Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Ribonucleoside-diphosphate reductase large subunit  

UniProtKB / Swiss-Prot ID :  RIR1_HUMAN

Gene Name (Synonyms) : 
RRM1, RR1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. 

Protein Function :  Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. 

Protein Sequence MHVIKRDGRQERVMFDKITSRIQKLCYGLNMDFVDPAQITMKVIQGLYSGVTTVELDTLAAETAATLTTK...
Predicted Secondary Structure CEEECCCCCEECCCHHHHHHHHHHHHHCCCCCCCCHHHHHHHHHHHHHCCCCHHHHHHHHHHHHHHHCCC...
Protein Variant
LocationDescription
590K -> Q (in dbSNP:rs2228123). VAR_052052
778V -> A (in dbSNP:rs2229196). VAR_052053
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
17Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VMFDKITSR
CCHHHHHHH
36.30Phosphositeplus
Link-
17N6-acetyllysineVMFDKITSR
CCHHHHHHH
36.30HPRD
Link-
17N6-acetyllysineVMFDKITSR
CCHHHHHHH
36.30Phosphositeplus
Link-
17N6-acetyllysine.VMFDKITSR
CCHHHHHHH
36.30UniProtKB
Link-
24Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SRIQKLCYG
HHHHHHHHC
37.85Phosphositeplus
Link-
92Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KETKKVFSD
HHHHHHHHH
56.80Phosphositeplus
Link
102PhosphotyrosineMEDLYNYIN
HHHHHHHHH
20.45Phosphositeplus
Link
104PhosphotyrosineDLYNYINPH
HHHHHHHHH
6.63Phosphositeplus
Link
111Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PHNGKHSPM
HHHCCCCHH
46.34Phosphositeplus
Link
128Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VLANKDRLN
HHHHHHHHH
38.32Phosphositeplus
Link
149Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YFGFKTLER
HHHHHHHHH
53.21Phosphositeplus
Link
158Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SYLLKINGK
HHHHHCCCC
31.37Phosphositeplus
Link
180Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VGIHKEDID
HHHCCCCHH
55.98Phosphositeplus
Link
236Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YDTLKQCAL
HHHHHHHHH
45.48Phosphositeplus
Link
376Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ASYEKQGRV
HHHHHCCCC
50.23Phosphositeplus
Link
376N6-acetyllysineASYEKQGRV
HHHHHCCCC
50.23HPRD
Link
376N6-acetyllysineASYEKQGRV
HHHHHCCCC
50.23Phosphositeplus
Link
376N6-acetyllysine.ASYEKQGRV
HHHHHCCCC
50.23UniProtKB
Link
414Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SCNRKSNQQ
CHHHCCCCC
39.50Phosphositeplus
Link
422PhosphothreonineQNLGTIKCS
CCCCCEECC
22.04HPRD
Link
422PhosphothreonineQNLGTIKCS
CCCCCEECC
22.04Phosphositeplus
Link
465Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YDFKKLAEV
CCHHHHHHH
53.58Phosphositeplus
Link
471Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AEVTKVVVR
HHHHHHHHH
37.90Phosphositeplus
Link
485PhosphotyrosineIDINYYPVP
HHHCCCCHH
14.96Phosphositeplus
Link
496Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)CLSNKRHRP
HHHHHHCCC
46.32Phosphositeplus
Link
590Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EKIAKYGIR
HHHHHCCCC
47.70Phosphositeplus
Link
643Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PHLLKDLTE
CHHHHHHHH
57.99Phosphositeplus
Link
681Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KQLYKTVWE
HHHHHHHHH
45.23Phosphositeplus
Link
689Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EISQKTVLK
HCCHHHHHH
33.53Phosphositeplus
Link
693Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KTVLKMAAE
HHHHHHHHH
23.35Phosphositeplus
Link
738PhosphotyrosineTGMYYLRTR
HHHHHHCCC
4.84Phosphositeplus
Link
754Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FTLNKEKLK
CCCCHHHHC
60.38Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
RIR2B_HUMANphysical interactionDIP:40168EDIP12615712
RIF1_HUMANphysical interactionEBI-733190
intact16169070
RIR2_HUMANin vitroHPRD:01588HPRD11781084
RIR1_HUMANin vitroHPRD:01588HPRD12578384
CA103_HUMANyeast 2-hybridHPRD:01588HPRD16169070
GLRX1_HUMANENSP00000300738STRING
RIR2B_HUMANENSP00000300738STRING
PNPT1_HUMANENSP00000300738STRING
KPYR_HUMANENSP00000300738STRING
RIR2_HUMANENSP00000300738STRING
KGUA_HUMANENSP00000300738STRING
KPYM_HUMANENSP00000300738STRING
KPYM_HUMANENSP00000300738STRING
ENTP2_HUMANENSP00000300738STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-17 AND LYS-376, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures