UniProt Accession

 FKBP8_HUMAN; Q14318; Q53GU3; Q7Z349; Q86YK6 

Genbank Protein ID

 AY225339; AY278607; BX538124; BX647405; AC005387; CH471106; L37033; AK222838; BC009966 

Genbank Nucleotide ID

 AAO39020.1; AAQ84561.1; CAD98028.1; AAC28753.1; EAW84709.1; AAB00102.1; BAD96558.1; AAH09966.1 

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
250	NSYDLAIKAITSSAK	ubiquitination	[1, 2]
272	EAQLLQLKVKCLNNL	ubiquitination	[1, 2]
274	QLLQLKVKCLNNLAA	ubiquitination	[1, 3]
285	NLAASQLKLDHYRAA	ubiquitination	[1]
308	EHQPDNIKALFRKGK	ubiquitination	[1]
315	KALFRKGKVLAQQGE	ubiquitination	[1, 2, 3]
335	PILRAALKLEPSNKT	ubiquitination	[1, 2]
341	LKLEPSNKTIHAELS	ubiquitination	[1]
349	TIHAELSKLVKKHAA	ubiquitination	[1]

Reference

 [1] 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]
 [2] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [3] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965] 

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

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