CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008138
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein farnesyltransferase subunit beta 
Protein Synonyms/Alias
 FTase-beta; CAAX farnesyltransferase subunit beta; Ras proteins prenyltransferase subunit beta 
Gene Name
 FNTB 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
50VTSIEQAKVEEKIQEubiquitination[1, 2]
54EQAKVEEKIQEVFSSubiquitination[2]
63QEVFSSYKFNHLVPRubiquitination[2, 3]
176YDIINREKLLQYLYSubiquitination[1]
418ATTYFLQKPVPGFEEubiquitination[1]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] 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]
 [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
Functional Description
 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. 
Sequence Annotation
 REPEAT 123 164 PFTB 1.
 REPEAT 174 215 PFTB 2.
 REPEAT 222 263 PFTB 3.
 REPEAT 270 312 PFTB 4.
 REPEAT 332 374 PFTB 5.
 METAL 297 297 Zinc.
 METAL 299 299 Zinc.
 METAL 362 362 Zinc.  
Keyword
 3D-structure; Complete proteome; Metal-binding; Prenyltransferase; Reference proteome; Repeat; Transferase; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 437 AA 
Protein Sequence
MASPSSFTYY CPPSSSPVWS EPLYSLRPEH ARERLQDDSV ETVTSIEQAK VEEKIQEVFS 60
SYKFNHLVPR LVLQREKHFH YLKRGLRQLT DAYECLDASR PWLCYWILHS LELLDEPIPQ 120
IVATDVCQFL ELCQSPEGGF GGGPGQYPHL APTYAAVNAL CIIGTEEAYD IINREKLLQY 180
LYSLKQPDGS FLMHVGGEVD VRSAYCAASV ASLTNIITPD LFEGTAEWIA RCQNWEGGIG 240
GVPGMEAHGG YTFCGLAALV ILKRERSLNL KSLLQWVTSR QMRFEGGFQG RCNKLVDGCY 300
SFWQAGLLPL LHRALHAQGD PALSMSHWMF HQQALQEYIL MCCQCPAGGL LDKPGKSRDF 360
YHTCYCLSGL SIAQHFGSGA MLHDVVLGVP ENALQPTHPV YNIGPDKVIQ ATTYFLQKPV 420
PGFEELKDET SAEPATD 437 
Gene Ontology
 GO:0005875; C:microtubule associated complex; IDA:BHF-UCL.
 GO:0005965; C:protein farnesyltransferase complex; IEA:InterPro.
 GO:0004311; F:farnesyltranstransferase activity; IEA:Compara.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004660; F:protein farnesyltransferase activity; IEA:EC.
 GO:0008285; P:negative regulation of cell proliferation; IEA:Compara.
 GO:0045787; P:positive regulation of cell cycle; IEA:Compara.
 GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Compara.
 GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IEA:Compara.
 GO:0018343; P:protein farnesylation; IDA:BHF-UCL.
 GO:0034097; P:response to cytokine stimulus; IEA:Compara.
 GO:0010035; P:response to inorganic substance; IEA:Compara.
 GO:0014070; P:response to organic cyclic compound; IEA:Compara.
 GO:0042060; P:wound healing; IEA:Compara. 
Interpro
 IPR026872; FTB.
 IPR001330; Prenyltrans.
 IPR008930; Terpenoid_cyclase/PrenylTrfase. 
Pfam
 PF00432; Prenyltrans 
SMART
  
PROSITE
  
PRINTS