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O60256

- KPRB_HUMAN

UniProt

O60256 - KPRB_HUMAN

Protein

Phosphoribosyl pyrophosphate synthase-associated protein 2

Gene

PRPSAP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      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. bone development Source: Ensembl
    2. negative regulation of catalytic activity Source: GOC
    3. nucleobase-containing compound metabolic process Source: ProtInc
    4. nucleotide biosynthetic process Source: UniProtKB-KW

    Keywords - Biological processi

    Nucleotide biosynthesis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoribosyl pyrophosphate synthase-associated protein 2
    Short name:
    PRPP synthase-associated protein 2
    Alternative name(s):
    41 kDa phosphoribosypyrophosphate synthetase-associated protein
    Short name:
    PAP41
    Gene namesi
    Name:PRPSAP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:9467. PRPSAP2.

    Subcellular locationi

    GO - Cellular componenti

    1. ribose phosphate diphosphokinase complex Source: Ensembl

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33822.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 369369Phosphoribosyl pyrophosphate synthase-associated protein 2PRO_0000141082Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei227 – 2271Phosphoserine6 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO60256.
    PaxDbiO60256.
    PeptideAtlasiO60256.
    PRIDEiO60256.

    PTM databases

    PhosphoSiteiO60256.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiO60256.
    BgeeiO60256.
    CleanExiHS_PRPSAP2.
    GenevestigatoriO60256.

    Organism-specific databases

    HPAiHPA021881.

    Interactioni

    Subunit structurei

    Binds to PRPS1 and PRPS2.

    Protein-protein interaction databases

    BioGridi111619. 10 interactions.
    IntActiO60256. 3 interactions.
    MINTiMINT-5003869.
    STRINGi9606.ENSP00000268835.

    Structurei

    Secondary structure

    1
    369
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi21 – 244
    Helixi29 – 324
    Helixi33 – 4210
    Beta strandi49 – 535
    Beta strandi59 – 635
    Beta strandi71 – 755
    Helixi82 – 9817
    Beta strandi102 – 1076
    Helixi126 – 13611
    Beta strandi141 – 1466
    Helixi150 – 1556
    Beta strandi156 – 1583
    Beta strandi160 – 1634
    Helixi166 – 17611
    Helixi180 – 1823
    Beta strandi183 – 1897
    Helixi190 – 1923
    Helixi193 – 20210
    Beta strandi206 – 2105
    Beta strandi256 – 2583
    Beta strandi263 – 27210
    Helixi276 – 28712
    Beta strandi292 – 3009
    Helixi306 – 3127
    Beta strandi317 – 3248
    Helixi327 – 3315
    Beta strandi336 – 3394
    Helixi342 – 35413
    Beta strandi362 – 3643

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JI4X-ray2.55A13-369[»]
    ProteinModelPortaliO60256.
    SMRiO60256. Positions 19-368.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO60256.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0462.
    HOGENOMiHOG000210451.
    HOVERGENiHBG001520.
    InParanoidiO60256.
    OMAiKLLAKMM.
    PhylomeDBiO60256.
    TreeFamiTF106367.

    Family and domain databases

    Gene3Di3.40.50.2020. 3 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 (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O60256-1) [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

    MFCVTPPELE TKMNITKGGL VLFSANSNSS CMELSKKIAE RLGVEMGKVQ    50
    VYQEPNRETR VQIQESVRGK DVFIIQTVSK DVNTTIMELL IMVYACKTSC 100
    AKSIIGVIPY FPYSKQCKMR KRGSIVSKLL ASMMCKAGLT HLITMDLHQK 150
    EIQGFFNIPV DNLRASPFLL QYIQEEIPDY RNAVIVAKSP ASAKRAQSFA 200
    ERLRLGIAVI HGEAQDAESD LVDGRHSPPM VRSVAAIHPS LEIPMLIPKE 250
    KPPITVVGDV GGRIAIIVDD IIDDVDSFLA AAETLKERGA YKIFVMATHG 300
    LLSSDAPRRI EESAIDEVVV TNTIPHEVQK LQCPKIKTVD ISMILSEAIR 350
    RIHNGESMSY LFRNIGLDD 369
    Length:369
    Mass (Da):40,926
    Last modified:August 1, 1998 - v1
    Checksum:i12A0E46BD4AC55BF
    GO
    Isoform 2 (identifier: O60256-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         41-80: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:329
    Mass (Da):36,297
    Checksum:i8920D91D0C8535EF
    GO
    Isoform 3 (identifier: O60256-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         269-317: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:320
    Mass (Da):35,548
    Checksum:i4844D7A06BBE45FC
    GO
    Isoform 4 (identifier: O60256-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-86: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:283
    Mass (Da):31,322
    Checksum:i25A38F2CDBFC3429
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti121 – 1211K → R in BAG64840. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 8686Missing in isoform 4. 1 PublicationVSP_054765Add
    BLAST
    Alternative sequencei41 – 8040Missing in isoform 2. 1 PublicationVSP_044731Add
    BLAST
    Alternative sequencei269 – 31749Missing in isoform 3. 1 PublicationVSP_046462Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB007851 mRNA. Translation: BAA25435.1.
    AK303911 mRNA. Translation: BAG64840.1.
    AK304544 mRNA. Translation: BAG65341.1.
    CR457082 mRNA. Translation: CAG33363.1.
    AC090286 Genomic DNA. No translation available.
    AC107982 Genomic DNA. No translation available.
    BC106050 mRNA. Translation: AAI06051.1.
    BC101670 mRNA. Translation: AAI01671.1.
    BC101672 mRNA. Translation: AAI01673.1.
    BC143475 mRNA. Translation: AAI43476.1.
    CCDSiCCDS11200.1. [O60256-1]
    CCDS58525.1. [O60256-3]
    CCDS58526.1. [O60256-2]
    CCDS58527.1. [O60256-4]
    RefSeqiNP_001230865.1. NM_001243936.1. [O60256-2]
    NP_001230869.1. NM_001243940.1. [O60256-3]
    NP_001230870.1. NM_001243941.1. [O60256-4]
    NP_001230871.1. NM_001243942.1. [O60256-4]
    NP_002758.1. NM_002767.3. [O60256-1]
    XP_005256781.1. XM_005256724.1. [O60256-1]
    XP_005256782.1. XM_005256725.1. [O60256-1]
    XP_005256783.1. XM_005256726.1. [O60256-1]
    XP_005256784.1. XM_005256727.2. [O60256-4]
    XP_005256786.1. XM_005256729.2. [O60256-4]
    UniGeneiHs.632236.

    Genome annotation databases

    EnsembliENST00000268835; ENSP00000268835; ENSG00000141127. [O60256-1]
    ENST00000419071; ENSP00000392536; ENSG00000141127. [O60256-2]
    ENST00000536323; ENSP00000443967; ENSG00000141127. [O60256-4]
    ENST00000542013; ENSP00000439129; ENSG00000141127. [O60256-3]
    GeneIDi5636.
    KEGGihsa:5636.
    UCSCiuc002guo.2. human. [O60256-1]
    uc010vyk.2. human.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB007851 mRNA. Translation: BAA25435.1 .
    AK303911 mRNA. Translation: BAG64840.1 .
    AK304544 mRNA. Translation: BAG65341.1 .
    CR457082 mRNA. Translation: CAG33363.1 .
    AC090286 Genomic DNA. No translation available.
    AC107982 Genomic DNA. No translation available.
    BC106050 mRNA. Translation: AAI06051.1 .
    BC101670 mRNA. Translation: AAI01671.1 .
    BC101672 mRNA. Translation: AAI01673.1 .
    BC143475 mRNA. Translation: AAI43476.1 .
    CCDSi CCDS11200.1. [O60256-1 ]
    CCDS58525.1. [O60256-3 ]
    CCDS58526.1. [O60256-2 ]
    CCDS58527.1. [O60256-4 ]
    RefSeqi NP_001230865.1. NM_001243936.1. [O60256-2 ]
    NP_001230869.1. NM_001243940.1. [O60256-3 ]
    NP_001230870.1. NM_001243941.1. [O60256-4 ]
    NP_001230871.1. NM_001243942.1. [O60256-4 ]
    NP_002758.1. NM_002767.3. [O60256-1 ]
    XP_005256781.1. XM_005256724.1. [O60256-1 ]
    XP_005256782.1. XM_005256725.1. [O60256-1 ]
    XP_005256783.1. XM_005256726.1. [O60256-1 ]
    XP_005256784.1. XM_005256727.2. [O60256-4 ]
    XP_005256786.1. XM_005256729.2. [O60256-4 ]
    UniGenei Hs.632236.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2JI4 X-ray 2.55 A 13-369 [» ]
    ProteinModelPortali O60256.
    SMRi O60256. Positions 19-368.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111619. 10 interactions.
    IntActi O60256. 3 interactions.
    MINTi MINT-5003869.
    STRINGi 9606.ENSP00000268835.

    Chemistry

    BindingDBi O60256.
    ChEMBLi CHEMBL2646.

    PTM databases

    PhosphoSitei O60256.

    Proteomic databases

    MaxQBi O60256.
    PaxDbi O60256.
    PeptideAtlasi O60256.
    PRIDEi O60256.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000268835 ; ENSP00000268835 ; ENSG00000141127 . [O60256-1 ]
    ENST00000419071 ; ENSP00000392536 ; ENSG00000141127 . [O60256-2 ]
    ENST00000536323 ; ENSP00000443967 ; ENSG00000141127 . [O60256-4 ]
    ENST00000542013 ; ENSP00000439129 ; ENSG00000141127 . [O60256-3 ]
    GeneIDi 5636.
    KEGGi hsa:5636.
    UCSCi uc002guo.2. human. [O60256-1 ]
    uc010vyk.2. human.

    Organism-specific databases

    CTDi 5636.
    GeneCardsi GC17P018702.
    HGNCi HGNC:9467. PRPSAP2.
    HPAi HPA021881.
    MIMi 603762. gene.
    neXtProti NX_O60256.
    PharmGKBi PA33822.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0462.
    HOGENOMi HOG000210451.
    HOVERGENi HBG001520.
    InParanoidi O60256.
    OMAi KLLAKMM.
    PhylomeDBi O60256.
    TreeFami TF106367.

    Miscellaneous databases

    ChiTaRSi PRPSAP2. human.
    EvolutionaryTracei O60256.
    GeneWikii PRPSAP2.
    GenomeRNAii 5636.
    NextBioi 21902.
    PROi O60256.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60256.
    Bgeei O60256.
    CleanExi HS_PRPSAP2.
    Genevestigatori O60256.

    Family and domain databases

    Gene3Di 3.40.50.2020. 3 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. "Molecular cloning of a human cDNA for the 41-kDa phosphoribosylpyrophosphate synthetase-associated protein."
      Katashima R., Iwahana H., Fujimura M., Yamaoka T., Ishizuka T., Tatibana M., Itakura M.
      Biochim. Biophys. Acta 1396:245-250(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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] (ISOFORMS 2 AND 4).
      Tissue: Trachea.
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "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].
    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 AND 3).
      Tissue: Brain and Uterus.
    6. Bienvenut W.V., Waridel P., Quadroni M.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 18-36; 49-57; 61-97; 103-115; 137-181; 205-232; 250-288; 293-330; 338-350 AND 352-363, PHOSPHORYLATION AT SER-227, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryonic kidney.
    7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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].
    10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Human phosphoribosylpyrophosphate synthetase-associated protein 41 (Pap41)."
      Structural genomics consortium (SGC)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 13-369.

    Entry informationi

    Entry nameiKPRB_HUMAN
    AccessioniPrimary (citable) accession number: O60256
    Secondary accession number(s): B4E1M8
    , B4E329, B7ZKZ1, E7EMY2, Q6IAS2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 25, 2002
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 113 of the entry and version 1 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, Direct protein sequencing, 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