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Protein

Glucocorticoid modulatory element-binding protein 2

Gene

GMEB2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Trans-acting factor that binds to glucocorticoid modulatory elements (GME) present in the TAT (tyrosine aminotransferase) promoter and increases sensitivity to low concentrations of glucocorticoids. Binds also to the transferrin receptor promoter. Essential auxiliary factor for the replication of parvoviruses.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi110 – 1101ZincBy similarity
Binding sitei136 – 1361DNABy similarity
Binding sitei140 – 1401DNABy similarity
Binding sitei143 – 1431DNABy similarity
Binding sitei154 – 1541DNABy similarity
Metal bindingi167 – 1671ZincBy similarity
Metal bindingi171 – 1711ZincBy similarity
Metal bindingi175 – 1751ZincBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Glucocorticoid modulatory element-binding protein 2
Short name:
GMEB-2
Alternative name(s):
DNA-binding protein p79PIF
Parvovirus initiation factor p79
Short name:
PIF p79
Gene namesi
Name:GMEB2
Synonyms:KIAA1269
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:4371. GMEB2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • nucleoplasm Source: HPA
  • nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28756.

Polymorphism and mutation databases

BioMutaiGMEB2.
DMDMi22001626.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 530530Glucocorticoid modulatory element-binding protein 2PRO_0000074092Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei373 – 3731PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9UKD1.
MaxQBiQ9UKD1.
PaxDbiQ9UKD1.
PRIDEiQ9UKD1.

PTM databases

iPTMnetiQ9UKD1.
PhosphoSiteiQ9UKD1.

Expressioni

Tissue specificityi

Expressed in peripheral blood lymphocytes and fetal liver. Expressed preferentially in reproductive and/or developmentally important cells, such as testis, placenta, bone marrow and fetal tissues.

Gene expression databases

BgeeiQ9UKD1.
CleanExiHS_GMEB2.
ExpressionAtlasiQ9UKD1. baseline and differential.
GenevisibleiQ9UKD1. HS.

Organism-specific databases

HPAiHPA009706.

Interactioni

Subunit structurei

Homodimer, and heterodimer of GMEB1 and GMEB2. GMEB1 and GMEB2 form the parvovirus initiator complex (PIF). Interacts with the glucocorticoid receptor (NR3C1). May interact with CREB-binding protein (CBP).

Protein-protein interaction databases

BioGridi117605. 13 interactions.
IntActiQ9UKD1. 2 interactions.
MINTiMINT-2871927.
STRINGi9606.ENSP00000266068.

Structurei

3D structure databases

ProteinModelPortaliQ9UKD1.
SMRiQ9UKD1. Positions 87-176.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini81 – 16383SANDPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili304 – 34845Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi57 – 648Poly-Ala

Sequence similaritiesi

Contains 1 SAND domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG4333. Eukaryota.
ENOG410ZMTP. LUCA.
GeneTreeiENSGT00410000025596.
HOVERGENiHBG051742.
InParanoidiQ9UKD1.
OMAiDDTFAFW.
PhylomeDBiQ9UKD1.
TreeFamiTF317090.

Family and domain databases

Gene3Di3.10.390.10. 1 hit.
InterProiIPR024830. GMEB1/2.
IPR000770. SAND_dom.
IPR010919. SAND_dom-like.
[Graphical view]
PANTHERiPTHR10417. PTHR10417. 1 hit.
PfamiPF01342. SAND. 1 hit.
[Graphical view]
SMARTiSM00258. SAND. 1 hit.
[Graphical view]
SUPFAMiSSF63763. SSF63763. 1 hit.
PROSITEiPS50864. SAND. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9UKD1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATPDVSVHM EEVVVVTTPD TAVDGSGVEG VKTVLVTTNL APHGGDLTED
60 70 80 90 100
NMETENAAAA AAAAFTASSQ LKEAVLVKMA EEGENLEAEI VYPITCGDSR
110 120 130 140 150
ANLIWRKFVC PGINVKCVQY DEHVISPKEF VHLAGKSTLK DWKRAIRMNG
160 170 180 190 200
IMLRKIMDSG ELDFYQHDKV CSNTCRSTKI DLSGARVSLS SPTSAEYIPL
210 220 230 240 250
TPAAADVNGS PATITIETCE DPGDWTAAIG DDTFTFWRGL KDAGLLDEVI
260 270 280 290 300
QEFHQELVET MRGLQQRVQD PPLQLRDAVL LNNIVQNFGM LDLVKKVLAS
310 320 330 340 350
HKCQMDRSRE QYARDLAALE QQCDEHRRRA KELKHKSQHL SNVLMTLTPV
360 370 380 390 400
SLPPPVKRPR LARATSGPAA MASQVLTQSA QLALGPGVPV PQLTSVPLGK
410 420 430 440 450
VVSTLPSTVL GKGSLQAPPA SSPASPLLGG YTVLASSGST YPSTVEIHPD
460 470 480 490 500
ASSLTVLSTA AVQDGSTVFK VVSPLQLLTL PGLGPTLQNV AQASPGSSTI
510 520 530
VTVPAGAAPG PEEHTATIEV AAMAEDHERK
Length:530
Mass (Da):56,421
Last modified:May 1, 2000 - v1
Checksum:iD2EEF49FD8206854
GO

Sequence cautioni

The sequence BAA86583.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 4421DGSGV…LAPHG → CPAGCALRDPDSILSSLHFT R (PubMed:17974005).CuratedAdd
BLAST
Sequence conflicti77 – 782Missing (PubMed:17974005).Curated
Sequence conflicti381 – 3822QL → PV in BAA86583 (PubMed:10574462).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF173867 mRNA. Translation: AAD51351.1.
AB033095 mRNA. Translation: BAA86583.1. Different initiation.
AL121907, AL353715 Genomic DNA. Translation: CAI22265.1.
AL353715, AL121907 Genomic DNA. Translation: CAI17956.1.
CH471077 Genomic DNA. Translation: EAW75253.1.
CH471077 Genomic DNA. Translation: EAW75254.1.
BC036305 mRNA. Translation: AAH36305.1.
AL133646 mRNA. Translation: CAB63765.1.
CCDSiCCDS13528.1.
RefSeqiNP_036516.1. NM_012384.4.
XP_005260259.1. XM_005260202.3.
UniGeneiHs.473286.

Genome annotation databases

EnsembliENST00000266068; ENSP00000266068; ENSG00000101216.
ENST00000370077; ENSP00000359094; ENSG00000101216.
GeneIDi26205.
KEGGihsa:26205.
UCSCiuc002yfp.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF173867 mRNA. Translation: AAD51351.1.
AB033095 mRNA. Translation: BAA86583.1. Different initiation.
AL121907, AL353715 Genomic DNA. Translation: CAI22265.1.
AL353715, AL121907 Genomic DNA. Translation: CAI17956.1.
CH471077 Genomic DNA. Translation: EAW75253.1.
CH471077 Genomic DNA. Translation: EAW75254.1.
BC036305 mRNA. Translation: AAH36305.1.
AL133646 mRNA. Translation: CAB63765.1.
CCDSiCCDS13528.1.
RefSeqiNP_036516.1. NM_012384.4.
XP_005260259.1. XM_005260202.3.
UniGeneiHs.473286.

3D structure databases

ProteinModelPortaliQ9UKD1.
SMRiQ9UKD1. Positions 87-176.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117605. 13 interactions.
IntActiQ9UKD1. 2 interactions.
MINTiMINT-2871927.
STRINGi9606.ENSP00000266068.

PTM databases

iPTMnetiQ9UKD1.
PhosphoSiteiQ9UKD1.

Polymorphism and mutation databases

BioMutaiGMEB2.
DMDMi22001626.

Proteomic databases

EPDiQ9UKD1.
MaxQBiQ9UKD1.
PaxDbiQ9UKD1.
PRIDEiQ9UKD1.

Protocols and materials databases

DNASUi26205.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000266068; ENSP00000266068; ENSG00000101216.
ENST00000370077; ENSP00000359094; ENSG00000101216.
GeneIDi26205.
KEGGihsa:26205.
UCSCiuc002yfp.1. human.

Organism-specific databases

CTDi26205.
GeneCardsiGMEB2.
HGNCiHGNC:4371. GMEB2.
HPAiHPA009706.
MIMi607451. gene.
neXtProtiNX_Q9UKD1.
PharmGKBiPA28756.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4333. Eukaryota.
ENOG410ZMTP. LUCA.
GeneTreeiENSGT00410000025596.
HOVERGENiHBG051742.
InParanoidiQ9UKD1.
OMAiDDTFAFW.
PhylomeDBiQ9UKD1.
TreeFamiTF317090.

Miscellaneous databases

GeneWikiiGMEB2.
GenomeRNAii26205.
NextBioi48332.
PROiQ9UKD1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UKD1.
CleanExiHS_GMEB2.
ExpressionAtlasiQ9UKD1. baseline and differential.
GenevisibleiQ9UKD1. HS.

Family and domain databases

Gene3Di3.10.390.10. 1 hit.
InterProiIPR024830. GMEB1/2.
IPR000770. SAND_dom.
IPR010919. SAND_dom-like.
[Graphical view]
PANTHERiPTHR10417. PTHR10417. 1 hit.
PfamiPF01342. SAND. 1 hit.
[Graphical view]
SMARTiSM00258. SAND. 1 hit.
[Graphical view]
SUPFAMiSSF63763. SSF63763. 1 hit.
PROSITEiPS50864. SAND. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Two new members of the emerging KDWK family of combinatorial transcription modulators bind as a heterodimer to flexibly spaced PuCGPy half-sites."
    Christensen J., Cotmore S.F., Tattersall P.
    Mol. Cell. Biol. 19:7741-7750(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 156-169.
    Tissue: Cervix carcinoma.
  2. "Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.
    DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  3. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 24-530.
    Tissue: Testis.
  7. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiGMEB2_HUMAN
AccessioniPrimary (citable) accession number: Q9UKD1
Secondary accession number(s): E1P5J3
, Q5TDS0, Q9H431, Q9H4X7, Q9H4X8, Q9UF78, Q9ULF1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: May 1, 2000
Last modified: April 13, 2016
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.