P21108 (PRPS3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	PRPS1L1
Synonyms:	PRPS3, PRPSL

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	318 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis.
Catalytic activity	ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate.
Cofactor	Magnesium.
Enzyme regulation	Activated by magnesium and inorganic phosphate.
Pathway	Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I): step 1/1.
Subunit structure	Homodimer. The active form is probably an hexamer composed of 3 homodimers By similarity.
Tissue specificity	Testis.
Sequence similarities	Belongs to the ribose-phosphate pyrophosphokinase family.
Caution	According to Ref.1, this sequence initiates from a non-AUG codon; N-terminal ACG codon did serve as a start codon.

Ontologies

Keywords
Biological process	Nucleotide biosynthesis
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	nucleoside metabolic process Inferred from electronic annotation. Source: InterPro ribonucleoside monophosphate biosynthetic process Non-traceable author statement. Source: UniProtKB
Molecular function	ATP binding Inferred from sequence or structural similarity. Source: UniProtKB kinase activity Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: InterPro protein homodimerization activity Inferred from sequence or structural similarity. Source: UniProtKB ribose phosphate diphosphokinase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.1
	Chain	2 – 318	317	Ribose-phosphate pyrophosphokinase 3		PRO_0000141078
Regions
	Nucleotide binding	96 – 101	6	ATP By similarity
	Region	212 – 227	16	Binding of phosphoribosylpyrophosphate Potential
Sites
	Metal binding	128	1	Magnesium Potential
	Metal binding	130	1	Magnesium Potential
	Metal binding	139	1	Magnesium Potential
	Metal binding	143	1	Magnesium Potential
	Binding site	130	1	ATP By similarity
Amino acid modifications
	Modified residue	194	1	N6-acetyllysine Ref.3
Natural variations
	Natural variant	279	1	E → D. Ref.2 Corresponds to variant rs3800962 [ dbSNP | Ensembl ].		VAR_050062

Sequences

	Sequence		Length	Mass (Da)
	P21108 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 6A4EDC798FB3B296	FASTA	318	34,839
	10 20 30 40 50 60 MPNIKIFSGS SHQDLSQKIA DRLGLELGKV VTKKFSNQET CVEIDESVRG EDVYIVQSGC 70 80 90 100 110 120 GEINDSLMEL LIMINACKIA SASRVTAVIP CFPYARQDKK DKSRSPISAK LVANMLSIAG 130 140 150 160 170 180 ADHIITMDLH ASQIQGFFDI PVDNLYAEPT VLKWIRENIP EWKNCIIVSP DAGGAKRVTS 190 200 210 220 230 240 IADQLNVDFA LIHKERKKAN EVDCIVLVGD VNDRVAILVD DMADTCVTIC LAADKLLSAG 250 260 270 280 290 300 ATRVYAILTH GIFSGPAISR INTACFEAVV VTNTIPQDEK MKHCSKIRVI DISMILAEAI 310 RRTHNGESVS YLFSHVPL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A human testis-specific mRNA for phosphoribosylpyrophosphate synthetase that initiates from a non-AUG codon." Taira M., Iizasa T., Shimada H., Kudoh J., Shimizu N., Tatibana M. J. Biol. Chem. 265:16491-16497(1990) [PubMed: 2168892] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-11. Tissue: Testis.
[2]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASP-279. Tissue: Testis.
[3]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-194, MASS SPECTROMETRY.
[4]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M57423 mRNA. Translation: AAB59463.1. BC062797 mRNA. Translation: AAH62797.2.
IPI	IPI00218371.
PIR	KIHUR3. A37893.
RefSeq	NP_787082.1. NM_175886.2.
UniGene	Hs.169284.
3D structure databases
ProteinModelPortal	P21108.
SMR	P21108. Positions 3-313.
ModBase	Search...
Protein-protein interaction databases
STRING	P21108.
PTM databases
PhosphoSite	P21108.
Polymorphism databases
DMDM	125585.
2D gel databases
SWISS-2DPAGE	P21108.
Proteomic databases
PRIDE	P21108.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000430993; ENSP00000390134; ENSG00000229937.
GeneID	221823.
KEGG	hsa:221823.
NMPDR	fig|9606.3.peg.28305.
UCSC	uc003stz.1. human.
Organism-specific databases
CTD	221823.
GeneCards	GC07M018032.
H-InvDB	HIX0033604.
HGNC	HGNC:9463. PRPS1L1.
MIM	611566. gene.
neXtProt	NX_P21108.
PharmGKB	PA33818.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG18675.
GeneTree	ENSGT00550000074583.
HOGENOM	HBG519284.
HOVERGEN	HBG001520.
InParanoid	P21108.
PhylomeDB	P21108.
Enzyme and pathway databases
Reactome	REACT_474. Metabolism of carbohydrates.
Gene expression databases
ArrayExpress	P21108.
CleanEx	HS_PRPS1L1.
Genevestigator	P21108.
GermOnline	ENSG00000153287. Homo sapiens.
Family and domain databases
InterPro	IPR000842. PRib_PP_synth_CS. IPR000836. PRibTrfase. IPR005946. Rib-P_diPkinase. [Graphical view]
KO	K00948.
Pfam	PF00156. Pribosyltran. 1 hit. [Graphical view]
TIGRFAMs	TIGR01251. RibP_PPkin. 1 hit.
PROSITE	PS00114. PRPP_SYNTHASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	91465.
SOURCE	Search...

Entry information

Entry name

PRPS3_HUMAN

Accession

Primary (citable) accession number: P21108
Secondary accession number(s): Q6P5P6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	January 23, 2007
Last modified:	December 14, 2011
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.