PCBP2_HUMAN
ID PCBP2_HUMAN Reviewed; 365 AA.
AC Q15366; A8K7X6; B4DXP5; F8VYL7; G3V0E8; I6L8F9; Q32Q82; Q59HD4; Q68Y55;
AC Q6IPF4; Q6PKG5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Poly(rC)-binding protein 2;
DE AltName: Full=Alpha-CP2;
DE AltName: Full=Heterogeneous nuclear ribonucleoprotein E2;
DE Short=hnRNP E2;
GN Name=PCBP2;
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).
RX PubMed=7607214; DOI=10.1111/j.1432-1033.1995.0447h.x;
RA Leffers H., Dejgaard K., Celis J.E.;
RT "Characterisation of two major cellular poly(rC)-binding human proteins,
RT each containing three K-homologous (KH) domains.";
RL Eur. J. Biochem. 230:447-453(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RA Sugiyama A., Inoue H., Oka M.;
RT "Homo sapiens mRNA.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 8).
RC TISSUE=Synovium, and Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RT "Homo sapiens protein coding cDNA.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 5).
RC TISSUE=Eye, Lung, and Mammary gland;
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 PROTEIN SEQUENCE OF 47-70; 102-115; 145-160 AND 323-354, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP FUNCTION.
RX PubMed=12414943; DOI=10.1128/jvi.76.23.12008-12022.2002;
RA Walter B.L., Parsley T.B., Ehrenfeld E., Semler B.L.;
RT "Distinct poly(rC) binding protein KH domain determinants for poliovirus
RT translation initiation and viral RNA replication.";
RL J. Virol. 76:12008-12022(2002).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [11]
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 [12]
RP IDENTIFICATION BY 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 IDENTIFICATION BY 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-272, AND IDENTIFICATION BY
RP 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=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [16]
RP FUNCTION, AND INTERACTION WITH IFIH1; RNF135; MAVS AND ITCH.
RX PubMed=19881509; DOI=10.1038/ni.1815;
RA You F., Sun H., Zhou X., Sun W., Liang S., Zhai Z., Jiang Z.;
RT "PCBP2 mediates degradation of the adaptor MAVS via the HECT ubiquitin
RT ligase AIP4.";
RL Nat. Immunol. 10:1300-1308(2009).
RN [17]
RP IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR LOCATION, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=19029303; DOI=10.1261/rna.1175909;
RA Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A.,
RA Buchmeier S., Wahle E., Huettelmaiery S.;
RT "Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs.";
RL RNA 15:104-115(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173; SER-189 AND SER-364, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [20]
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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173; SER-364 AND SER-365, 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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [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 [23]
RP IDENTIFICATION BY 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 [24]
RP FUNCTION (MICROBIAL INFECTION), AND CLEAVAGE BY PICORNAVIRUS PROTEINASE 3CD
RP (MICROBIAL INFECTION).
RX PubMed=24371074; DOI=10.1128/jvi.02503-13;
RA Chase A.J., Daijogo S., Semler B.L.;
RT "Inhibition of poliovirus-induced cleavage of cellular protein PCBP2
RT reduces the levels of viral RNA replication.";
RL J. Virol. 88:3192-3201(2014).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [26]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-115; LYS-185 AND LYS-322, AND
RP IDENTIFICATION BY MASS 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 [27]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 11-82 IN COMPLEX WITH DNA.
RX PubMed=16186123; DOI=10.1074/jbc.m508183200;
RA Du Z., Lee J.K., Tjhen R., Li S., Pan H., Stroud R.M., James T.L.;
RT "Crystal structure of the first KH domain of human poly(C)-binding protein-
RT 2 in complex with a C-rich strand of human telomeric DNA at 1.7 A.";
RL J. Biol. Chem. 280:38823-38830(2005).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 285-359 IN COMPLEX WITH DNA.
RX PubMed=17426136; DOI=10.1093/nar/gkm139;
RA Fenn S., Du Z., Lee J.K., Tjhen R., Stroud R.M., James T.L.;
RT "Crystal structure of the third KH domain of human poly(C)-binding protein-
RT 2 in complex with a C-rich strand of human telomeric DNA at 1.6 A
RT resolution.";
RL Nucleic Acids Res. 35:2651-2660(2007).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 11-82 IN COMPLEX WITH DNA.
RX PubMed=17526645; DOI=10.1261/rna.410107;
RA Du Z., Lee J.K., Fenn S., Tjhen R., Stroud R.M., James T.L.;
RT "X-ray crystallographic and NMR studies of protein-protein and protein-
RT nucleic acid interactions involving the KH domains from human poly(C)-
RT binding protein-2.";
RL RNA 13:1043-1051(2007).
RN [30]
RP STRUCTURE BY NMR OF 11-169.
RX PubMed=18701464; DOI=10.1074/jbc.m803046200;
RA Du Z., Fenn S., Tjhen R., James T.L.;
RT "Structure of a construct of a human poly(C)-binding protein containing the
RT first and second KH domains reveals insights into its regulatory
RT mechanisms.";
RL J. Biol. Chem. 283:28757-28766(2008).
CC -!- FUNCTION: Single-stranded nucleic acid binding protein that binds
CC preferentially to oligo dC. Major cellular poly(rC)-binding protein.
CC Binds also poly(rU). Negatively regulates cellular antiviral responses
CC mediated by MAVS signaling (PubMed:19881509). It acts as an adapter
CC between MAVS and the E3 ubiquitin ligase ITCH, therefore triggering
CC MAVS ubiquitination and degradation (PubMed:19881509).
CC {ECO:0000269|PubMed:12414943, ECO:0000269|PubMed:19881509}.
CC -!- FUNCTION: (Microbial infection) In case of infection by poliovirus,
CC binds to the viral internal ribosome entry site (IRES) and stimulates
CC the IRES-mediated translation (PubMed:12414943, PubMed:24371074). Also
CC plays a role in initiation of viral RNA replication in concert with the
CC viral protein 3CD (PubMed:12414943). {ECO:0000269|PubMed:12414943,
CC ECO:0000269|PubMed:24371074}.
CC -!- SUBUNIT: Identified in a mRNP complex, at least composed of DHX9,
CC DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1,
CC STAU2, SYNCRIP and YBX1. Interacts with IFIH1 and RNF135. Interacts
CC with MAVS (via C-terminus) and ITCH (via WW domains).
CC {ECO:0000269|PubMed:16186123, ECO:0000269|PubMed:17426136,
CC ECO:0000269|PubMed:17526645, ECO:0000269|PubMed:19029303,
CC ECO:0000269|PubMed:19881509}.
CC -!- INTERACTION:
CC Q15366; Q15365: PCBP1; NbExp=2; IntAct=EBI-945799, EBI-946095;
CC Q15366; P09012: SNRPA; NbExp=3; IntAct=EBI-945799, EBI-607085;
CC Q15366; P84103: SRSF3; NbExp=3; IntAct=EBI-945799, EBI-372557;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19029303}. Cytoplasm
CC {ECO:0000269|PubMed:19029303}. Note=Loosely bound in the nucleus. May
CC shuttle between the nucleus and the cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1;
CC IsoId=Q15366-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15366-2; Sequence=VSP_042833;
CC Name=3;
CC IsoId=Q15366-3; Sequence=VSP_043161, VSP_042833;
CC Name=4;
CC IsoId=Q15366-4; Sequence=VSP_043161, VSP_043362, VSP_042833;
CC Name=5;
CC IsoId=Q15366-5; Sequence=VSP_043362, VSP_042833;
CC Name=6;
CC IsoId=Q15366-6; Sequence=VSP_043161;
CC Name=7;
CC IsoId=Q15366-7; Sequence=VSP_043161, VSP_043362, VSP_054045;
CC Name=8;
CC IsoId=Q15366-8; Sequence=VSP_043362, VSP_054045;
CC -!- TISSUE SPECIFICITY: Detected in all tissues examined.
CC -!- DOMAIN: The KH domains mediates poly(C) binding.
CC -!- PTM: Phosphorylated. The non-phosphorylated form(s) exhibited the
CC strongest poly(rC)-binding activity.
CC -!- PTM: (Microbial infection) Proteolyticaly cleaved by picornavirus
CC proteinase 3CD. {ECO:0000269|PubMed:24371074}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92062.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X78136; CAA55015.1; -; mRNA.
DR EMBL; AB188306; BAD36897.1; -; mRNA.
DR EMBL; AK292141; BAF84830.1; -; mRNA.
DR EMBL; AK302067; BAG63457.1; -; mRNA.
DR EMBL; AB208825; BAD92062.1; ALT_INIT; mRNA.
DR EMBL; AC023509; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC068889; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW96706.1; -; Genomic_DNA.
DR EMBL; CH471054; EAW96707.1; -; Genomic_DNA.
DR EMBL; CH471054; EAW96709.1; -; Genomic_DNA.
DR EMBL; CH471054; EAW96711.1; -; Genomic_DNA.
DR EMBL; BC001155; AAH01155.1; -; mRNA.
DR EMBL; BC071942; AAH71942.1; -; mRNA.
DR EMBL; BC107688; AAI07689.1; -; mRNA.
DR CCDS; CCDS44900.1; -. [Q15366-2]
DR CCDS; CCDS44901.1; -. [Q15366-1]
DR CCDS; CCDS44902.1; -. [Q15366-5]
DR CCDS; CCDS44903.1; -. [Q15366-4]
DR CCDS; CCDS44904.1; -. [Q15366-7]
DR CCDS; CCDS55830.1; -. [Q15366-6]
DR CCDS; CCDS8859.1; -. [Q15366-3]
DR PIR; S65679; S42471.
DR RefSeq; NP_001092090.1; NM_001098620.2. [Q15366-4]
DR RefSeq; NP_001122383.1; NM_001128911.1. [Q15366-1]
DR RefSeq; NP_001122384.1; NM_001128912.1. [Q15366-6]
DR RefSeq; NP_001122385.1; NM_001128913.1. [Q15366-5]
DR RefSeq; NP_001122386.1; NM_001128914.1. [Q15366-7]
DR RefSeq; NP_005007.2; NM_005016.5. [Q15366-2]
DR RefSeq; NP_114366.1; NM_031989.4. [Q15366-3]
DR PDB; 2AXY; X-ray; 1.70 A; A/B/C/D=11-82.
DR PDB; 2JZX; NMR; -; A=11-169.
DR PDB; 2P2R; X-ray; 1.60 A; A=285-359.
DR PDB; 2PQU; X-ray; 2.12 A; A/B/C/D=11-82.
DR PDB; 2PY9; X-ray; 2.56 A; A/B/C/D=11-82.
DR PDBsum; 2AXY; -.
DR PDBsum; 2JZX; -.
DR PDBsum; 2P2R; -.
DR PDBsum; 2PQU; -.
DR PDBsum; 2PY9; -.
DR AlphaFoldDB; Q15366; -.
DR SASBDB; Q15366; -.
DR SMR; Q15366; -.
DR BioGRID; 111127; 224.
DR DIP; DIP-58934N; -.
DR IntAct; Q15366; 77.
DR MINT; Q15366; -.
DR STRING; 9606.ENSP00000352438; -.
DR ChEMBL; CHEMBL4295826; -.
DR GlyGen; Q15366; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15366; -.
DR MetOSite; Q15366; -.
DR PhosphoSitePlus; Q15366; -.
DR SwissPalm; Q15366; -.
DR BioMuta; PCBP2; -.
DR DMDM; 6707736; -.
DR EPD; Q15366; -.
DR jPOST; Q15366; -.
DR MassIVE; Q15366; -.
DR MaxQB; Q15366; -.
DR PaxDb; Q15366; -.
DR PeptideAtlas; Q15366; -.
DR PRIDE; Q15366; -.
DR ProteomicsDB; 32176; -.
DR ProteomicsDB; 5458; -.
DR ProteomicsDB; 60542; -. [Q15366-1]
DR ProteomicsDB; 60543; -. [Q15366-2]
DR ProteomicsDB; 60544; -. [Q15366-3]
DR ProteomicsDB; 60545; -. [Q15366-4]
DR ProteomicsDB; 60546; -. [Q15366-5]
DR Antibodypedia; 15218; 279 antibodies from 36 providers.
DR DNASU; 5094; -.
DR Ensembl; ENST00000359282.9; ENSP00000352228.5; ENSG00000197111.16. [Q15366-4]
DR Ensembl; ENST00000359462.9; ENSP00000352438.5; ENSG00000197111.16. [Q15366-2]
DR Ensembl; ENST00000437231.5; ENSP00000390304.1; ENSG00000197111.16. [Q15366-7]
DR Ensembl; ENST00000439930.7; ENSP00000408949.2; ENSG00000197111.16. [Q15366-1]
DR Ensembl; ENST00000447282.5; ENSP00000394116.1; ENSG00000197111.16. [Q15366-5]
DR Ensembl; ENST00000455667.7; ENSP00000388008.3; ENSG00000197111.16. [Q15366-7]
DR Ensembl; ENST00000546463.6; ENSP00000448762.2; ENSG00000197111.16. [Q15366-3]
DR Ensembl; ENST00000548933.5; ENSP00000449062.1; ENSG00000197111.16. [Q15366-5]
DR Ensembl; ENST00000552296.6; ENSP00000448927.2; ENSG00000197111.16. [Q15366-6]
DR Ensembl; ENST00000552819.5; ENSP00000449070.1; ENSG00000197111.16. [Q15366-8]
DR GeneID; 5094; -.
DR KEGG; hsa:5094; -.
DR MANE-Select; ENST00000546463.6; ENSP00000448762.2; NM_031989.5; NP_114366.1. [Q15366-3]
DR UCSC; uc001sdb.5; human. [Q15366-1]
DR UCSC; uc058oqk.1; human.
DR CTD; 5094; -.
DR DisGeNET; 5094; -.
DR GeneCards; PCBP2; -.
DR HGNC; HGNC:8648; PCBP2.
DR HPA; ENSG00000197111; Low tissue specificity.
DR MIM; 601210; gene.
DR neXtProt; NX_Q15366; -.
DR OpenTargets; ENSG00000197111; -.
DR PharmGKB; PA32987; -.
DR VEuPathDB; HostDB:ENSG00000197111; -.
DR eggNOG; KOG2190; Eukaryota.
DR GeneTree; ENSGT00940000154129; -.
DR HOGENOM; CLU_022670_0_1_1; -.
DR InParanoid; Q15366; -.
DR OMA; SIAKEPH; -.
DR OrthoDB; 954970at2759; -.
DR PhylomeDB; Q15366; -.
DR TreeFam; TF318292; -.
DR PathwayCommons; Q15366; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR Reactome; R-HSA-936440; Negative regulators of DDX58/IFIH1 signaling.
DR SignaLink; Q15366; -.
DR SIGNOR; Q15366; -.
DR BioGRID-ORCS; 5094; 728 hits in 1095 CRISPR screens.
DR ChiTaRS; PCBP2; human.
DR EvolutionaryTrace; Q15366; -.
DR GeneWiki; PCBP2; -.
DR GenomeRNAi; 5094; -.
DR Pharos; Q15366; Tbio.
DR PRO; PR:Q15366; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q15366; protein.
DR Bgee; ENSG00000197111; Expressed in ganglionic eminence and 203 other tissues.
DR ExpressionAtlas; Q15366; baseline and differential.
DR Genevisible; Q15366; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:1990829; F:C-rich single-stranded DNA binding; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0075522; P:IRES-dependent viral translational initiation; IDA:UniProtKB.
DR GO; GO:0016071; P:mRNA metabolic process; NAS:UniProtKB.
DR GO; GO:0050687; P:negative regulation of defense response to virus; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0051252; P:regulation of RNA metabolic process; IBA:GO_Central.
DR GO; GO:0039694; P:viral RNA genome replication; IDA:UniProtKB.
DR Gene3D; 3.30.1370.10; -; 3.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR Pfam; PF00013; KH_1; 3.
DR SMART; SM00322; KH; 3.
DR SUPFAM; SSF54791; SSF54791; 3.
DR PROSITE; PS50084; KH_TYPE_1; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Antiviral defense; Cytoplasm;
KW Direct protein sequencing; DNA-binding; Host-virus interaction; Immunity;
KW Innate immunity; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
KW Ubl conjugation; Viral RNA replication.
FT CHAIN 1..365
FT /note="Poly(rC)-binding protein 2"
FT /id="PRO_0000050090"
FT DOMAIN 13..75
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 97..162
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 287..351
FT /note="KH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT SITE 253..254
FT /note="Cleavage, by viral proteinase 3CD"
FT /evidence="ECO:0000269|PubMed:24371074"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CROSSLNK 115
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 185
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 322
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 169..172
FT /note="Missing (in isoform 3, isoform 4, isoform 6 and
FT isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2,
FT ECO:0000303|Ref.4"
FT /id="VSP_043161"
FT VAR_SEQ 198..228
FT /note="Missing (in isoform 4, isoform 5, isoform 7 and
FT isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_043362"
FT VAR_SEQ 267..279
FT /note="GIESSSPEVKGYW -> A (in isoform 7 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054045"
FT VAR_SEQ 279
FT /note="W -> WA (in isoform 2, isoform 3, isoform 4 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_042833"
FT STRAND 14..21
FT /evidence="ECO:0007829|PDB:2AXY"
FT HELIX 22..29
FT /evidence="ECO:0007829|PDB:2AXY"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:2AXY"
FT HELIX 34..43
FT /evidence="ECO:0007829|PDB:2AXY"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:2AXY"
FT STRAND 55..63
FT /evidence="ECO:0007829|PDB:2AXY"
FT HELIX 65..80
FT /evidence="ECO:0007829|PDB:2AXY"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:2JZX"
FT STRAND 97..105
FT /evidence="ECO:0007829|PDB:2JZX"
FT HELIX 106..113
FT /evidence="ECO:0007829|PDB:2JZX"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:2JZX"
FT HELIX 118..127
FT /evidence="ECO:0007829|PDB:2JZX"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:2JZX"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:2JZX"
FT HELIX 152..168
FT /evidence="ECO:0007829|PDB:2JZX"
FT STRAND 288..295
FT /evidence="ECO:0007829|PDB:2P2R"
FT HELIX 296..303
FT /evidence="ECO:0007829|PDB:2P2R"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:2P2R"
FT HELIX 308..317
FT /evidence="ECO:0007829|PDB:2P2R"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:2P2R"
FT STRAND 331..339
FT /evidence="ECO:0007829|PDB:2P2R"
FT HELIX 341..355
FT /evidence="ECO:0007829|PDB:2P2R"
SQ SEQUENCE 365 AA; 38580 MW; 43F035D76FDC2C63 CRC64;
MDTGVIEGGL NVTLTIRLLM HGKEVGSIIG KKGESVKKMR EESGARINIS EGNCPERIIT
LAGPTNAIFK AFAMIIDKLE EDISSSMTNS TAASRPPVTL RLVVPASQCG SLIGKGGCKI
KEIRESTGAQ VQVAGDMLPN STERAITIAG IPQSIIECVK QICVVMLETL SQSPPKGVTI
PYRPKPSSSP VIFAGGQDRY STGSDSASFP HTTPSMCLNP DLEGPPLEAY TIQGQYAIPQ
PDLTKLHQLA MQQSHFPMTH GNTGFSGIES SSPEVKGYWG LDASAQTTSH ELTIPNDLIG
CIIGRQGAKI NEIRQMSGAQ IKIANPVEGS TDRQVTITGS AASISLAQYL INVRLSSETG
GMGSS
