CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012075
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 C-terminal-binding protein 1 
Protein Synonyms/Alias
 CtBP1 
Gene Name
 CTBP1 
Gene Synonyms/Alias
 CTBP 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
88LTREDLEKFKALRIIubiquitination[1]
273RGGLVDEKALAQALKubiquitination[1, 2]
280KALAQALKEGRIRGAubiquitination[1, 2, 3, 4]
348GRIPDSLKNCVNKDHubiquitination[1]
428PSPGQTVKPEADRDHsumoylation[5, 6, 7]
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]
 [2] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [5] The polycomb protein Pc2 is a SUMO E3.
 Kagey MH, Melhuish TA, Wotton D.
 Cell. 2003 Apr 4;113(1):127-37. [PMID: 12679040]
 [6] Opposed regulation of corepressor CtBP by SUMOylation and PDZ binding.
 Lin X, Sun B, Liang M, Liang YY, Gast A, Hildebrand J, Brunicardi FC, Melchior F, Feng XH.
 Mol Cell. 2003 May;11(5):1389-96. [PMID: 12769861]
 [7] Inhibition of CtBP1 activity by Akt-mediated phosphorylation.
 Merrill JC, Kagey MH, Melhuish TA, Powers SE, Zerlanko BJ, Wotton D.
 J Mol Biol. 2010 May 21;398(5):657-71. [PMID: 20361981] 
Functional Description
 Involved in controlling the equilibrium between tubular and stacked structures in the Golgi complex. Functions in brown adipose tissue (BAT) differentiation. Corepressor targeting diverse transcription regulators such as GLIS2. Has dehydrogenase activity. 
Sequence Annotation
 NP_BIND 180 185 NAD (By similarity).
 NP_BIND 237 243 NAD (By similarity).
 NP_BIND 264 266 NAD (By similarity).
 NP_BIND 315 318 NAD (By similarity).
 REGION 1 70 Interaction with GLIS2 1 (By similarity).
 REGION 288 360 Interaction with GLIS2 2 (By similarity).
 ACT_SITE 266 266 By similarity.
 ACT_SITE 295 295 By similarity.
 ACT_SITE 315 315 Proton donor (By similarity).
 BINDING 100 100 NAD (By similarity).
 BINDING 204 204 NAD (By similarity).
 BINDING 290 290 NAD (By similarity).
 MOD_RES 300 300 Phosphoserine.
 MOD_RES 422 422 Phosphoserine; by HIPK2.
 CROSSLNK 428 428 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; ADP-ribosylation; Alternative splicing; Complete proteome; Cytoplasm; Differentiation; Direct protein sequencing; Host-virus interaction; Isopeptide bond; NAD; Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome; Repressor; Transcription; Transcription regulation; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 440 AA 
Protein Sequence
MGSSHLLNKG LPLGVRPPIM NGPLHPRPLV ALLDGRDCTV EMPILKDVAT VAFCDAQSTQ 60
EIHEKVLNEA VGALMYHTIT LTREDLEKFK ALRIIVRIGS GFDNIDIKSA GDLGIAVCNV 120
PAASVEETAD STLCHILNLY RRATWLHQAL REGTRVQSVE QIREVASGAA RIRGETLGII 180
GLGRVGQAVA LRAKAFGFNV LFYDPYLSDG VERALGLQRV STLQDLLFHS DCVTLHCGLN 240
EHNHHLINDF TVKQMRQGAF LVNTARGGLV DEKALAQALK EGRIRGAALD VHESEPFSFS 300
QGPLKDAPNL ICTPHAAWYS EQASIEMREE AAREIRRAIT GRIPDSLKNC VNKDHLTAAT 360
HWASMDPAVV HPELNGAAYR YPPGVVGVAP TGIPAAVEGI VPSAMSLSHG LPPVAHPPHA 420
PSPGQTVKPE ADRDHASDQL 440 
Gene Ontology
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0005667; C:transcription factor complex; IEA:Compara.
 GO:0017053; C:transcriptional repressor complex; ISS:UniProtKB.
 GO:0051287; F:NAD binding; ISS:UniProtKB.
 GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
 GO:0008022; F:protein C-terminus binding; TAS:ProtInc.
 GO:0019904; F:protein domain specific binding; IDA:BHF-UCL.
 GO:0001106; F:RNA polymerase II transcription corepressor activity; IDA:BHF-UCL.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:Compara.
 GO:0007030; P:Golgi organization; IEA:Compara.
 GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
 GO:0090241; P:negative regulation of histone H4 acetylation; IMP:BHF-UCL.
 GO:0031065; P:positive regulation of histone deacetylation; IMP:BHF-UCL.
 GO:0006468; P:protein phosphorylation; TAS:ProtInc.
 GO:0051726; P:regulation of cell cycle; IMP:BHF-UCL.
 GO:0034401; P:regulation of transcription by chromatin organization; IMP:BHF-UCL.
 GO:0019079; P:viral genome replication; TAS:ProtInc.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW.
 GO:0050872; P:white fat cell differentiation; ISS:UniProtKB. 
Interpro
 IPR006139; D-isomer_2_OHA_DH_cat_dom.
 IPR006140; D-isomer_2_OHA_DH_NAD-bd.
 IPR016040; NAD(P)-bd_dom. 
Pfam
 PF00389; 2-Hacid_dh
 PF02826; 2-Hacid_dh_C 
SMART
  
PROSITE
 PS00065; D_2_HYDROXYACID_DH_1
 PS00670; D_2_HYDROXYACID_DH_2
 PS00671; D_2_HYDROXYACID_DH_3 
PRINTS