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Proliferation-associated protein 2G4 (Cell cycle protein p38-2G4 homolog) (hG4-1) (ErbB3-binding protein 1)

 PA2G4_HUMAN             Reviewed;         394 AA.
Q9UQ80; O43846; Q9UM59;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 181.
RecName: Full=Proliferation-associated protein 2G4;
AltName: Full=Cell cycle protein p38-2G4 homolog;
Short=hG4-1;
AltName: Full=ErbB3-binding protein 1;
Name=PA2G4; Synonyms=EBP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9345902;
Lamartine J., Seri M., Cinti R., Heitzmann F., Creaven M.,
Radomski N., Jost E., Lenoir G.M., Romeo G., Sylla B.S.;
"Molecular cloning and mapping of a human cDNA (PA2G4) that encodes a
protein highly homologous to the mouse cell cycle protein p38-2G4.";
Cytogenet. Cell Genet. 78:31-35(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH ERBB3,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=10682683; DOI=10.1054/bjoc.1999.0981;
Yoo J.Y., Wang X.W., Rishi A.K., Lessor T., Xia X.M., Gustafson T.A.,
Hamburger A.W.;
"Interaction of the PA2G4 (EBP1) protein with ErbB-3 and regulation of
this binding by heregulin.";
Br. J. Cancer 82:683-690(2000).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Caroli F., Lamartine J., Sylla B.S., Romeo G., Seri M.;
"Genomic structure of the human PA2G4 gene.";
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 2-20; 23-30; 34-62; 73-101; 156-172; 200-211;
216-236; 264-281 AND 299-364, CLEAVAGE OF INITIATOR METHIONINE,
ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=B-cell lymphoma, Mammary carcinoma, and Ovarian carcinoma;
Bienvenut W.V., Matallanas D., Cooper W.N., Boldt K.,
von Kriegsheim A.F., Kolch W.;
Submitted (JAN-2010) to UniProtKB.
[6]
PROTEIN SEQUENCE OF 34-51; 216-236; 264-271; 299-311; 333-344 AND
377-394, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[7]
INTERACTION WITH ERBB3, PHOSPHORYLATION, PHOSPHORYLATION BY PKC,
PHOSPHORYLATION AT THR-366, AND MUTAGENESIS OF SER-363 AND THR-366.
PubMed=11325528; DOI=10.1016/S0303-7207(01)00387-2;
Lessor T.J., Hamburger A.W.;
"Regulation of the ErbB3 binding protein Ebp1 by protein kinase C.";
Mol. Cell. Endocrinol. 175:185-191(2001).
[8]
FUNCTION IN TRANSCRIPTION REPRESSION, AND INTERACTION WITH RB1.
PubMed=11268000; DOI=10.1002/jcp.1075;
Xia X., Cheng A., Lessor T., Zhang Y., Hamburger A.W.;
"Ebp1, an ErbB-3 binding protein, interacts with Rb and affects Rb
transcriptional regulation.";
J. Cell. Physiol. 187:209-217(2001).
[9]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=12429849; DOI=10.1091/mbc.E02-05-0271;
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
Greco A., Hochstrasser D.F., Diaz J.-J.;
"Functional proteomic analysis of human nucleolus.";
Mol. Biol. Cell 13:4100-4109(2002).
[10]
FUNCTION IN E2F1-MEDIATED TRANSCRIPTION REPRESSION, AND INTERACTION
WITH HDAC2.
PubMed=12682367; DOI=10.1093/nar/gkg318;
Zhang Y., Woodford N., Xia X., Hamburger A.W.;
"Repression of E2F1-mediated transcription by the ErbB3 binding
protein Ebp1 involves histone deacetylases.";
Nucleic Acids Res. 31:2168-2177(2003).
[11]
FUNCTION IN RRNA PROCESSING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RNA-BINDING, IDENTIFICATION IN A RIBONUCLEOPROTEIN COMPLEX,
ASSOCIATION WITH RRNA, ASSOCIATION WITH U3 SNORNA, AND MUTAGENESIS OF
20-LYS--LYS-22 AND 364-ARG-LYS-365.
PubMed=15064750; DOI=10.1038/sj.onc.1207579;
Squatrito M., Mancino M., Donzelli M., Areces L.B., Draetta G.F.;
"EBP1 is a nucleolar growth-regulating protein that is part of pre-
ribosomal ribonucleoprotein complexes.";
Oncogene 23:4454-4465(2004).
[12]
FUNCTION IN TRANSCRIPTION REPRESSION, AND INTERACTION WITH ERBB3 AND
AR.
PubMed=15583694; DOI=10.1038/sj.bjc.6602257;
Zhang Y., Hamburger A.W.;
"Specificity and heregulin regulation of Ebp1 (ErbB3 binding protein
1) mediated repression of androgen receptor signalling.";
Br. J. Cancer 92:140-146(2005).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND THR-386, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-386, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[15]
ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION,
INTERACTION WITH ERBB3, PHOSPHORYLATION AT SER-361, AND MUTAGENESIS OF
SER-361.
PubMed=16832058; DOI=10.1073/pnas.0602923103;
Liu Z., Ahn J.Y., Liu X., Ye K.;
"Ebp1 isoforms distinctively regulate cell survival and
differentiation.";
Proc. Natl. Acad. Sci. U.S.A. 103:10917-10922(2006).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361 AND THR-386, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[18]
POLYUBIQUITINATION, SUBCELLULAR LOCATION, INTERACTION WITH RNF20 AND
HUWE1, TISSUE SPECIFICITY, AND MUTAGENESIS OF SER-361.
PubMed=19037095; DOI=10.1091/mbc.E08-09-0983;
Liu Z., Oh S.M., Okada M., Liu X., Cheng D., Peng J., Brat D.J.,
Sun S.Y., Zhou W., Gu W., Ye K.;
"Human BRE1 is an E3 ubiquitin ligase for Ebp1 tumor suppressor.";
Mol. Biol. Cell 20:757-768(2009).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-386, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-2; SER-361 AND THR-386, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[22]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-2 AND THR-386, CLEAVAGE OF INITIATOR METHIONINE
[LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[23]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[24]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-335 AND SER-361,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[28]
INTERACTION WITH DNAJC21.
PubMed=27346687; DOI=10.1016/j.ajhg.2016.05.002;
Tummala H., Walne A.J., Williams M., Bockett N., Collopy L.,
Cardoso S., Ellison A., Wynn R., Leblanc T., Fitzgibbon J.,
Kelsell D.P., van Heel D.A., Payne E., Plagnol V., Dokal I.,
Vulliamy T.;
"DNAJC21 mutations link a cancer-prone bone marrow failure syndrome to
corruption in 60S ribosome subunit maturation.";
Am. J. Hum. Genet. 99:115-124(2016).
[29]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-298, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[30]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), INTERACTION WITH 5S RIBOSOMAL
RNA, AND LACK OF AMINOPEPTIDASE ACTIVITY.
PubMed=17765895; DOI=10.1016/j.febslet.2007.08.024;
Kowalinski E., Bange G., Bradatsch B., Hurt E., Wild K., Sinning I.;
"The crystal structure of Ebp1 reveals a methionine aminopeptidase
fold as binding platform for multiple interactions.";
FEBS Lett. 581:4450-4454(2007).
-!- FUNCTION: May play a role in a ERBB3-regulated signal transduction
pathway. Seems be involved in growth regulation. Acts a
corepressor of the androgen receptor (AR) and is regulated by the
ERBB3 ligand neuregulin-1/heregulin (HRG). Inhibits transcription
of some E2F1-regulated promoters, probably by recruiting histone
acetylase (HAT) activity. Binds RNA. Associates with 28S, 18S and
5.8S mature rRNAs, several rRNA precursors and probably U3 small
nucleolar RNA. May be involved in regulation of intermediate and
late steps of rRNA processing. May be involved in ribosome
assembly. Mediates cap-independent translation of specific viral
IRESs (internal ribosomal entry site) (By similarity). Regulates
cell proliferation, differentiation, and survival. Isoform 1
suppresses apoptosis whereas isoform 2 promotes cell
differentiation (By similarity). {ECO:0000250|UniProtKB:P50580,
ECO:0000250|UniProtKB:Q6AYD3, ECO:0000269|PubMed:11268000,
ECO:0000269|PubMed:12682367, ECO:0000269|PubMed:15064750,
ECO:0000269|PubMed:15583694, ECO:0000269|PubMed:16832058}.
-!- SUBUNIT: Isoform 2 interacts with the cytoplasmic domain of non-
phosphorylated ERBB3; the interaction requires PKC activity.
Interacts with AR. Treatment with HRG leads to dissociation from
ERBB3 and increases association with AR. Interacts with
NCL/nucleolin. Component of a ribonucleoprotein complex containing
at least PA2G4, NCL, TOP1, PABPC2, RPLP0, acetylated histone H1
(HIST1H1A or H1F1), histone H1 2/4, RPL4, RPL8, RPL15, RPL18,
RPL18A, RPL21, RPL11, RPL12, RPL28, RPL27, RPLP2 and RPL24.
Interacts with HDAC2. Interacts with RB1; the interaction is
enhanced upon PA2G4 dephosphorylation. Interacts with AKT1 (By
similarity). Isoform 1 and isoform 2 interact with RNF20. Isoform
2 interacts with HUWE1. Interacts with DNAJC21 (PubMed:27346687).
{ECO:0000250|UniProtKB:Q6AYD3, ECO:0000269|PubMed:10682683,
ECO:0000269|PubMed:11268000, ECO:0000269|PubMed:11325528,
ECO:0000269|PubMed:12682367, ECO:0000269|PubMed:15064750,
ECO:0000269|PubMed:15583694, ECO:0000269|PubMed:16832058,
ECO:0000269|PubMed:17765895, ECO:0000269|PubMed:19037095,
ECO:0000269|PubMed:27346687}.
-!- INTERACTION:
P19338:NCL; NbExp=2; IntAct=EBI-924893, EBI-346967;
P06400:RB1; NbExp=4; IntAct=EBI-924893, EBI-491274;
Q96ST3:SIN3A; NbExp=4; IntAct=EBI-924893, EBI-347218;
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm
{ECO:0000269|PubMed:16832058, ECO:0000269|PubMed:19037095}.
Nucleus, nucleolus {ECO:0000269|PubMed:16832058,
ECO:0000269|PubMed:19037095}. Note=Translocates to the nucleus
upon treatment with HRG. Phosphorylation at Ser-361 by PKC/PRKCD
regulates its nucleolar localization.
{ECO:0000269|PubMed:16832058}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm
{ECO:0000269|PubMed:16832058, ECO:0000269|PubMed:19037095}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1 {ECO:0000305}; Synonyms=p48 {ECO:0000303|PubMed:16832058};
IsoId=Q9UQ80-1; Sequence=Displayed;
Name=2 {ECO:0000305}; Synonyms=p42 {ECO:0000303|PubMed:16832058};
IsoId=Q9UQ80-2; Sequence=VSP_057325;
-!- TISSUE SPECIFICITY: Isoform 2 is undetectable whereas isoform 1 is
strongly expressed in cancer cells (at protein level). Isoform 1
and isoform 2 are widely expressed, including heart, brain, lung,
pancreas, skeletal muscle, kidney, placenta and liver.
{ECO:0000269|PubMed:10682683, ECO:0000269|PubMed:15064750,
ECO:0000269|PubMed:19037095}.
-!- PTM: Phosphorylated on serine and threonine residues.
Phosphorylation is enhanced by HRG treatment. Basal
phosphorylation is PKC-dependent and HRG-induced phosphorylation
is predominantly PKC-independent. Phosphorylation at Ser-361 by
PKC/PRKCD regulates its nucleolar localization.
{ECO:0000269|PubMed:11325528, ECO:0000269|PubMed:16832058,
ECO:0000269|PubMed:19037095}.
-!- PTM: In cancer cells, isoform 2 is polyubiquitinated leading to
its proteasomal degradation and phosphorylation by PKC/PRKCD
enhances polyubiquitination. {ECO:0000269|PubMed:19037095}.
-!- SIMILARITY: Belongs to the peptidase M24 family. {ECO:0000305}.
-!- CAUTION: Although it belongs to the peptidase M24 family, it does
not contain metal cofactors and lacks aminopeptidase activity.
{ECO:0000305|PubMed:17765895}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PA2G4ID41628ch12q13.html";
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EMBL; U59435; AAB91536.1; -; mRNA.
EMBL; U87954; AAD00646.1; -; mRNA.
EMBL; AF104670; AAD05561.1; -; Genomic_DNA.
EMBL; AF104668; AAD05561.1; JOINED; Genomic_DNA.
EMBL; AF104669; AAD05561.1; JOINED; Genomic_DNA.
EMBL; BC001951; AAH01951.1; -; mRNA.
EMBL; BC007561; AAH07561.1; -; mRNA.
EMBL; BC069786; AAH69786.1; -; mRNA.
CCDS; CCDS8902.1; -. [Q9UQ80-1]
RefSeq; NP_006182.2; NM_006191.2. [Q9UQ80-1]
UniGene; Hs.524498; -.
UniGene; Hs.745109; -.
PDB; 2Q8K; X-ray; 1.60 A; A=2-394.
PDB; 3J2I; EM; 11.90 A; A=1-394.
PDBsum; 2Q8K; -.
PDBsum; 3J2I; -.
ProteinModelPortal; Q9UQ80; -.
SMR; Q9UQ80; -.
BioGrid; 111075; 137.
DIP; DIP-31275N; -.
ELM; Q9UQ80; -.
IntAct; Q9UQ80; 62.
MINT; MINT-5000754; -.
STRING; 9606.ENSP00000302886; -.
MEROPS; M24.973; -.
iPTMnet; Q9UQ80; -.
PhosphoSitePlus; Q9UQ80; -.
SwissPalm; Q9UQ80; -.
BioMuta; PA2G4; -.
DMDM; 13632817; -.
SWISS-2DPAGE; Q9UQ80; -.
EPD; Q9UQ80; -.
PaxDb; Q9UQ80; -.
PeptideAtlas; Q9UQ80; -.
PRIDE; Q9UQ80; -.
DNASU; 5036; -.
Ensembl; ENST00000303305; ENSP00000302886; ENSG00000170515. [Q9UQ80-1]
GeneID; 5036; -.
KEGG; hsa:5036; -.
UCSC; uc001sjm.4; human. [Q9UQ80-1]
CTD; 5036; -.
DisGeNET; 5036; -.
EuPathDB; HostDB:ENSG00000170515.13; -.
GeneCards; PA2G4; -.
HGNC; HGNC:8550; PA2G4.
HPA; CAB011711; -.
HPA; CAB012428; -.
HPA; HPA016484; -.
MIM; 602145; gene.
neXtProt; NX_Q9UQ80; -.
OpenTargets; ENSG00000170515; -.
PharmGKB; PA32877; -.
eggNOG; KOG2776; Eukaryota.
eggNOG; COG0024; LUCA.
GeneTree; ENSGT00530000063220; -.
HOGENOM; HOG000168207; -.
HOVERGEN; HBG053117; -.
InParanoid; Q9UQ80; -.
OMA; HTVLLMP; -.
OrthoDB; EOG091G0B89; -.
PhylomeDB; Q9UQ80; -.
TreeFam; TF300010; -.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SIGNOR; Q9UQ80; -.
ChiTaRS; PA2G4; human.
EvolutionaryTrace; Q9UQ80; -.
GeneWiki; PA2G4; -.
GenomeRNAi; 5036; -.
PRO; PR:Q9UQ80; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000170515; -.
CleanEx; HS_PA2G4; -.
ExpressionAtlas; Q9UQ80; baseline and differential.
Genevisible; Q9UQ80; HS.
GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0007050; P:cell cycle arrest; TAS:ProtInc.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0045597; P:positive regulation of cell differentiation; ISS:UniProtKB.
GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR036005; Creatinase/aminopeptidase-like.
InterPro; IPR004545; PA2G4.
InterPro; IPR000994; Pept_M24.
InterPro; IPR018349; Pept_M24A_MAP2_BS.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF00557; Peptidase_M24; 1.
SUPFAM; SSF46785; SSF46785; 1.
SUPFAM; SSF55920; SSF55920; 2.
TIGRFAMs; TIGR00495; crvDNA_42K; 1.
PROSITE; PS01202; MAP_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; Isopeptide bond; Nucleus;
Phosphoprotein; Reference proteome; Repressor; Ribonucleoprotein;
RNA-binding; rRNA processing; Transcription; Transcription regulation;
Translation regulation; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.5}.
CHAIN 2 394 Proliferation-associated protein 2G4.
/FTId=PRO_0000148989.
REGION 2 48 Necessary for nucleolar localization.
{ECO:0000269|PubMed:15064750}.
REGION 46 54 RNA-binding.
{ECO:0000269|PubMed:15064750}.
REGION 301 394 Necessary for nucleolar localization.
{ECO:0000269|PubMed:15064750}.
REGION 361 375 Interaction with RNA.
{ECO:0000250|UniProtKB:P50580}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.5}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 335 335 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 361 361 Phosphoserine; by PKC/PRKCD.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:16832058}.
MOD_RES 366 366 Phosphothreonine.
{ECO:0000305|PubMed:11325528}.
MOD_RES 386 386 Phosphothreonine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
CROSSLNK 298 298 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 54 Missing (in isoform 2).
{ECO:0000269|PubMed:16832058}.
/FTId=VSP_057325.
MUTAGEN 20 22 KYK->AYA: Loss of nucleolar localization.
{ECO:0000269|PubMed:15064750}.
MUTAGEN 361 361 S->A: Loss of phosphorylation and
interaction with ERBB3 and HUWE1.
{ECO:0000269|PubMed:16832058}.
MUTAGEN 361 361 S->D: No effect on phosphorylation and
loss of nucleolar localization.
{ECO:0000269|PubMed:16832058}.
MUTAGEN 363 363 S->A: No effect on in vitro
phosphorylation by PKC.
{ECO:0000269|PubMed:11325528}.
MUTAGEN 364 365 RK->AA: Only partial nucleolar
localization.
{ECO:0000269|PubMed:15064750}.
MUTAGEN 366 366 T->A: Decreases in vitro phosphorylation
by PKC. {ECO:0000269|PubMed:11325528}.
CONFLICT 381 381 A -> P (in Ref. 1; AAB91536).
{ECO:0000305}.
HELIX 15 38 {ECO:0000244|PDB:2Q8K}.
HELIX 45 61 {ECO:0000244|PDB:2Q8K}.
STRAND 72 82 {ECO:0000244|PDB:2Q8K}.
STRAND 85 87 {ECO:0000244|PDB:2Q8K}.
STRAND 105 114 {ECO:0000244|PDB:2Q8K}.
STRAND 117 126 {ECO:0000244|PDB:2Q8K}.
HELIX 137 156 {ECO:0000244|PDB:2Q8K}.
HELIX 163 175 {ECO:0000244|PDB:2Q8K}.
TURN 176 178 {ECO:0000244|PDB:2Q8K}.
STRAND 186 191 {ECO:0000244|PDB:2Q8K}.
STRAND 194 196 {ECO:0000244|PDB:2Q8K}.
STRAND 200 204 {ECO:0000244|PDB:2Q8K}.
HELIX 207 212 {ECO:0000244|PDB:2Q8K}.
STRAND 223 233 {ECO:0000244|PDB:2Q8K}.
STRAND 246 249 {ECO:0000244|PDB:2Q8K}.
HELIX 260 273 {ECO:0000244|PDB:2Q8K}.
HELIX 280 282 {ECO:0000244|PDB:2Q8K}.
HELIX 287 298 {ECO:0000244|PDB:2Q8K}.
STRAND 301 305 {ECO:0000244|PDB:2Q8K}.
STRAND 316 326 {ECO:0000244|PDB:2Q8K}.
STRAND 329 332 {ECO:0000244|PDB:2Q8K}.
HELIX 340 342 {ECO:0000244|PDB:2Q8K}.
HELIX 352 359 {ECO:0000244|PDB:2Q8K}.
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


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