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Reviewed, UniProtKB/Swiss-Prot Q14558 (KPRA_HUMAN)

Last modified June 16, 2009. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Phosphoribosyl pyrophosphate synthetase-associated protein 1
      Short name=PRPP synthetase-associated protein 1
Alternative name(s):
    39 kDa phosphoribosypyrophosphate synthetase-associated protein
      Short name=PAP39
Gene names
Name: PRPSAP1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length356 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Seems to play a negative regulatory role in 5-phosphoribose 1-diphosphate synthesis.

Subunit structure

Binds to PRPS1 and PRPS2.

Tissue specificity

Ubiquitous.

Sequence similarities

Belongs to the ribose-phosphate pyrophosphokinase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 356356Phosphoribosyl pyrophosphate synthetase-associated protein 1
PRO_0000141079

Amino acid modifications

Modified residue2151Phosphoserine Ref.3

Experimental info

Sequence conflict121S → L in BAA09612. Ref.1
Sequence conflict541S → F in BAA09612. Ref.1

Secondary structure

............................................................ 356
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q14558-1 [UniParc].

Last modified October 25, 2002. Version 2.
Checksum: 38CC87AB2C555717

FASTA35639,394
        10         20         30         40         50         60 
MNAARTGYRV FSANSTAACT ELAKRITERL GAELGKSVVY QETNGETRVE IKESVRGQDI 

        70         80         90        100        110        120 
FIIQTIPRDV NTAVMELLIM AYALKTACAR NIIGVIPYFP YSKQSKMRKR GSIVCKLLAS 

       130        140        150        160        170        180 
MLAKAGLTHI ITMDLHQKEI QGFFSFPVDN LRASPFLLQY IQEEIPNYRN AVIVAKSPDA 

       190        200        210        220        230        240 
AKRAQSYAER LRLGLAVIHG EAQCTELDMD DGRHSPPMVK NATVHPGLEL PLMMAKEKPP 

       250        260        270        280        290        300 
ITVVGDVGGR IAIIVDDIID DVESFVAAAE ILKERGAYKI YVMATHGILS AEAPRLIEES 

       310        320        330        340        350 
SVDEVVVTNT VPHEVQKLQC PKIKTVDISL ILSEAIRRIH NGESMAYLFR NITVDD 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequencing of human complementary DNA for the phosphoribosylpyrophosphate synthetase-associated protein 39."
Ishizuka T., Kita K., Sonoda T., Ishijima S., Sawa K., Suzuki N., Tatibana M.
Biochim. Biophys. Acta 1306:27-30(1996) [PubMed: 8611620] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Hepatoma.
[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].
Tissue: Brain.
[3]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, MASS SPECTROMETRY.
[4]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

Cross-references

Sequence databases

D61391 mRNA. Translation: BAA09612.1.
BC009012 mRNA. Translation: AAH09012.1.
IPIIPI00291578.
PIRS71460.
UniGeneHs.77498

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2C4KX-ray2.65A/B/C/D/E/F5-351[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ14558. 13 interactions.

PTM databases

PhosphoSiteQ14558.

Proteomic databases

PRIDEQ14558.

Genome annotation databases

EnsemblENSG00000161542. Homo sapiens. [Contig view]

Organism-specific databases

GeneCardsGC17M071818.
H-InvDBHIX0014196.
HGNCHGNC:9466. PRPSAP1.
MIM601249. gene.
PharmGKBPA33821.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ14558.
HOVERGENQ14558.
OMAQ14558. CAKNIIG.

Gene expression databases

ArrayExpressQ14558.
BgeeQ14558.
CleanExHS_PRPSAP1.
GermOnlineENSG00000161542. Homo sapiens.

Family and domain databases

InterProIPR000836. PRibTrfase.
IPR005946. PRPP_kinase.
[Graphical view]
PfamPF00156. Pribosyltran. 1 hit.
[Graphical view]
TIGRFAMsTIGR01251. ribP_PPkin. 1 hit.
ProtoNetSearch...

Other Resources

NextBio21898.
SOURCESearch...

Entry information

Entry nameKPRA_HUMAN
AccessionPrimary (citable) accession number: Q14558
Secondary accession number(s): Q96H06
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2002
Last sequence update: October 25, 2002
Last modified: June 16, 2009
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents