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P31350

- RIR2_HUMAN

UniProt

P31350 - RIR2_HUMAN

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Protein

Ribonucleoside-diphosphate reductase subunit M2

Gene

RRM2

Organism
Homo sapiens (Human)
Status
Reviewed - 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. Inhibits Wnt signaling.

Catalytic activityi

2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.PROSITE-ProRule annotation

Cofactori

Binds 2 iron ions per subunit.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi138 – 1381Iron 1PROSITE-ProRule annotation
Metal bindingi169 – 1691Iron 1PROSITE-ProRule annotation
Metal bindingi169 – 1691Iron 2By similarity
Metal bindingi172 – 1721Iron 1PROSITE-ProRule annotation
Active sitei176 – 1761PROSITE-ProRule annotation
Metal bindingi232 – 2321Iron 2By similarity
Metal bindingi266 – 2661Iron 2By similarity
Metal bindingi269 – 2691Iron 2By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. deoxyribonucleoside diphosphate metabolic process Source: InterPro
  2. deoxyribonucleotide biosynthetic process Source: UniProtKB
  3. DNA replication Source: UniProtKB-UniPathway
  4. G1/S transition of mitotic cell cycle Source: Reactome
  5. mitotic cell cycle Source: Reactome
  6. nucleobase-containing small molecule interconversion Source: Reactome
  7. nucleobase-containing small molecule metabolic process Source: Reactome
  8. protein heterotetramerization Source: Ensembl
  9. regulation of transcription involved in G1/S transition of mitotic cell cycle Source: Reactome
  10. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS10398-MONOMER.
ReactomeiREACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.
REACT_471. E2F mediated regulation of DNA replication.
REACT_683. G1/S-Specific Transcription.
UniPathwayiUPA00326.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonucleoside-diphosphate reductase subunit M2 (EC:1.17.4.1)
Alternative name(s):
Ribonucleotide reductase small chain
Ribonucleotide reductase small subunit
Gene namesi
Name:RRM2
Synonyms:RR2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:10452. RRM2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. nucleoplasm Source: Reactome
  4. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi20 – 201S → A: Enhances inhibitory effect on Wnt signaling.
Mutagenesisi20 – 201S → E: Prevents inhibitory effect on Wnt signaling.

Organism-specific databases

PharmGKBiPA299.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 389389Ribonucleoside-diphosphate reductase subunit M2PRO_0000190447Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei20 – 201Phosphoserine8 Publications
Modified residuei33 – 331Phosphothreonine2 Publications

Post-translational modificationi

Phosphorylation on Ser-20 relieves the inhibitory effect on Wnt signaling.8 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP31350.
PaxDbiP31350.
PRIDEiP31350.

PTM databases

PhosphoSiteiP31350.

Miscellaneous databases

PMAP-CutDBP31350.

Expressioni

Gene expression databases

BgeeiP31350.
CleanExiHS_RRM2.
ExpressionAtlasiP31350. baseline and differential.
GenevestigatoriP31350.

Organism-specific databases

HPAiHPA056994.

Interactioni

Subunit structurei

Heterodimer of a large and a small subunit.

Binary interactionsi

WithEntry#Exp.IntActNotes
CCNFP4100212EBI-2339245,EBI-1207574
FZR1Q9UM112EBI-2339245,EBI-724997
RRM1P239213EBI-2339245,EBI-717006

Protein-protein interaction databases

BioGridi112155. 19 interactions.
DIPiDIP-24232N.
IntActiP31350. 7 interactions.
STRINGi9606.ENSP00000302955.

Structurei

Secondary structure

1
389
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni71 – 733
Turni77 – 804
Helixi88 – 9912
Helixi104 – 1063
Helixi110 – 1123
Helixi113 – 1186
Helixi121 – 14727
Helixi149 – 1524
Helixi156 – 18328
Helixi187 – 1948
Helixi196 – 1994
Helixi201 – 2033
Helixi204 – 21512
Beta strandi217 – 2193
Helixi221 – 23313
Turni234 – 2363
Helixi237 – 24812
Helixi253 – 27826
Helixi286 – 30520
Helixi310 – 3134
Helixi317 – 33519

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2UW2X-ray2.80A60-389[»]
3OLJX-ray2.10A/B/C/D66-350[»]
3VPMX-ray2.70A/B66-350[»]
3VPNX-ray2.25A/B66-350[»]
3VPOX-ray2.30A/B66-350[»]
ProteinModelPortaliP31350.
SMRiP31350. Positions 66-350.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31350.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0208.
GeneTreeiENSGT00390000013305.
HOGENOMiHOG000255975.
HOVERGENiHBG001647.
InParanoidiP31350.
KOiK10808.
OMAiGVMNSTK.
OrthoDBiEOG7VMP5N.
PhylomeDBiP31350.
TreeFamiTF300465.

Family and domain databases

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

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P31350-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLSLRVPLAP ITDPQQLQLS PLKGLSLVDK ENTPPALSGT RVLASKTARR
60 70 80 90 100
IFQEPTEPKT KAAAPGVEDE PLLRENPRRF VIFPIEYHDI WQMYKKAEAS
110 120 130 140 150
FWTAEEVDLS KDIQHWESLK PEERYFISHV LAFFAASDGI VNENLVERFS
160 170 180 190 200
QEVQITEARC FYGFQIAMEN IHSEMYSLLI DTYIKDPKER EFLFNAIETM
210 220 230 240 250
PCVKKKADWA LRWIGDKEAT YGERVVAFAA VEGIFFSGSF ASIFWLKKRG
260 270 280 290 300
LMPGLTFSNE LISRDEGLHC DFACLMFKHL VHKPSEERVR EIIINAVRIE
310 320 330 340 350
QEFLTEALPV KLIGMNCTLM KQYIEFVADR LMLELGFSKV FRVENPFDFM
360 370 380
ENISLEGKTN FFEKRVGEYQ RMGVMSSPTE NSFTLDADF
Length:389
Mass (Da):44,878
Last modified:July 1, 1993 - v1
Checksum:i10E6F5F84D34DA94
GO
Isoform 2 (identifier: P31350-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGRVGGMAQPMGRAGAPKPMGRAGSARRGRFKGCWSEGSPVHPVPAVLSWLLALLRCASTM

Note: No experimental confirmation available.Curated

Show »
Length:449
Mass (Da):51,093
Checksum:iDFEA2E41A26BD80E
GO

Sequence cautioni

The sequence DA477511 differs from that shown. Reason: Frameshift at position 87.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Isoform 2 (identifier: P31350-2)
Sequence conflicti28 – 281R → H in DA477511. (PubMed:14702039)Curated
Sequence conflicti59 – 591S → A in DA477511. (PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MGRVGGMAQPMGRAGAPKPM GRAGSARRGRFKGCWSEGSP VHPVPAVLSWLLALLRCAST M in isoform 2. 1 PublicationVSP_044917

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X59618 mRNA. Translation: CAA42181.1.
S40301 mRNA. Translation: AAA09577.1.
AY032750 Genomic DNA. Translation: AAK51163.1.
AK313719 mRNA. Translation: BAG36462.1.
DA477511 mRNA. No translation available.
AC104794 Genomic DNA. Translation: AAX93099.1.
AC118058 Genomic DNA. No translation available.
BC001886 mRNA. Translation: AAH01886.1.
BC030154 mRNA. Translation: AAH30154.1.
CCDSiCCDS1669.1. [P31350-1]
CCDS54334.1. [P31350-2]
PIRiS25854.
RefSeqiNP_001025.1. NM_001034.3. [P31350-1]
NP_001159403.1. NM_001165931.1. [P31350-2]
UniGeneiHs.226390.

Genome annotation databases

EnsembliENST00000304567; ENSP00000302955; ENSG00000171848. [P31350-1]
ENST00000360566; ENSP00000353770; ENSG00000171848. [P31350-2]
ENST00000615152; ENSP00000484183; ENSG00000171848. [P31350-2]
GeneIDi6241.
KEGGihsa:6241.
UCSCiuc021vdr.1. human. [P31350-1]

Polymorphism databases

DMDMi400979.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Wikipedia

Ribonucleotide reductase entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X59618 mRNA. Translation: CAA42181.1 .
S40301 mRNA. Translation: AAA09577.1 .
AY032750 Genomic DNA. Translation: AAK51163.1 .
AK313719 mRNA. Translation: BAG36462.1 .
DA477511 mRNA. No translation available.
AC104794 Genomic DNA. Translation: AAX93099.1 .
AC118058 Genomic DNA. No translation available.
BC001886 mRNA. Translation: AAH01886.1 .
BC030154 mRNA. Translation: AAH30154.1 .
CCDSi CCDS1669.1. [P31350-1 ]
CCDS54334.1. [P31350-2 ]
PIRi S25854.
RefSeqi NP_001025.1. NM_001034.3. [P31350-1 ]
NP_001159403.1. NM_001165931.1. [P31350-2 ]
UniGenei Hs.226390.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2UW2 X-ray 2.80 A 60-389 [» ]
3OLJ X-ray 2.10 A/B/C/D 66-350 [» ]
3VPM X-ray 2.70 A/B 66-350 [» ]
3VPN X-ray 2.25 A/B 66-350 [» ]
3VPO X-ray 2.30 A/B 66-350 [» ]
ProteinModelPortali P31350.
SMRi P31350. Positions 66-350.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112155. 19 interactions.
DIPi DIP-24232N.
IntActi P31350. 7 interactions.
STRINGi 9606.ENSP00000302955.

Chemistry

BindingDBi P31350.
ChEMBLi CHEMBL1954.
DrugBanki DB00242. Cladribine.
DB05260. Gallium nitrate.
GuidetoPHARMACOLOGYi 2631.

PTM databases

PhosphoSitei P31350.

Polymorphism databases

DMDMi 400979.

Proteomic databases

MaxQBi P31350.
PaxDbi P31350.
PRIDEi P31350.

Protocols and materials databases

DNASUi 6241.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000304567 ; ENSP00000302955 ; ENSG00000171848 . [P31350-1 ]
ENST00000360566 ; ENSP00000353770 ; ENSG00000171848 . [P31350-2 ]
ENST00000615152 ; ENSP00000484183 ; ENSG00000171848 . [P31350-2 ]
GeneIDi 6241.
KEGGi hsa:6241.
UCSCi uc021vdr.1. human. [P31350-1 ]

Organism-specific databases

CTDi 6241.
GeneCardsi GC02P010262.
HGNCi HGNC:10452. RRM2.
HPAi HPA056994.
MIMi 180390. gene.
neXtProti NX_P31350.
PharmGKBi PA299.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0208.
GeneTreei ENSGT00390000013305.
HOGENOMi HOG000255975.
HOVERGENi HBG001647.
InParanoidi P31350.
KOi K10808.
OMAi GVMNSTK.
OrthoDBi EOG7VMP5N.
PhylomeDBi P31350.
TreeFami TF300465.

Enzyme and pathway databases

UniPathwayi UPA00326 .
BioCyci MetaCyc:HS10398-MONOMER.
Reactomei REACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.
REACT_471. E2F mediated regulation of DNA replication.
REACT_683. G1/S-Specific Transcription.

Miscellaneous databases

EvolutionaryTracei P31350.
GeneWikii RRM2.
GenomeRNAii 6241.
NextBioi 24237.
PMAP-CutDB P31350.
PROi P31350.
SOURCEi Search...

Gene expression databases

Bgeei P31350.
CleanExi HS_RRM2.
ExpressionAtlasi P31350. baseline and differential.
Genevestigatori P31350.

Family and domain databases

Gene3Di 1.10.620.20. 1 hit.
InterProi IPR009078. Ferritin-like_SF.
IPR012348. RNR-rel.
IPR000358. RNR_small.
[Graphical view ]
PANTHERi PTHR23409. PTHR23409. 1 hit.
Pfami PF00268. Ribonuc_red_sm. 1 hit.
[Graphical view ]
SUPFAMi SSF47240. SSF47240. 1 hit.
PROSITEi PS00368. RIBORED_SMALL. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORM 1).
    Tissue: Mammary carcinoma.
  2. "Characterization of the human ribonucleotide reductase M2 subunit gene; genomic structure and promoter analyses."
    Zhou B., Yen Y.
    Cytogenet. Cell Genet. 95:52-59(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-94 (ISOFORM 2).
    Tissue: Neonatal skin.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 1).
    Tissue: Muscle and Skin.
  6. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
    Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
    Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20 AND THR-33, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20 AND THR-33, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRIR2_HUMAN
AccessioniPrimary (citable) accession number: P31350
Secondary accession number(s): B2R9B5, J3KP43, Q5WRU7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: October 29, 2014
This is version 157 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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3