CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005871
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Peptidyl-prolyl cis-trans isomerase FKBP4 
Protein Synonyms/Alias
 PPIase FKBP4; 52 kDa FK506-binding protein; 52 kDa FKBP; FKBP-52; 59 kDa immunophilin; p59; FK506-binding protein 4; FKBP-4; FKBP59; HSP-binding immunophilin; HBI; Immunophilin FKBP52; Rotamase; Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed 
Gene Name
 Fkbp4 
Gene Synonyms/Alias
 Fkpb52 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
28EGVDISPKQDEGVLKubiquitination[1]
74FDSSLDRKDKFSFDLubiquitination[1]
83KFSFDLGKGEVIKAWubiquitination[1]
222EHSIVYLKPSYAFGSubiquitination[1]
232YAFGSVGKERFQIPPubiquitination[1]
354ELDSNNEKGLFRRGEacetylation[2, 3]
354ELDSNNEKGLFRRGEubiquitination[1]
387LQLYPSNKAAKTQLAubiquitination[1]
390YPSNKAAKTQLAVCQubiquitination[1]
409RQLAREKKLYANMFEubiquitination[1]
441HPTDAEMKGERNNVAubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337] 
Functional Description
 Immunophilin protein with PPIase and co-chaperone activities (By similarity). Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90) (By similarity). May play a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments (By similarity). The isomerase activity controls neuronal growth cones via regulation of TRPC1 channel opening (By similarity). Acts also as a regulator of microtubule dynamics by inhibiting MAPT/TAU ability to promote microtubule assembly. May have a protective role against oxidative stress in mitochondria (By similarity). 
Sequence Annotation
 DOMAIN 50 138 PPIase FKBP-type 1.
 DOMAIN 167 253 PPIase FKBP-type 2.
 REPEAT 270 303 TPR 1.
 REPEAT 319 352 TPR 2.
 REPEAT 353 386 TPR 3.
 REGION 267 400 Interaction with tubulin (By similarity).
 MOD_RES 1 1 N-acetylmethionine; in peptidyl-prolyl
 MOD_RES 2 2 N-acetylthreonine; in peptidyl-prolyl
 MOD_RES 143 143 Phosphothreonine; by CK2 (By similarity).
 MOD_RES 282 282 N6-acetyllysine (By similarity).
 MOD_RES 452 452 Phosphoserine (By similarity).  
Keyword
 Acetylation; Chaperone; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Isomerase; Microtubule; Mitochondrion; Nucleus; Phosphoprotein; Reference proteome; Repeat; Rotamase; TPR repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 458 AA 
Protein Sequence
MTAEEMKAAE NGAQSAPLPL EGVDISPKQD EGVLKVIKRE GTGTETPMIG DRVFVHYTGW 60
LLDGTKFDSS LDRKDKFSFD LGKGEVIKAW DIAVATMKVG EVCHITCKPE YAYGAAGSPP 120
KIPPNATLVF EVELFEFKGE DLTEEEDGGI IRRIRTRGEG YARPNDGAMV EVALEGYHKD 180
RLFDQRELCF EVGEGESLDL PCGLEEAIQR MEKGEHSIVY LKPSYAFGSV GKERFQIPPH 240
AELRYEVRLK SFEKAKESWE MSSAEKLEQS NIVKERGTAY FKEGKYKQAL LQYKKIVSWL 300
EYESSFSGEE MQKVHALRLA SHLNLAMCHL KLQAFSAAIE SCNKALELDS NNEKGLFRRG 360
EAHLAVNDFD LARADFQKVL QLYPSNKAAK TQLAVCQQRT RRQLAREKKL YANMFERLAE 420
EEHKVKAEVA AGDHPTDAEM KGERNNVAEN QSRVETEA 458 
Gene Ontology
 GO:0044295; C:axonal growth cone; ISS:UniProtKB.
 GO:0005829; C:cytosol; ISS:UniProtKB.
 GO:0016020; C:membrane; IBA:RefGenome.
 GO:0005874; C:microtubule; IEA:UniProtKB-KW.
 GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
 GO:0043025; C:neuronal cell body; IEA:Compara.
 GO:0005634; C:nucleus; IDA:MGI.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:Compara.
 GO:0005524; F:ATP binding; IDA:MGI.
 GO:0005528; F:FK506 binding; IBA:RefGenome.
 GO:0035259; F:glucocorticoid receptor binding; IDA:MGI.
 GO:0005525; F:GTP binding; IDA:MGI.
 GO:0031072; F:heat shock protein binding; IDA:MGI.
 GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISS:UniProtKB.
 GO:0051219; F:phosphoprotein binding; IDA:MGI.
 GO:0030521; P:androgen receptor signaling pathway; IMP:MGI.
 GO:0061077; P:chaperone-mediated protein folding; ISS:UniProtKB.
 GO:0006825; P:copper ion transport; IEA:Compara.
 GO:0007566; P:embryo implantation; IMP:MGI.
 GO:0046661; P:male sex differentiation; IMP:MGI.
 GO:0031115; P:negative regulation of microtubule polymerization; IEA:Compara.
 GO:0031111; P:negative regulation of microtubule polymerization or depolymerization; ISS:UniProtKB.
 GO:0010977; P:negative regulation of neuron projection development; ISS:UniProtKB.
 GO:0030850; P:prostate gland development; IMP:MGI.
 GO:0031503; P:protein complex localization; IDA:MGI.
 GO:0006463; P:steroid hormone receptor complex assembly; IDA:MGI. 
Interpro
 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
 SM00028; TPR 
PROSITE
 PS50059; FKBP_PPIASE
 PS50005; TPR
 PS50293; TPR_REGION 
PRINTS