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Protein

Ribonucleoside-diphosphate reductase subunit M2

Gene

rrm2

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
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.PROSITE-ProRule annotation

Cofactori

Fe cationBy similarityNote: Binds 2 iron ions per subunit.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi135 – 1351Iron 1PROSITE-ProRule annotation
Metal bindingi166 – 1661Iron 1PROSITE-ProRule annotation
Metal bindingi166 – 1661Iron 2By similarity
Metal bindingi169 – 1691Iron 1PROSITE-ProRule annotation
Active sitei173 – 1731PROSITE-ProRule annotation
Metal bindingi229 – 2291Iron 2By similarity
Metal bindingi263 – 2631Iron 2By similarity
Metal bindingi266 – 2661Iron 2By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. deoxyribonucleoside diphosphate metabolic process Source: InterPro
  2. deoxyribonucleotide biosynthetic process Source: InterPro
  3. DNA replication Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_321941. E2F mediated regulation of DNA replication.
REACT_323825. G1/S-Specific Transcription.
REACT_328545. Synthesis and interconversion of nucleotide di- and triphosphates.
UniPathwayiUPA00326.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonucleoside-diphosphate reductase subunit M2 (EC:1.17.4.1)
Alternative name(s):
Ribonucleotide reductase protein R2 class I
Ribonucleotide reductase small chain
Ribonucleotide reductase small subunit
Gene namesi
Name:rrm2
Synonyms:r2
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
ProteomesiUP000000437 Componentsi: Chromosome 19, Chromosome 20

Organism-specific databases

ZFINiZDB-GENE-990415-25. rrm2.

Subcellular locationi

GO - Cellular componenti

  1. ribonucleoside-diphosphate reductase complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 386386Ribonucleoside-diphosphate reductase subunit M2PRO_0000190452Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei6 – 61Phosphoserine1 Publication
Modified residuei31 – 311Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP79733.

Expressioni

Gene expression databases

BgeeiP79733.

Interactioni

Subunit structurei

Heterodimer of a large and a small subunit.

Protein-protein interaction databases

STRINGi7955.ENSDARP00000008907.

Structurei

3D structure databases

ProteinModelPortaliP79733.
SMRiP79733. Positions 26-349.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0208.
GeneTreeiENSGT00390000013305.
HOGENOMiHOG000255975.
HOVERGENiHBG001647.
InParanoidiP79733.
KOiK10808.
OMAiLNIEREF.
OrthoDBiEOG7VMP5N.
PhylomeDBiP79733.
TreeFamiTF300465.

Family and domain databases

Gene3Di1.10.620.20. 1 hit.
InterProiIPR009078. Ferritin-like_SF.
IPR012348. RNR-rel.
IPR000358. RNR_small.
IPR030475. RNR_small_AS.
[Graphical view]
PANTHERiPTHR23409. PTHR23409. 1 hit.
PfamiPF00268. Ribonuc_red_sm. 1 hit.
[Graphical view]
PIRSFiPIRSF000355. NrdB. 1 hit.
SUPFAMiSSF47240. SSF47240. 1 hit.
PROSITEiPS00368. RIBORED_SMALL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P79733-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSTRSPLKT KNENTISTKM NNMSFVDKEN TPPSLSSTRI LASKTARKIF
60 70 80 90 100
DESEGQSKAK KGAVEEEPLL KENPHRFVIF PIQYHDIWQM YKKAEASFWT
110 120 130 140 150
AEEVDLSKDL QHWDSLKDEE RYFISHVLAF FAASDGIVNE NLVERFTQEV
160 170 180 190 200
QVTEARCFYG FQIAMENIHS EMYSLLIDTY IKDSKEREFL FNAIETMPCV
210 220 230 240 250
KKKADWALNW IGDKNARYGE RVVAFAAVEG IFFSGSFASI FWLKKRGLMP
260 270 280 290 300
GLTFSNELIS RDEGLHCDFA CLMFKHLINK PSEETVKKII MNAVEIEQEF
310 320 330 340 350
LTDALPVKLI GMNCDLMKQY IEFVADRLLL ELGFDKVYRV ENPFDFMENI
360 370 380
SLEGKTNFFE KRVGEYQRMG VMSGTTDNTF TLDADF
Length:386
Mass (Da):44,594
Last modified:May 1, 1997 - v1
Checksum:iC168846FB57F9F4E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti279 – 2791N → S in AAH75746 (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U57965 mRNA. Translation: AAB37103.1.
BX248136 Genomic DNA. Translation: CAI21240.1.
BC044355 mRNA. Translation: AAH44355.1.
BC075746 mRNA. Translation: AAH75746.1.
RefSeqiNP_571525.1. NM_131450.2.
XP_002665783.1. XM_002665737.3.
UniGeneiDr.75098.

Genome annotation databases

EnsembliENSDART00000027851; ENSDARP00000008907; ENSDARG00000020711.
ENSDART00000112155; ENSDARP00000103553; ENSDARG00000078069.
GeneIDi100330864.
30733.
KEGGidre:100330864.
dre:30733.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U57965 mRNA. Translation: AAB37103.1.
BX248136 Genomic DNA. Translation: CAI21240.1.
BC044355 mRNA. Translation: AAH44355.1.
BC075746 mRNA. Translation: AAH75746.1.
RefSeqiNP_571525.1. NM_131450.2.
XP_002665783.1. XM_002665737.3.
UniGeneiDr.75098.

3D structure databases

ProteinModelPortaliP79733.
SMRiP79733. Positions 26-349.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7955.ENSDARP00000008907.

Proteomic databases

PRIDEiP79733.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSDART00000027851; ENSDARP00000008907; ENSDARG00000020711.
ENSDART00000112155; ENSDARP00000103553; ENSDARG00000078069.
GeneIDi100330864.
30733.
KEGGidre:100330864.
dre:30733.

Organism-specific databases

CTDi6241.
ZFINiZDB-GENE-990415-25. rrm2.

Phylogenomic databases

eggNOGiCOG0208.
GeneTreeiENSGT00390000013305.
HOGENOMiHOG000255975.
HOVERGENiHBG001647.
InParanoidiP79733.
KOiK10808.
OMAiLNIEREF.
OrthoDBiEOG7VMP5N.
PhylomeDBiP79733.
TreeFamiTF300465.

Enzyme and pathway databases

UniPathwayiUPA00326.
ReactomeiREACT_321941. E2F mediated regulation of DNA replication.
REACT_323825. G1/S-Specific Transcription.
REACT_328545. Synthesis and interconversion of nucleotide di- and triphosphates.

Miscellaneous databases

NextBioi20807081.
PROiP79733.

Gene expression databases

BgeeiP79733.

Family and domain databases

Gene3Di1.10.620.20. 1 hit.
InterProiIPR009078. Ferritin-like_SF.
IPR012348. RNR-rel.
IPR000358. RNR_small.
IPR030475. RNR_small_AS.
[Graphical view]
PANTHERiPTHR23409. PTHR23409. 1 hit.
PfamiPF00268. Ribonuc_red_sm. 1 hit.
[Graphical view]
PIRSFiPIRSF000355. NrdB. 1 hit.
SUPFAMiSSF47240. SSF47240. 1 hit.
PROSITEiPS00368. RIBORED_SMALL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequencing of cDNAs encoding ribonucleotide reductase from zebrafish Danio rerio."
    Mathews C.Z., Sjoeberg B.-M., Karlsson M.
    Mol. Mar. Biol. Biotechnol. 5:284-287(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The zebrafish reference genome sequence and its relationship to the human genome."
    Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.
    , White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G., Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.
    Nature 496:498-503(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Tuebingen.
  3. NIH - Zebrafish Gene Collection (ZGC) project
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: AB.
    Tissue: Embryo.
  4. "Online automated in vivo zebrafish phosphoproteomics: from large-scale analysis down to a single embryo."
    Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J., Slijper M., Heck A.J.R.
    J. Proteome Res. 7:1555-1564(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND THR-31, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiRIR2_DANRE
AccessioniPrimary (citable) accession number: P79733
Secondary accession number(s): Q6DI44
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: May 1, 1997
Last modified: April 1, 2015
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.