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Q14558

- KPRA_HUMAN

UniProt

Q14558 - KPRA_HUMAN

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Protein

Phosphoribosyl pyrophosphate synthase-associated protein 1

Gene
PRPSAP1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  1. enzyme inhibitor activity Source: ProtInc
  2. magnesium ion binding Source: InterPro
  3. ribose phosphate diphosphokinase activity Source: InterPro

GO - Biological processi

  1. negative regulation of kinase activity Source: Ensembl
  2. nucleobase-containing compound metabolic process Source: ProtInc
  3. nucleotide biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Nucleotide biosynthesis

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoribosyl pyrophosphate synthase-associated protein 1
Short name:
PRPP synthase-associated protein 1
Alternative name(s):
39 kDa phosphoribosypyrophosphate synthase-associated protein
Short name:
PAP39
Gene namesi
Name:PRPSAP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:9466. PRPSAP1.

Subcellular locationi

GO - Cellular componenti

  1. ribose phosphate diphosphokinase complex Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33821.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 356356Phosphoribosyl pyrophosphate synthase-associated protein 1PRO_0000141079Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei215 – 2151Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ14558.
PaxDbiQ14558.
PRIDEiQ14558.

PTM databases

PhosphoSiteiQ14558.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

ArrayExpressiQ14558.
BgeeiQ14558.
CleanExiHS_PRPSAP1.
GenevestigatoriQ14558.

Interactioni

Subunit structurei

Binds to PRPS1 and PRPS2.

Protein-protein interaction databases

BioGridi111618. 24 interactions.
IntActiQ14558. 4 interactions.
MINTiMINT-1387668.
STRINGi9606.ENSP00000414624.

Structurei

Secondary structure

1
356
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 124
Turni17 – 204
Helixi21 – 299
Beta strandi37 – 415
Beta strandi47 – 515
Beta strandi60 – 634
Helixi70 – 8617
Beta strandi92 – 987
Turni100 – 1056
Beta strandi109 – 1113
Helixi114 – 12411
Beta strandi129 – 1346
Helixi138 – 1436
Beta strandi148 – 1514
Helixi154 – 16411
Helixi168 – 1703
Beta strandi172 – 1776
Helixi178 – 1803
Helixi181 – 19111
Beta strandi194 – 1985
Beta strandi243 – 2453
Beta strandi250 – 2556
Beta strandi257 – 2615
Helixi263 – 27311
Turni274 – 2763
Beta strandi277 – 28711
Helixi293 – 2997
Beta strandi304 – 3085
Helixi314 – 3196
Beta strandi323 – 3264
Helixi329 – 34113
Helixi346 – 3494

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C4KX-ray2.65A/B/C/D/E/F5-351[»]
ProteinModelPortaliQ14558.
SMRiQ14558. Positions 7-350.

Miscellaneous databases

EvolutionaryTraceiQ14558.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0462.
HOGENOMiHOG000210451.
HOVERGENiHBG001520.
InParanoidiQ14558.
OMAiTIFIIQT.
OrthoDBiEOG793BB1.
PhylomeDBiQ14558.
TreeFamiTF106367.

Family and domain databases

Gene3Di3.40.50.2020. 2 hits.
InterProiIPR029099. Pribosyltran_N.
IPR029057. PRTase-like.
IPR005946. Rib-P_diPkinase.
[Graphical view]
PfamiPF14572. Pribosyl_synth. 1 hit.
PF13793. Pribosyltran_N. 1 hit.
[Graphical view]
SUPFAMiSSF53271. SSF53271. 2 hits.
TIGRFAMsiTIGR01251. ribP_PPkin. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q14558-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MNAARTGYRV FSANSTAACT ELAKRITERL GAELGKSVVY QETNGETRVE    50
IKESVRGQDI FIIQTIPRDV NTAVMELLIM AYALKTACAR NIIGVIPYFP 100
YSKQSKMRKR GSIVCKLLAS MLAKAGLTHI ITMDLHQKEI QGFFSFPVDN 150
LRASPFLLQY IQEEIPNYRN AVIVAKSPDA AKRAQSYAER LRLGLAVIHG 200
EAQCTELDMD DGRHSPPMVK NATVHPGLEL PLMMAKEKPP ITVVGDVGGR 250
IAIIVDDIID DVESFVAAAE ILKERGAYKI YVMATHGILS AEAPRLIEES 300
SVDEVVVTNT VPHEVQKLQC PKIKTVDISL ILSEAIRRIH NGESMAYLFR 350
NITVDD 356
Length:356
Mass (Da):39,394
Last modified:October 25, 2002 - v2
Checksum:i38CC87AB2C555717
GO
Isoform 2 (identifier: Q14558-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MPKKLLLLPPPSASSAFRVPRARPVPPPAM

Show »
Length:385
Mass (Da):42,467
Checksum:i3B9521CCB154F05D
GO

Sequence cautioni

The sequence BAG35521.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MPKKLLLLPPPSASSAFRVP RARPVPPPAM in isoform 2. VSP_039062

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121S → L in BAA09612. 1 Publication
Sequence conflicti54 – 541S → F in BAA09612. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D61391 mRNA. Translation: BAA09612.1.
AK312637 mRNA. Translation: BAG35521.1. Different initiation.
AC090699 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89386.1.
BC009012 mRNA. Translation: AAH09012.1.
CCDSiCCDS11743.2. [Q14558-2]
PIRiS71460.
RefSeqiNP_002757.2. NM_002766.2. [Q14558-2]
UniGeneiHs.77498.

Genome annotation databases

EnsembliENST00000446526; ENSP00000414624; ENSG00000161542. [Q14558-2]
GeneIDi5635.
KEGGihsa:5635.
UCSCiuc010wta.1. human. [Q14558-2]
uc010wtb.1. human. [Q14558-1]

Polymorphism databases

DMDMi24418495.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D61391 mRNA. Translation: BAA09612.1 .
AK312637 mRNA. Translation: BAG35521.1 . Different initiation.
AC090699 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89386.1 .
BC009012 mRNA. Translation: AAH09012.1 .
CCDSi CCDS11743.2. [Q14558-2 ]
PIRi S71460.
RefSeqi NP_002757.2. NM_002766.2. [Q14558-2 ]
UniGenei Hs.77498.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2C4K X-ray 2.65 A/B/C/D/E/F 5-351 [» ]
ProteinModelPortali Q14558.
SMRi Q14558. Positions 7-350.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111618. 24 interactions.
IntActi Q14558. 4 interactions.
MINTi MINT-1387668.
STRINGi 9606.ENSP00000414624.

PTM databases

PhosphoSitei Q14558.

Polymorphism databases

DMDMi 24418495.

Proteomic databases

MaxQBi Q14558.
PaxDbi Q14558.
PRIDEi Q14558.

Protocols and materials databases

DNASUi 5635.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000446526 ; ENSP00000414624 ; ENSG00000161542 . [Q14558-2 ]
GeneIDi 5635.
KEGGi hsa:5635.
UCSCi uc010wta.1. human. [Q14558-2 ]
uc010wtb.1. human. [Q14558-1 ]

Organism-specific databases

CTDi 5635.
GeneCardsi GC17M074306.
HGNCi HGNC:9466. PRPSAP1.
MIMi 601249. gene.
neXtProti NX_Q14558.
PharmGKBi PA33821.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0462.
HOGENOMi HOG000210451.
HOVERGENi HBG001520.
InParanoidi Q14558.
OMAi TIFIIQT.
OrthoDBi EOG793BB1.
PhylomeDBi Q14558.
TreeFami TF106367.

Miscellaneous databases

EvolutionaryTracei Q14558.
GeneWikii PRPSAP1.
GenomeRNAii 5635.
NextBioi 21898.
PROi Q14558.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q14558.
Bgeei Q14558.
CleanExi HS_PRPSAP1.
Genevestigatori Q14558.

Family and domain databases

Gene3Di 3.40.50.2020. 2 hits.
InterProi IPR029099. Pribosyltran_N.
IPR029057. PRTase-like.
IPR005946. Rib-P_diPkinase.
[Graphical view ]
Pfami PF14572. Pribosyl_synth. 1 hit.
PF13793. Pribosyltran_N. 1 hit.
[Graphical view ]
SUPFAMi SSF53271. SSF53271. 2 hits.
TIGRFAMsi TIGR01251. ribP_PPkin. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Hepatoma.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Lung.
  3. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1/2).
    Tissue: Brain.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Crystal structure of human phosphoribosylpyrophosphate synthetase-associated protein 39 (Pap39)."
    Structural genomics consortium (SGC)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 5-361.

Entry informationi

Entry nameiKPRA_HUMAN
AccessioniPrimary (citable) accession number: Q14558
Secondary accession number(s): B2R6M4, Q96H06
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2002
Last sequence update: October 25, 2002
Last modified: July 9, 2014
This is version 125 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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