CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010940
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
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
83EKHFHYLKRGLRQLTacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405
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; Direct protein sequencing; Metal-binding; Prenyltransferase; Reference proteome; Repeat; Transferase; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 437 AA 
Protein Sequence
MASSSSFTYY CPPSSSPVWS EPLYSLRPEH ARERLQDDSV ETVTSIEQAK VEEKIQEVFS 60
SYKFNHLVPR LVLQREKHFH YLKRGLRQLT DAYECLDASR PWLCYWILHS LELLDEPIPQ 120
IVATDVCQFL ELCQSPDGGF GGGPGQYPHL APTYAAVNAL CIIGTEEAYN VINREKLLQY 180
LYSLKQPDGS FLMHVGGEVD VRSAYCAASV ASLTNIITPD LFEGTAEWIA RCQNWEGGIG 240
GVPGMEAHGG YTFCGLAALV ILKKERSLNL KSLLQWVTSR QMRFEGGFQG RCNKLVDGCY 300
SFWQAGLLPL LHRALHAQGD PALSMSHWMF HQQALQEYIL MCCQCPAGGL LDKPGKSRDF 360
YHTCYCLSGL SIAQHFGSGA MLHDVVMGVP ENVLQPTHPV YNIGPDKVIQ ATTHFLQKPV 420
PGFEECEDAV TSDPATD 437 
Gene Ontology
 GO:0005875; C:microtubule associated complex; IEA:Compara.
 GO:0043234; C:protein complex; IDA:RGD.
 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; IDA:RGD.
 GO:0008285; P:negative regulation of cell proliferation; IEA:Compara.
 GO:0045787; P:positive regulation of cell cycle; IMP:RGD.
 GO:0008284; P:positive regulation of cell proliferation; IMP:RGD.
 GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Compara.
 GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IMP:RGD.
 GO:0018343; P:protein farnesylation; IEA:InterPro.
 GO:0034097; P:response to cytokine stimulus; IMP:RGD.
 GO:0010035; P:response to inorganic substance; IMP:RGD.
 GO:0014070; P:response to organic cyclic compound; IMP:RGD.
 GO:0042060; P:wound healing; IEA:Compara. 
Interpro
 IPR026872; FTB.
 IPR001330; Prenyltrans.
 IPR008930; Terpenoid_cyclase/PrenylTrfase. 
Pfam
 PF00432; Prenyltrans 
SMART
  
PROSITE
  
PRINTS