Full text data of RRM1
RRM1
(RR1)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Ribonucleoside-diphosphate reductase large subunit; 1.17.4.1 (Ribonucleoside-diphosphate reductase subunit M1; Ribonucleotide reductase large subunit)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ribonucleoside-diphosphate reductase large subunit; 1.17.4.1 (Ribonucleoside-diphosphate reductase subunit M1; Ribonucleotide reductase large subunit)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00013871
IPI00013871 Ribonucleoside-diphosphate reductase large subunit Provides the precursors necessary for DNA synthesis, under complex allosterical control, 2-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00013871 Ribonucleoside-diphosphate reductase large subunit Provides the precursors necessary for DNA synthesis, under complex allosterical control, 2-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
P23921
ID RIR1_HUMAN Reviewed; 792 AA.
AC P23921; Q9UNN2;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-1992, sequence version 1.
DT 22-JAN-2014, entry version 145.
DE RecName: Full=Ribonucleoside-diphosphate reductase large subunit;
DE EC=1.17.4.1;
DE AltName: Full=Ribonucleoside-diphosphate reductase subunit M1;
DE AltName: Full=Ribonucleotide reductase large subunit;
GN Name=RRM1; Synonyms=RR1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Bone marrow;
RX PubMed=1840662; DOI=10.1093/nar/19.13.3741;
RA Parker N.J., Begley C.G., Fox R.M.;
RT "Human M1 subunit of ribonucleotide reductase: cDNA sequence and
RT expression in stimulated lymphocytes.";
RL Nucleic Acids Res. 19:3741-3741(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mammary carcinoma;
RX PubMed=1627826;
RA Pavloff N., Rivard D., Masson S., Shen S.-H., Mes-Masson A.-M.;
RT "Sequence analysis of the large and small subunits of human
RT ribonucleotide reductase.";
RL DNA Seq. 2:227-234(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9933563; DOI=10.1006/geno.1998.5659;
RA Bepler G., O'Briant K.C., Kim Y.-C., Schreiber G., Pitterle D.M.;
RT "A 1.4-Mb high-resolution physical map and contig of chromosome
RT segment 11p15.5 and genes in the LOH11A metastasis suppressor
RT region.";
RL Genomics 55:164-175(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
RC TISSUE=Placenta;
RX PubMed=8188248; DOI=10.1006/geno.1994.1017;
RA Parker N.J., Begley C.G., Fox R.M.;
RT "Human R1 subunit of ribonucleotide reductase (RRM1): 5' flanking
RT region of the gene.";
RL Genomics 19:91-96(1994).
RN [6]
RP ENZYME REGULATION.
RX PubMed=1867633; DOI=10.1016/0006-2952(91)90033-2;
RA Harrington J.A., Spector T.;
RT "Human ribonucleotide reductase. Activation and inhibition by analogs
RT of ATP.";
RL Biochem. Pharmacol. 42:759-763(1991).
RN [7]
RP INTERACTION WITH RRM2B.
RX PubMed=12615712;
RA Xue L., Zhou B., Liu X., Qiu W., Jin Z., Yen Y.;
RT "Wild-type p53 regulates human ribonucleotide reductase by protein-
RT protein interaction with p53R2 as well as hRRM2 subunits.";
RL Cancer Res. 63:980-986(2003).
RN [8]
RP CATALYTIC ACTIVITY, SUBUNIT, AND ENZYME REGULATION.
RX PubMed=16376858; DOI=10.1016/j.bbrc.2005.12.019;
RA Qiu W., Zhou B., Darwish D., Shao J., Yen Y.;
RT "Characterization of enzymatic properties of human ribonucleotide
RT reductase holoenzyme reconstituted in vitro from hRRM1, hRRM2, and
RT p53R2 subunits.";
RL Biochem. Biophys. Res. Commun. 340:428-434(2006).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-17 AND LYS-376, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 75-742 IN COMPLEX WITH
RP ALLOSTERIC EFFECTOR ATP AND MAGNESIUM IONS.
RX PubMed=21336276; DOI=10.1038/nsmb.2007;
RA Fairman J.W., Wijerathna S.R., Ahmad M.F., Xu H., Nakano R., Jha S.,
RA Prendergast J., Welin R.M., Flodin S., Roos A., Nordlund P., Li Z.,
RA Walz T., Dealwis C.G.;
RT "Structural basis for allosteric regulation of human ribonucleotide
RT reductase by nucleotide-induced oligomerization.";
RL Nat. Struct. Mol. Biol. 18:316-322(2011).
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides.
CC -!- CATALYTIC ACTIVITY: 2'-deoxyribonucleoside diphosphate +
CC thioredoxin disulfide + H(2)O = ribonucleoside diphosphate +
CC thioredoxin.
CC -!- ENZYME REGULATION: Under complex allosteric control mediated by
CC deoxynucleoside triphosphates and ATP binding to separate
CC specificity and activation sites on the M1 subunit. The type of
CC nucleotide bound at the specificity site determines substrate
CC preference. It seems probable that ATP makes the enzyme reduce CDP
CC and UDP, dGTP favors ADP reduction and dTTP favors GDP reduction.
CC Stimulated by ATP and inhibited by dATP binding to the activity
CC site.
CC -!- PATHWAY: Genetic information processing; DNA replication.
CC -!- SUBUNIT: Heterodimer of a large and a small subunit. Heterodimer
CC with small subunit RRM2 or RRM2B. The heterodimer with RRM2 has
CC higher catalytic activity than the heterodimer with RRM2B.
CC -!- INTERACTION:
CC P31350:RRM2; NbExp=3; IntAct=EBI-717006, EBI-2339245;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: Two distinct regulatory sites have been defined:
CC the specificity site, which controls substrate specificity, and
CC the activity site which regulates overall catalytic activity. A
CC substrate-binding catalytic site, located on M1, is formed only in
CC the presence of the second subunit M2.
CC -!- MISCELLANEOUS: The level of the enzyme activity is closely
CC correlated with the growth rate of a cell and appears to vary with
CC the cell cycle.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase
CC large chain family.
CC -!- SIMILARITY: Contains 1 ATP-cone domain.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Ribonucleotide reductase entry;
CC URL="http://en.wikipedia.org/wiki/Ribonucleotide_reductase";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RRM1ID42174ch11p15.html";
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DR EMBL; X59543; CAA42118.1; -; mRNA.
DR EMBL; X59617; CAA42180.1; -; mRNA.
DR EMBL; AF107045; AAD37491.1; -; Genomic_DNA.
DR EMBL; BC006498; AAH06498.1; -; mRNA.
DR EMBL; L10342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S16680; S16680.
DR RefSeq; NP_001024.1; NM_001033.3.
DR UniGene; Hs.445705; -.
DR PDB; 2WGH; X-ray; 2.30 A; A/B=75-742.
DR PDB; 3HNC; X-ray; 2.41 A; A/B=1-792.
DR PDB; 3HND; X-ray; 3.21 A; A/B=1-792.
DR PDB; 3HNE; X-ray; 3.11 A; A/B=1-792.
DR PDB; 3HNF; X-ray; 3.16 A; A/B=1-792.
DR PDBsum; 2WGH; -.
DR PDBsum; 3HNC; -.
DR PDBsum; 3HND; -.
DR PDBsum; 3HNE; -.
DR PDBsum; 3HNF; -.
DR ProteinModelPortal; P23921; -.
DR SMR; P23921; 14-742.
DR DIP; DIP-24233N; -.
DR IntAct; P23921; 4.
DR MINT; MINT-1406473; -.
DR STRING; 9606.ENSP00000300738; -.
DR BindingDB; P23921; -.
DR ChEMBL; CHEMBL2095215; -.
DR DrugBank; DB00631; Clofarabine.
DR DrugBank; DB01073; Fludarabine.
DR DrugBank; DB00441; Gemcitabine.
DR DrugBank; DB01005; Hydroxyurea.
DR PhosphoSite; P23921; -.
DR DMDM; 132608; -.
DR PaxDb; P23921; -.
DR PeptideAtlas; P23921; -.
DR PRIDE; P23921; -.
DR DNASU; 6240; -.
DR Ensembl; ENST00000300738; ENSP00000300738; ENSG00000167325.
DR GeneID; 6240; -.
DR KEGG; hsa:6240; -.
DR UCSC; uc001lyw.4; human.
DR CTD; 6240; -.
DR GeneCards; GC11P004115; -.
DR HGNC; HGNC:10451; RRM1.
DR HPA; CAB022093; -.
DR MIM; 180410; gene.
DR neXtProt; NX_P23921; -.
DR PharmGKB; PA298; -.
DR eggNOG; COG0209; -.
DR HOGENOM; HOG000057035; -.
DR HOVERGEN; HBG003447; -.
DR InParanoid; P23921; -.
DR KO; K10807; -.
DR OMA; KSHIQFY; -.
DR OrthoDB; EOG7BGHK2; -.
DR PhylomeDB; P23921; -.
DR BioCyc; MetaCyc:HS09541-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00326; -.
DR ChiTaRS; RRM1; human.
DR EvolutionaryTrace; P23921; -.
DR GeneWiki; RRM1; -.
DR GenomeRNAi; 6240; -.
DR NextBio; 24233; -.
DR PRO; PR:P23921; -.
DR ArrayExpress; P23921; -.
DR Bgee; P23921; -.
DR CleanEx; HS_RRM1; -.
DR Genevestigator; P23921; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; NAS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; ISS:UniProtKB.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006260; P:DNA replication; NAS:UniProtKB.
DR GO; GO:0015949; P:nucleobase-containing small molecule interconversion; TAS:Reactome.
DR GO; GO:0051290; P:protein heterotetramerization; IEA:Ensembl.
DR InterPro; IPR005144; ATP-cone.
DR InterPro; IPR013346; NrdE_NrdA.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR Pfam; PF03477; ATP-cone; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF48168; SSF48168; 1.
DR TIGRFAMs; TIGR02506; NrdE_NrdA; 1.
DR PROSITE; PS51161; ATP_CONE; 1.
DR PROSITE; PS00089; RIBORED_LARGE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Allosteric enzyme; ATP-binding;
KW Complete proteome; Cytoplasm; Disulfide bond; DNA replication;
KW Nucleotide-binding; Oxidoreductase; Polymorphism; Reference proteome.
FT CHAIN 1 792 Ribonucleoside-diphosphate reductase
FT large subunit.
FT /FTId=PRO_0000187190.
FT DOMAIN 1 92 ATP-cone.
FT REGION 11 17 Allosteric activator binding (By
FT similarity).
FT REGION 217 218 Substrate binding (By similarity).
FT REGION 285 288 Allosteric effector binding, determines
FT substrate specificity.
FT REGION 427 431 Substrate binding (By similarity).
FT REGION 603 607 Substrate binding (By similarity).
FT ACT_SITE 427 427 Proton acceptor (By similarity).
FT ACT_SITE 429 429 Cysteine radical intermediate (By
FT similarity).
FT ACT_SITE 431 431 Proton acceptor (By similarity).
FT BINDING 5 5 Allosteric activator (By similarity).
FT BINDING 53 53 Allosteric activator (By similarity).
FT BINDING 88 88 Allosteric activator (By similarity).
FT BINDING 202 202 Substrate (By similarity).
FT BINDING 247 247 Substrate; via amide nitrogen (By
FT similarity).
FT SITE 218 218 Important for hydrogen atom transfer (By
FT similarity).
FT SITE 226 226 Allosteric effector binding, determines
FT substrate specificity.
FT SITE 256 256 Allosteric effector binding, determines
FT substrate specificity.
FT SITE 444 444 Important for hydrogen atom transfer (By
FT similarity).
FT SITE 737 737 Important for electron transfer (By
FT similarity).
FT SITE 738 738 Important for electron transfer (By
FT similarity).
FT SITE 787 787 Interacts with thioredoxin/glutaredoxin
FT (By similarity).
FT SITE 790 790 Interacts with thioredoxin/glutaredoxin
FT (By similarity).
FT MOD_RES 17 17 N6-acetyllysine.
FT MOD_RES 376 376 N6-acetyllysine.
FT DISULFID 218 444 Redox-active (By similarity).
FT VARIANT 590 590 K -> Q (in dbSNP:rs2228123).
FT /FTId=VAR_052052.
FT VARIANT 778 778 V -> A (in dbSNP:rs2229196).
FT /FTId=VAR_052053.
FT CONFLICT 6 6 R -> Q (in Ref. 3; AAD37491).
FT HELIX 15 23
FT TURN 31 33
FT HELIX 36 44
FT STRAND 48 50
FT HELIX 53 66
FT HELIX 67 69
FT HELIX 78 88
FT HELIX 94 103
FT TURN 107 109
FT HELIX 118 126
FT HELIX 128 133
FT HELIX 137 142
FT HELIX 145 154
FT STRAND 158 163
FT HELIX 167 179
FT HELIX 183 195
FT STRAND 197 200
FT HELIX 202 207
FT STRAND 210 212
FT STRAND 218 222
FT HELIX 228 243
FT STRAND 247 251
FT STRAND 258 261
FT HELIX 263 265
FT STRAND 268 270
FT HELIX 272 285
FT STRAND 287 293
FT STRAND 297 301
FT HELIX 308 311
FT TURN 312 315
FT STRAND 317 319
FT HELIX 321 323
FT STRAND 328 334
FT HELIX 336 343
FT STRAND 347 351
FT TURN 353 355
FT HELIX 359 361
FT HELIX 365 376
FT STRAND 381 385
FT HELIX 386 400
FT STRAND 404 407
FT HELIX 408 413
FT HELIX 418 420
FT STRAND 428 430
FT STRAND 442 444
FT STRAND 446 450
FT HELIX 451 454
FT STRAND 459 461
FT HELIX 463 483
FT HELIX 489 498
FT STRAND 502 506
FT HELIX 508 514
FT STRAND 519 521
FT HELIX 522 550
FT HELIX 554 556
FT HELIX 561 563
FT HELIX 567 570
FT STRAND 577 579
FT HELIX 581 591
FT HELIX 607 611
FT STRAND 623 629
FT STRAND 632 637
FT HELIX 639 648
FT HELIX 653 661
FT TURN 662 664
FT STRAND 670 672
FT HELIX 674 679
FT TURN 683 685
FT HELIX 688 699
FT HELIX 717 729
FT STRAND 733 737
SQ SEQUENCE 792 AA; 90070 MW; 4470A76C61E8F86A CRC64;
MHVIKRDGRQ ERVMFDKITS RIQKLCYGLN MDFVDPAQIT MKVIQGLYSG VTTVELDTLA
AETAATLTTK HPDYAILAAR IAVSNLHKET KKVFSDVMED LYNYINPHNG KHSPMVAKST
LDIVLANKDR LNSAIIYDRD FSYNYFGFKT LERSYLLKIN GKVAERPQHM LMRVSVGIHK
EDIDAAIETY NLLSERWFTH ASPTLFNAGT NRPQLSSCFL LSMKDDSIEG IYDTLKQCAL
ISKSAGGIGV AVSCIRATGS YIAGTNGNSN GLVPMLRVYN NTARYVDQGG NKRPGAFAIY
LEPWHLDIFE FLDLKKNTGK EEQRARDLFF ALWIPDLFMK RVETNQDWSL MCPNECPGLD
EVWGEEFEKL YASYEKQGRV RKVVKAQQLW YAIIESQTET GTPYMLYKDS CNRKSNQQNL
GTIKCSNLCT EIVEYTSKDE VAVCNLASLA LNMYVTSEHT YDFKKLAEVT KVVVRNLNKI
IDINYYPVPE ACLSNKRHRP IGIGVQGLAD AFILMRYPFE SAEAQLLNKQ IFETIYYGAL
EASCDLAKEQ GPYETYEGSP VSKGILQYDM WNVTPTDLWD WKVLKEKIAK YGIRNSLLIA
PMPTASTAQI LGNNESIEPY TSNIYTRRVL SGEFQIVNPH LLKDLTERGL WHEEMKNQII
ACNGSIQSIP EIPDDLKQLY KTVWEISQKT VLKMAAERGA FIDQSQSLNI HIAEPNYGKL
TSMHFYGWKQ GLKTGMYYLR TRPAANPIQF TLNKEKLKDK EKVSKEEEEK ERNTAAMVCS
LENRDECLMC GS
//
ID RIR1_HUMAN Reviewed; 792 AA.
AC P23921; Q9UNN2;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-1992, sequence version 1.
DT 22-JAN-2014, entry version 145.
DE RecName: Full=Ribonucleoside-diphosphate reductase large subunit;
DE EC=1.17.4.1;
DE AltName: Full=Ribonucleoside-diphosphate reductase subunit M1;
DE AltName: Full=Ribonucleotide reductase large subunit;
GN Name=RRM1; Synonyms=RR1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Bone marrow;
RX PubMed=1840662; DOI=10.1093/nar/19.13.3741;
RA Parker N.J., Begley C.G., Fox R.M.;
RT "Human M1 subunit of ribonucleotide reductase: cDNA sequence and
RT expression in stimulated lymphocytes.";
RL Nucleic Acids Res. 19:3741-3741(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mammary carcinoma;
RX PubMed=1627826;
RA Pavloff N., Rivard D., Masson S., Shen S.-H., Mes-Masson A.-M.;
RT "Sequence analysis of the large and small subunits of human
RT ribonucleotide reductase.";
RL DNA Seq. 2:227-234(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9933563; DOI=10.1006/geno.1998.5659;
RA Bepler G., O'Briant K.C., Kim Y.-C., Schreiber G., Pitterle D.M.;
RT "A 1.4-Mb high-resolution physical map and contig of chromosome
RT segment 11p15.5 and genes in the LOH11A metastasis suppressor
RT region.";
RL Genomics 55:164-175(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
RC TISSUE=Placenta;
RX PubMed=8188248; DOI=10.1006/geno.1994.1017;
RA Parker N.J., Begley C.G., Fox R.M.;
RT "Human R1 subunit of ribonucleotide reductase (RRM1): 5' flanking
RT region of the gene.";
RL Genomics 19:91-96(1994).
RN [6]
RP ENZYME REGULATION.
RX PubMed=1867633; DOI=10.1016/0006-2952(91)90033-2;
RA Harrington J.A., Spector T.;
RT "Human ribonucleotide reductase. Activation and inhibition by analogs
RT of ATP.";
RL Biochem. Pharmacol. 42:759-763(1991).
RN [7]
RP INTERACTION WITH RRM2B.
RX PubMed=12615712;
RA Xue L., Zhou B., Liu X., Qiu W., Jin Z., Yen Y.;
RT "Wild-type p53 regulates human ribonucleotide reductase by protein-
RT protein interaction with p53R2 as well as hRRM2 subunits.";
RL Cancer Res. 63:980-986(2003).
RN [8]
RP CATALYTIC ACTIVITY, SUBUNIT, AND ENZYME REGULATION.
RX PubMed=16376858; DOI=10.1016/j.bbrc.2005.12.019;
RA Qiu W., Zhou B., Darwish D., Shao J., Yen Y.;
RT "Characterization of enzymatic properties of human ribonucleotide
RT reductase holoenzyme reconstituted in vitro from hRRM1, hRRM2, and
RT p53R2 subunits.";
RL Biochem. Biophys. Res. Commun. 340:428-434(2006).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-17 AND LYS-376, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 75-742 IN COMPLEX WITH
RP ALLOSTERIC EFFECTOR ATP AND MAGNESIUM IONS.
RX PubMed=21336276; DOI=10.1038/nsmb.2007;
RA Fairman J.W., Wijerathna S.R., Ahmad M.F., Xu H., Nakano R., Jha S.,
RA Prendergast J., Welin R.M., Flodin S., Roos A., Nordlund P., Li Z.,
RA Walz T., Dealwis C.G.;
RT "Structural basis for allosteric regulation of human ribonucleotide
RT reductase by nucleotide-induced oligomerization.";
RL Nat. Struct. Mol. Biol. 18:316-322(2011).
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides.
CC -!- CATALYTIC ACTIVITY: 2'-deoxyribonucleoside diphosphate +
CC thioredoxin disulfide + H(2)O = ribonucleoside diphosphate +
CC thioredoxin.
CC -!- ENZYME REGULATION: Under complex allosteric control mediated by
CC deoxynucleoside triphosphates and ATP binding to separate
CC specificity and activation sites on the M1 subunit. The type of
CC nucleotide bound at the specificity site determines substrate
CC preference. It seems probable that ATP makes the enzyme reduce CDP
CC and UDP, dGTP favors ADP reduction and dTTP favors GDP reduction.
CC Stimulated by ATP and inhibited by dATP binding to the activity
CC site.
CC -!- PATHWAY: Genetic information processing; DNA replication.
CC -!- SUBUNIT: Heterodimer of a large and a small subunit. Heterodimer
CC with small subunit RRM2 or RRM2B. The heterodimer with RRM2 has
CC higher catalytic activity than the heterodimer with RRM2B.
CC -!- INTERACTION:
CC P31350:RRM2; NbExp=3; IntAct=EBI-717006, EBI-2339245;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: Two distinct regulatory sites have been defined:
CC the specificity site, which controls substrate specificity, and
CC the activity site which regulates overall catalytic activity. A
CC substrate-binding catalytic site, located on M1, is formed only in
CC the presence of the second subunit M2.
CC -!- MISCELLANEOUS: The level of the enzyme activity is closely
CC correlated with the growth rate of a cell and appears to vary with
CC the cell cycle.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase
CC large chain family.
CC -!- SIMILARITY: Contains 1 ATP-cone domain.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Ribonucleotide reductase entry;
CC URL="http://en.wikipedia.org/wiki/Ribonucleotide_reductase";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RRM1ID42174ch11p15.html";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
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DR EMBL; X59543; CAA42118.1; -; mRNA.
DR EMBL; X59617; CAA42180.1; -; mRNA.
DR EMBL; AF107045; AAD37491.1; -; Genomic_DNA.
DR EMBL; BC006498; AAH06498.1; -; mRNA.
DR EMBL; L10342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S16680; S16680.
DR RefSeq; NP_001024.1; NM_001033.3.
DR UniGene; Hs.445705; -.
DR PDB; 2WGH; X-ray; 2.30 A; A/B=75-742.
DR PDB; 3HNC; X-ray; 2.41 A; A/B=1-792.
DR PDB; 3HND; X-ray; 3.21 A; A/B=1-792.
DR PDB; 3HNE; X-ray; 3.11 A; A/B=1-792.
DR PDB; 3HNF; X-ray; 3.16 A; A/B=1-792.
DR PDBsum; 2WGH; -.
DR PDBsum; 3HNC; -.
DR PDBsum; 3HND; -.
DR PDBsum; 3HNE; -.
DR PDBsum; 3HNF; -.
DR ProteinModelPortal; P23921; -.
DR SMR; P23921; 14-742.
DR DIP; DIP-24233N; -.
DR IntAct; P23921; 4.
DR MINT; MINT-1406473; -.
DR STRING; 9606.ENSP00000300738; -.
DR BindingDB; P23921; -.
DR ChEMBL; CHEMBL2095215; -.
DR DrugBank; DB00631; Clofarabine.
DR DrugBank; DB01073; Fludarabine.
DR DrugBank; DB00441; Gemcitabine.
DR DrugBank; DB01005; Hydroxyurea.
DR PhosphoSite; P23921; -.
DR DMDM; 132608; -.
DR PaxDb; P23921; -.
DR PeptideAtlas; P23921; -.
DR PRIDE; P23921; -.
DR DNASU; 6240; -.
DR Ensembl; ENST00000300738; ENSP00000300738; ENSG00000167325.
DR GeneID; 6240; -.
DR KEGG; hsa:6240; -.
DR UCSC; uc001lyw.4; human.
DR CTD; 6240; -.
DR GeneCards; GC11P004115; -.
DR HGNC; HGNC:10451; RRM1.
DR HPA; CAB022093; -.
DR MIM; 180410; gene.
DR neXtProt; NX_P23921; -.
DR PharmGKB; PA298; -.
DR eggNOG; COG0209; -.
DR HOGENOM; HOG000057035; -.
DR HOVERGEN; HBG003447; -.
DR InParanoid; P23921; -.
DR KO; K10807; -.
DR OMA; KSHIQFY; -.
DR OrthoDB; EOG7BGHK2; -.
DR PhylomeDB; P23921; -.
DR BioCyc; MetaCyc:HS09541-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00326; -.
DR ChiTaRS; RRM1; human.
DR EvolutionaryTrace; P23921; -.
DR GeneWiki; RRM1; -.
DR GenomeRNAi; 6240; -.
DR NextBio; 24233; -.
DR PRO; PR:P23921; -.
DR ArrayExpress; P23921; -.
DR Bgee; P23921; -.
DR CleanEx; HS_RRM1; -.
DR Genevestigator; P23921; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; NAS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; ISS:UniProtKB.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006260; P:DNA replication; NAS:UniProtKB.
DR GO; GO:0015949; P:nucleobase-containing small molecule interconversion; TAS:Reactome.
DR GO; GO:0051290; P:protein heterotetramerization; IEA:Ensembl.
DR InterPro; IPR005144; ATP-cone.
DR InterPro; IPR013346; NrdE_NrdA.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR Pfam; PF03477; ATP-cone; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF48168; SSF48168; 1.
DR TIGRFAMs; TIGR02506; NrdE_NrdA; 1.
DR PROSITE; PS51161; ATP_CONE; 1.
DR PROSITE; PS00089; RIBORED_LARGE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Allosteric enzyme; ATP-binding;
KW Complete proteome; Cytoplasm; Disulfide bond; DNA replication;
KW Nucleotide-binding; Oxidoreductase; Polymorphism; Reference proteome.
FT CHAIN 1 792 Ribonucleoside-diphosphate reductase
FT large subunit.
FT /FTId=PRO_0000187190.
FT DOMAIN 1 92 ATP-cone.
FT REGION 11 17 Allosteric activator binding (By
FT similarity).
FT REGION 217 218 Substrate binding (By similarity).
FT REGION 285 288 Allosteric effector binding, determines
FT substrate specificity.
FT REGION 427 431 Substrate binding (By similarity).
FT REGION 603 607 Substrate binding (By similarity).
FT ACT_SITE 427 427 Proton acceptor (By similarity).
FT ACT_SITE 429 429 Cysteine radical intermediate (By
FT similarity).
FT ACT_SITE 431 431 Proton acceptor (By similarity).
FT BINDING 5 5 Allosteric activator (By similarity).
FT BINDING 53 53 Allosteric activator (By similarity).
FT BINDING 88 88 Allosteric activator (By similarity).
FT BINDING 202 202 Substrate (By similarity).
FT BINDING 247 247 Substrate; via amide nitrogen (By
FT similarity).
FT SITE 218 218 Important for hydrogen atom transfer (By
FT similarity).
FT SITE 226 226 Allosteric effector binding, determines
FT substrate specificity.
FT SITE 256 256 Allosteric effector binding, determines
FT substrate specificity.
FT SITE 444 444 Important for hydrogen atom transfer (By
FT similarity).
FT SITE 737 737 Important for electron transfer (By
FT similarity).
FT SITE 738 738 Important for electron transfer (By
FT similarity).
FT SITE 787 787 Interacts with thioredoxin/glutaredoxin
FT (By similarity).
FT SITE 790 790 Interacts with thioredoxin/glutaredoxin
FT (By similarity).
FT MOD_RES 17 17 N6-acetyllysine.
FT MOD_RES 376 376 N6-acetyllysine.
FT DISULFID 218 444 Redox-active (By similarity).
FT VARIANT 590 590 K -> Q (in dbSNP:rs2228123).
FT /FTId=VAR_052052.
FT VARIANT 778 778 V -> A (in dbSNP:rs2229196).
FT /FTId=VAR_052053.
FT CONFLICT 6 6 R -> Q (in Ref. 3; AAD37491).
FT HELIX 15 23
FT TURN 31 33
FT HELIX 36 44
FT STRAND 48 50
FT HELIX 53 66
FT HELIX 67 69
FT HELIX 78 88
FT HELIX 94 103
FT TURN 107 109
FT HELIX 118 126
FT HELIX 128 133
FT HELIX 137 142
FT HELIX 145 154
FT STRAND 158 163
FT HELIX 167 179
FT HELIX 183 195
FT STRAND 197 200
FT HELIX 202 207
FT STRAND 210 212
FT STRAND 218 222
FT HELIX 228 243
FT STRAND 247 251
FT STRAND 258 261
FT HELIX 263 265
FT STRAND 268 270
FT HELIX 272 285
FT STRAND 287 293
FT STRAND 297 301
FT HELIX 308 311
FT TURN 312 315
FT STRAND 317 319
FT HELIX 321 323
FT STRAND 328 334
FT HELIX 336 343
FT STRAND 347 351
FT TURN 353 355
FT HELIX 359 361
FT HELIX 365 376
FT STRAND 381 385
FT HELIX 386 400
FT STRAND 404 407
FT HELIX 408 413
FT HELIX 418 420
FT STRAND 428 430
FT STRAND 442 444
FT STRAND 446 450
FT HELIX 451 454
FT STRAND 459 461
FT HELIX 463 483
FT HELIX 489 498
FT STRAND 502 506
FT HELIX 508 514
FT STRAND 519 521
FT HELIX 522 550
FT HELIX 554 556
FT HELIX 561 563
FT HELIX 567 570
FT STRAND 577 579
FT HELIX 581 591
FT HELIX 607 611
FT STRAND 623 629
FT STRAND 632 637
FT HELIX 639 648
FT HELIX 653 661
FT TURN 662 664
FT STRAND 670 672
FT HELIX 674 679
FT TURN 683 685
FT HELIX 688 699
FT HELIX 717 729
FT STRAND 733 737
SQ SEQUENCE 792 AA; 90070 MW; 4470A76C61E8F86A CRC64;
MHVIKRDGRQ ERVMFDKITS RIQKLCYGLN MDFVDPAQIT MKVIQGLYSG VTTVELDTLA
AETAATLTTK HPDYAILAAR IAVSNLHKET KKVFSDVMED LYNYINPHNG KHSPMVAKST
LDIVLANKDR LNSAIIYDRD FSYNYFGFKT LERSYLLKIN GKVAERPQHM LMRVSVGIHK
EDIDAAIETY NLLSERWFTH ASPTLFNAGT NRPQLSSCFL LSMKDDSIEG IYDTLKQCAL
ISKSAGGIGV AVSCIRATGS YIAGTNGNSN GLVPMLRVYN NTARYVDQGG NKRPGAFAIY
LEPWHLDIFE FLDLKKNTGK EEQRARDLFF ALWIPDLFMK RVETNQDWSL MCPNECPGLD
EVWGEEFEKL YASYEKQGRV RKVVKAQQLW YAIIESQTET GTPYMLYKDS CNRKSNQQNL
GTIKCSNLCT EIVEYTSKDE VAVCNLASLA LNMYVTSEHT YDFKKLAEVT KVVVRNLNKI
IDINYYPVPE ACLSNKRHRP IGIGVQGLAD AFILMRYPFE SAEAQLLNKQ IFETIYYGAL
EASCDLAKEQ GPYETYEGSP VSKGILQYDM WNVTPTDLWD WKVLKEKIAK YGIRNSLLIA
PMPTASTAQI LGNNESIEPY TSNIYTRRVL SGEFQIVNPH LLKDLTERGL WHEEMKNQII
ACNGSIQSIP EIPDDLKQLY KTVWEISQKT VLKMAAERGA FIDQSQSLNI HIAEPNYGKL
TSMHFYGWKQ GLKTGMYYLR TRPAANPIQF TLNKEKLKDK EKVSKEEEEK ERNTAAMVCS
LENRDECLMC GS
//
MIM
180410
*RECORD*
*FIELD* NO
180410
*FIELD* TI
*180410 RIBONUCLEOTIDE REDUCTASE, M1 SUBUNIT; RRM1
;;RIBONUCLEOTIDE REDUCTASE, LARGE SUBUNIT;;
read moreRIBONUCLEOTIDE REDUCTASE, R1 SUBUNIT; R1
*FIELD* TX
DESCRIPTION
The RRM1 gene encodes the large subunit (R1) of ribonucleotide
reductase, the heterodimeric enzyme that catalyzes the rate-limiting
step in deoxyribonucleotide synthesis.
CLONING
Pavloff et al. (1992) cloned human RRM1 and RRM2 (180390) cDNAs from a
breast carcinoma cDNA library. The deduced 792-amino acid RRM1 protein
has a molecular mass of 90 kD and shares about 98% sequence homology
with the mouse Rrm1 protein.
MAPPING
By immunoblotting of somatic cell hybrid extracts, Engstrom and Francke
(1985) mapped the gene for the R1 subunit of ribonucleotide reductase to
11pter-p11. This assignment was confirmed by Southern analysis of hybrid
cell DNAs, and the RRM1 locus was sublocalized to the distal band 11p15
by in situ hybridization (Brissenden et al., 1988).
Byrne and Smith (1991) identified a RFLP at the RRM1 locus, which is
useful in the mapping of 11p.
GENE STRUCTURE
Parker et al. (1994) used a fragment of human RRM1 cDNA to isolate a
genomic clone that encompassed the 5-prime flanking region of RRM1.
Primer extension and PCR experiments defined 6 potential cap sites.
Parker et al. (1995) characterized the TATA-less promoter region of the
human RRM1 gene and found 2 domains that were conserved with respect to
the mouse sequence. One of these sequences was shown to bind the
transcription factor SP1 (189906).
Pitterle et al. (1999) demonstrated that the RRM1 gene contains 19
exons, spans over 45 kb, and is oriented from telomere to centromere
with exon 19 nearest to D11S12.
GENE FUNCTION
In dividing cells, ribonucleotide reductase is essential for the
production of deoxyribonucleotides before DNA synthesis in S phase.
Neither of its 2 subunits, R1 or R2 (180390), are detectable in
quiescent cells. In cycling cells, RRM1 mRNA and protein are present
throughout the cell cycle (summary by Parker et al., 1994).
Byrne and Smith (1993) found that the RRM1 gene, which is located at
11p15.5, is not imprinted in Wilms tumor or in hepatoblastoma. They
demonstrated transcription of both alleles in 6 Wilms tumors, 1
hepatoblastoma, and samples from adjacent kidney and liver from
individuals who were constitutionally heterozygous for a TaqI
polymorphism.
Because the RRM1 gene is located in a region of loss of heterozygosity
(LOH) in lung tumors, Pitterle et al. (1999) screened all 19 RRM1 exons
in 12 pairs of normal and tumor DNA samples and identified no mutations.
*FIELD* RF
1. Brissenden, J. E.; Caras, I.; Thelander, L.; Francke, U.: The
structural gene for the M1 subunit of human ribonucleotide reductase
maps to chromosome 11, band p15, in human and to chromosome 7 in mouse. Exp.
Cell Res. 174: 302-308, 1988.
2. Byrne, J.; Smith, P.: Human polymorphic probe pE1.8 detects SacI
polymorphism in the ribonucleotide reductase M1 subunit gene. Hum.
Genet. 87: 376 only, 1991.
3. Byrne, J. A.; Smith, P. J.: The 11p15.5 ribonucleotide reductase
M1 subunit locus is not imprinted in Wilms' tumour and hepatoblastoma. Hum.
Genet. 91: 275-277, 1993.
4. Engstrom, Y.; Francke, U.: Assignment of the structural gene for
subunit M1 of human ribonucleotide reductase to the short arm of chromosome
11. Exp. Cell Res. 158: 477-483, 1985.
5. Parker, N. J.; Begley, C. G.; Fox, R. M.: Human R1 subunit of
ribonucleotide reductase (RRM1): 5-prime flanking region of the gene. Genomics 19:
91-96, 1994.
6. Parker, N. J.; Begley, C. G.; Fox, R. M.: Human gene for the large
subunit of ribonucleotide reductase (RRM1): functional analysis of
the promoter. Genomics 27: 280-285, 1995.
7. Pavloff, N.; Rivard, D.; Masson, S.; Shen, S.-H.; Mes-Masson, A.-M.
: Sequence analysis of the large and small subunits of human ribonucleotide
reductase. DNA Seq. 2: 227-234, 1992.
8. Pitterle, D. M.; Kim, Y.-C.; Jolicoeur, E. M. C.; Cao, Y.; O'Briant,
K. C.; Bepler, G.: Lung cancer and the human gene for ribonucleotide
reductase subunit M1 (RRM1). Mammalian Genome 10: 916-922, 1999.
*FIELD* CN
Carol A. Bocchini - updated: 6/9/2008
Alan F. Scott - updated: 9/17/1995
*FIELD* CD
Victor A. McKusick: 6/2/1986
*FIELD* ED
carol: 03/16/2012
carol: 7/8/2008
carol: 6/9/2008
alopez: 3/22/2000
carol: 6/18/1998
joanna: 5/8/1998
mark: 9/17/1995
carol: 2/7/1994
carol: 6/25/1993
carol: 7/24/1992
supermim: 3/16/1992
carol: 9/24/1991
*RECORD*
*FIELD* NO
180410
*FIELD* TI
*180410 RIBONUCLEOTIDE REDUCTASE, M1 SUBUNIT; RRM1
;;RIBONUCLEOTIDE REDUCTASE, LARGE SUBUNIT;;
read moreRIBONUCLEOTIDE REDUCTASE, R1 SUBUNIT; R1
*FIELD* TX
DESCRIPTION
The RRM1 gene encodes the large subunit (R1) of ribonucleotide
reductase, the heterodimeric enzyme that catalyzes the rate-limiting
step in deoxyribonucleotide synthesis.
CLONING
Pavloff et al. (1992) cloned human RRM1 and RRM2 (180390) cDNAs from a
breast carcinoma cDNA library. The deduced 792-amino acid RRM1 protein
has a molecular mass of 90 kD and shares about 98% sequence homology
with the mouse Rrm1 protein.
MAPPING
By immunoblotting of somatic cell hybrid extracts, Engstrom and Francke
(1985) mapped the gene for the R1 subunit of ribonucleotide reductase to
11pter-p11. This assignment was confirmed by Southern analysis of hybrid
cell DNAs, and the RRM1 locus was sublocalized to the distal band 11p15
by in situ hybridization (Brissenden et al., 1988).
Byrne and Smith (1991) identified a RFLP at the RRM1 locus, which is
useful in the mapping of 11p.
GENE STRUCTURE
Parker et al. (1994) used a fragment of human RRM1 cDNA to isolate a
genomic clone that encompassed the 5-prime flanking region of RRM1.
Primer extension and PCR experiments defined 6 potential cap sites.
Parker et al. (1995) characterized the TATA-less promoter region of the
human RRM1 gene and found 2 domains that were conserved with respect to
the mouse sequence. One of these sequences was shown to bind the
transcription factor SP1 (189906).
Pitterle et al. (1999) demonstrated that the RRM1 gene contains 19
exons, spans over 45 kb, and is oriented from telomere to centromere
with exon 19 nearest to D11S12.
GENE FUNCTION
In dividing cells, ribonucleotide reductase is essential for the
production of deoxyribonucleotides before DNA synthesis in S phase.
Neither of its 2 subunits, R1 or R2 (180390), are detectable in
quiescent cells. In cycling cells, RRM1 mRNA and protein are present
throughout the cell cycle (summary by Parker et al., 1994).
Byrne and Smith (1993) found that the RRM1 gene, which is located at
11p15.5, is not imprinted in Wilms tumor or in hepatoblastoma. They
demonstrated transcription of both alleles in 6 Wilms tumors, 1
hepatoblastoma, and samples from adjacent kidney and liver from
individuals who were constitutionally heterozygous for a TaqI
polymorphism.
Because the RRM1 gene is located in a region of loss of heterozygosity
(LOH) in lung tumors, Pitterle et al. (1999) screened all 19 RRM1 exons
in 12 pairs of normal and tumor DNA samples and identified no mutations.
*FIELD* RF
1. Brissenden, J. E.; Caras, I.; Thelander, L.; Francke, U.: The
structural gene for the M1 subunit of human ribonucleotide reductase
maps to chromosome 11, band p15, in human and to chromosome 7 in mouse. Exp.
Cell Res. 174: 302-308, 1988.
2. Byrne, J.; Smith, P.: Human polymorphic probe pE1.8 detects SacI
polymorphism in the ribonucleotide reductase M1 subunit gene. Hum.
Genet. 87: 376 only, 1991.
3. Byrne, J. A.; Smith, P. J.: The 11p15.5 ribonucleotide reductase
M1 subunit locus is not imprinted in Wilms' tumour and hepatoblastoma. Hum.
Genet. 91: 275-277, 1993.
4. Engstrom, Y.; Francke, U.: Assignment of the structural gene for
subunit M1 of human ribonucleotide reductase to the short arm of chromosome
11. Exp. Cell Res. 158: 477-483, 1985.
5. Parker, N. J.; Begley, C. G.; Fox, R. M.: Human R1 subunit of
ribonucleotide reductase (RRM1): 5-prime flanking region of the gene. Genomics 19:
91-96, 1994.
6. Parker, N. J.; Begley, C. G.; Fox, R. M.: Human gene for the large
subunit of ribonucleotide reductase (RRM1): functional analysis of
the promoter. Genomics 27: 280-285, 1995.
7. Pavloff, N.; Rivard, D.; Masson, S.; Shen, S.-H.; Mes-Masson, A.-M.
: Sequence analysis of the large and small subunits of human ribonucleotide
reductase. DNA Seq. 2: 227-234, 1992.
8. Pitterle, D. M.; Kim, Y.-C.; Jolicoeur, E. M. C.; Cao, Y.; O'Briant,
K. C.; Bepler, G.: Lung cancer and the human gene for ribonucleotide
reductase subunit M1 (RRM1). Mammalian Genome 10: 916-922, 1999.
*FIELD* CN
Carol A. Bocchini - updated: 6/9/2008
Alan F. Scott - updated: 9/17/1995
*FIELD* CD
Victor A. McKusick: 6/2/1986
*FIELD* ED
carol: 03/16/2012
carol: 7/8/2008
carol: 6/9/2008
alopez: 3/22/2000
carol: 6/18/1998
joanna: 5/8/1998
mark: 9/17/1995
carol: 2/7/1994
carol: 6/25/1993
carol: 7/24/1992
supermim: 3/16/1992
carol: 9/24/1991