Full text data of PCNP
PCNP
[Confidence: low (only semi-automatic identification from reviews)]
PEST proteolytic signal-containing nuclear protein; PCNP; PEST-containing nuclear protein
Note: presumably soluble (membrane word is not in UniProt keywords or features)
PEST proteolytic signal-containing nuclear protein; PCNP; PEST-containing nuclear protein
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q8WW12
ID PCNP_HUMAN Reviewed; 178 AA.
AC Q8WW12; B2RBE7; D3DN52; Q53GF3; Q6AI44; Q96CU3; Q9NS81;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 07-JUN-2005, sequence version 2.
DT 22-JAN-2014, entry version 87.
DE RecName: Full=PEST proteolytic signal-containing nuclear protein;
DE Short=PCNP;
DE Short=PEST-containing nuclear protein;
GN Name=PCNP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP INTERACTION WITH UHRF2.
RC TISSUE=Brain;
RX PubMed=12176013; DOI=10.1016/S0006-291X(02)00890-2;
RA Mori T., Li Y., Hata H., Ono K., Kochi H.;
RT "NIRF, a novel RING finger protein, is involved in cell-cycle
RT regulation.";
RL Biochem. Biophys. Res. Commun. 296:530-536(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Small intestine;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain cortex;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP UBIQUITINATION, AND INTERACTION WITH UHRF2.
RX PubMed=14741369; DOI=10.1016/S0014-5793(03)01495-9;
RA Mori T., Li Y., Hata H., Kochi H.;
RT "NIRF is a ubiquitin ligase that is capable of ubiquitinating PCNP, a
RT PEST-containing nuclear protein.";
RL FEBS Lett. 557:209-214(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87; SER-119 AND THR-139,
RP AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-64; LYS-150 AND LYS-152, AND
RP MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP ACETYLATION AT ALA-2 BY NATA ACETYLTRANSFERASE COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20154145; DOI=10.1128/MCB.01199-09;
RA Arnesen T., Starheim K.K., Van Damme P., Evjenth R., Dinh H.,
RA Betts M.J., Ryningen A., Vandekerckhove J., Gevaert K., Anderson D.;
RT "The chaperone-like protein HYPK acts together with NatA in
RT cotranslational N-terminal acetylation and prevention of Huntingtin
RT aggregation.";
RL Mol. Cell. Biol. 30:1898-1909(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119 AND SER-147, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: May be involved in cell cycle regulation.
CC -!- SUBUNIT: Interacts with UHRF2/NIRF.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8WW12-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WW12-2; Sequence=VSP_013880, VSP_013881;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q8WW12-3; Sequence=VSP_013879;
CC -!- PTM: Ubiquitinated; mediated by UHRF2 and leading to its
CC subsequent proteasomal degradation.
CC -!- PTM: N-terminally acetylated in a HYPK-dependent manner by the
CC NatA acetyltransferase complex which is composed of NAA10 and
CC NAA15.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAW79790.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=EAW79792.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; AB037675; BAB03501.1; -; mRNA.
DR EMBL; AK314629; BAG37194.1; -; mRNA.
DR EMBL; AK222978; BAD96698.1; -; mRNA.
DR EMBL; CR627371; CAH10470.1; -; mRNA.
DR EMBL; CH471052; EAW79790.1; ALT_INIT; Genomic_DNA.
DR EMBL; CH471052; EAW79792.1; ALT_INIT; Genomic_DNA.
DR EMBL; BC013916; AAH13916.1; -; mRNA.
DR EMBL; BC022001; AAH22001.1; -; mRNA.
DR RefSeq; NP_065090.1; NM_020357.1.
DR UniGene; Hs.744968; -.
DR ProteinModelPortal; Q8WW12; -.
DR STRING; 9606.ENSP00000265260; -.
DR PhosphoSite; Q8WW12; -.
DR DMDM; 67460963; -.
DR PaxDb; Q8WW12; -.
DR PRIDE; Q8WW12; -.
DR DNASU; 57092; -.
DR Ensembl; ENST00000265260; ENSP00000265260; ENSG00000081154.
DR Ensembl; ENST00000296024; ENSP00000296024; ENSG00000081154.
DR Ensembl; ENST00000469941; ENSP00000470810; ENSG00000081154.
DR GeneID; 57092; -.
DR KEGG; hsa:57092; -.
DR UCSC; uc003dva.3; human.
DR CTD; 57092; -.
DR GeneCards; GC03P101292; -.
DR HGNC; HGNC:30023; PCNP.
DR HPA; HPA035011; -.
DR MIM; 615210; gene.
DR neXtProt; NX_Q8WW12; -.
DR PharmGKB; PA143485572; -.
DR eggNOG; NOG46363; -.
DR HOVERGEN; HBG059581; -.
DR InParanoid; Q8WW12; -.
DR OMA; PAKMSKF; -.
DR OrthoDB; EOG7J70HR; -.
DR PhylomeDB; Q8WW12; -.
DR ChiTaRS; PCNP; human.
DR GenomeRNAi; 57092; -.
DR NextBio; 35489760; -.
DR PRO; PR:Q8WW12; -.
DR ArrayExpress; Q8WW12; -.
DR Bgee; Q8WW12; -.
DR CleanEx; HS_PCNP; -.
DR Genevestigator; Q8WW12; -.
DR GO; GO:0005634; C:nucleus; IDA:HGNC.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:HGNC.
DR GO; GO:0016567; P:protein ubiquitination; IDA:HGNC.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell cycle; Complete proteome;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 178 PEST proteolytic signal-containing
FT nuclear protein.
FT /FTId=PRO_0000058253.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 64 64 N6-acetyllysine.
FT MOD_RES 87 87 Phosphoserine.
FT MOD_RES 119 119 Phosphoserine.
FT MOD_RES 139 139 Phosphothreonine.
FT MOD_RES 147 147 Phosphoserine.
FT MOD_RES 150 150 N6-acetyllysine.
FT MOD_RES 152 152 N6-acetyllysine.
FT VAR_SEQ 1 123 Missing (in isoform 3).
FT /FTId=VSP_013879.
FT VAR_SEQ 119 130 SEPEEMPPEAKM -> GYTNISWTKLLQ (in isoform
FT 2).
FT /FTId=VSP_013880.
FT VAR_SEQ 131 178 Missing (in isoform 2).
FT /FTId=VSP_013881.
FT CONFLICT 126 126 P -> Q (in Ref. 6; AAH22001).
FT CONFLICT 150 150 K -> E (in Ref. 3; BAD96698).
SQ SEQUENCE 178 AA; 18925 MW; B79D49B362892AE1 CRC64;
MADGKAGDEK PEKSQRAGAA GGPEEEAEKP VKTKTVSSSN GGESSSRSAE KRSAEEEAAD
LPTKPTKISK FGFAIGSQTT KKASAISIKL GSSKPKETVP TLAPKTLSVA AAFNEDEDSE
PEEMPPEAKM RMKNIGRDTP TSAGPNSFNK GKHGFSDNQK LWERNIKSHL GNVHDQDN
//
ID PCNP_HUMAN Reviewed; 178 AA.
AC Q8WW12; B2RBE7; D3DN52; Q53GF3; Q6AI44; Q96CU3; Q9NS81;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 07-JUN-2005, sequence version 2.
DT 22-JAN-2014, entry version 87.
DE RecName: Full=PEST proteolytic signal-containing nuclear protein;
DE Short=PCNP;
DE Short=PEST-containing nuclear protein;
GN Name=PCNP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP INTERACTION WITH UHRF2.
RC TISSUE=Brain;
RX PubMed=12176013; DOI=10.1016/S0006-291X(02)00890-2;
RA Mori T., Li Y., Hata H., Ono K., Kochi H.;
RT "NIRF, a novel RING finger protein, is involved in cell-cycle
RT regulation.";
RL Biochem. Biophys. Res. Commun. 296:530-536(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Small intestine;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain cortex;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP UBIQUITINATION, AND INTERACTION WITH UHRF2.
RX PubMed=14741369; DOI=10.1016/S0014-5793(03)01495-9;
RA Mori T., Li Y., Hata H., Kochi H.;
RT "NIRF is a ubiquitin ligase that is capable of ubiquitinating PCNP, a
RT PEST-containing nuclear protein.";
RL FEBS Lett. 557:209-214(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87; SER-119 AND THR-139,
RP AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-64; LYS-150 AND LYS-152, AND
RP MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP ACETYLATION AT ALA-2 BY NATA ACETYLTRANSFERASE COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20154145; DOI=10.1128/MCB.01199-09;
RA Arnesen T., Starheim K.K., Van Damme P., Evjenth R., Dinh H.,
RA Betts M.J., Ryningen A., Vandekerckhove J., Gevaert K., Anderson D.;
RT "The chaperone-like protein HYPK acts together with NatA in
RT cotranslational N-terminal acetylation and prevention of Huntingtin
RT aggregation.";
RL Mol. Cell. Biol. 30:1898-1909(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119 AND SER-147, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: May be involved in cell cycle regulation.
CC -!- SUBUNIT: Interacts with UHRF2/NIRF.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8WW12-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WW12-2; Sequence=VSP_013880, VSP_013881;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q8WW12-3; Sequence=VSP_013879;
CC -!- PTM: Ubiquitinated; mediated by UHRF2 and leading to its
CC subsequent proteasomal degradation.
CC -!- PTM: N-terminally acetylated in a HYPK-dependent manner by the
CC NatA acetyltransferase complex which is composed of NAA10 and
CC NAA15.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAW79790.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=EAW79792.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; AB037675; BAB03501.1; -; mRNA.
DR EMBL; AK314629; BAG37194.1; -; mRNA.
DR EMBL; AK222978; BAD96698.1; -; mRNA.
DR EMBL; CR627371; CAH10470.1; -; mRNA.
DR EMBL; CH471052; EAW79790.1; ALT_INIT; Genomic_DNA.
DR EMBL; CH471052; EAW79792.1; ALT_INIT; Genomic_DNA.
DR EMBL; BC013916; AAH13916.1; -; mRNA.
DR EMBL; BC022001; AAH22001.1; -; mRNA.
DR RefSeq; NP_065090.1; NM_020357.1.
DR UniGene; Hs.744968; -.
DR ProteinModelPortal; Q8WW12; -.
DR STRING; 9606.ENSP00000265260; -.
DR PhosphoSite; Q8WW12; -.
DR DMDM; 67460963; -.
DR PaxDb; Q8WW12; -.
DR PRIDE; Q8WW12; -.
DR DNASU; 57092; -.
DR Ensembl; ENST00000265260; ENSP00000265260; ENSG00000081154.
DR Ensembl; ENST00000296024; ENSP00000296024; ENSG00000081154.
DR Ensembl; ENST00000469941; ENSP00000470810; ENSG00000081154.
DR GeneID; 57092; -.
DR KEGG; hsa:57092; -.
DR UCSC; uc003dva.3; human.
DR CTD; 57092; -.
DR GeneCards; GC03P101292; -.
DR HGNC; HGNC:30023; PCNP.
DR HPA; HPA035011; -.
DR MIM; 615210; gene.
DR neXtProt; NX_Q8WW12; -.
DR PharmGKB; PA143485572; -.
DR eggNOG; NOG46363; -.
DR HOVERGEN; HBG059581; -.
DR InParanoid; Q8WW12; -.
DR OMA; PAKMSKF; -.
DR OrthoDB; EOG7J70HR; -.
DR PhylomeDB; Q8WW12; -.
DR ChiTaRS; PCNP; human.
DR GenomeRNAi; 57092; -.
DR NextBio; 35489760; -.
DR PRO; PR:Q8WW12; -.
DR ArrayExpress; Q8WW12; -.
DR Bgee; Q8WW12; -.
DR CleanEx; HS_PCNP; -.
DR Genevestigator; Q8WW12; -.
DR GO; GO:0005634; C:nucleus; IDA:HGNC.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:HGNC.
DR GO; GO:0016567; P:protein ubiquitination; IDA:HGNC.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell cycle; Complete proteome;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 178 PEST proteolytic signal-containing
FT nuclear protein.
FT /FTId=PRO_0000058253.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 64 64 N6-acetyllysine.
FT MOD_RES 87 87 Phosphoserine.
FT MOD_RES 119 119 Phosphoserine.
FT MOD_RES 139 139 Phosphothreonine.
FT MOD_RES 147 147 Phosphoserine.
FT MOD_RES 150 150 N6-acetyllysine.
FT MOD_RES 152 152 N6-acetyllysine.
FT VAR_SEQ 1 123 Missing (in isoform 3).
FT /FTId=VSP_013879.
FT VAR_SEQ 119 130 SEPEEMPPEAKM -> GYTNISWTKLLQ (in isoform
FT 2).
FT /FTId=VSP_013880.
FT VAR_SEQ 131 178 Missing (in isoform 2).
FT /FTId=VSP_013881.
FT CONFLICT 126 126 P -> Q (in Ref. 6; AAH22001).
FT CONFLICT 150 150 K -> E (in Ref. 3; BAD96698).
SQ SEQUENCE 178 AA; 18925 MW; B79D49B362892AE1 CRC64;
MADGKAGDEK PEKSQRAGAA GGPEEEAEKP VKTKTVSSSN GGESSSRSAE KRSAEEEAAD
LPTKPTKISK FGFAIGSQTT KKASAISIKL GSSKPKETVP TLAPKTLSVA AAFNEDEDSE
PEEMPPEAKM RMKNIGRDTP TSAGPNSFNK GKHGFSDNQK LWERNIKSHL GNVHDQDN
//
MIM
615210
*RECORD*
*FIELD* NO
615210
*FIELD* TI
*615210 PEST-CONTAINING NUCLEAR PROTEIN; PCNP
*FIELD* TX
CLONING
By searching a database for genes encoding proteins containing PEST
read moremotifs, followed by 5-prime cap-site hunting with a human brain cDNA
library, Mori et al. (2002) cloned PCNP. The deduced 178-amino acid
protein contains 2 PEST sequences, each with a potential phosphorylation
site. Fluorescence-tagged PCNP localized to nucleoplasm of transfected
COS-7 cells.
GENE FUNCTION
Using yeast 2-hybrid analysis of a fetal brain cDNA library, mammalian
2-hybrid analysis of transfected COS-7 cells, and in vitro protein
pull-down assays, Mori et al. (2002) found that PCNP interacted with
NIRF (UHRF2; 615211).
MAPPING
Hartz (2013) mapped the PCNP gene to chromosome 3q12.3 based on an
alignment of the PCNP sequence (GenBank GENBANK AB037675) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 4/30/2013.
2. Mori, T.; Li, Y.; Hata, H.; Ono, K.; Kochi, H.: NIRF, a novel
RING finger protein, is involved in cell-cycle regulation. Biochem.
Biophys. Res. Commun. 296: 530-536, 2002.
*FIELD* CD
Patricia A. Hartz: 4/30/2013
*FIELD* ED
mgross: 04/30/2013
*RECORD*
*FIELD* NO
615210
*FIELD* TI
*615210 PEST-CONTAINING NUCLEAR PROTEIN; PCNP
*FIELD* TX
CLONING
By searching a database for genes encoding proteins containing PEST
read moremotifs, followed by 5-prime cap-site hunting with a human brain cDNA
library, Mori et al. (2002) cloned PCNP. The deduced 178-amino acid
protein contains 2 PEST sequences, each with a potential phosphorylation
site. Fluorescence-tagged PCNP localized to nucleoplasm of transfected
COS-7 cells.
GENE FUNCTION
Using yeast 2-hybrid analysis of a fetal brain cDNA library, mammalian
2-hybrid analysis of transfected COS-7 cells, and in vitro protein
pull-down assays, Mori et al. (2002) found that PCNP interacted with
NIRF (UHRF2; 615211).
MAPPING
Hartz (2013) mapped the PCNP gene to chromosome 3q12.3 based on an
alignment of the PCNP sequence (GenBank GENBANK AB037675) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 4/30/2013.
2. Mori, T.; Li, Y.; Hata, H.; Ono, K.; Kochi, H.: NIRF, a novel
RING finger protein, is involved in cell-cycle regulation. Biochem.
Biophys. Res. Commun. 296: 530-536, 2002.
*FIELD* CD
Patricia A. Hartz: 4/30/2013
*FIELD* ED
mgross: 04/30/2013