GMEB2_HUMAN
ID GMEB2_HUMAN Reviewed; 530 AA.
AC Q9UKD1; E1P5J3; Q5TDS0; Q9H431; Q9H4X7; Q9H4X8; Q9UF78; Q9ULF1;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Glucocorticoid modulatory element-binding protein 2;
DE Short=GMEB-2;
DE AltName: Full=DNA-binding protein p79PIF;
DE AltName: Full=Parvovirus initiation factor p79;
DE Short=PIF p79;
GN Name=GMEB2; Synonyms=KIAA1269;
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], AND PROTEIN SEQUENCE OF 156-169.
RC TISSUE=Cervix carcinoma;
RX PubMed=10523663; DOI=10.1128/mcb.19.11.7741;
RA Christensen J., Cotmore S.F., Tattersall P.;
RT "Two new members of the emerging KDWK family of combinatorial transcription
RT modulators bind as a heterodimer to flexibly spaced PuCGPy half-sites.";
RL Mol. Cell. Biol. 19:7741-7750(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 24-530.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373, 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 [8]
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 [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-155, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-155, 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).
CC -!- FUNCTION: Trans-acting factor that binds to glucocorticoid modulatory
CC elements (GME) present in the TAT (tyrosine aminotransferase) promoter
CC and increases sensitivity to low concentrations of glucocorticoids.
CC Binds also to the transferrin receptor promoter. Essential auxiliary
CC factor for the replication of parvoviruses.
CC -!- SUBUNIT: Homodimer, and heterodimer of GMEB1 and GMEB2. GMEB1 and GMEB2
CC form the parvovirus initiator complex (PIF). Interacts with the
CC glucocorticoid receptor (NR3C1). May interact with CREB-binding protein
CC (CBP).
CC -!- INTERACTION:
CC Q9UKD1; P54253: ATXN1; NbExp=5; IntAct=EBI-948296, EBI-930964;
CC Q9UKD1; O00311: CDC7; NbExp=3; IntAct=EBI-948296, EBI-374980;
CC Q9UKD1; Q96LK0: CEP19; NbExp=3; IntAct=EBI-948296, EBI-741885;
CC Q9UKD1; Q14192: FHL2; NbExp=3; IntAct=EBI-948296, EBI-701903;
CC Q9UKD1; Q9UKD1: GMEB2; NbExp=3; IntAct=EBI-948296, EBI-948296;
CC Q9UKD1; P25791-3: LMO2; NbExp=6; IntAct=EBI-948296, EBI-11959475;
CC Q9UKD1; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-948296, EBI-11742507;
CC Q9UKD1; Q9BXW4: MAP1LC3C; NbExp=3; IntAct=EBI-948296, EBI-2603996;
CC Q9UKD1; Q9H8S9: MOB1A; NbExp=3; IntAct=EBI-948296, EBI-748229;
CC Q9UKD1; Q9BRK3: MXRA8; NbExp=3; IntAct=EBI-948296, EBI-11721798;
CC Q9UKD1; Q13526: PIN1; NbExp=3; IntAct=EBI-948296, EBI-714158;
CC Q9UKD1; Q7Z3K3: POGZ; NbExp=3; IntAct=EBI-948296, EBI-1389308;
CC Q9UKD1; P78424: POU6F2; NbExp=3; IntAct=EBI-948296, EBI-12029004;
CC Q9UKD1; Q13114: TRAF3; NbExp=3; IntAct=EBI-948296, EBI-357631;
CC Q9UKD1; Q9UNY4-2: TTF2; NbExp=3; IntAct=EBI-948296, EBI-11980463;
CC Q9UKD1; Q96E35: ZMYND19; NbExp=3; IntAct=EBI-948296, EBI-746595;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=May be also cytoplasmic.
CC -!- TISSUE SPECIFICITY: Expressed in peripheral blood lymphocytes and fetal
CC liver. Expressed preferentially in reproductive and/or developmentally
CC important cells, such as testis, placenta, bone marrow and fetal
CC tissues.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86583.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF173867; AAD51351.1; -; mRNA.
DR EMBL; AB033095; BAA86583.1; ALT_INIT; mRNA.
DR EMBL; AL121907; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL353715; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75253.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75254.1; -; Genomic_DNA.
DR EMBL; BC036305; AAH36305.1; -; mRNA.
DR EMBL; AL133646; CAB63765.1; -; mRNA.
DR CCDS; CCDS13528.1; -.
DR RefSeq; NP_036516.1; NM_012384.4.
DR RefSeq; XP_005260259.1; XM_005260202.4.
DR AlphaFoldDB; Q9UKD1; -.
DR SMR; Q9UKD1; -.
DR BioGRID; 117605; 48.
DR IntAct; Q9UKD1; 29.
DR STRING; 9606.ENSP00000266068; -.
DR GlyConnect; 2845; 1 O-Linked glycan (1 site).
DR GlyGen; Q9UKD1; 15 sites, 2 O-linked glycans (15 sites).
DR iPTMnet; Q9UKD1; -.
DR PhosphoSitePlus; Q9UKD1; -.
DR BioMuta; GMEB2; -.
DR DMDM; 22001626; -.
DR EPD; Q9UKD1; -.
DR jPOST; Q9UKD1; -.
DR MassIVE; Q9UKD1; -.
DR MaxQB; Q9UKD1; -.
DR PaxDb; Q9UKD1; -.
DR PeptideAtlas; Q9UKD1; -.
DR PRIDE; Q9UKD1; -.
DR ProteomicsDB; 84767; -.
DR ABCD; Q9UKD1; 1 sequenced antibody.
DR Antibodypedia; 1759; 111 antibodies from 24 providers.
DR DNASU; 26205; -.
DR Ensembl; ENST00000266068.5; ENSP00000266068.1; ENSG00000101216.11.
DR Ensembl; ENST00000370077.2; ENSP00000359094.1; ENSG00000101216.11.
DR GeneID; 26205; -.
DR KEGG; hsa:26205; -.
DR MANE-Select; ENST00000370077.2; ENSP00000359094.1; NM_012384.5; NP_036516.1.
DR UCSC; uc002yfp.1; human.
DR CTD; 26205; -.
DR GeneCards; GMEB2; -.
DR HGNC; HGNC:4371; GMEB2.
DR HPA; ENSG00000101216; Low tissue specificity.
DR MIM; 607451; gene.
DR neXtProt; NX_Q9UKD1; -.
DR OpenTargets; ENSG00000101216; -.
DR PharmGKB; PA28756; -.
DR VEuPathDB; HostDB:ENSG00000101216; -.
DR eggNOG; KOG4333; Eukaryota.
DR GeneTree; ENSGT00410000025596; -.
DR InParanoid; Q9UKD1; -.
DR OMA; PGTVEIH; -.
DR OrthoDB; 692814at2759; -.
DR PhylomeDB; Q9UKD1; -.
DR TreeFam; TF317090; -.
DR PathwayCommons; Q9UKD1; -.
DR SignaLink; Q9UKD1; -.
DR BioGRID-ORCS; 26205; 37 hits in 1101 CRISPR screens.
DR ChiTaRS; GMEB2; human.
DR GeneWiki; GMEB2; -.
DR GenomeRNAi; 26205; -.
DR Pharos; Q9UKD1; Tdark.
DR PRO; PR:Q9UKD1; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9UKD1; protein.
DR Bgee; ENSG00000101216; Expressed in parotid gland and 197 other tissues.
DR ExpressionAtlas; Q9UKD1; baseline and differential.
DR Genevisible; Q9UKD1; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR Gene3D; 3.10.390.10; -; 1.
DR InterPro; IPR024830; GMEB1/2.
DR InterPro; IPR010919; SAND-like_dom_sf.
DR InterPro; IPR000770; SAND_dom.
DR PANTHER; PTHR10417; PTHR10417; 1.
DR Pfam; PF01342; SAND; 1.
DR SMART; SM00258; SAND; 1.
DR SUPFAM; SSF63763; SSF63763; 1.
DR PROSITE; PS50864; SAND; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc.
FT CHAIN 1..530
FT /note="Glucocorticoid modulatory element-binding protein 2"
FT /id="PRO_0000074092"
FT DOMAIN 81..163
FT /note="SAND"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00185"
FT COILED 304..348
FT /evidence="ECO:0000255"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
FT BINDING 140
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT CROSSLNK 155
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 155
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CONFLICT 24..44
FT /note="DGSGVEGVKTVLVTTNLAPHG -> CPAGCALRDPDSILSSLHFTR (in
FT Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 77..78
FT /note="Missing (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 381..382
FT /note="QL -> PV (in Ref. 2; BAA86583)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 530 AA; 56421 MW; D2EEF49FD8206854 CRC64;
MATPDVSVHM EEVVVVTTPD TAVDGSGVEG VKTVLVTTNL APHGGDLTED NMETENAAAA
AAAAFTASSQ LKEAVLVKMA EEGENLEAEI VYPITCGDSR ANLIWRKFVC PGINVKCVQY
DEHVISPKEF VHLAGKSTLK DWKRAIRMNG IMLRKIMDSG ELDFYQHDKV CSNTCRSTKI
DLSGARVSLS SPTSAEYIPL TPAAADVNGS PATITIETCE DPGDWTAAIG DDTFTFWRGL
KDAGLLDEVI QEFHQELVET MRGLQQRVQD PPLQLRDAVL LNNIVQNFGM LDLVKKVLAS
HKCQMDRSRE QYARDLAALE QQCDEHRRRA KELKHKSQHL SNVLMTLTPV SLPPPVKRPR
LARATSGPAA MASQVLTQSA QLALGPGVPV PQLTSVPLGK VVSTLPSTVL GKGSLQAPPA
SSPASPLLGG YTVLASSGST YPSTVEIHPD ASSLTVLSTA AVQDGSTVFK VVSPLQLLTL
PGLGPTLQNV AQASPGSSTI VTVPAGAAPG PEEHTATIEV AAMAEDHERK
