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Q14558

- KPRA_HUMAN

UniProt

Q14558 - KPRA_HUMAN

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
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 2 (25 Oct 2002)
      Previous versions | rss
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    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

    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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti12 – 121S → L in BAA09612. (PubMed:8611620)Curated
    Sequence conflicti54 – 541S → F in BAA09612. (PubMed:8611620)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MPKKLLLLPPPSASSAFRVP RARPVPPPAM in isoform 2. 1 PublicationVSP_039062

    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

    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: October 1, 2014
    This is version 126 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