PPHLN_HUMAN
ID PPHLN_HUMAN Reviewed; 458 AA.
AC Q8NEY8; E9PAX8; Q86YT2; Q8IXN3; Q8TB09; Q96NB9; Q9NXL4; Q9P0P6; Q9P0R9;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Periphilin-1 {ECO:0000303|PubMed:12853457};
DE AltName: Full=CDC7 expression repressor {ECO:0000303|PubMed:15474462};
DE Short=CR {ECO:0000303|PubMed:15474462};
DE AltName: Full=Gastric cancer antigen Ga50 {ECO:0000303|PubMed:12087473};
GN Name=PPHLN1 {ECO:0000312|HGNC:HGNC:19369}; ORFNames=HSPC206, HSPC232;
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).
RC TISSUE=Gastric adenocarcinoma;
RX PubMed=12087473; DOI=10.1038/sj.bjc.6600321;
RA Line A., Stengrevics A., Slucka Z., Li G., Jankevics E., Rees R.C.;
RT "Serological identification and expression analysis of gastric cancer-
RT associated genes.";
RL Br. J. Cancer 86:1824-1830(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING,
RP HOMODIMERIZATION, INTERACTION WITH PPL, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Keratinocyte;
RX PubMed=12853457; DOI=10.1074/jbc.m303896200;
RA Kazerounian S., Aho S.;
RT "Characterization of periphilin, a widespread, highly insoluble nuclear
RT protein and potential constituent of the keratinocyte cornified envelope.";
RL J. Biol. Chem. 278:36707-36717(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 7 AND 8).
RC TISSUE=Colon;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9).
RC TISSUE=Placenta;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5).
RC TISSUE=Brain, and Skin;
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 [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15474462; DOI=10.1016/j.bbrc.2004.09.083;
RA Kurita M., Suzuki H., Masai H., Mizumoto K., Ogata E., Nishimoto I.,
RA Aiso S., Matsuoka M.;
RT "Overexpression of CR/periphilin downregulates Cdc7 expression and induces
RT S-phase arrest.";
RL Biochem. Biophys. Res. Commun. 324:554-561(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133 AND SER-140, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [11]
RP FUNCTION, AND INTERACTION WITH SIN3A AND HDAC1.
RX PubMed=17963697; DOI=10.1016/j.bbrc.2007.10.090;
RA Kurita M., Suzuki H., Kawano Y., Aiso S., Matsuoka M.;
RT "CR/periphilin is a transcriptional co-repressor involved in cell cycle
RT progression.";
RL Biochem. Biophys. Res. Commun. 364:930-936(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133 AND SER-197, 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 [15]
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 [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-235 AND LYS-240, 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; SER-133; SER-161;
RP SER-167 AND SER-205, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133 AND SER-205, 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; SER-114; SER-133;
RP SER-197; SER-201 AND SER-325, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE 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).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-240 AND LYS-453, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-240, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [23]
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE HUSH COMPLEX.
RX PubMed=26022416; DOI=10.1126/science.aaa7227;
RA Tchasovnikarova I.A., Timms R.T., Matheson N.J., Wals K., Antrobus R.,
RA Goettgens B., Dougan G., Dawson M.A., Lehner P.J.;
RT "Epigenetic silencing by the HUSH complex mediates position-effect
RT variegation in human cells.";
RL Science 348:1481-1485(2015).
RN [24]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-109; LYS-160; LYS-180; LYS-199;
RP LYS-227; LYS-235; LYS-240 AND LYS-328, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [25]
RP FUNCTION.
RX PubMed=30487602; DOI=10.1038/s41586-018-0750-6;
RA Zhu Y., Wang G.Z., Cingoez O., Goff S.P.;
RT "NP220 mediates silencing of unintegrated retroviral DNA.";
RL Nature 564:278-282(2018).
RN [26]
RP VARIANT [LARGE SCALE ANALYSIS] MET-173.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Component of the HUSH complex, a multiprotein complex that
CC mediates epigenetic repression. The HUSH complex is recruited to
CC genomic loci rich in H3K9me3 and is probably required to maintain
CC transcriptional silencing by promoting recruitment of SETDB1, a histone
CC methyltransferase that mediates further deposition of H3K9me3. In the
CC HUSH complex, contributes to the maintenance of the complex at
CC chromatin (PubMed:26022416). Acts as a transcriptional corepressor and
CC regulates the cell cycle, probably via the HUSH complex
CC (PubMed:15474462, PubMed:17963697). The HUSH complex is also involved
CC in the silencing of unintegrated retroviral DNA: some part of the
CC retroviral DNA formed immediately after infection remains unintegrated
CC in the host genome and is transcriptionally repressed
CC (PubMed:30487602). May be involved in epithelial differentiation by
CC contributing to epidermal integrity and barrier formation
CC (PubMed:12853457). {ECO:0000269|PubMed:15474462,
CC ECO:0000269|PubMed:17963697, ECO:0000269|PubMed:26022416,
CC ECO:0000269|PubMed:30487602, ECO:0000305|PubMed:12853457}.
CC -!- SUBUNIT: Homodimer (PubMed:12853457). Component of the HUSH complex; at
CC least composed of TASOR, PPHLN1 and MPHOSPH8 (PubMed:26022416).
CC Interacts with SIN3A and HDAC1 (PubMed:17963697). May interact with PPL
CC (PubMed:12853457). {ECO:0000269|PubMed:12853457,
CC ECO:0000269|PubMed:17963697, ECO:0000269|PubMed:26022416}.
CC -!- INTERACTION:
CC Q8NEY8; Q2TAC2: CCDC57; NbExp=3; IntAct=EBI-474076, EBI-2808286;
CC Q8NEY8; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-474076, EBI-742948;
CC Q8NEY8; Q9BZW7: TSGA10; NbExp=3; IntAct=EBI-474076, EBI-744794;
CC Q8NEY8-5; P51114-2: FXR1; NbExp=3; IntAct=EBI-22734102, EBI-11022345;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12853457,
CC ECO:0000269|PubMed:15474462, ECO:0000269|PubMed:26022416}. Cytoplasm
CC {ECO:0000269|PubMed:12853457}. Chromosome
CC {ECO:0000269|PubMed:26022416}. Note=In undifferentiated keratinocytes
CC expressed in speckle-type nuclear granules and at the nuclear membrane,
CC but in the differentiated keratinocytes colocalized with periplakin at
CC the cell periphery and at cell-cell junctions (PubMed:12853457).
CC Localizes to chromatin (PubMed:26022416). {ECO:0000269|PubMed:12853457,
CC ECO:0000269|PubMed:26022416}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1;
CC IsoId=Q8NEY8-1; Sequence=Displayed;
CC Name=2; Synonyms=CR {ECO:0000303|PubMed:15474462};
CC IsoId=Q8NEY8-2; Sequence=VSP_009899, VSP_009905, VSP_009906;
CC Name=3;
CC IsoId=Q8NEY8-3; Sequence=VSP_009900, VSP_009907;
CC Name=5;
CC IsoId=Q8NEY8-5; Sequence=VSP_009899, VSP_009900, VSP_009903,
CC VSP_009904;
CC Name=6; Synonyms=CR-S {ECO:0000303|PubMed:15474462};
CC IsoId=Q8NEY8-6; Sequence=VSP_009899, VSP_009900, VSP_009905,
CC VSP_009906;
CC Name=7;
CC IsoId=Q8NEY8-7; Sequence=VSP_009898, VSP_009902, VSP_009903,
CC VSP_009904;
CC Name=8;
CC IsoId=Q8NEY8-8; Sequence=VSP_009905, VSP_009906;
CC Name=9;
CC IsoId=Q8NEY8-9; Sequence=VSP_054078, VSP_009905, VSP_009906;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12853457}.
CC -!- PTM: Substrate of transglutaminase (in vitro).
CC {ECO:0000269|PubMed:12853457}.
CC -!- MISCELLANEOUS: [Isoform 5]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 7]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH25306.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- SEQUENCE CAUTION: [Isoform 6]:
CC Sequence=AAF36126.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAF36152.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY039238; AAK68657.1; -; mRNA.
DR EMBL; AY157850; AAO16497.1; -; mRNA.
DR EMBL; AF151040; AAF36126.1; ALT_FRAME; mRNA.
DR EMBL; AF151066; AAF36152.1; ALT_FRAME; mRNA.
DR EMBL; AK055690; BAB70985.1; -; mRNA.
DR EMBL; AK000186; BAA90996.1; -; mRNA.
DR EMBL; CR621833; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC020629; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079601; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025306; AAH25306.1; ALT_INIT; mRNA.
DR EMBL; BC039832; AAH39832.1; -; mRNA.
DR CCDS; CCDS31777.1; -. [Q8NEY8-1]
DR CCDS; CCDS41773.1; -. [Q8NEY8-2]
DR CCDS; CCDS44860.1; -. [Q8NEY8-3]
DR CCDS; CCDS44861.1; -. [Q8NEY8-9]
DR CCDS; CCDS55817.1; -. [Q8NEY8-6]
DR CCDS; CCDS8741.1; -. [Q8NEY8-8]
DR RefSeq; NP_001137259.1; NM_001143787.1. [Q8NEY8-3]
DR RefSeq; NP_001137260.1; NM_001143788.1. [Q8NEY8-9]
DR RefSeq; NP_057572.5; NM_016488.6. [Q8NEY8-1]
DR RefSeq; NP_958846.1; NM_201438.1. [Q8NEY8-5]
DR RefSeq; NP_958847.1; NM_201439.1. [Q8NEY8-8]
DR RefSeq; NP_958848.1; NM_201440.1. [Q8NEY8-6]
DR RefSeq; NP_958923.1; NM_201515.1. [Q8NEY8-2]
DR PDB; 6SWG; X-ray; 2.51 A; A/B=285-341.
DR PDBsum; 6SWG; -.
DR AlphaFoldDB; Q8NEY8; -.
DR SMR; Q8NEY8; -.
DR BioGRID; 119596; 127.
DR CORUM; Q8NEY8; -.
DR DIP; DIP-49051N; -.
DR IntAct; Q8NEY8; 59.
DR MINT; Q8NEY8; -.
DR STRING; 9606.ENSP00000378935; -.
DR iPTMnet; Q8NEY8; -.
DR PhosphoSitePlus; Q8NEY8; -.
DR BioMuta; PPHLN1; -.
DR DMDM; 46396942; -.
DR EPD; Q8NEY8; -.
DR jPOST; Q8NEY8; -.
DR MassIVE; Q8NEY8; -.
DR MaxQB; Q8NEY8; -.
DR PaxDb; Q8NEY8; -.
DR PeptideAtlas; Q8NEY8; -.
DR PRIDE; Q8NEY8; -.
DR ProteomicsDB; 19102; -.
DR ProteomicsDB; 73240; -. [Q8NEY8-1]
DR ProteomicsDB; 73241; -. [Q8NEY8-2]
DR ProteomicsDB; 73242; -. [Q8NEY8-3]
DR ProteomicsDB; 73243; -. [Q8NEY8-5]
DR ProteomicsDB; 73244; -. [Q8NEY8-6]
DR ProteomicsDB; 73245; -. [Q8NEY8-7]
DR ProteomicsDB; 73246; -. [Q8NEY8-8]
DR Antibodypedia; 25050; 156 antibodies from 28 providers.
DR DNASU; 51535; -.
DR Ensembl; ENST00000358314.12; ENSP00000351066.7; ENSG00000134283.18. [Q8NEY8-8]
DR Ensembl; ENST00000395568.6; ENSP00000378935.2; ENSG00000134283.18. [Q8NEY8-1]
DR Ensembl; ENST00000395580.7; ENSP00000378947.3; ENSG00000134283.18. [Q8NEY8-2]
DR Ensembl; ENST00000432191.6; ENSP00000393965.2; ENSG00000134283.18. [Q8NEY8-3]
DR Ensembl; ENST00000449194.6; ENSP00000390681.2; ENSG00000134283.18. [Q8NEY8-9]
DR Ensembl; ENST00000552761.5; ENSP00000449331.1; ENSG00000134283.18. [Q8NEY8-6]
DR Ensembl; ENST00000610488.4; ENSP00000479913.1; ENSG00000134283.18. [Q8NEY8-1]
DR Ensembl; ENST00000613154.4; ENSP00000478872.1; ENSG00000134283.18. [Q8NEY8-9]
DR Ensembl; ENST00000619544.4; ENSP00000477681.1; ENSG00000134283.18. [Q8NEY8-3]
DR GeneID; 51535; -.
DR KEGG; hsa:51535; -.
DR MANE-Select; ENST00000358314.12; ENSP00000351066.7; NM_201439.2; NP_958847.1. [Q8NEY8-8]
DR UCSC; uc001rnb.4; human. [Q8NEY8-1]
DR CTD; 51535; -.
DR DisGeNET; 51535; -.
DR GeneCards; PPHLN1; -.
DR HGNC; HGNC:19369; PPHLN1.
DR HPA; ENSG00000134283; Low tissue specificity.
DR MIM; 608150; gene.
DR neXtProt; NX_Q8NEY8; -.
DR OpenTargets; ENSG00000134283; -.
DR PharmGKB; PA134881011; -.
DR VEuPathDB; HostDB:ENSG00000134283; -.
DR eggNOG; ENOG502QW3I; Eukaryota.
DR GeneTree; ENSGT00390000016228; -.
DR HOGENOM; CLU_051689_1_0_1; -.
DR InParanoid; Q8NEY8; -.
DR OrthoDB; 924482at2759; -.
DR PhylomeDB; Q8NEY8; -.
DR TreeFam; TF335813; -.
DR PathwayCommons; Q8NEY8; -.
DR SignaLink; Q8NEY8; -.
DR BioGRID-ORCS; 51535; 53 hits in 1082 CRISPR screens.
DR ChiTaRS; PPHLN1; human.
DR GeneWiki; PPHLN1; -.
DR GenomeRNAi; 51535; -.
DR Pharos; Q8NEY8; Tbio.
DR PRO; PR:Q8NEY8; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8NEY8; protein.
DR Bgee; ENSG00000134283; Expressed in pancreatic ductal cell and 192 other tissues.
DR ExpressionAtlas; Q8NEY8; baseline and differential.
DR Genevisible; Q8NEY8; HS.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0031424; P:keratinization; IEA:UniProtKB-KW.
DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0090309; P:positive regulation of DNA methylation-dependent heterochromatin assembly; IDA:UniProtKB.
DR GO; GO:0097355; P:protein localization to heterochromatin; IDA:UniProtKB.
DR InterPro; IPR028851; Pphln1.
DR PANTHER; PTHR15836; PTHR15836; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chromosome; Cytoplasm;
KW Isopeptide bond; Keratinization; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..458
FT /note="Periphilin-1"
FT /id="PRO_0000058537"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 103..109
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 235
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 240
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 109
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 160
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 180
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 199
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 227
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 235
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 240
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 328
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 453
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT VAR_SEQ 1..184
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_009898"
FT VAR_SEQ 1
FT /note="M -> MAYRRDEM (in isoform 2, isoform 5 and isoform
FT 6)"
FT /evidence="ECO:0000303|PubMed:11042152,
FT ECO:0000303|PubMed:12853457, ECO:0000303|PubMed:15489334"
FT /id="VSP_009899"
FT VAR_SEQ 25..79
FT /note="Missing (in isoform 3, isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:11042152,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_009900"
FT VAR_SEQ 170..190
FT /note="RKSVRPGASYKRQNEGNPERD -> RN (in isoform 9)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_054078"
FT VAR_SEQ 185..189
FT /note="GNPER -> MFSYI (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_009902"
FT VAR_SEQ 305..306
FT /note="YR -> RV (in isoform 5 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_009903"
FT VAR_SEQ 307..458
FT /note="Missing (in isoform 5 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_009904"
FT VAR_SEQ 342..367
FT /note="ESAGQTWQQVPPVRNTEMDHDGTPEN -> GERCVEELKHFIAEYDTSTQDF
FT GEPF (in isoform 2, isoform 6, isoform 8 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:11042152,
FT ECO:0000303|PubMed:12853457, ECO:0000303|PubMed:14702039,
FT ECO:0000303|Ref.5"
FT /id="VSP_009905"
FT VAR_SEQ 368..458
FT /note="Missing (in isoform 2, isoform 6, isoform 8 and
FT isoform 9)"
FT /evidence="ECO:0000303|PubMed:11042152,
FT ECO:0000303|PubMed:12853457, ECO:0000303|PubMed:14702039,
FT ECO:0000303|Ref.5"
FT /id="VSP_009906"
FT VAR_SEQ 376
FT /note="A -> ALFGFQHDASNHTIVGLGPNQVPEMKETTLQA (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009907"
FT VARIANT 173
FT /note="V -> M (in a breast cancer sample; somatic mutation;
FT dbSNP:rs140585847)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036233"
FT CONFLICT 97
FT /note="P -> L (in Ref. 3; AAF36126)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="S -> F (in Ref. 2; AAO16497)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="S -> P (in Ref. 3; AAF36126)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="E -> K (in Ref. 3; AAF36126)"
FT /evidence="ECO:0000305"
FT HELIX 291..322
FT /evidence="ECO:0007829|PDB:6SWG"
FT HELIX 326..341
FT /evidence="ECO:0007829|PDB:6SWG"
FT CONFLICT Q8NEY8-3:341
FT /note="Q -> P (in Ref. 7; AAH25306)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 458 AA; 52737 MW; FE5AAC9A6875A455 CRC64;
MWSEGRYEYE RIPRERAPPR SHPSDGYNRL VNIVPKKPPL LDRPGEGSYN RYYSHVDYRD
YDEGRSFSHD RRSGPPHRGD ESGYRWTRDD HSASRQPEYR DMRDGFRRKS FYSSHYARER
SPYKRDNTFF RESPVGRKDS PHSRSGSSVS SRSYSPERSK SYSFHQSQHR KSVRPGASYK
RQNEGNPERD KERPVQSLKT SRDTSPSSGS AVSSSKVLDK PSRLTEKELA EAASKWAAEK
LEKSDESNLP EISEYEAGST APLFTDQPEE PESNTTHGIE LFEDSQLTTR SKAIASKTKE
IEQVYRQDCE TFGMVVKMLI EKDPSLEKSI QFALRQNLHE IESAGQTWQQ VPPVRNTEMD
HDGTPENEGE ETAQSAPQPP QAPQPLQPRK KRVRRTTQLR RTTGAPDITW GMLKKTTQEA
ERILLRTQTP FTPENLFLAM LSVVHCNSRK DVKPENKQ
