity
    Sitei737 – 7371Important for electron transferBy similarity
    Sitei738 – 7381Important for electron transferBy similarity
    Sitei787 – 7871Interacts with thioredoxin/glutaredoxinBy similarity
    Sitei790 – 7901Interacts with thioredoxin/glutaredoxinBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. cell proliferation in forebrain Source: Ensembl
    2. deoxyribonucleotide biosynthetic process Source: UniProtKB
    3. DNA replication Source: UniProtKB-UniPathway
    4. male gonad development Source: Ensembl
    5. mitotic cell cycle Source: Ensembl
    6. nucleobase-containing small molecule interconversion Source: Reactome
    7. nucleobase-containing small molecule metabolic process Source: Reactome
    8. protein heterotetramerization Source: Ensembl
    9. pyrimidine nucleobase metabolic process Source: Ensembl
    10. response to ionizing radiation Source: Ensembl
    11. retina development in camera-type eye Source: Ensembl
    12. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    DNA replication

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS09541-MONOMER.
    ReactomeiREACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.
    UniPathwayiUPA00326.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribonucleoside-diphosphate reductase large subunit (EC:1.17.4.1)
    Alternative name(s):
    Ribonucleoside-diphosphate reductase subunit M1
    Ribonucleotide reductase large subunit
    Gene namesi
    Name:RRM1
    Synonyms:RR1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:10451. RRM1.

    Subcellular locationi

    GO - Cellular componenti

    1. cell projection Source: Ensembl
    2. cytoplasm Source: HPA
    3. cytosol Source: Reactome
    4. extracellular vesicular exosome Source: UniProt
    5. neuronal cell body Source: Ensembl
    6. nuclear envelope Source: Ensembl
    7. nucleoplasm Source: Reactome
    8. ribonucleoside-diphosphate reductase complex Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA298.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 792792Ribonucleoside-diphosphate reductase large subunitPRO_0000187190Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei17 – 171N6-acetyllysine1 Publication
    Disulfide bondi218 ↔ 444Redox-activeBy similarity
    Modified residuei376 – 3761N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Disulfide bond

    Proteomic databases

    MaxQBiP23921.
    PaxDbiP23921.
    PeptideAtlasiP23921.
    PRIDEiP23921.

    PTM databases

    PhosphoSiteiP23921.

    Expressioni

    Gene expression databases

    ArrayExpressiP23921.
    BgeeiP23921.
    CleanExiHS_RRM1.
    GenevestigatoriP23921.

    Organism-specific databases

    HPAiCAB022093.
    HPA057265.

    Interactioni

    Subunit structurei

    Heterodimer of a large and a small subunit. Heterodimer with small subunit RRM2 or RRM2B. The heterodimer with RRM2 has higher catalytic activity than the heterodimer with RRM2B.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RRM2P313503EBI-717006,EBI-2339245

    Protein-protein interaction databases

    BioGridi112154. 21 interactions.
    DIPiDIP-24233N.
    IntActiP23921. 4 interactions.
    MINTiMINT-1406473.
    STRINGi9606.ENSP00000300738.

    Structurei

    Secondary structure

    1
    792
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi15 – 239
    Turni31 – 333
    Helixi36 – 449
    Beta strandi48 – 503
    Helixi53 – 6614
    Helixi67 – 693
    Helixi78 – 8811
    Helixi94 – 10310
    Turni107 – 1093
    Helixi118 – 1269
    Helixi128 – 1336
    Helixi137 – 1426
    Helixi145 – 15410
    Beta strandi158 – 1636
    Helixi167 – 17913
    Helixi183 – 19513
    Beta strandi197 – 2004
    Helixi202 – 2076
    Beta strandi210 – 2123
    Beta strandi218 – 2225
    Helixi228 – 24316
    Beta strandi247 – 2515
    Beta strandi258 – 2614
    Helixi263 – 2653
    Beta strandi268 – 2703
    Helixi272 – 28514
    Beta strandi287 – 2937
    Beta strandi297 – 3015
    Helixi308 – 3114
    Turni312 – 3154
    Beta strandi317 – 3193
    Helixi321 – 3233
    Beta strandi328 – 3347
    Helixi336 – 3438
    Beta strandi347 – 3515
    Turni353 – 3553
    Helixi359 – 3613
    Helixi365 – 37612
    Beta strandi381 – 3855
    Helixi386 – 40015
    Beta strandi404 – 4074
    Helixi408 – 4136
    Helixi418 – 4203
    Beta strandi428 – 4303
    Beta strandi442 – 4443
    Beta strandi446 – 4505
    Helixi451 – 4544
    Beta strandi459 – 4613
    Helixi463 – 48321
    Helixi489 – 49810
    Beta strandi502 – 5065
    Helixi508 – 5147
    Beta strandi519 – 5213
    Helixi522 – 55029
    Helixi554 – 5563
    Helixi561 – 5633
    Helixi567 – 5704
    Beta strandi577 – 5793
    Helixi581 – 59111
    Helixi607 – 6115
    Beta strandi623 – 6297
    Beta strandi632 – 6376
    Helixi639 – 64810
    Helixi653 – 6619
    Turni662 – 6643
    Beta strandi670 – 6723
    Helixi674 – 6796
    Turni683 – 6853
    Helixi688 – 69912
    Helixi717 – 72913
    Beta strandi733 – 7375

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2WGHX-ray2.30A/B75-742[»]
    3HNCX-ray2.41A/B1-792[»]
    3HNDX-ray3.21A/B1-792[»]
    3HNEX-ray3.11A/B1-792[»]
    3HNFX-ray3.16A/B1-792[»]
    ProteinModelPortaliP23921.
    SMRiP23921. Positions 14-742.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23921.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 9292ATP-conePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni11 – 177Allosteric activator bindingBy similarity
    Regioni217 – 2182Substrate bindingBy similarity
    Regioni285 – 2884Allosteric effector binding, determines substrate specificity
    Regioni427 – 4315Substrate bindingBy similarity
    Regioni603 – 6075Substrate bindingBy similarity

    Sequence similaritiesi

    Contains 1 ATP-cone domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0209.
    HOGENOMiHOG000057035.
    HOVERGENiHBG003447.
    InParanoidiP23921.
    KOiK10807.
    OMAiEACLMCQ.
    OrthoDBiEOG7BGHK2.
    PhylomeDBiP23921.
    TreeFamiTF300578.

    Family and domain databases

    InterProiIPR005144. ATP-cone.
    IPR013346. NrdE_NrdA.
    IPR000788. RNR_lg_C.
    IPR013509. RNR_lsu_N.
    IPR008926. RNR_R1-su_N.
    [Graphical view]
    PfamiPF03477. ATP-cone. 1 hit.
    PF02867. Ribonuc_red_lgC. 1 hit.
    PF00317. Ribonuc_red_lgN. 1 hit.
    [Graphical view]
    PRINTSiPR01183. RIBORDTASEM1.
    SUPFAMiSSF48168. SSF48168. 1 hit.
    TIGRFAMsiTIGR02506. NrdE_NrdA. 1 hit.
    PROSITEiPS51161. ATP_CONE. 1 hit.
    PS00089. RIBORED_LARGE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P23921-1 [UniParc]FASTAAdd to Basket

    « Hide

    MHVIKRDGRQ ERVMFDKITS RIQKLCYGLN MDFVDPAQIT MKVIQGLYSG    50
    VTTVELDTLA AETAATLTTK HPDYAILAAR IAVSNLHKET KKVFSDVMED 100
    LYNYINPHNG KHSPMVAKST LDIVLANKDR LNSAIIYDRD FSYNYFGFKT 150
    LERSYLLKIN GKVAERPQHM LMRVSVGIHK EDIDAAIETY NLLSERWFTH 200
    ASPTLFNAGT NRPQLSSCFL LSMKDDSIEG IYDTLKQCAL ISKSAGGIGV 250
    AVSCIRATGS YIAGTNGNSN GLVPMLRVYN NTARYVDQGG NKRPGAFAIY 300
    LEPWHLDIFE FLDLKKNTGK EEQRARDLFF ALWIPDLFMK RVETNQDWSL 350
    MCPNECPGLD EVWGEEFEKL YASYEKQGRV RKVVKAQQLW YAIIESQTET 400
    GTPYMLYKDS CNRKSNQQNL GTIKCSNLCT EIVEYTSKDE VAVCNLASLA 450
    LNMYVTSEHT YDFKKLAEVT KVVVRNLNKI IDINYYPVPE ACLSNKRHRP 500
    IGIGVQGLAD AFILMRYPFE SAEAQLLNKQ IFETIYYGAL EASCDLAKEQ 550
    GPYETYEGSP VSKGILQYDM WNVTPTDLWD WKVLKEKIAK YGIRNSLLIA 600
    PMPTASTAQI LGNNESIEPY TSNIYTRRVL SGEFQIVNPH LLKDLTERGL 650
    WHEEMKNQII ACNGSIQSIP EIPDDLKQLY KTVWEISQKT VLKMAAERGA 700
    FIDQSQSLNI HIAEPNYGKL TSMHFYGWKQ GLKTGMYYLR TRPAANPIQF 750
    TLNKEKLKDK EKVSKEEEEK ERNTAAMVCS LENRDECLMC GS 792
    Length:792
    Mass (Da):90,070
    Last modified:March 1, 1992 - v1
    Checksum:i4470A76C61E8F86A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti6 – 61R → Q in AAD37491. (PubMed:9933563)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti590 – 5901K → Q.
    Corresponds to variant rs2228123 [ dbSNP | Ensembl ].
    VAR_052052
    Natural varianti778 – 7781V → A.
    Corresponds to variant rs2229196 [ dbSNP | Ensembl ].
    VAR_052053

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59543 mRNA. Translation: CAA42118.1.
    X59617 mRNA. Translation: CAA42180.1.
    AF107045 Genomic DNA. Translation: AAD37491.1.
    BC006498 mRNA. Translation: AAH06498.1.
    L10342 Genomic DNA. No translation available.
    CCDSiCCDS7750.1.
    PIRiS16680.
    RefSeqiNP_001024.1. NM_001033.3.
    UniGeneiHs.445705.

    Genome annotation databases

    EnsembliENST00000300738; ENSP00000300738; ENSG00000167325.
    GeneIDi6240.
    KEGGihsa:6240.
    UCSCiuc001lyw.4. human.

    Polymorphism databases

    DMDMi132608.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Ribonucleotide reductase entry

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59543 mRNA. Translation: CAA42118.1 .
    X59617 mRNA. Translation: CAA42180.1 .
    AF107045 Genomic DNA. Translation: AAD37491.1 .
    BC006498 mRNA. Translation: AAH06498.1 .
    L10342 Genomic DNA. No translation available.
    CCDSi CCDS7750.1.
    PIRi S16680.
    RefSeqi NP_001024.1. NM_001033.3.
    UniGenei Hs.445705.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2WGH X-ray 2.30 A/B 75-742 [» ]
    3HNC X-ray 2.41 A/B 1-792 [» ]
    3HND X-ray 3.21 A/B 1-792 [» ]
    3HNE X-ray 3.11 A/B 1-792 [» ]
    3HNF X-ray 3.16 A/B 1-792 [» ]
    ProteinModelPortali P23921.
    SMRi P23921. Positions 14-742.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112154. 21 interactions.
    DIPi DIP-24233N.
    IntActi P23921. 4 interactions.
    MINTi MINT-1406473.
    STRINGi 9606.ENSP00000300738.

    Chemistry

    BindingDBi P23921.
    ChEMBLi CHEMBL2095215.
    DrugBanki DB00631. Clofarabine.
    DB01073. Fludarabine.
    DB00441. Gemcitabine.
    DB01005. Hydroxyurea.
    GuidetoPHARMACOLOGYi 2630.

    PTM databases

    PhosphoSitei P23921.

    Polymorphism databases

    DMDMi 132608.

    Proteomic databases

    MaxQBi P23921.
    PaxDbi P23921.
    PeptideAtlasi P23921.
    PRIDEi P23921.

    Protocols and materials databases

    DNASUi 6240.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000300738 ; ENSP00000300738 ; ENSG00000167325 .
    GeneIDi 6240.
    KEGGi hsa:6240.
    UCSCi uc001lyw.4. human.

    Organism-specific databases

    CTDi 6240.
    GeneCardsi GC11P004115.
    HGNCi HGNC:10451. RRM1.
    HPAi CAB022093.
    HPA057265.
    MIMi 180410. gene.
    neXtProti NX_P23921.
    PharmGKBi PA298.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0209.
    HOGENOMi HOG000057035.
    HOVERGENi HBG003447.
    InParanoidi P23921.
    KOi K10807.
    OMAi EACLMCQ.
    OrthoDBi EOG7BGHK2.
    PhylomeDBi P23921.
    TreeFami TF300578.

    Enzyme and pathway databases

    UniPathwayi UPA00326 .
    BioCyci MetaCyc:HS09541-MONOMER.
    Reactomei REACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.

    Miscellaneous databases

    ChiTaRSi RRM1. human.
    EvolutionaryTracei P23921.
    GeneWikii RRM1.
    GenomeRNAii 6240.
    NextBioi 24233.
    PROi P23921.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P23921.
    Bgeei P23921.
    CleanExi HS_RRM1.
    Genevestigatori P23921.

    Family and domain databases

    InterProi IPR005144. ATP-cone.
    IPR013346. NrdE_NrdA.
    IPR000788. RNR_lg_C.
    IPR013509. RNR_lsu_N.
    IPR008926. RNR_R1-su_N.
    [Graphical view ]
    Pfami PF03477. ATP-cone. 1 hit.
    PF02867. Ribonuc_red_lgC. 1 hit.
    PF00317. Ribonuc_red_lgN. 1 hit.
    [Graphical view ]
    PRINTSi PR01183. RIBORDTASEM1.
    SUPFAMi SSF48168. SSF48168. 1 hit.
    TIGRFAMsi TIGR02506. NrdE_NrdA. 1 hit.
    PROSITEi PS51161. ATP_CONE. 1 hit.
    PS00089. RIBORED_LARGE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human M1 subunit of ribonucleotide reductase: cDNA sequence and expression in stimulated lymphocytes."
      Parker N.J., Begley C.G., Fox R.M.
      Nucleic Acids Res. 19:3741-3741(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Bone marrow.
    2. "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].
      Tissue: Mammary carcinoma.
    3. "A 1.4-Mb high-resolution physical map and contig of chromosome segment 11p15.5 and genes in the LOH11A metastasis suppressor region."
      Bepler G., O'Briant K.C., Kim Y.-C., Schreiber G., Pitterle D.M.
      Genomics 55:164-175(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "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].
      Tissue: Lymph.
    5. "Human R1 subunit of ribonucleotide reductase (RRM1): 5' flanking region of the gene."
      Parker N.J., Begley C.G., Fox R.M.
      Genomics 19:91-96(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
      Tissue: Placenta.
    6. "Human ribonucleotide reductase. Activation and inhibition by analogs of ATP."
      Harrington J.A., Spector T.
      Biochem. Pharmacol. 42:759-763(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    7. "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: INTERACTION WITH RRM2B.
    8. "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, ENZYME REGULATION.
    9. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-17 AND LYS-376, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization."
      Fairman J.W., Wijerathna S.R., Ahmad M.F., Xu H., Nakano R., Jha S., Prendergast J., Welin R.M., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis C.G.
      Nat. Struct. Mol. Biol. 18:316-322(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 75-742 IN COMPLEX WITH ALLOSTERIC EFFECTOR ATP AND MAGNESIUM IONS.

    Entry informationi

    Entry nameiRIR1_HUMAN
    AccessioniPrimary (citable) accession number: P23921
    Secondary accession number(s): Q9UNN2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: March 1, 1992
    Last modified: October 1, 2014
    This is version 153 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.
    The level of the enzyme activity is closely correlated with the growth rate of a cell and appears to vary with the cell cycle.

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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