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HUMAN:RIR1

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Species (Taxon ID) Homo sapiens (Human). (9606)
Gene Name(s) RRM1 (synonyms: RR1)
Protein Name(s) Ribonucleoside-diphosphate reductase large subunit

Ribonucleoside-diphosphate reductase subunit M1 Ribonucleotide reductase large subunit

External Links
UniProt P23921
EMBL X59543
X59617
AF107045
BC006498
L10342
CCDS CCDS7750.1
PIR S16680
RefSeq NP_001024.1
NP_001304993.1
NP_001304994.1
UniGene Hs.445705
PDB 2WGH
3HNC
3HND
3HNE
3HNF
4X3V
5D1Y
PDBsum 2WGH
3HNC
3HND
3HNE
3HNF
4X3V
5D1Y
ProteinModelPortal P23921
SMR P23921
BioGrid 112154
DIP DIP-24233N
IntAct P23921
MINT MINT-1406473
STRING 9606.ENSP00000300738
BindingDB P23921
ChEMBL CHEMBL2095215
DrugBank DB00242
DB00631
DB01073
DB00441
DB01005
GuidetoPHARMACOLOGY 2630
iPTMnet P23921
PhosphoSite P23921
SwissPalm P23921
BioMuta RRM1
DMDM 132608
EPD P23921
MaxQB P23921
PaxDb P23921
PeptideAtlas P23921
PRIDE P23921
DNASU 6240
Ensembl ENST00000300738
GeneID 6240
KEGG hsa:6240
UCSC uc001lyw.5
CTD 6240
GeneCards RRM1
HGNC HGNC:10451
HPA CAB022093
HPA057265
MIM 180410
neXtProt NX_P23921
PharmGKB PA298
eggNOG KOG1112
COG0209
GeneTree ENSGT00390000001372
HOGENOM HOG000057035
HOVERGEN HBG003447
InParanoid P23921
KO K10807
OMA YELLWQM
OrthoDB EOG7BGHK2
PhylomeDB P23921
TreeFam TF300578
BioCyc MetaCyc:HS09541-MONOMER
BRENDA 1.17.4.1
Reactome R-HSA-499943
UniPathway UPA00326
ChiTaRS RRM1
EvolutionaryTrace P23921
GeneWiki RRM1
GenomeRNAi 6240
NextBio 24233
PRO PR:P23921
Proteomes UP000005640
Bgee P23921
CleanEx HS_RRM1
ExpressionAtlas P23921
Genevisible P23921
GO GO:0042995
GO:0005737
GO:0005829
GO:0070062
GO:0043025
GO:0005635
GO:0005654
GO:0005971
GO:0005524
GO:0004748
GO:0021846
GO:0009263
GO:0006260
GO:0008584
GO:0000278
GO:0015949
GO:0055086
GO:0051290
GO:0006206
GO:0010212
GO:0060041
GO:0044281
InterPro IPR005144
IPR013346
IPR000788
IPR013509
IPR008926
Pfam PF03477
PF02867
PF00317
PRINTS PR01183
SUPFAM SSF48168
TIGRFAMs TIGR02506
PROSITE PS51161
PS00089

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0061731

ribonucleoside-diphosphate reductase activity

PMID:21336276[1]

ECO:0000315

F

Figure 3e shows the activity of wild-type ribonucleotide reductase relative to two mutant types which was determined using [3H]-CDP and [14C]-ADP reduction assays. ATP binds to the complex and activates it through an allosteric mechanism. This allows the ribonucleotide-diphosphate reductase complex to catalyze the formation of deoxyribonucleotides from ribonucleotides. The D16R mutant protein was not able to be activated by ATP at the allosteric site, and therefore had 45% reduced reductase activity (conversion of ADP to dADP). In the H2E mutant, the reductase activity relative to the wild-type was reduced by 44%.

complete
CACAO 12018

Contributes to

GO:0061731

ribonucleoside-diphosphate reductase activity

PMID:21336276[1]

ECO:0000255

F

Fairman et al modeled different hexamer formations based on the crystal structures of two subunits of the ribonucleoside-diphosphate reductase complex and used Phaser (PMID:19461840[2]) to model the hexamer holocomplex (see figure 4).

Missing: with/from
CACAO 12089

involved_in

GO:0009263

deoxyribonucleotide biosynthetic process

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P07742

P

Seeded From UniProt

complete

enables

GO:0004748

ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P07742

F

Seeded From UniProt

complete

involved_in

GO:0009263

deoxyribonucleotide biosynthetic process

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10660
EcoGene:EG20257
MGI:MGI:98180
PANTHER:PTN000171388
SGD:S000000872
SGD:S000001328
UniProtKB:P9WH75

P

Seeded From UniProt

complete

part_of

GO:0005971

ribonucleoside-diphosphate reductase complex

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10660
EcoGene:EG20257
MGI:MGI:98180
PANTHER:PTN000171388
PomBase:SPAC1F7.05
SGD:S000000872
UniProtKB:P9WH75
UniProtKB:Q9I4I1

C

Seeded From UniProt

complete

enables

GO:0004748

ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10660
EcoGene:EG20257
MGI:MGI:98180
PANTHER:PTN000171388
SGD:S000000872
SGD:S000001328
UniProtKB:P9WH75
UniProtKB:Q08698

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:25416956[4]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P23921

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:21336276[1]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P23921

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:17726094[5]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P23921

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

GO_REF:0000052

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0097718

disordered domain specific binding

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P07742
ensembl:ENSMUSP00000033283

F

Seeded From UniProt

complete

involved_in

GO:0051290

protein heterotetramerization

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P07742
ensembl:ENSMUSP00000033283

P

Seeded From UniProt

complete

involved_in

GO:0051259

protein complex oligomerization

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P07742
ensembl:ENSMUSP00000033283

P

Seeded From UniProt

complete

enables

GO:0017076

purine nucleotide binding

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P07742
ensembl:ENSMUSP00000033283

F

Seeded From UniProt

complete

involved_in

GO:0009263

deoxyribonucleotide biosynthetic process

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P07742
ensembl:ENSMUSP00000033283

P

Seeded From UniProt

complete

part_of

GO:0005971

ribonucleoside-diphosphate reductase complex

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P07742
ensembl:ENSMUSP00000033283

C

Seeded From UniProt

complete

enables

GO:0004748

ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P07742
ensembl:ENSMUSP00000033283

F

Seeded From UniProt

complete

involved_in

GO:0060041

retina development in camera-type eye

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q5U2Q5
ensembl:ENSRNOP00000064166

P

Seeded From UniProt

complete

part_of

GO:0043025

neuronal cell body

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q5U2Q5
ensembl:ENSRNOP00000064166

C

Seeded From UniProt

complete

part_of

GO:0042995

cell projection

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q5U2Q5
ensembl:ENSRNOP00000064166

C

Seeded From UniProt

complete

involved_in

GO:0021846

cell proliferation in forebrain

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q5U2Q5
ensembl:ENSRNOP00000064166

P

Seeded From UniProt

complete

involved_in

GO:0010212

response to ionizing radiation

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q5U2Q5
ensembl:ENSRNOP00000064166

P

Seeded From UniProt

complete

involved_in

GO:0008584

male gonad development

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q5U2Q5
ensembl:ENSRNOP00000064166

P

Seeded From UniProt

complete

involved_in

GO:0006206

pyrimidine nucleobase metabolic process

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q5U2Q5
ensembl:ENSRNOP00000064166

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q5U2Q5
ensembl:ENSRNOP00000064166

C

Seeded From UniProt

complete

part_of

GO:0005635

nuclear envelope

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q5U2Q5
ensembl:ENSRNOP00000064166

C

Seeded From UniProt

complete

involved_in

GO:0000278

mitotic cell cycle

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q5U2Q5
ensembl:ENSRNOP00000064166

P

Seeded From UniProt

complete

enables

GO:0004748

ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR013509

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR013509

F

Seeded From UniProt

complete

involved_in

GO:0006260

DNA replication

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000788
InterPro:IPR013509

P

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000788
InterPro:IPR013346
InterPro:IPR013509

P

Seeded From UniProt

complete

enables

GO:0004748

ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.17.4.1

F

Seeded From UniProt

complete

involved_in

GO:0015949

nucleobase-containing small molecule interconversion

Reactome:R-HSA-499943

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

Reactome:R-HSA-8866405
Reactome:R-HSA-111804
Reactome:R-HSA-111751
Reactome:R-HSA-111742

ECO:0000304

author statement supported by traceable reference used in manual assertion




C

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0021

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

P

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

involved_in

GO:0008152

metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0021

P

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

F

Seeded From UniProt

complete

involved_in

GO:0006260

DNA replication

GO_REF:0000037
GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0235
UniPathway:UPA00326

P

Seeded From UniProt

complete

edit table

Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ 1.0 1.1 1.2 Fairman, JW et al. (2011) Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Nat. Struct. Mol. Biol. 18 316-22 PubMed GONUTS page
  2. ↑ McCoy, AJ et al. (2007) Phaser crystallographic software. J Appl Crystallogr 40 658-674 PubMed GONUTS page
  3. ↑ 3.0 3.1 3.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  4. ↑ Rolland, T et al. (2014) A proteome-scale map of the human interactome network. Cell 159 1212-26 PubMed GONUTS page
  5. ↑ Wang, J et al. (2007) Enhanced subunit interactions with gemcitabine-5'-diphosphate inhibit ribonucleotide reductases. Proc. Natl. Acad. Sci. U.S.A. 104 14324-9 PubMed GONUTS page
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