CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012305
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Peptidyl-prolyl cis-trans isomerase FKBP8 
Protein Synonyms/Alias
 PPIase FKBP8; 38 kDa FK506-binding protein; 38 kDa FKBP; FKBP-38; hFKBP38; FK506-binding protein 8; FKBP-8; FKBPR38; Rotamase 
Gene Name
 FKBP8 
Gene Synonyms/Alias
 FKBP38 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
271EAQLLQLKVKCLNNLubiquitination[1]
314KALFRKGKVLAQQGEubiquitination[1]
348TIHAELSKLVKKHAAacetylation[2]
Reference
 [1] 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]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 
Functional Description
 Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis. 
Sequence Annotation
 DOMAIN 120 204 PPIase FKBP-type.
 REPEAT 221 254 TPR 1.
 REPEAT 272 305 TPR 2.
 REPEAT 306 339 TPR 3.  
Keyword
 3D-structure; Alternative splicing; Apoptosis; Calcium; Complete proteome; Host-virus interaction; Isomerase; Membrane; Mitochondrion; Polymorphism; Reference proteome; Repeat; Rotamase; TPR repeat; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 412 AA 
Protein Sequence
MASCAEPSEP SAPLPAGVPP LEDFEVLDGV EDAEGEEEEE EEEEEEDDLS ELPPLEDMGQ 60
PPAEEAEQPG ALAREFLAAM EPEPAPAPAP EEWLDILGNG LLRKKTLVPG PPGSSRPVKG 120
QVVTVHLQTS LENGTRVQEE PELVFTLGDC DVIQALDLSV PLMDVGETAM VTADSKYCYG 180
PQGRSPYIPP HAALCLEVTL KTAVDGPDLE MLTGQERVAL ANRKRECGNA HYQRADFVLA 240
ANSYDLAIKA ITSSAKVDMT FEEEAQLLQL KVKCLNNLAA SQLKLDHYRA ALRSCSLVLE 300
HQPDNIKALF RKGKVLAQQG EYSEAIPILR AALKLEPSNK TIHAELSKLV KKHAAQRSTE 360
TALYRKMLGN PSRLPAKCPG KGAWSIPWKW LFGATAVALG GVALSVVIAA RN 412 
Gene Ontology
 GO:0030176; C:integral to endoplasmic reticulum membrane; IBA:RefGenome.
 GO:0005740; C:mitochondrial envelope; IBA:RefGenome.
 GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
 GO:0005528; F:FK506 binding; IBA:RefGenome.
 GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:RefGenome.
 GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
 GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
 GO:0006457; P:protein folding; IEA:UniProtKB-KW.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR023114; Elongated_TPR_rpt_dom.
 IPR023566; PPIase_FKBP.
 IPR001179; PPIase_FKBP_dom.
 IPR001440; TPR-1.
 IPR013026; TPR-contain_dom.
 IPR011990; TPR-like_helical.
 IPR019734; TPR_repeat. 
Pfam
 PF00254; FKBP_C
 PF00515; TPR_1 
SMART
  
PROSITE
 PS50059; FKBP_PPIASE
 PS50005; TPR
 PS50293; TPR_REGION 
PRINTS