PCNP_HUMAN
ID PCNP_HUMAN Reviewed; 178 AA.
AC Q8WW12; B2RBE7; D3DN52; Q53GF3; Q6AI44; Q96CU3; Q9NS81;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 144.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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 PEST-
RT 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, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA 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 IDENTIFICATION
RP 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., Betts M.J.,
RA Ryningen A., Vandekerckhove J., Gevaert K., Anderson D.;
RT "The chaperone-like protein HYPK acts together with NatA in cotranslational
RT N-terminal acetylation and prevention of Huntingtin 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., Buerckstuemmer T.,
RA 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT 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., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53; SER-77; SER-87; SER-119;
RP THR-139 AND SER-147, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: May be involved in cell cycle regulation.
CC -!- SUBUNIT: Interacts with UHRF2/NIRF. {ECO:0000269|PubMed:12176013,
CC ECO:0000269|PubMed:14741369}.
CC -!- INTERACTION:
CC Q8WW12; Q92876: KLK6; NbExp=3; IntAct=EBI-10972020, EBI-2432309;
CC Q8WW12; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-10972020, EBI-750109;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12176013}.
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 Name=3;
CC IsoId=Q8WW12-3; Sequence=VSP_013879;
CC -!- PTM: Ubiquitinated; mediated by UHRF2 and leading to its subsequent
CC proteasomal degradation. {ECO:0000269|PubMed:14741369}.
CC -!- PTM: N-terminally acetylated in a HYPK-dependent manner by the NatA
CC acetyltransferase complex which is composed of NAA10 and NAA15.
CC {ECO:0000269|PubMed:20154145}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAW79790.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=EAW79792.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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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 CCDS; CCDS2942.1; -. [Q8WW12-1]
DR RefSeq; NP_001307324.1; NM_001320395.1. [Q8WW12-2]
DR RefSeq; NP_001307326.1; NM_001320397.1.
DR RefSeq; NP_001307327.1; NM_001320398.1.
DR RefSeq; NP_001307328.1; NM_001320399.1.
DR RefSeq; NP_001307329.1; NM_001320400.1.
DR RefSeq; NP_001307330.1; NM_001320401.1.
DR RefSeq; NP_065090.1; NM_020357.2. [Q8WW12-1]
DR AlphaFoldDB; Q8WW12; -.
DR BioGRID; 121360; 50.
DR IntAct; Q8WW12; 17.
DR STRING; 9606.ENSP00000265260; -.
DR GlyGen; Q8WW12; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8WW12; -.
DR PhosphoSitePlus; Q8WW12; -.
DR BioMuta; PCNP; -.
DR DMDM; 67460963; -.
DR EPD; Q8WW12; -.
DR jPOST; Q8WW12; -.
DR MassIVE; Q8WW12; -.
DR MaxQB; Q8WW12; -.
DR PaxDb; Q8WW12; -.
DR PeptideAtlas; Q8WW12; -.
DR PRIDE; Q8WW12; -.
DR ProteomicsDB; 74842; -. [Q8WW12-1]
DR ProteomicsDB; 74843; -. [Q8WW12-2]
DR ProteomicsDB; 74844; -. [Q8WW12-3]
DR TopDownProteomics; Q8WW12-1; -. [Q8WW12-1]
DR TopDownProteomics; Q8WW12-2; -. [Q8WW12-2]
DR TopDownProteomics; Q8WW12-3; -. [Q8WW12-3]
DR Antibodypedia; 32287; 176 antibodies from 27 providers.
DR DNASU; 57092; -.
DR Ensembl; ENST00000265260.8; ENSP00000265260.3; ENSG00000081154.12. [Q8WW12-1]
DR Ensembl; ENST00000469941.5; ENSP00000470810.1; ENSG00000081154.12. [Q8WW12-3]
DR GeneID; 57092; -.
DR KEGG; hsa:57092; -.
DR MANE-Select; ENST00000265260.8; ENSP00000265260.3; NM_020357.3; NP_065090.1.
DR UCSC; uc003dva.4; human. [Q8WW12-1]
DR CTD; 57092; -.
DR DisGeNET; 57092; -.
DR GeneCards; PCNP; -.
DR HGNC; HGNC:30023; PCNP.
DR HPA; ENSG00000081154; Low tissue specificity.
DR MIM; 615210; gene.
DR neXtProt; NX_Q8WW12; -.
DR OpenTargets; ENSG00000081154; -.
DR PharmGKB; PA143485572; -.
DR VEuPathDB; HostDB:ENSG00000081154; -.
DR eggNOG; ENOG502QWEZ; Eukaryota.
DR GeneTree; ENSGT00390000010218; -.
DR HOGENOM; CLU_118645_1_0_1; -.
DR InParanoid; Q8WW12; -.
DR OMA; NVHDQEN; -.
DR OrthoDB; 1616182at2759; -.
DR PhylomeDB; Q8WW12; -.
DR TreeFam; TF333058; -.
DR PathwayCommons; Q8WW12; -.
DR SignaLink; Q8WW12; -.
DR BioGRID-ORCS; 57092; 56 hits in 1041 CRISPR screens.
DR ChiTaRS; PCNP; human.
DR GenomeRNAi; 57092; -.
DR Pharos; Q8WW12; Tbio.
DR PRO; PR:Q8WW12; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q8WW12; protein.
DR Bgee; ENSG00000081154; Expressed in calcaneal tendon and 209 other tissues.
DR ExpressionAtlas; Q8WW12; baseline and differential.
DR Genevisible; Q8WW12; HS.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:HGNC-UCL.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:HGNC-UCL.
DR GO; GO:0016567; P:protein ubiquitination; IDA:HGNC-UCL.
DR InterPro; IPR029169; PCNP.
DR PANTHER; PTHR16523; PTHR16523; 1.
DR Pfam; PF15473; PCNP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell cycle; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:20154145"
FT CHAIN 2..178
FT /note="PEST proteolytic signal-containing nuclear protein"
FT /id="PRO_0000058253"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:20154145"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 64
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 139
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 150
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 152
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1..123
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_013879"
FT VAR_SEQ 119..130
FT /note="SEPEEMPPEAKM -> GYTNISWTKLLQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013880"
FT VAR_SEQ 131..178
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013881"
FT CONFLICT 126
FT /note="P -> Q (in Ref. 6; AAH22001)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="K -> E (in Ref. 3; BAD96698)"
FT /evidence="ECO:0000305"
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
