PA2G4_HUMAN
ID PA2G4_HUMAN Reviewed; 394 AA.
AC Q9UQ80; O43846; Q9UM59;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=Proliferation-associated protein 2G4;
DE AltName: Full=Cell cycle protein p38-2G4 homolog;
DE Short=hG4-1;
DE AltName: Full=ErbB3-binding protein 1;
GN Name=PA2G4; Synonyms=EBP1;
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=9345902; DOI=10.1159/000134621;
RA Lamartine J., Seri M., Cinti R., Heitzmann F., Creaven M., Radomski N.,
RA Jost E., Lenoir G.M., Romeo G., Sylla B.S.;
RT "Molecular cloning and mapping of a human cDNA (PA2G4) that encodes a
RT protein highly homologous to the mouse cell cycle protein p38-2G4.";
RL Cytogenet. Cell Genet. 78:31-35(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH ERBB3, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10682683; DOI=10.1054/bjoc.1999.0981;
RA Yoo J.Y., Wang X.W., Rishi A.K., Lessor T., Xia X.M., Gustafson T.A.,
RA Hamburger A.W.;
RT "Interaction of the PA2G4 (EBP1) protein with ErbB-3 and regulation of this
RT binding by heregulin.";
RL Br. J. Cancer 82:683-690(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Caroli F., Lamartine J., Sylla B.S., Romeo G., Seri M.;
RT "Genomic structure of the human PA2G4 gene.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, 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 [5]
RP PROTEIN SEQUENCE OF 2-20; 23-30; 34-62; 73-101; 156-172; 200-211; 216-236;
RP 264-281 AND 299-364, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma, Mammary carcinoma, and Ovarian carcinoma;
RA Bienvenut W.V., Matallanas D., Cooper W.N., Boldt K., von Kriegsheim A.F.,
RA Kolch W.;
RL Submitted (JAN-2010) to UniProtKB.
RN [6]
RP PROTEIN SEQUENCE OF 34-51; 216-236; 264-271; 299-311; 333-344 AND 377-394,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [7]
RP INTERACTION WITH ERBB3, PHOSPHORYLATION, PHOSPHORYLATION BY PKC,
RP PHOSPHORYLATION AT THR-366, AND MUTAGENESIS OF SER-363 AND THR-366.
RX PubMed=11325528; DOI=10.1016/s0303-7207(01)00387-2;
RA Lessor T.J., Hamburger A.W.;
RT "Regulation of the ErbB3 binding protein Ebp1 by protein kinase C.";
RL Mol. Cell. Endocrinol. 175:185-191(2001).
RN [8]
RP FUNCTION IN TRANSCRIPTION REPRESSION, AND INTERACTION WITH RB1.
RX PubMed=11268000; DOI=10.1002/jcp.1075;
RA Xia X., Cheng A., Lessor T., Zhang Y., Hamburger A.W.;
RT "Ebp1, an ErbB-3 binding protein, interacts with Rb and affects Rb
RT transcriptional regulation.";
RL J. Cell. Physiol. 187:209-217(2001).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [10]
RP FUNCTION IN E2F1-MEDIATED TRANSCRIPTION REPRESSION, AND INTERACTION WITH
RP HDAC2.
RX PubMed=12682367; DOI=10.1093/nar/gkg318;
RA Zhang Y., Woodford N., Xia X., Hamburger A.W.;
RT "Repression of E2F1-mediated transcription by the ErbB3 binding protein
RT Ebp1 involves histone deacetylases.";
RL Nucleic Acids Res. 31:2168-2177(2003).
RN [11]
RP FUNCTION IN RRNA PROCESSING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP RNA-BINDING, IDENTIFICATION IN A RIBONUCLEOPROTEIN COMPLEX, ASSOCIATION
RP WITH RRNA, ASSOCIATION WITH U3 SNORNA, AND MUTAGENESIS OF 20-LYS--LYS-22
RP AND 364-ARG-LYS-365.
RX PubMed=15064750; DOI=10.1038/sj.onc.1207579;
RA Squatrito M., Mancino M., Donzelli M., Areces L.B., Draetta G.F.;
RT "EBP1 is a nucleolar growth-regulating protein that is part of pre-
RT ribosomal ribonucleoprotein complexes.";
RL Oncogene 23:4454-4465(2004).
RN [12]
RP FUNCTION IN TRANSCRIPTION REPRESSION, AND INTERACTION WITH ERBB3 AND AR.
RX PubMed=15583694; DOI=10.1038/sj.bjc.6602257;
RA Zhang Y., Hamburger A.W.;
RT "Specificity and heregulin regulation of Ebp1 (ErbB3 binding protein 1)
RT mediated repression of androgen receptor signalling.";
RL Br. J. Cancer 92:140-146(2005).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND THR-386, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-386, 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 [15]
RP ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, INTERACTION
RP WITH ERBB3, PHOSPHORYLATION AT SER-361, AND MUTAGENESIS OF SER-361.
RX PubMed=16832058; DOI=10.1073/pnas.0602923103;
RA Liu Z., Ahn J.Y., Liu X., Ye K.;
RT "Ebp1 isoforms distinctively regulate cell survival and differentiation.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:10917-10922(2006).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361 AND THR-386, 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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [18]
RP POLYUBIQUITINATION, SUBCELLULAR LOCATION, INTERACTION WITH RNF20 AND HUWE1,
RP TISSUE SPECIFICITY, AND MUTAGENESIS OF SER-361.
RX PubMed=19037095; DOI=10.1091/mbc.e08-09-0983;
RA Liu Z., Oh S.M., Okada M., Liu X., Cheng D., Peng J., Brat D.J., Sun S.Y.,
RA Zhou W., Gu W., Ye K.;
RT "Human BRE1 is an E3 ubiquitin ligase for Ebp1 tumor suppressor.";
RL Mol. Biol. Cell 20:757-768(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-386, 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 [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-2; SER-361 AND THR-386, CLEAVAGE OF INITIATOR METHIONINE
RP [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP 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 [21]
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 [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-2 AND THR-386, CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-335 AND SER-361, AND
RP IDENTIFICATION BY 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 [26]
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 [27]
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 [28]
RP INTERACTION WITH DNAJC21.
RX PubMed=27346687; DOI=10.1016/j.ajhg.2016.05.002;
RA Tummala H., Walne A.J., Williams M., Bockett N., Collopy L., Cardoso S.,
RA Ellison A., Wynn R., Leblanc T., Fitzgibbon J., Kelsell D.P.,
RA van Heel D.A., Payne E., Plagnol V., Dokal I., Vulliamy T.;
RT "DNAJC21 mutations link a cancer-prone bone marrow failure syndrome to
RT corruption in 60S ribosome subunit maturation.";
RL Am. J. Hum. Genet. 99:115-124(2016).
RN [29]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-298, 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 [30]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), INTERACTION WITH 5S RIBOSOMAL RNA,
RP AND LACK OF AMINOPEPTIDASE ACTIVITY.
RX PubMed=17765895; DOI=10.1016/j.febslet.2007.08.024;
RA Kowalinski E., Bange G., Bradatsch B., Hurt E., Wild K., Sinning I.;
RT "The crystal structure of Ebp1 reveals a methionine aminopeptidase fold as
RT binding platform for multiple interactions.";
RL FEBS Lett. 581:4450-4454(2007).
CC -!- FUNCTION: May play a role in a ERBB3-regulated signal transduction
CC pathway. Seems be involved in growth regulation. Acts a corepressor of
CC the androgen receptor (AR) and is regulated by the ERBB3 ligand
CC neuregulin-1/heregulin (HRG). Inhibits transcription of some E2F1-
CC regulated promoters, probably by recruiting histone acetylase (HAT)
CC activity. Binds RNA. Associates with 28S, 18S and 5.8S mature rRNAs,
CC several rRNA precursors and probably U3 small nucleolar RNA. May be
CC involved in regulation of intermediate and late steps of rRNA
CC processing. May be involved in ribosome assembly. Mediates cap-
CC independent translation of specific viral IRESs (internal ribosomal
CC entry site) (By similarity). Regulates cell proliferation,
CC differentiation, and survival. Isoform 1 suppresses apoptosis whereas
CC isoform 2 promotes cell differentiation (By similarity).
CC {ECO:0000250|UniProtKB:P50580, ECO:0000250|UniProtKB:Q6AYD3,
CC ECO:0000269|PubMed:11268000, ECO:0000269|PubMed:12682367,
CC ECO:0000269|PubMed:15064750, ECO:0000269|PubMed:15583694,
CC ECO:0000269|PubMed:16832058}.
CC -!- SUBUNIT: Isoform 2 interacts with the cytoplasmic domain of non-
CC phosphorylated ERBB3; the interaction requires PKC activity. Interacts
CC with AR. Treatment with HRG leads to dissociation from ERBB3 and
CC increases association with AR. Interacts with NCL/nucleolin. Component
CC of a ribonucleoprotein complex containing at least PA2G4, NCL, TOP1,
CC PABPC2, RPLP0, acetylated histone H1 (HIST1H1A or H1F1), histone H1
CC 2/4, RPL4, RPL8, RPL15, RPL18, RPL18A, RPL21, RPL11, RPL12, RPL28,
CC RPL27, RPLP2 and RPL24. Interacts with HDAC2. Interacts with RB1; the
CC interaction is enhanced upon PA2G4 dephosphorylation. Interacts with
CC AKT1 (By similarity). Isoform 1 and isoform 2 interact with RNF20.
CC Isoform 2 interacts with HUWE1. Interacts with DNAJC21
CC (PubMed:27346687). {ECO:0000250|UniProtKB:Q6AYD3,
CC ECO:0000269|PubMed:10682683, ECO:0000269|PubMed:11268000,
CC ECO:0000269|PubMed:11325528, ECO:0000269|PubMed:12682367,
CC ECO:0000269|PubMed:15064750, ECO:0000269|PubMed:15583694,
CC ECO:0000269|PubMed:16832058, ECO:0000269|PubMed:17765895,
CC ECO:0000269|PubMed:19037095, ECO:0000269|PubMed:27346687}.
CC -!- INTERACTION:
CC Q9UQ80; P19338: NCL; NbExp=2; IntAct=EBI-924893, EBI-346967;
CC Q9UQ80; P06400: RB1; NbExp=4; IntAct=EBI-924893, EBI-491274;
CC Q9UQ80; Q96ST3: SIN3A; NbExp=4; IntAct=EBI-924893, EBI-347218;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm
CC {ECO:0000269|PubMed:16832058, ECO:0000269|PubMed:19037095}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:16832058, ECO:0000269|PubMed:19037095}.
CC Note=Translocates to the nucleus upon treatment with HRG.
CC Phosphorylation at Ser-361 by PKC/PRKCD regulates its nucleolar
CC localization. {ECO:0000269|PubMed:16832058}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:16832058, ECO:0000269|PubMed:19037095}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000305}; Synonyms=p48 {ECO:0000303|PubMed:16832058};
CC IsoId=Q9UQ80-1; Sequence=Displayed;
CC Name=2 {ECO:0000305}; Synonyms=p42 {ECO:0000303|PubMed:16832058};
CC IsoId=Q9UQ80-2; Sequence=VSP_057325;
CC -!- TISSUE SPECIFICITY: Isoform 2 is undetectable whereas isoform 1 is
CC strongly expressed in cancer cells (at protein level). Isoform 1 and
CC isoform 2 are widely expressed, including heart, brain, lung, pancreas,
CC skeletal muscle, kidney, placenta and liver.
CC {ECO:0000269|PubMed:10682683, ECO:0000269|PubMed:15064750,
CC ECO:0000269|PubMed:19037095}.
CC -!- PTM: Phosphorylated on serine and threonine residues. Phosphorylation
CC is enhanced by HRG treatment. Basal phosphorylation is PKC-dependent
CC and HRG-induced phosphorylation is predominantly PKC-independent.
CC Phosphorylation at Ser-361 by PKC/PRKCD regulates its nucleolar
CC localization. {ECO:0000269|PubMed:11325528,
CC ECO:0000269|PubMed:16832058, ECO:0000269|PubMed:19037095}.
CC -!- PTM: In cancer cells, isoform 2 is polyubiquitinated leading to its
CC proteasomal degradation and phosphorylation by PKC/PRKCD enhances
CC polyubiquitination. {ECO:0000269|PubMed:19037095}.
CC -!- SIMILARITY: Belongs to the peptidase M24 family. {ECO:0000305}.
CC -!- CAUTION: Although it belongs to the peptidase M24 family, it does not
CC contain metal cofactors and lacks aminopeptidase activity.
CC {ECO:0000305|PubMed:17765895}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PA2G4ID41628ch12q13.html";
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DR EMBL; U59435; AAB91536.1; -; mRNA.
DR EMBL; U87954; AAD00646.1; -; mRNA.
DR EMBL; AF104670; AAD05561.1; -; Genomic_DNA.
DR EMBL; AF104668; AAD05561.1; JOINED; Genomic_DNA.
DR EMBL; AF104669; AAD05561.1; JOINED; Genomic_DNA.
DR EMBL; BC001951; AAH01951.1; -; mRNA.
DR EMBL; BC007561; AAH07561.1; -; mRNA.
DR EMBL; BC069786; AAH69786.1; -; mRNA.
DR CCDS; CCDS8902.1; -. [Q9UQ80-1]
DR RefSeq; NP_006182.2; NM_006191.2. [Q9UQ80-1]
DR PDB; 2Q8K; X-ray; 1.60 A; A=2-394.
DR PDB; 3J2I; EM; 11.90 A; A=1-394.
DR PDB; 6CHT; X-ray; 3.17 A; C/F/I/L=349-368.
DR PDB; 6LSR; EM; 3.13 A; z=1-394.
DR PDB; 6SXO; EM; 3.30 A; A=1-394.
DR PDB; 6WM8; X-ray; 2.60 A; A/B/C=2-362.
DR PDB; 6Z6L; EM; 3.00 A; CA=1-394.
DR PDB; 6Z6M; EM; 3.10 A; CA=1-394.
DR PDB; 6Z6N; EM; 2.90 A; CA=1-394.
DR PDB; 6ZM7; EM; 2.70 A; CA=1-394.
DR PDB; 6ZME; EM; 3.00 A; CA=1-394.
DR PDB; 6ZMI; EM; 2.60 A; CA=1-394.
DR PDB; 6ZMO; EM; 3.10 A; CA=1-394.
DR PDB; 7BHP; EM; 3.30 A; A=1-394.
DR PDBsum; 2Q8K; -.
DR PDBsum; 3J2I; -.
DR PDBsum; 6CHT; -.
DR PDBsum; 6LSR; -.
DR PDBsum; 6SXO; -.
DR PDBsum; 6WM8; -.
DR PDBsum; 6Z6L; -.
DR PDBsum; 6Z6M; -.
DR PDBsum; 6Z6N; -.
DR PDBsum; 6ZM7; -.
DR PDBsum; 6ZME; -.
DR PDBsum; 6ZMI; -.
DR PDBsum; 6ZMO; -.
DR PDBsum; 7BHP; -.
DR AlphaFoldDB; Q9UQ80; -.
DR SMR; Q9UQ80; -.
DR BioGRID; 111075; 218.
DR DIP; DIP-31275N; -.
DR ELM; Q9UQ80; -.
DR IntAct; Q9UQ80; 126.
DR MINT; Q9UQ80; -.
DR STRING; 9606.ENSP00000302886; -.
DR MEROPS; M24.973; -.
DR GlyGen; Q9UQ80; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UQ80; -.
DR MetOSite; Q9UQ80; -.
DR PhosphoSitePlus; Q9UQ80; -.
DR SwissPalm; Q9UQ80; -.
DR BioMuta; PA2G4; -.
DR DMDM; 13632817; -.
DR SWISS-2DPAGE; Q9UQ80; -.
DR EPD; Q9UQ80; -.
DR jPOST; Q9UQ80; -.
DR MassIVE; Q9UQ80; -.
DR MaxQB; Q9UQ80; -.
DR PaxDb; Q9UQ80; -.
DR PeptideAtlas; Q9UQ80; -.
DR PRIDE; Q9UQ80; -.
DR ProteomicsDB; 85517; -. [Q9UQ80-1]
DR Antibodypedia; 3192; 453 antibodies from 36 providers.
DR DNASU; 5036; -.
DR Ensembl; ENST00000303305.11; ENSP00000302886.6; ENSG00000170515.14. [Q9UQ80-1]
DR GeneID; 5036; -.
DR KEGG; hsa:5036; -.
DR MANE-Select; ENST00000303305.11; ENSP00000302886.6; NM_006191.3; NP_006182.2.
DR UCSC; uc001sjm.4; human. [Q9UQ80-1]
DR CTD; 5036; -.
DR DisGeNET; 5036; -.
DR GeneCards; PA2G4; -.
DR HGNC; HGNC:8550; PA2G4.
DR HPA; ENSG00000170515; Low tissue specificity.
DR MIM; 602145; gene.
DR neXtProt; NX_Q9UQ80; -.
DR OpenTargets; ENSG00000170515; -.
DR PharmGKB; PA32877; -.
DR VEuPathDB; HostDB:ENSG00000170515; -.
DR eggNOG; KOG2776; Eukaryota.
DR GeneTree; ENSGT00940000154281; -.
DR HOGENOM; CLU_041451_2_1_1; -.
DR InParanoid; Q9UQ80; -.
DR OMA; FPFAERW; -.
DR PhylomeDB; Q9UQ80; -.
DR TreeFam; TF300010; -.
DR PathwayCommons; Q9UQ80; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q9UQ80; -.
DR SIGNOR; Q9UQ80; -.
DR BioGRID-ORCS; 5036; 208 hits in 1057 CRISPR screens.
DR ChiTaRS; PA2G4; human.
DR EvolutionaryTrace; Q9UQ80; -.
DR GeneWiki; PA2G4; -.
DR GenomeRNAi; 5036; -.
DR Pharos; Q9UQ80; Tbio.
DR PRO; PR:Q9UQ80; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9UQ80; protein.
DR Bgee; ENSG00000170515; Expressed in skin of leg and 213 other tissues.
DR ExpressionAtlas; Q9UQ80; baseline and differential.
DR Genevisible; Q9UQ80; HS.
DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003676; F:nucleic acid binding; IDA:MGI.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0045597; P:positive regulation of cell differentiation; ISS:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.90.230.10; -; 1.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR004545; PA2G4.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR018349; Pept_M24A_MAP2_BS.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00557; Peptidase_M24; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF55920; SSF55920; 1.
DR TIGRFAMs; TIGR00495; crvDNA_42K; 1.
DR PROSITE; PS01202; MAP_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Ribonucleoprotein; RNA-binding;
KW rRNA processing; Transcription; Transcription regulation;
KW Translation regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..394
FT /note="Proliferation-associated protein 2G4"
FT /id="PRO_0000148989"
FT REGION 2..48
FT /note="Necessary for nucleolar localization"
FT /evidence="ECO:0000269|PubMed:15064750"
FT REGION 46..54
FT /note="RNA-binding"
FT /evidence="ECO:0000269|PubMed:15064750"
FT REGION 301..394
FT /note="Necessary for nucleolar localization"
FT /evidence="ECO:0000269|PubMed:15064750"
FT REGION 358..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..375
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250|UniProtKB:P50580"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 361
FT /note="Phosphoserine; by PKC/PRKCD"
FT /evidence="ECO:0000269|PubMed:16832058,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 366
FT /note="Phosphothreonine"
FT /evidence="ECO:0000305|PubMed:11325528"
FT MOD_RES 386
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT CROSSLNK 298
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..54
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000269|PubMed:16832058"
FT /id="VSP_057325"
FT MUTAGEN 20..22
FT /note="KYK->AYA: Loss of nucleolar localization."
FT /evidence="ECO:0000269|PubMed:15064750"
FT MUTAGEN 361
FT /note="S->A: Loss of phosphorylation and interaction with
FT ERBB3 and HUWE1."
FT /evidence="ECO:0000269|PubMed:16832058"
FT MUTAGEN 361
FT /note="S->D: No effect on phosphorylation and loss of
FT nucleolar localization."
FT /evidence="ECO:0000269|PubMed:16832058"
FT MUTAGEN 363
FT /note="S->A: No effect on in vitro phosphorylation by PKC."
FT /evidence="ECO:0000269|PubMed:11325528"
FT MUTAGEN 364..365
FT /note="RK->AA: Only partial nucleolar localization."
FT /evidence="ECO:0000269|PubMed:15064750"
FT MUTAGEN 366
FT /note="T->A: Decreases in vitro phosphorylation by PKC."
FT /evidence="ECO:0000269|PubMed:11325528"
FT CONFLICT 381
FT /note="A -> P (in Ref. 1; AAB91536)"
FT /evidence="ECO:0000305"
FT HELIX 15..38
FT /evidence="ECO:0007829|PDB:2Q8K"
FT HELIX 45..61
FT /evidence="ECO:0007829|PDB:2Q8K"
FT STRAND 72..82
FT /evidence="ECO:0007829|PDB:2Q8K"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:2Q8K"
FT STRAND 105..114
FT /evidence="ECO:0007829|PDB:2Q8K"
FT STRAND 117..126
FT /evidence="ECO:0007829|PDB:2Q8K"
FT HELIX 137..156
FT /evidence="ECO:0007829|PDB:2Q8K"
FT HELIX 163..175
FT /evidence="ECO:0007829|PDB:2Q8K"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:2Q8K"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:2Q8K"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:2Q8K"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:2Q8K"
FT HELIX 207..212
FT /evidence="ECO:0007829|PDB:2Q8K"
FT STRAND 223..233
FT /evidence="ECO:0007829|PDB:2Q8K"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:2Q8K"
FT HELIX 260..273
FT /evidence="ECO:0007829|PDB:2Q8K"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:2Q8K"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:6WM8"
FT HELIX 287..298
FT /evidence="ECO:0007829|PDB:2Q8K"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:2Q8K"
FT STRAND 316..326
FT /evidence="ECO:0007829|PDB:2Q8K"
FT STRAND 329..332
FT /evidence="ECO:0007829|PDB:2Q8K"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:2Q8K"
FT HELIX 352..359
FT /evidence="ECO:0007829|PDB:2Q8K"
SQ SEQUENCE 394 AA; 43787 MW; CD45466507AD6047 CRC64;
MSGEDEQQEQ TIAEDLVVTK YKMGGDIANR VLRSLVEASS SGVSVLSLCE KGDAMIMEET
GKIFKKEKEM KKGIAFPTSI SVNNCVCHFS PLKSDQDYIL KEGDLVKIDL GVHVDGFIAN
VAHTFVVDVA QGTQVTGRKA DVIKAAHLCA EAALRLVKPG NQNTQVTEAW NKVAHSFNCT
PIEGMLSHQL KQHVIDGEKT IIQNPTDQQK KDHEKAEFEV HEVYAVDVLV SSGEGKAKDA
GQRTTIYKRD PSKQYGLKMK TSRAFFSEVE RRFDAMPFTL RAFEDEKKAR MGVVECAKHE
LLQPFNVLYE KEGEFVAQFK FTVLLMPNGP MRITSGPFEP DLYKSEMEVQ DAELKALLQS
SASRKTQKKK KKKASKTAEN ATSGETLEEN EAGD
