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Protein Page:
RRM2 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
RRM2 Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Inhibits Wnt signaling. Belongs to the ribonucleoside diphosphate reductase small chain family. Note: This description may include information from UniProtKB.
Protein type: Nucleotide Metabolism - purine; Nucleotide Metabolism - pyrimidine; Other Amino Acids Metabolism - glutathione; Oxidoreductase; EC 1.17.4.1
Cellular Component: nucleoplasm; cytoplasm; nucleus; cytosol
Molecular Function: protein binding; metal ion binding; ribonucleoside-diphosphate reductase activity
Biological Process: G1/S-specific transcription in mitotic cell cycle; deoxyribonucleoside diphosphate metabolic process; nucleobase, nucleoside and nucleotide interconversion; nucleobase, nucleoside and nucleotide metabolic process; protein heterotetramerization; deoxyribonucleotide biosynthetic process; mitotic cell cycle; DNA replication; G1/S transition of mitotic cell cycle
Reference #:  P31350 (UniProtKB)
Alt. Names/Synonyms: R2; Ribonucleoside-diphosphate reductase subunit M2; ribonucleotide reductase M2; ribonucleotide reductase M2 polypeptide; Ribonucleotide reductase small chain; Ribonucleotide reductase small subunit; RIR2; RR2; RR2M; RRM2
Gene Symbols: RRM2
Molecular weight: 44,878 Da
Basal Isoelectric point: 5.28  Predict pI for various phosphorylation states
Select Structure to View Below

RRM2

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 V6 __MLSLRVPLAPItD
0 2 T12-p RVPLAPItDPQQLQL
4 115 S20-p DPQQLQLsPLkGLsL
0 14 K23-u QLQLsPLkGLsLVdk
0 4 S26-p LsPLkGLsLVdkENt
0 1 D29-ca LkGLsLVdkENtPPA
0 8 K30-u kGLsLVdkENtPPAL
1 39 T33-p sLVdkENtPPALsGt
0 2 S38-p ENtPPALsGtRVLAS
0 3 T40-p tPPALsGtRVLASkt
0 10 K46-u GtRVLASktARRIFQ
0 6 T47-p tRVLASktARRIFQE
0 1 T56-p RRIFQEPtEPKTkAA
0 10 K61-u EPtEPKTkAAAPGVE
0 1 K120-u IQHWESLkPEERYFI
0 4 K217-u ALRWIGDkEATyGER
1 1 Y221-p IGDkEATyGERVVAF
0 2 K283-u MFKHLVHkPSEERVR
0 6 K311-u LTEALPVkLIGMNCt
0 1 T318-p kLIGMNCtLMKQYIE
0 4 K364-u GKTNFFEkRVGEyQR
0 54 Y369-p FEkRVGEyQRMGVMS
0 2 S377-p QRMGVMSsPTENSFT
  mouse

 
T6-p __MLSVRtPLATIAD
A12 RtPLATIADQQQLQL
S20-p DQQQLQLsPLKRLTL
K23 QLQLsPLKRLTLADK
T26 LsPLKRLTLADKENt
D29 LKRLTLADKENtPPT
K30 KRLTLADKENtPPTL
T33-p TLADKENtPPTLSST
S38 ENtPPTLSSTRVLAS
T40 tPPTLSSTRVLASKA
K46 STRVLASKAARRIFQ
A47 TRVLASKAARRIFQD
A56 RRIFQDSAELESkAP
K61-u DSAELESkAPTNPSV
K121 IQHWEALKPDERHFI
K218 ALRWIGDKEATYGER
Y222 IGDKEATYGERVVAF
K284 MFKHLVHKPAEQRVR
K312 LTEALPVKLIGMNCT
T319 KLIGMNCTLMKQYIE
K365 GKTNFFEKRVGEYQR
Y370 FEKRVGEYQRMGVMS
N378 QRMGVMSNSTENSFT
  rat

 
A6 __MLSVRAPLATIAD
A12 RAPLATIADQQQLHL
S20 DQQQLHLSPLKRLSL
K23 QLHLSPLKRLSLADK
S26 LSPLKRLSLADKENT
D29 LKRLSLADKENTPPT
K30 KRLSLADKENTPPTL
T33 SLADKENTPPTLSSA
S38 ENTPPTLSSARVLAS
A40 TPPTLSSARVLASKA
K46 SARVLASKAARRIFQ
A47 ARVLASKAARRIFQD
- under review  
K61 DSAELESKAPTKPSI
K121 IQHWEALKPDERHFI
K218 ALRWIGDKEATYGER
Y222 IGDKEATYGERVVAF
K284 MFKHLVHKPSEQRVK
K312 LTEALPVKLIGMNCT
T319 KLIGMNCTLMKQYIE
K365 GKTNFFEKRVGEYQR
Y370 FEKRVGEYQRMGVMS
N378 QRMGVMSNSTENSFT
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