CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023974
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glucocorticoid modulatory element-binding protein 1 
Protein Synonyms/Alias
 GMEB-1; DNA-binding protein p96PIF; Parvovirus initiation factor p96; PIF p96 
Gene Name
 GMEB1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
110KAILLWKKFVCPGINubiquitination[1]
119VCPGINVKCVKFNDQubiquitination[1]
122GINVKCVKFNDQLISubiquitination[1]
131NDQLISPKHFVHLAGubiquitination[1]
143LAGKSTLKDWKRAIRubiquitination[1]
158LGGIMLRKMMDSGQIubiquitination[1]
182SNTCRSTKFDLLISSubiquitination[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 82 166 SAND.
 METAL 113 113 Zinc.
 METAL 170 170 Zinc.
 METAL 174 174 Zinc.
 METAL 178 178 Zinc.
 BINDING 139 139 DNA.
 BINDING 143 143 DNA.
 BINDING 146 146 DNA.
 BINDING 157 157 DNA.
 MOD_RES 2 2 N-acetylalanine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Coiled coil; Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding; Metal-binding; Nucleus; Polymorphism; Reference proteome; Transcription; Transcription regulation; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 573 AA 
Protein Sequence
MANAEVSVPV GDVVVVPTEG NEGENPEDTK TQVILQLQPV QQGLFIDGHF YNRIYEAGSE 60
NNTAVVAVET HTIHKIEEGI DTGTIEANED MEIAYPITCG ESKAILLWKK FVCPGINVKC 120
VKFNDQLISP KHFVHLAGKS TLKDWKRAIR LGGIMLRKMM DSGQIDFYQH DKVCSNTCRS 180
TKFDLLISSA RAPVPGQQTS VVQTPTSADG SITQIAISEE SMEEAGLEWN SALTAAVTMA 240
TEEGVKKDSE EISEDTLMFW KGIADVGLME EVVCNIQKEI EELLRGVQQR LIQAPFQVTD 300
AAVLNNVAHT FGLMDTVKKV LDNRRNQVEQ GEEQFLYTLT DLERQLEEQK KQGQDHRLKS 360
QTVQNVVLMP VSTPKPPKRP RLQRPASTTV LSPSPPVQQP QFTVISPITI TPVGQSFSMG 420
NIPVATLSQG SSPVTVHTLP SGPQLFRYAT VVSSAKSSSP DTVTIHPSSS LALLSSTAMQ 480
DGSTLGNMTT MVSPVELVAM ESGLTSAIQA VESTSEDGQT IIEIDPAPDP EAEDTEGKAV 540
ILETELRTEE KVVAEMEEHQ HQVHNVEIVV LED 573 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:Compara.
 GO:0003713; F:transcription coactivator activity; TAS:ProtInc.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR024830; GMEB1/2.
 IPR000770; SAND_dom.
 IPR010919; SAND_dom-like. 
Pfam
 PF01342; SAND 
SMART
 SM00258; SAND 
PROSITE
 PS50864; SAND 
PRINTS