CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023088
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glucocorticoid modulatory element-binding protein 2 
Protein Synonyms/Alias
 GMEB-2; DNA-binding protein p79PIF; Parvovirus initiation factor p79; PIF p79 
Gene Name
 GMEB2 
Gene Synonyms/Alias
 KIAA1269 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
116VCPGINVKCVQYDEHubiquitination[1]
155MNGIMLRKIMDSGELubiquitination[1]
169LDFYQHDKVCSNTCRubiquitination[1]
296GMLDLVKKVLASHKCubiquitination[1]
302KKVLASHKCQMDRSRubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961
Functional Description
 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. 
Sequence Annotation
 DOMAIN 81 163 SAND.
 METAL 110 110 Zinc (By similarity).
 METAL 167 167 Zinc (By similarity).
 METAL 171 171 Zinc (By similarity).
 METAL 175 175 Zinc (By similarity).
 BINDING 136 136 DNA (By similarity).
 BINDING 140 140 DNA (By similarity).
 BINDING 143 143 DNA (By similarity).
 BINDING 154 154 DNA (By similarity).
 MOD_RES 373 373 Phosphoserine.  
Keyword
 Coiled coil; Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription; Transcription regulation; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 530 AA 
Protein Sequence
MATPDVSVHM EEVVVVTTPD TAVDGSGVEG VKTVLVTTNL APHGGDLTED NMETENAAAA 60
AAAAFTASSQ LKEAVLVKMA EEGENLEAEI VYPITCGDSR ANLIWRKFVC PGINVKCVQY 120
DEHVISPKEF VHLAGKSTLK DWKRAIRMNG IMLRKIMDSG ELDFYQHDKV CSNTCRSTKI 180
DLSGARVSLS SPTSAEYIPL TPAAADVNGS PATITIETCE DPGDWTAAIG DDTFTFWRGL 240
KDAGLLDEVI QEFHQELVET MRGLQQRVQD PPLQLRDAVL LNNIVQNFGM LDLVKKVLAS 300
HKCQMDRSRE QYARDLAALE QQCDEHRRRA KELKHKSQHL SNVLMTLTPV SLPPPVKRPR 360
LARATSGPAA MASQVLTQSA QLALGPGVPV PQLTSVPLGK VVSTLPSTVL GKGSLQAPPA 420
SSPASPLLGG YTVLASSGST YPSTVEIHPD ASSLTVLSTA AVQDGSTVFK VVSPLQLLTL 480
PGLGPTLQNV AQASPGSSTI VTVPAGAAPG PEEHTATIEV AAMAEDHERK 530 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0003713; F:transcription coactivator activity; IEA:InterPro.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc. 
Interpro
 IPR024830; GMEB1/2.
 IPR000770; SAND_dom.
 IPR010919; SAND_dom-like. 
Pfam
 PF01342; SAND 
SMART
 SM00258; SAND 
PROSITE
 PS50864; SAND 
PRINTS