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 FKBP3  

UniProtKB / Swiss-Prot ID :  FKBP3_HUMAN

Gene Name (Synonyms) : 
FKBP3, FKBP25  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. 

Protein Function :  FK506- and rapamycin-binding proteins (FKBPs) constitute a family of receptors for the two immunosuppressants which inhibit T-cell proliferation by arresting two distinct cytoplasmic signal transmission pathways. PPIases accelerate the folding of proteins. 

Protein Sequence MAAAVPQRAWTVEQLRSEQLPKKDIIKFLQEHGSDSFLAEHKLLGNIKNVAKTANKDHLVTAYNHLFETK...
Predicted Secondary Structure CCCCCCCCCEEHHHHCCCCCCHHHHHHHHHHCCCHHHHHHHHHCCCCHHHHHHCCHHHHHHHHHHHHHHC...
Protein Variant -
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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
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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
2N-acetylalanine.---MAAAVP
---CCCCCC
12.25UniProtKB
Link-
27Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KDIIKFLQE
HHHHHHHHH
40.11Phosphositeplus
Link-
36PhosphoserineHGSDSFLAE
CCCHHHHHH
24.69HPRD
Link-
36PhosphoserineHGSDSFLAE
CCCHHHHHH
24.69Phosphositeplus
Link-
77PhosphoserineKGTESISKV
EEEEEEEEC
31.81HPRD
Link-
77PhosphoserineKGTESISKV
EEEEEEEEC
31.81Phosphositeplus
Link-
79PhosphoserineTESISKVSE
EEEEEECCC
35.96HPRD
Link-
98PhosphothreonineKPKETKSEE
CCCHHCCHH
46.10Phosphositeplus
Link-
147PhosphothreonineTVFDTNIQT
EEECCCCCC
23.82HPRD
Link
152PhosphoserineNIQTSAKKK
CCCCCCCCC
23.01HPRD
Link
152PhosphoserineNIQTSAKKK
CCCCCCCCC
23.01PhosphoELM
Link
152PhosphoserineNIQTSAKKK
CCCCCCCCC
23.01Phosphositeplus
Link
152Phosphoserine.NIQTSAKKK
CCCCCCCCC
23.01UniProtKB
Link
160N6-acetyllysineKKNAKPLSF
CCCCCCEEE
56.75HPRD
Link
160N6-acetyllysineKKNAKPLSF
CCCCCCEEE
56.75Phosphositeplus
Link
160N6-acetyllysine.KKNAKPLSF
CCCCCCEEE
56.75UniProtKB
Link
170N6-acetyllysineVGVGKVIRG
ECCCCCCHH
31.89HPRD
Link
170N6-acetyllysineVGVGKVIRG
ECCCCCCHH
31.89Phosphositeplus
Link
170N6-acetyllysine.VGVGKVIRG
ECCCCCCHH
31.89UniProtKB
Link
181PhosphothreonineEALLTMSKG
HHHHCCCCC
21.90HPRD
Link
181PhosphothreonineEALLTMSKG
HHHHCCCCC
21.90Phosphositeplus
Link
183PhosphoserineLLTMSKGEK
HHCCCCCCE
32.07HPRD
Link
183PhosphoserineLLTMSKGEK
HHCCCCCCE
32.07Phosphositeplus
Link
198PhosphotyrosinePEWAYGKKG
CCCCCCCCC
30.47HPRD
Link
198PhosphotyrosinePEWAYGKKG
CCCCCCCCC
30.47Phosphositeplus
Link
200N6-acetyllysineWAYGKKGQP
CCCCCCCCC
40.84HPRD
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
CSK21_HUMANin vitro
in vivo
HPRD:01743HPRD7689229
CSK22_HUMANin vitro
in vivo
HPRD:01743HPRD7689229
CSK2B_HUMANin vitro
in vivo
HPRD:01743HPRD7689229
TYY1_HUMANENSP00000216330STRING
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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
"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-160 AND LYS-170, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-152, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures