Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Peptidyl-prolyl cis-trans isomerase FKBP4  

UniProtKB / Swiss-Prot ID :  FKBP4_HUMAN

Gene Name (Synonyms) : 
FKBP4, FKBP52  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm, cytosol (By similarity). Nucleus. Cytoplasm, cytoskeleton (By similarity). 

Protein Function :  Immunophilin protein with PPIase and co-chaperone activities (By similarity). Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). 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. Acts also as a regulator of microtubule dynamics by inhibiting MAPT/TAU ability to promote microtubule assembly. 

Protein Sequence MTAEEMKATESGAQSAPLPMEGVDISPKQDEGVLKVIKREGTGTEMPMIGDRVFVHYTGWLLDGTKFDSS...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCEEEEEEECCCCCCCCCCCCEEEEEEEEEECCCEEEECC...
Protein Variant
LocationDescription
436T -> P (in dbSNP:rs1042228). VAR_050624
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
1N-acetylmethionine; in FK506-bindingprotein 4; alternate.----MTAEE
----CCCCC
7.86UniProtKB
Link-
2N-acetylthreonine; in FK506-bindingprotein 4, N-terminally processed;---MTAEEM
---CCCCCC
42.66UniProtKB
Link-
28Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DISPKQDEG
CCCCCCCCC
64.69Phosphositeplus
Link
76Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DRKDKFSFD
CCCCCEEEE
46.04Phosphositeplus
Link
83Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FDLGKGEVI
EEECCCCCC
60.23Phosphositeplus
Link
88Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GEVIKAWDI
CCCCHHHHH
48.91Phosphositeplus
Link
143Phosphothreonine (CSNK2A1)GEDLTEEED
CCCCCCCCC
54.39HPRD
Link-
161PhosphotyrosineRGEGYAKPN
CCCCCCCCC
13.72Phosphositeplus
Link-
181Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YYKDKLFDQ
EECCEEECC
47.07Phosphositeplus
Link-
220PhosphotyrosineHSIVYLKPS
CCEEEECCC
13.82Phosphositeplus
Link-
222Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IVYLKPSYA
EEEECCCCC
17.77Phosphositeplus
Link-
244Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NAELKYELH
CCCHHHHHH
28.34Phosphositeplus
Link-
250Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ELHLKSFEK
HHHHHHCCC
42.21Phosphositeplus
Link-
274Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)STIVKERGT
HHHHHHHHH
37.53Phosphositeplus
Link-
274N6-acetyllysineSTIVKERGT
HHHHHHHHH
37.53Phosphositeplus
Link-
274N6-acetyllysine.STIVKERGT
HHHHHHHHH
37.53UniProtKB
Link-
282N6-acetyllysineTVYFKEGKY
HHHHHHCCH
48.12HPRD
Link-
282N6-acetyllysineTVYFKEGKY
HHHHHHCCH
48.12Phosphositeplus
Link-
282N6-acetyllysine.TVYFKEGKY
HHHHHHCCH
48.12UniProtKB
Link-
286PhosphotyrosineKEGKYKQAL
HHCCHHHHH
21.13Phosphositeplus
Link-
293PhosphotyrosineALLQYKKIV
HHHHHHHHH
17.76HPRD
Link-
293PhosphotyrosineALLQYKKIV
HHHHHHHHH
17.76Phosphositeplus
Link-
354Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SNNEKGLFR
CCCHHHHHH
64.14Phosphositeplus
Link-
378Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ADFQKVLQL
HHHHHHHHH
44.93Phosphositeplus
Link-
409Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AREKKLYAN
HHHHHHHHH
41.81Phosphositeplus
Link-
411PhosphotyrosineEKKLYANMF
HHHHHHHHH
12.57HPRD
Link-
411PhosphotyrosineEKKLYANMF
HHHHHHHHH
12.57Phosphositeplus
Link-
411PhosphotyrosineEKKLYANMF
HHHHHHHHH
12.57SysPTM
Link-
426Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ENKAKAEAS
HHHHHCCCC
48.66Phosphositeplus
Link-
451PhosphoserineNTAGSQSQV
CCCCCCCCC
24.97HPRD
Link-
451PhosphoserineNTAGSQSQV
CCCCCCCCC
24.97PhosphoELM
Link-
451PhosphoserineNTAGSQSQV
CCCCCCCCC
24.97Phosphositeplus
Link-
451PhosphoserineNTAGSQSQV
CCCCCCCCC
24.97SysPTM
Link-
451Phosphoserine.NTAGSQSQV
CCCCCCCCC
24.97UniProtKB
Link-
453PhosphoserineAGSQSQVET
CCCCCCCCC
37.58HPRD
Link-
453PhosphoserineAGSQSQVET
CCCCCCCCC
37.58PhosphoELM
Link-
453PhosphoserineAGSQSQVET
CCCCCCCCC
37.58Phosphositeplus
Link-
453PhosphoserineAGSQSQVET
CCCCCCCCC
37.58SysPTM
Link-
453Phosphoserine.AGSQSQVET
CCCCCCCCC
37.58UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
1433Z_HUMANphysical interactionMINT-3319393MINT15161933
LOXH1_HUMANphysical interactionEBI-1085116
intact17353931
SAE1_HUMANphysical interactionEBI-1079127
intact17353931
GCR_HUMANin vitroHPRD:11794HPRD8341706
FKB1A_HUMANin vitro
yeast 2-hybrid
HPRD:11794HPRD11164950
GLMN_HUMANin vitro
in vivo
HPRD:11794HPRD8955134
MCR_HUMANin vitroHPRD:11794HPRD9392437
IRF4_HUMANin vitro
in vivo
HPRD:11794HPRD10714679
PAHX_HUMANin vitroHPRD:11794HPRD10051602
SMUF2_HUMANin vivoHPRD:11794HPRD15761153
ATOX1_HUMANin vitro
yeast 2-hybrid
HPRD:11794HPRD15133031
PAHX_HUMANENSP00000001008STRING
PRGR_HUMANENSP00000001008STRING
HS90A_HUMANENSP00000001008STRING
HS90A_HUMANENSP00000001008STRING
HS90A_HUMANENSP00000001008STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey.";
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
Mol. Cell 23:607-618(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-274, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-282, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451 AND SER-453, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451 AND SER-453, ANDMASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures