P11908 (PRPS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribose-phosphate pyrophosphokinase 2
EC=2.7.6.1

Alternative name(s):
PPRibP
Phosphoribosyl pyrophosphate synthase II
Short name=PRS-II

Gene names

Name:

PRPS2

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. Competitively or non-competitively inhibited by ADP, 2,3-bisphosphoglyceride or GDP.
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.
Sequence similarities	Belongs to the ribose-phosphate pyrophosphokinase family.
Sequence caution	The sequence AAH30019.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Nucleotide biosynthesis
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase
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 Inferred from electronic annotation. Source: InterPro
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...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P11908-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P11908-2)

The sequence of this isoform differs from the canonical sequence as follows:
     102-102: K → KVGE

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.5
	Chain	2 – 318	317	Ribose-phosphate pyrophosphokinase 2		PRO_0000141074
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
	Site	2	1	Not acetylated
Natural variations
	Alternative sequence	102	1	K → KVGE in isoform 2.		VSP_027769

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 72A2873408250C31	FASTA	318	34,769
	10 20 30 40 50 60 MPNIVLFSGS SHQDLSQRVA DRLGLELGKV VTKKFSNQET SVEIGESVRG EDVYIIQSGC 70 80 90 100 110 120 GEINDNLMEL LIMINACKIA SSSRVTAVIP CFPYARQDKK DKSRAPISAK LVANMLSVAG 130 140 150 160 170 180 ADHIITMDLH ASQIQGFFDI PVDNLYAEPA VLQWIRENIA EWKNCIIVSP DAGGAKRVTS 190 200 210 220 230 240 IADRLNVEFA LIHKERKKAN EVDRMVLVGD VKDRVAILVD DMADTCGTIC HAADKLLSAG 250 260 270 280 290 300 ATKVYAILTH GIFSGPAISR INNAAFEAVV VTNTIPQEDK MKHCTKIQVI DISMILAEAI 310 RRTHNGESVS YLFSHVPL
	Isoform 2 [UniParc]. Checksum: EDD88B9D33A55A37	FASTA	321	35,054
	10 20 30 40 50 60 MPNIVLFSGS SHQDLSQRVA DRLGLELGKV VTKKFSNQET SVEIGESVRG EDVYIIQSGC 70 80 90 100 110 120 GEINDNLMEL LIMINACKIA SSSRVTAVIP CFPYARQDKK DKVGESRAPI SAKLVANMLS 130 140 150 160 170 180 VAGADHIITM DLHASQIQGF FDIPVDNLYA EPAVLQWIRE NIAEWKNCII VSPDAGGAKR 190 200 210 220 230 240 VTSIADRLNV EFALIHKERK KANEVDRMVL VGDVKDRVAI LVDDMADTCG TICHAADKLL 250 260 270 280 290 300 SAGATKVYAI LTHGIFSGPA ISRINNAAFE AVVVTNTIPQ EDKMKHCTKI QVIDISMILA 310 320 EAIRRTHNGE SVSYLFSHVP L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and sequencing of human cDNA for phosphoribosyl pyrophosphate synthetase subunit II." Iizasa T., Taira M., Shimada H., Ishijima S., Tatibana M. FEBS Lett. 244:47-50(1989) [PubMed: 2538352] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Testis.
[2]	"Deduced amino acid sequence from human phosphoribosylpyrophosphate synthetase subunit II cDNA." Iizasa T., Taira M., Shimada H., Tatibana M. Adv. Exp. Med. Biol. 253A:519-523(1989) [PubMed: 2560337] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Testis.
[3]	"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] (ISOFORMS 1 AND 2). Tissue: Testis and Uterus.
[4]	"Promoter regions of the human X-linked housekeeping genes PRPS1 and PRPS2 encoding phosphoribosylpyrophosphate synthetase subunit I and II isoforms." Ishizuka T., Iizasa T., Taira M., Ishijima S., Sonoda T., Shimada H., Nagatake N., Tatibana M. Biochim. Biophys. Acta 1130:139-148(1992) [PubMed: 1314091] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40. Tissue: Leukocyte.
[5]	Bienvenut W.V., Calvo F., Bensaad K., Vousden K.H., Matallanas D., Cooper W.N., Kolch W., Lourenco F., Olson M.F. Submitted (DEC-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-29; 34-49; 85-96; 164-196; 205-214; 244-282 AND 287-318, CLEAVAGE OF INITIATOR METHIONINE, LACK OF N-TERMINAL ACETYLATION, MASS SPECTROMETRY. Tissue: Cervix carcinoma, Mammary carcinoma and Osteosarcoma.
[6]	"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	Y00971 mRNA. Translation: CAA68785.1. BC030019 mRNA. Translation: AAH30019.2. Different initiation. BC040483 mRNA. Translation: AAH40483.3. BC110875 mRNA. Translation: AAI10876.2. BC119662 mRNA. Translation: AAI19663.1. BC119663 mRNA. Translation: AAI19664.1. D28134 Genomic DNA. Translation: BAA05676.1.
IPI	IPI00219617. IPI00718888.
PIR	KIHUR2. S02778.
RefSeq	NP_001034180.1. NM_001039091.2. NP_002756.1. NM_002765.4.
UniGene	Hs.654581.
3D structure databases
ProteinModelPortal	P11908.
SMR	P11908. Positions 3-317.
ModBase	Search...
Protein-protein interaction databases
STRING	P11908.
PTM databases
PhosphoSite	P11908.
Polymorphism databases
DMDM	125583.
2D gel databases
REPRODUCTION-2DPAGE	IPI00219617. P11908.
Proteomic databases
PRIDE	P11908.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000380668; ENSP00000370043; ENSG00000101911.
GeneID	5634.
KEGG	hsa:5634.
UCSC	uc004cva.1. human. uc004cvb.1. human.
Organism-specific databases
CTD	5634.
GeneCards	GC0XP012719.
H-InvDB	HIX0028452.
HGNC	HGNC:9465. PRPS2.
MIM	311860. gene.
neXtProt	NX_P11908.
PharmGKB	PA33820.
GenAtlas	Search...
Phylogenomic databases
eggNOG	maNOG05340.
GeneTree	ENSGT00550000074583.
HOVERGEN	HBG001520.
OMA	TRISPTE.
PhylomeDB	P11908.
Enzyme and pathway databases
Reactome	REACT_474. Metabolism of carbohydrates.
Gene expression databases
ArrayExpress	P11908.
Bgee	P11908.
CleanEx	HS_PRPS2.
Genevestigator	P11908.
GermOnline	ENSG00000101911. 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	21892.
SOURCE	Search...

Entry information

Entry name

PRPS2_HUMAN

Accession

Primary (citable) accession number: P11908
Secondary accession number(s): Q0VDH9 , Q0VDI0, Q15245, Q2TAK7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 131 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.