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Protein Page:
RRM1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
RRM1 an enzyme involved in DNA replication that provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Belongs to the ribonucleoside diphosphate reductase large chain family. 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. 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. 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. Patients with advanced non-small cell lung cancer responded favorably to gemcitabine. Note: This description may include information from UniProtKB.
Protein type: DNA replication; Nucleotide Metabolism - pyrimidine; Oxidoreductase; EC 1.17.4.1; Other Amino Acids Metabolism - glutathione; Nucleotide Metabolism - purine
Cellular Component: nucleoplasm; cell projection; cell soma; cytoplasm; ribonucleoside-diphosphate reductase complex; nuclear envelope; cytosol
Molecular Function: protein binding; ATP binding; ribonucleoside-diphosphate reductase activity
Biological Process: pyrimidine base metabolic process; nucleobase, nucleoside and nucleotide metabolic process; retina development in camera-type eye; nucleobase, nucleoside and nucleotide interconversion; cell proliferation in forebrain; male gonad development; protein heterotetramerization; deoxyribonucleotide biosynthetic process; mitotic cell cycle; response to ionizing radiation; DNA replication
Reference #:  P23921 (UniProtKB)
Alt. Names/Synonyms: R1; Ribonucleoside-diphosphate reductase large subunit; Ribonucleoside-diphosphate reductase subunit M1; Ribonucleotide reductase large subunit; ribonucleotide reductase M1; ribonucleotide reductase M1 polypeptide; ribonucleotide reductase, large subunit; ribonucleotide reductase, R1 subunit; RIR1; RR1; RRM1
Gene Symbols: RRM1
Molecular weight: 90,070 Da
Basal Isoelectric point: 6.76  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

RRM1

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 K17-ac QERVMFDkITSRIQk
0 2 K17-ub QERVMFDkITSRIQk
0 1 K24-ub kITSRIQkLCYGLNM
0 1 K70-ub TAATLTTkHPDYAIL
0 5 K92-ub NLHKETKkVFSDVME
0 9 Y102-p SDVMEDLyNyINPHN
0 2 Y104-p VMEDLyNyINPHNGk
0 1 K111-ub yINPHNGkHSPMVAK
0 1 K128-ub LDIVLANkDRLNSAI
0 1 S142-p IIYDRDFsYNYFGFk
0 14 K149-ub sYNYFGFkTLERSYL
0 11 K158-ub LERSYLLkINGKVAE
0 1 K180-ub RVSVGIHkEDIDAAI
0 5 Y232-p DDSIEGIyDTLkQCA
0 1 K236-ub EGIyDTLkQCALISK
0 1 S253-p GGIGVAVsCIRATGS
0 1 K320-m2 DLKKNTGkEEQRARD
0 1 K376-ac KLYASYEkQGRVRKV
0 4 K376-ub KLYASYEkQGRVRKV
0 5 K414-ub YKDSCNRkSNQQNLG
0 1 T422-p SNQQNLGtIKCSNLC
0 2 K465-ub EHTYDFKkLAEVTkV
0 16 K471-ub KkLAEVTkVVVRNLN
0 12 Y485-p NKIIDINyyPVPEAC
0 2 Y486-p KIIDINyyPVPEACL
0 49 K496-ac PEACLSNkRHRPIGI
0 10 K496-ub PEACLSNkRHRPIGI
0 2 Y553-p LAKEQGPyEtyEGsP
0 1 T555-p KEQGPyEtyEGsPVS
0 3 Y556-p EQGPyEtyEGsPVSK
0 1 S559-p PyEtyEGsPVSKGIL
0 1 K590 VLKEKIAKYGIRNSL
0 1 K590-ub VLKEKIAkYGIRNSL
0 1 T604-p LLIAPMPtASTAQIL
0 11 K643-ub IVNPHLLkDLTERGL
0 1 K681-ub DDLKQLYkTVWEISQ
0 1 K689-ub TVWEISQkTVLkMAA
0 1 K693-ub ISQkTVLkMAAERGA
0 2 Y726-p KLTSMHFyGWKQGLK
0 1 Y738-p GLKTGMYyLRTRPAA
0 26 T751-p AANPIQFtLNkEKLK
0 3 K754-ub PIQFtLNkEKLKDKE
0 1 T774-p EEEKERNtAAMVCsL
0 1 S780-p NtAAMVCsLENRDEC
0 1 S792-p DECLMCGs_______
  mouse

 
K17 QERVMFDKITSRIQK
K17 QERVMFDKITSRIQK
K24 KITSRIQKLCYGLNM
K70 TAATLTTKHPDYAIL
K92 NLHKETKKVFSDVME
Y102-p SDVMEDLyNYINPHN
Y104 VMEDLyNYINPHNGR
R111 YINPHNGRHSPMVAS
K128 LDIVMANKDRLNSAI
S142 IIYDRDFSYNYFGFK
K149 SYNYFGFKTLERSYL
K158 LERSYLLKINGKVAE
K180 RVSVGIHKEDIDAAI
Y232 DDSIEGIYDTLKQCA
K236 EGIYDTLKQCALISK
S253 GGIGVAVSCIRATGS
K320 DLKKNTGKEEQRARD
K376 KLYESYEKQGRVRKV
K376 KLYESYEKQGRVRKV
K414 YKDSCNRKSNQQNLG
T422 SNQQNLGTIKCSNLC
K465 EHTYDFEKLAEVTkV
K471-ub EKLAEVTkVIVRNLN
Y485 NKIIDINYYPIPEAH
Y486 KIIDINYYPIPEAHL
K496 PEAHLSNKRHRPIGI
K496 PEAHLSNKRHRPIGI
Y553 LAKEYGPYETYEGSP
T555 KEYGPYETYEGSPVS
Y556 EYGPYETYEGSPVSK
S559 PYETYEGSPVSKGIL
K590-ac PLKEKIAkYGIRNSL
K590 PLKEKIAKYGIRNSL
T604 LLIAPMPTASTAQIL
K643 IVNPHLLKDLTERGL
K681 DDLKQLYKTVWEISQ
K689 TVWEISQKTVLKMAA
K693 ISQKTVLKMAAERGA
Y726 KLTSMHFYGWKQGLK
Y738 GLKTGMYYLRTRPAA
T751-p AANPIQFtLNKEKLK
K754 PIQFtLNKEKLKDKE
T774 EEEKERNTAAMVCSL
S780 NTAAMVCSLENREEC
S792 EECLMCGS_______
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