Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  C-terminal-binding protein 1  

UniProtKB / Swiss-Prot ID :  CTBP1_HUMAN

Gene Name (Synonyms) : 
CTBP1, CTBP  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Nucleus. 

Protein Function :  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. 

Protein Sequence MGSSHLLNKGLPLGVRPPIMNGPLHPRPLVALLDGRDCTVEMPILKDVATVAFCDAQSTQEIHEKVLNEA...
Predicted Secondary Structure CCCCCCCCCCCCEEECCCEECCCCCCCCEEEEEECCCCHHHHHHHCCCEEEEEECCCCCHHHHHHHHCCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
100PhosphoserineVRIGSGFDN
EEECCCCCH
33.64Phosphositeplus
Link
144PhosphothreonineYRRATWLHQ
HHCCHHHHH
27.09Phosphositeplus
Link
158PhosphoserineTRVQSVEQI
CCCCCCCCC
25.43Phosphositeplus
Link
273Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LVDEKALAQ
EECHHHHHH
44.21Phosphositeplus
Link
280Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AQALKEGRI
HHHHHCCCE
62.23Phosphositeplus
Link
300PhosphoserinePFSFSQGPL
CCCCCCCHH
32.79HPRD
Link
300PhosphoserinePFSFSQGPL
CCCCCCCHH
32.79PhosphoELM
Link
300PhosphoserinePFSFSQGPL
CCCCCCCHH
32.79Phosphositeplus
Link
300Phosphoserine.PFSFSQGPL
CCCCCCCHH
32.79UniProtKB
Link
381PhosphotyrosineAAYRYPPGV
HHHCCCCCE
10.91HPRD
Link-
422PhosphoserinePHAPSPGQT
CCCCCCCCC
42.31HPRD
Link-
422PhosphoserinePHAPSPGQT
CCCCCCCCC
42.31Phosphositeplus
Link-
422Phosphoserine; by HIPK2.PHAPSPGQT
CCCCCCCCC
42.31UniProtKB
Link-
428Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)GQTVKPEAD
CCCCCCCCC
40.29HPRD
Link-
428Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)GQTVKPEAD
CCCCCCCCC
40.29Phosphositeplus
Link-
428Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO).GQTVKPEAD
CCCCCCCCC
40.29UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
ZEB1_HUMANphysical interactionMINT-17555MINT10359772
BRCA1_HUMANphysical interactionMINT-16218MINT9738006
IKZF1_HUMANphysical interactionMINT-19404MINT10766745
TGIF1_HUMANphysical interactionMINT-14492MINT10995736
LDB2_HUMANphysical interactionDIP:40203EDIP11751867
RBBP8_HUMANphysical interactionDIP:40197EDIP10449734
LMO4_HUMANphysical interaction
physical interaction
DIP:40198EDIP11751867
11751867
BRCA1_HUMANin vitro
in vivo
HPRD:04015HPRD10196224
EF1D_HUMANin vitro
yeast 2-hybrid
HPRD:04015HPRD10567582
HD_HUMANin vivoHPRD:04015HPRD11739372
NOS1_HUMANin vitro
in vivo
HPRD:04015HPRD11590170
EVI1_HUMANin vitro
in vivo
HPRD:04015HPRD11313276
11328817
RB_HUMANin vivoHPRD:04015HPRD11583618
ZEB1_HUMANyeast 2-hybridHPRD:04015HPRD10359772
12714599
ELK3_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:04015HPRD10369679
BMPR2_HUMANin vitroHPRD:04015HPRD15188402
HDAC1_HUMANin vitro
in vivo
HPRD:04015HPRD9650586
NRIP1_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:04015HPRD11509661
CTBP1_HUMANin vitro
in vivo
HPRD:04015HPRD11313276
PCAF_HUMANin vitroHPRD:04015HPRD15834423
EP300_HUMANin vitro
in vivo
HPRD:04015HPRD15834423
PININ_HUMANENSP00000290921STRING
ELK3_HUMANENSP00000290921STRING
HDAC9_HUMANENSP00000290921STRING
GLIS2_HUMANENSP00000290921STRING
EP300_HUMANENSP00000290921STRING
HIPK2_HUMANENSP00000290921STRING
PCAF_HUMANENSP00000290921STRING
SUMO1_HUMANENSP00000290921STRING
CBX4_HUMANENSP00000290921STRING
HIC1_HUMANENSP00000290921STRING
ZEB1_HUMANENSP00000290921STRING
NRIP1_HUMANENSP00000290921STRING
UBA1_HUMANENSP00000290921STRING
TF7L2_HUMANENSP00000290921STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Homeodomain interacting protein kinase 2 promotes apoptosis bydownregulating the transcriptional corepressor CtBP.";
Zhang Q., Yoshimatsu Y., Hildebrand J., Frisch S.M., Goodman R.H.;
Cell 115:177-186(2003).
Cited for: INTERACTION WITH HIPK2, PHOSPHORYLATION AT SER-422, AND MUTAGENESIS OFSER-422.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300, AND MASSSPECTROMETRY.
Sumoylation
ReferencePubMed
"The polycomb protein Pc2 is a SUMO E3.";
Kagey M.H., Melhuish T.A., Wotton D.;
Cell 113:127-137(2003).
Cited for: SUMOYLATION AT LYS-428, AND SUBCELLULAR LOCATION.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures