CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012108
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Peptidyl-prolyl cis-trans isomerase FKBP5 
Protein Synonyms/Alias
 PPIase FKBP5; 51 kDa FK506-binding protein; 51 kDa FKBP; FKBP-51; 54 kDa progesterone receptor-associated immunophilin; Androgen-regulated protein 6; FF1 antigen; FK506-binding protein 5; FKBP-5; FKBP54; p54; HSP90-binding immunophilin; Rotamase 
Gene Name
 FKBP5 
Gene Synonyms/Alias
 AIG6; FKBP51 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
28QGEDITSKKDRGVLKubiquitination[1, 2]
204DIPIGIDKALEKMQRubiquitination[2]
342KAVECCDKALGLDSAubiquitination[3]
352GLDSANEKGLYRRGEubiquitination[3, 4, 5, 6]
376SAKGDFEKVLEVNPQubiquitination[4]
385LEVNPQNKAARLQISubiquitination[3, 5]
441SEGVTNEKGTDSQAMubiquitination[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] 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] 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]
 [4] 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]
 [5] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [6] 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
 Interacts with functionally mature heterooligomeric progesterone receptor complexes along with HSP90 and TEBP. 
Sequence Annotation
 DOMAIN 42 130 PPIase FKBP-type 1.
 DOMAIN 157 243 PPIase FKBP-type 2.
 REPEAT 268 301 TPR 1.
 REPEAT 317 350 TPR 2.
 REPEAT 351 384 TPR 3.
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 445 445 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Chaperone; Complete proteome; Cytoplasm; Isomerase; Nucleus; Phosphoprotein; Reference proteome; Repeat; Rotamase; TPR repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 457 AA 
Protein Sequence
MTTDEGAKNN EESPTATVAE QGEDITSKKD RGVLKIVKRV GNGEETPMIG DKVYVHYKGK 60
LSNGKKFDSS HDRNEPFVFS LGKGQVIKAW DIGVATMKKG EICHLLCKPE YAYGSAGSLP 120
KIPSNATLFF EIELLDFKGE DLFEDGGIIR RTKRKGEGYS NPNEGATVEI HLEGRCGGRM 180
FDCRDVAFTV GEGEDHDIPI GIDKALEKMQ REEQCILYLG PRYGFGEAGK PKFGIEPNAE 240
LIYEVTLKSF EKAKESWEMD TKEKLEQAAI VKEKGTVYFK GGKYMQAVIQ YGKIVSWLEM 300
EYGLSEKESK ASESFLLAAF LNLAMCYLKL REYTKAVECC DKALGLDSAN EKGLYRRGEA 360
QLLMNEFESA KGDFEKVLEV NPQNKAARLQ ISMCQKKAKE HNERDRRIYA NMFKKFAEQD 420
AKEEANKAMG KKTSEGVTNE KGTDSQAMEE EKPEGHV 457 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0016020; C:membrane; IBA:RefGenome.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0005528; F:FK506 binding; IBA:RefGenome.
 GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:UniProtKB.
 GO:0061077; P:chaperone-mediated protein folding; IDA:UniProtKB. 
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