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Q8WW12

- PCNP_HUMAN

UniProt

Q8WW12 - PCNP_HUMAN

Protein

PEST proteolytic signal-containing nuclear protein

Gene

PCNP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 2 (07 Jun 2005)
      Previous versions | rss
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    Functioni

    May be involved in cell cycle regulation.

    GO - Molecular functioni

    1. protein binding Source: HGNC

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. proteasome-mediated ubiquitin-dependent protein catabolic process Source: HGNC
    3. protein ubiquitination Source: HGNC

    Keywords - Biological processi

    Cell cycle

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    PEST proteolytic signal-containing nuclear protein
    Short name:
    PCNP
    Short name:
    PEST-containing nuclear protein
    Gene namesi
    Name:PCNP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:30023. PCNP.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. nucleus Source: HGNC

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA143485572.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 178177PEST proteolytic signal-containing nuclear proteinPRO_0000058253Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei64 – 641N6-acetyllysine1 Publication
    Modified residuei87 – 871Phosphoserine1 Publication
    Modified residuei119 – 1191Phosphoserine2 Publications
    Modified residuei139 – 1391Phosphothreonine1 Publication
    Modified residuei147 – 1471Phosphoserine1 Publication
    Modified residuei150 – 1501N6-acetyllysine1 Publication
    Modified residuei152 – 1521N6-acetyllysine1 Publication

    Post-translational modificationi

    Ubiquitinated; mediated by UHRF2 and leading to its subsequent proteasomal degradation.1 Publication
    N-terminally acetylated in a HYPK-dependent manner by the NatA acetyltransferase complex which is composed of NAA10 and NAA15.2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ8WW12.
    PaxDbiQ8WW12.
    PRIDEiQ8WW12.

    PTM databases

    PhosphoSiteiQ8WW12.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8WW12.
    BgeeiQ8WW12.
    CleanExiHS_PCNP.
    GenevestigatoriQ8WW12.

    Organism-specific databases

    HPAiHPA035011.

    Interactioni

    Subunit structurei

    Interacts with UHRF2/NIRF.2 Publications

    Protein-protein interaction databases

    BioGridi121360. 7 interactions.
    STRINGi9606.ENSP00000265260.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8WW12.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Phylogenomic databases

    eggNOGiNOG46363.
    HOVERGENiHBG059581.
    InParanoidiQ8WW12.
    OMAiPAKMSKF.
    OrthoDBiEOG7J70HR.
    PhylomeDBiQ8WW12.
    TreeFamiTF333058.

    Family and domain databases

    InterProiIPR029169. PCNP.
    [Graphical view]
    PANTHERiPTHR16523. PTHR16523. 1 hit.
    PfamiPF15473. PCNP. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8WW12-1) [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

    MADGKAGDEK PEKSQRAGAA GGPEEEAEKP VKTKTVSSSN GGESSSRSAE    50
    KRSAEEEAAD LPTKPTKISK FGFAIGSQTT KKASAISIKL GSSKPKETVP 100
    TLAPKTLSVA AAFNEDEDSE PEEMPPEAKM RMKNIGRDTP TSAGPNSFNK 150
    GKHGFSDNQK LWERNIKSHL GNVHDQDN 178
    Length:178
    Mass (Da):18,925
    Last modified:June 7, 2005 - v2
    Checksum:iB79D49B362892AE1
    GO
    Isoform 2 (identifier: Q8WW12-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         119-130: SEPEEMPPEAKM → GYTNISWTKLLQ
         131-178: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:130
    Mass (Da):13,544
    Checksum:i60256023D3435196
    GO
    Isoform 3 (identifier: Q8WW12-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-123: Missing.

    Show »
    Length:55
    Mass (Da):6,233
    Checksum:iC95818E33C1461F0
    GO

    Sequence cautioni

    The sequence EAW79790.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence EAW79792.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti126 – 1261P → Q in AAH22001. (PubMed:15489334)Curated
    Sequence conflicti150 – 1501K → E in BAD96698. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 123123Missing in isoform 3. 1 PublicationVSP_013879Add
    BLAST
    Alternative sequencei119 – 13012SEPEE…PEAKM → GYTNISWTKLLQ in isoform 2. 1 PublicationVSP_013880Add
    BLAST
    Alternative sequencei131 – 17848Missing in isoform 2. 1 PublicationVSP_013881Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB037675 mRNA. Translation: BAB03501.1.
    AK314629 mRNA. Translation: BAG37194.1.
    AK222978 mRNA. Translation: BAD96698.1.
    CR627371 mRNA. Translation: CAH10470.1.
    CH471052 Genomic DNA. Translation: EAW79790.1. Different initiation.
    CH471052 Genomic DNA. Translation: EAW79792.1. Different initiation.
    BC013916 mRNA. Translation: AAH13916.1.
    BC022001 mRNA. Translation: AAH22001.1.
    CCDSiCCDS2942.1. [Q8WW12-1]
    RefSeqiNP_065090.1. NM_020357.1. [Q8WW12-1]
    UniGeneiHs.744968.

    Genome annotation databases

    EnsembliENST00000265260; ENSP00000265260; ENSG00000081154. [Q8WW12-1]
    ENST00000469941; ENSP00000470810; ENSG00000081154. [Q8WW12-3]
    GeneIDi57092.
    KEGGihsa:57092.
    UCSCiuc003dva.3. human. [Q8WW12-1]
    uc003dvd.3. human. [Q8WW12-2]

    Polymorphism databases

    DMDMi67460963.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB037675 mRNA. Translation: BAB03501.1 .
    AK314629 mRNA. Translation: BAG37194.1 .
    AK222978 mRNA. Translation: BAD96698.1 .
    CR627371 mRNA. Translation: CAH10470.1 .
    CH471052 Genomic DNA. Translation: EAW79790.1 . Different initiation.
    CH471052 Genomic DNA. Translation: EAW79792.1 . Different initiation.
    BC013916 mRNA. Translation: AAH13916.1 .
    BC022001 mRNA. Translation: AAH22001.1 .
    CCDSi CCDS2942.1. [Q8WW12-1 ]
    RefSeqi NP_065090.1. NM_020357.1. [Q8WW12-1 ]
    UniGenei Hs.744968.

    3D structure databases

    ProteinModelPortali Q8WW12.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121360. 7 interactions.
    STRINGi 9606.ENSP00000265260.

    PTM databases

    PhosphoSitei Q8WW12.

    Polymorphism databases

    DMDMi 67460963.

    Proteomic databases

    MaxQBi Q8WW12.
    PaxDbi Q8WW12.
    PRIDEi Q8WW12.

    Protocols and materials databases

    DNASUi 57092.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265260 ; ENSP00000265260 ; ENSG00000081154 . [Q8WW12-1 ]
    ENST00000469941 ; ENSP00000470810 ; ENSG00000081154 . [Q8WW12-3 ]
    GeneIDi 57092.
    KEGGi hsa:57092.
    UCSCi uc003dva.3. human. [Q8WW12-1 ]
    uc003dvd.3. human. [Q8WW12-2 ]

    Organism-specific databases

    CTDi 57092.
    GeneCardsi GC03P101292.
    HGNCi HGNC:30023. PCNP.
    HPAi HPA035011.
    MIMi 615210. gene.
    neXtProti NX_Q8WW12.
    PharmGKBi PA143485572.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG46363.
    HOVERGENi HBG059581.
    InParanoidi Q8WW12.
    OMAi PAKMSKF.
    OrthoDBi EOG7J70HR.
    PhylomeDBi Q8WW12.
    TreeFami TF333058.

    Miscellaneous databases

    ChiTaRSi PCNP. human.
    GenomeRNAii 57092.
    NextBioi 35489760.
    PROi Q8WW12.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8WW12.
    Bgeei Q8WW12.
    CleanExi HS_PCNP.
    Genevestigatori Q8WW12.

    Family and domain databases

    InterProi IPR029169. PCNP.
    [Graphical view ]
    PANTHERi PTHR16523. PTHR16523. 1 hit.
    Pfami PF15473. PCNP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "NIRF, a novel RING finger protein, is involved in cell-cycle regulation."
      Mori T., Li Y., Hata H., Ono K., Kochi H.
      Biochem. Biophys. Res. Commun. 296:530-536(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INTERACTION WITH UHRF2.
      Tissue: Brain.
    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 1).
    3. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Small intestine.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Brain cortex.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 2).
      Tissue: Brain and Testis.
    7. "NIRF is a ubiquitin ligase that is capable of ubiquitinating PCNP, a PEST-containing nuclear protein."
      Mori T., Li Y., Hata H., Kochi H.
      FEBS Lett. 557:209-214(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, INTERACTION WITH UHRF2.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87; SER-119 AND THR-139, 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-64; LYS-150 AND LYS-152, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "The chaperone-like protein HYPK acts together with NatA in cotranslational N-terminal acetylation and prevention of Huntingtin aggregation."
      Arnesen T., Starheim K.K., Van Damme P., Evjenth R., Dinh H., Betts M.J., Ryningen A., Vandekerckhove J., Gevaert K., Anderson D.
      Mol. Cell. Biol. 30:1898-1909(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT ALA-2 BY NATA ACETYLTRANSFERASE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    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-119 AND SER-147, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPCNP_HUMAN
    AccessioniPrimary (citable) accession number: Q8WW12
    Secondary accession number(s): B2RBE7
    , D3DN52, Q53GF3, Q6AI44, Q96CU3, Q9NS81
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: June 7, 2005
    Last modified: October 1, 2014
    This is version 93 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

    External Data

    Dasty 3