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Protein

Ribose-phosphate pyrophosphokinase 3

Gene

PRPS1L1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis.

Catalytic activityi

ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate.

Cofactori

Enzyme regulationi

Activated by magnesium and inorganic phosphate.

Pathwayi: 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I).
Proteins known to be involved in this subpathway in this organism are:
  1. Ribose-phosphate pyrophosphokinase 3 (PRPS1L1), Ribose-phosphate pyrophosphokinase 1 (PRPS1), Ribose-phosphate pyrophosphokinase 2 (PRPS2)
This subpathway is part of the pathway 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I), the pathway 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis and in Metabolic intermediate biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi128MagnesiumSequence analysis1
Metal bindingi130MagnesiumSequence analysis1
Binding sitei130ATPBy similarity1
Metal bindingi139MagnesiumSequence analysis1
Metal bindingi143MagnesiumSequence analysis1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi96 – 101ATPBy similarity6

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Nucleotide biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS11931-MONOMER.
ZFISH:HS11931-MONOMER.
ReactomeiR-HSA-73843. 5-Phosphoribose 1-diphosphate biosynthesis.
UniPathwayiUPA00087; UER00172.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribose-phosphate pyrophosphokinase 3 (EC:2.7.6.1)
Alternative name(s):
Phosphoribosyl pyrophosphate synthase 1-like 1
Short name:
PRPS1-like 1
Phosphoribosyl pyrophosphate synthase III
Short name:
PRS-III
Gene namesi
Name:PRPS1L1
Synonyms:PRPS3, PRPSL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:9463. PRPS1L1.

Pathology & Biotechi

Organism-specific databases

DisGeNETi221823.
PharmGKBiPA33818.

Polymorphism and mutation databases

BioMutaiPRPS1L1.
DMDMi125585.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001410782 – 318Ribose-phosphate pyrophosphokinase 3Add BLAST317

Proteomic databases

EPDiP21108.
MaxQBiP21108.
PaxDbiP21108.
PeptideAtlasiP21108.
PRIDEiP21108.

2D gel databases

SWISS-2DPAGEP21108.

PTM databases

iPTMnetiP21108.
PhosphoSitePlusiP21108.

Expressioni

Tissue specificityi

Testis.

Gene expression databases

CleanExiHS_PRPS1L1.

Interactioni

Subunit structurei

Homodimer. The active form is probably a hexamer composed of 3 homodimers (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi128758. 6 interactors.
STRINGi9606.ENSP00000424595.

Structurei

3D structure databases

ProteinModelPortaliP21108.
SMRiP21108.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni212 – 227Binding of phosphoribosylpyrophosphateSequence analysisAdd BLAST16

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1448. Eukaryota.
COG0462. LUCA.
HOGENOMiHOG000210451.
HOVERGENiHBG001520.
InParanoidiP21108.
KOiK00948.
PhylomeDBiP21108.

Family and domain databases

CDDicd06223. PRTases_typeI. 1 hit.
Gene3Di3.40.50.2020. 2 hits.
HAMAPiMF_00583_B. RibP_PPkinase_B. 1 hit.
InterProiIPR000842. PRib_PP_synth_CS.
IPR029099. Pribosyltran_N.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
IPR005946. Rib-P_diPkinase.
[Graphical view]
PfamiPF14572. Pribosyl_synth. 1 hit.
PF13793. Pribosyltran_N. 1 hit.
[Graphical view]
SUPFAMiSSF53271. SSF53271. 1 hit.
TIGRFAMsiTIGR01251. ribP_PPkin. 1 hit.
PROSITEiPS00114. PRPP_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P21108-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPNIKIFSGS SHQDLSQKIA DRLGLELGKV VTKKFSNQET CVEIDESVRG
60 70 80 90 100
EDVYIVQSGC GEINDSLMEL LIMINACKIA SASRVTAVIP CFPYARQDKK
110 120 130 140 150
DKSRSPISAK LVANMLSIAG ADHIITMDLH ASQIQGFFDI PVDNLYAEPT
160 170 180 190 200
VLKWIRENIP EWKNCIIVSP DAGGAKRVTS IADQLNVDFA LIHKERKKAN
210 220 230 240 250
EVDCIVLVGD VNDRVAILVD DMADTCVTIC LAADKLLSAG ATRVYAILTH
260 270 280 290 300
GIFSGPAISR INTACFEAVV VTNTIPQDEK MKHCSKIRVI DISMILAEAI
310
RRTHNGESVS YLFSHVPL
Length:318
Mass (Da):34,839
Last modified:January 23, 2007 - v2
Checksum:i6A4EDC798FB3B296
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_050062279E → D.1 PublicationCorresponds to variant rs3800962dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57423 mRNA. Translation: AAB59463.1.
BC062797 mRNA. Translation: AAH62797.2.
CCDSiCCDS47552.1.
PIRiA37893. KIHUR3.
RefSeqiNP_787082.1. NM_175886.2.
UniGeneiHs.169284.

Genome annotation databases

GeneIDi221823.
KEGGihsa:221823.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57423 mRNA. Translation: AAB59463.1.
BC062797 mRNA. Translation: AAH62797.2.
CCDSiCCDS47552.1.
PIRiA37893. KIHUR3.
RefSeqiNP_787082.1. NM_175886.2.
UniGeneiHs.169284.

3D structure databases

ProteinModelPortaliP21108.
SMRiP21108.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128758. 6 interactors.
STRINGi9606.ENSP00000424595.

PTM databases

iPTMnetiP21108.
PhosphoSitePlusiP21108.

Polymorphism and mutation databases

BioMutaiPRPS1L1.
DMDMi125585.

2D gel databases

SWISS-2DPAGEP21108.

Proteomic databases

EPDiP21108.
MaxQBiP21108.
PaxDbiP21108.
PeptideAtlasiP21108.
PRIDEiP21108.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi221823.
KEGGihsa:221823.

Organism-specific databases

CTDi221823.
DisGeNETi221823.
GeneCardsiPRPS1L1.
H-InvDBHIX0033604.
HGNCiHGNC:9463. PRPS1L1.
MIMi611566. gene.
neXtProtiNX_P21108.
PharmGKBiPA33818.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1448. Eukaryota.
COG0462. LUCA.
HOGENOMiHOG000210451.
HOVERGENiHBG001520.
InParanoidiP21108.
KOiK00948.
PhylomeDBiP21108.

Enzyme and pathway databases

UniPathwayiUPA00087; UER00172.
BioCyciMetaCyc:HS11931-MONOMER.
ZFISH:HS11931-MONOMER.
ReactomeiR-HSA-73843. 5-Phosphoribose 1-diphosphate biosynthesis.

Miscellaneous databases

GenomeRNAii221823.
PROiP21108.
SOURCEiSearch...

Gene expression databases

CleanExiHS_PRPS1L1.

Family and domain databases

CDDicd06223. PRTases_typeI. 1 hit.
Gene3Di3.40.50.2020. 2 hits.
HAMAPiMF_00583_B. RibP_PPkinase_B. 1 hit.
InterProiIPR000842. PRib_PP_synth_CS.
IPR029099. Pribosyltran_N.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
IPR005946. Rib-P_diPkinase.
[Graphical view]
PfamiPF14572. Pribosyl_synth. 1 hit.
PF13793. Pribosyltran_N. 1 hit.
[Graphical view]
SUPFAMiSSF53271. SSF53271. 1 hit.
TIGRFAMsiTIGR01251. ribP_PPkin. 1 hit.
PROSITEiPS00114. PRPP_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPRPS3_HUMAN
AccessioniPrimary (citable) accession number: P21108
Secondary accession number(s): Q6P5P6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 145 of the entry and version 2 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

Caution

According to PubMed:2168892, this sequence initiates from a non-AUG codon; N-terminal ACG codon did serve as a start codon.Curated

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

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 one 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.