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 27-MAR-2024, entry version 153. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 85. DR IntAct; Q8WW12; 19. DR STRING; 9606.ENSP00000265260; -. DR GlyCosmos; Q8WW12; 1 site, 1 glycan. DR GlyGen; Q8WW12; 7 sites, 1 O-linked glycan (7 sites). 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; 9606-ENSP00000265260; -. DR PeptideAtlas; Q8WW12; -. DR ProteomicsDB; 74842; -. [Q8WW12-1] DR ProteomicsDB; 74843; -. [Q8WW12-2] DR ProteomicsDB; 74844; -. [Q8WW12-3] DR Pumba; Q8WW12; -. DR TopDownProteomics; Q8WW12-1; -. [Q8WW12-1] DR TopDownProteomics; Q8WW12-2; -. [Q8WW12-2] DR TopDownProteomics; Q8WW12-3; -. [Q8WW12-3] DR Antibodypedia; 32287; 204 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 AGR; HGNC:30023; -. 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; EKDMMAD; -. DR OrthoDB; 5398331at2759; -. DR PhylomeDB; Q8WW12; -. DR TreeFam; TF333058; -. DR PathwayCommons; Q8WW12; -. DR SignaLink; Q8WW12; -. DR SIGNOR; Q8WW12; -. DR BioGRID-ORCS; 57092; 67 hits in 1119 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 211 other cell types or tissues. DR ExpressionAtlas; Q8WW12; baseline and differential. 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; PEST PROTEOLYTIC SIGNAL-CONTAINING NUCLEAR PROTEIN; 1. DR PANTHER; PTHR16523:SF8; PEST PROTEOLYTIC SIGNAL-CONTAINING NUCLEAR PROTEIN; 1. DR Pfam; PF15473; PCNP; 1. DR Genevisible; Q8WW12; HS. 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 //