Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Protein farnesyltransferase subunit beta  

UniProtKB / Swiss-Prot ID :  FNTB_HUMAN

Gene Name (Synonyms) : 
FNTB  

Species :  Homo sapiens (Human). 

Subcellular Localization :   

Protein Function :  Catalyzes the transfer of a farnesyl moiety from farnesyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins. The beta subunit is responsible for peptide-binding. 

Protein Sequence MASPSSFTYYCPPSSSPVWSEPLYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFSSYKFNHLVPR...
Predicted Secondary Structure  -
Protein Variant -
- top -

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
- top -

Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
8PhosphothreoninePSSFTYYCP
18.61HPRD
Link-
8PhosphothreoninePSSFTYYCP
18.61SysPTM
Link-
50Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IEQAKVEEK
50.28Phosphositeplus
Link
63Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FSSYKFNHL
41.45Phosphositeplus
Link
176Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)INREKLLQY
51.78Phosphositeplus
Link
180PhosphotyrosineKLLQYLYSL
13.94Phosphositeplus
Link
300PhosphotyrosineVDGCYSFWQ
16.66HPRD
Link
300PhosphotyrosineVDGCYSFWQ
16.66PhosphoELM
Link
300PhosphotyrosineVDGCYSFWQ
16.66Phosphositeplus
Link
300Phosphotyrosine.VDGCYSFWQ
16.66UniProtKB
Link
418Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YFLQKPVPG
50.56Phosphositeplus
Link
430PhosphothreonineLKDETSAEP
43.29HPRD
Link-
- top -

Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
- top -

Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
- top -
Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-300, AND MASSSPECTROMETRY.
- top -
Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures