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Protein

Ribonucleoside-diphosphate reductase large subunit

Gene

RRM1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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, the dATP inhibition is mediated by AHCYL1 which stabilizes dATP in the site.3 Publications

Pathway:iDNA replication

This protein is involved in the pathway DNA replication, which is part of Genetic information processing.
View all proteins of this organism that are known to be involved in the pathway DNA replication and in Genetic information processing.

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS09541-MONOMER.
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 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 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:10451. RRM1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi57 – 571D → N: Severely decreases interaction with AHCYL1 in the presence of dATP. 1 Publication

Organism-specific databases

PharmGKBiPA298.

Chemistry

DrugBankiDB00242. Cladribine.
DB00631. Clofarabine.
DB01073. Fludarabine.
DB00441. Gemcitabine.
DB01005. Hydroxyurea.

Polymorphism and mutation databases

BioMutaiRRM1.
DMDMi132608.

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

BgeeiP23921.
CleanExiHS_RRM1.
ExpressionAtlasiP23921. baseline and differential.
GenevisibleiP23921. HS.

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. Interacts with AHCYL1 which inhibits its activity.3 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
Beta strandi2 – 43Combined sources
Beta strandi10 – 123Combined sources
Helixi15 – 239Combined sources
Turni31 – 333Combined sources
Helixi36 – 449Combined sources
Beta strandi48 – 503Combined sources
Helixi53 – 6614Combined sources
Helixi67 – 693Combined sources
Helixi78 – 8811Combined sources
Helixi94 – 10310Combined sources
Turni107 – 1093Combined sources
Helixi118 – 1269Combined sources
Helixi128 – 1336Combined sources
Helixi137 – 1426Combined sources
Helixi145 – 15410Combined sources
Beta strandi158 – 1636Combined sources
Helixi167 – 17913Combined sources
Helixi183 – 19513Combined sources
Beta strandi197 – 2004Combined sources
Helixi202 – 2076Combined sources
Beta strandi210 – 2123Combined sources
Beta strandi218 – 2225Combined sources
Helixi228 – 24316Combined sources
Beta strandi247 – 2515Combined sources
Beta strandi258 – 2614Combined sources
Helixi263 – 2653Combined sources
Beta strandi268 – 2703Combined sources
Helixi272 – 28514Combined sources
Beta strandi287 – 2937Combined sources
Beta strandi297 – 3015Combined sources
Helixi308 – 3114Combined sources
Turni312 – 3154Combined sources
Beta strandi317 – 3193Combined sources
Helixi321 – 3233Combined sources
Beta strandi328 – 3347Combined sources
Helixi336 – 3438Combined sources
Beta strandi347 – 3515Combined sources
Turni353 – 3553Combined sources
Helixi359 – 3613Combined sources
Helixi365 – 37612Combined sources
Beta strandi381 – 3855Combined sources
Helixi386 – 40015Combined sources
Beta strandi404 – 4074Combined sources
Helixi408 – 4136Combined sources
Helixi418 – 4203Combined sources
Beta strandi428 – 4303Combined sources
Beta strandi442 – 4443Combined sources
Beta strandi446 – 4505Combined sources
Helixi451 – 4544Combined sources
Beta strandi459 – 4613Combined sources
Helixi463 – 48321Combined sources
Helixi489 – 49810Combined sources
Beta strandi502 – 5065Combined sources
Helixi508 – 5147Combined sources
Beta strandi519 – 5213Combined sources
Helixi522 – 55029Combined sources
Helixi554 – 5563Combined sources
Helixi561 – 5633Combined sources
Helixi567 – 5704Combined sources
Beta strandi577 – 5793Combined sources
Helixi581 – 59111Combined sources
Helixi607 – 6115Combined sources
Beta strandi623 – 6297Combined sources
Beta strandi632 – 6376Combined sources
Helixi639 – 64810Combined sources
Helixi655 – 6617Combined sources
Turni662 – 6643Combined sources
Beta strandi670 – 6723Combined sources
Helixi674 – 6796Combined sources
Turni683 – 6853Combined sources
Helixi688 – 69912Combined sources
Helixi717 – 72913Combined sources
Beta strandi733 – 7375Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000001372.
HOGENOMiHOG000057035.
HOVERGENiHBG003447.
InParanoidiP23921.
KOiK10807.
OMAiYELLWQM.
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

        10         20         30         40         50
MHVIKRDGRQ ERVMFDKITS RIQKLCYGLN MDFVDPAQIT MKVIQGLYSG
60 70 80 90 100
VTTVELDTLA AETAATLTTK HPDYAILAAR IAVSNLHKET KKVFSDVMED
110 120 130 140 150
LYNYINPHNG KHSPMVAKST LDIVLANKDR LNSAIIYDRD FSYNYFGFKT
160 170 180 190 200
LERSYLLKIN GKVAERPQHM LMRVSVGIHK EDIDAAIETY NLLSERWFTH
210 220 230 240 250
ASPTLFNAGT NRPQLSSCFL LSMKDDSIEG IYDTLKQCAL ISKSAGGIGV
260 270 280 290 300
AVSCIRATGS YIAGTNGNSN GLVPMLRVYN NTARYVDQGG NKRPGAFAIY
310 320 330 340 350
LEPWHLDIFE FLDLKKNTGK EEQRARDLFF ALWIPDLFMK RVETNQDWSL
360 370 380 390 400
MCPNECPGLD EVWGEEFEKL YASYEKQGRV RKVVKAQQLW YAIIESQTET
410 420 430 440 450
GTPYMLYKDS CNRKSNQQNL GTIKCSNLCT EIVEYTSKDE VAVCNLASLA
460 470 480 490 500
LNMYVTSEHT YDFKKLAEVT KVVVRNLNKI IDINYYPVPE ACLSNKRHRP
510 520 530 540 550
IGIGVQGLAD AFILMRYPFE SAEAQLLNKQ IFETIYYGAL EASCDLAKEQ
560 570 580 590 600
GPYETYEGSP VSKGILQYDM WNVTPTDLWD WKVLKEKIAK YGIRNSLLIA
610 620 630 640 650
PMPTASTAQI LGNNESIEPY TSNIYTRRVL SGEFQIVNPH LLKDLTERGL
660 670 680 690 700
WHEEMKNQII ACNGSIQSIP EIPDDLKQLY KTVWEISQKT VLKMAAERGA
710 720 730 740 750
FIDQSQSLNI HIAEPNYGKL TSMHFYGWKQ GLKTGMYYLR TRPAANPIQF
760 770 780 790
TLNKEKLKDK EKVSKEEEEK ERNTAAMVCS LENRDECLMC GS
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:
EMBLi
GenBanki
DDBJi
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.

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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

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

Chemistry

BindingDBiP23921.
ChEMBLiCHEMBL2095215.
DrugBankiDB00242. Cladribine.
DB00631. Clofarabine.
DB01073. Fludarabine.
DB00441. Gemcitabine.
DB01005. Hydroxyurea.
GuidetoPHARMACOLOGYi2630.

PTM databases

PhosphoSiteiP23921.

Polymorphism and mutation databases

BioMutaiRRM1.
DMDMi132608.

Proteomic databases

MaxQBiP23921.
PaxDbiP23921.
PeptideAtlasiP23921.
PRIDEiP23921.

Protocols and materials databases

DNASUi6240.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi6240.
GeneCardsiGC11P004115.
HGNCiHGNC:10451. RRM1.
HPAiCAB022093.
HPA057265.
MIMi180410. gene.
neXtProtiNX_P23921.
PharmGKBiPA298.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0209.
GeneTreeiENSGT00390000001372.
HOGENOMiHOG000057035.
HOVERGENiHBG003447.
InParanoidiP23921.
KOiK10807.
OMAiYELLWQM.
OrthoDBiEOG7BGHK2.
PhylomeDBiP23921.
TreeFamiTF300578.

Enzyme and pathway databases

UniPathwayiUPA00326.
BioCyciMetaCyc:HS09541-MONOMER.
BRENDAi1.17.4.1. 2681.
ReactomeiREACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.

Miscellaneous databases

ChiTaRSiRRM1. human.
EvolutionaryTraceiP23921.
GeneWikiiRRM1.
GenomeRNAii6240.
NextBioi24233.
PROiP23921.
SOURCEiSearch...

Gene expression databases

BgeeiP23921.
CleanExiHS_RRM1.
ExpressionAtlasiP23921. baseline and differential.
GenevisibleiP23921. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "Enzyme regulation. IRBIT is a novel regulator of ribonucleotide reductase in higher eukaryotes."
    Arnaoutov A., Dasso M.
    Science 345:1512-1515(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, MUTAGENESIS OF ASP-57, INTERACTION WITH AHCYL1.
  12. "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: July 22, 2015
This is version 162 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.