FKB1A_HUMAN - dbPTM
FKB1A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FKB1A_HUMAN
UniProt AC P62942
Protein Name Peptidyl-prolyl cis-trans isomerase FKBP1A
Gene Name FKBP1A
Organism Homo sapiens (Human).
Sequence Length 108
Subcellular Localization Cytoplasm, cytosol . Sarcoplasmic reticulum membrane
Peripheral membrane protein
Cytoplasmic side .
Protein Description Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruits SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides..
Protein Sequence MGVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGHPGIIPPHATLVFDVELLKLE
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
7Phosphorylation-MGVQVETISPGDGR
-CCCEEEEECCCCCC		28.0930266825
9PhosphorylationGVQVETISPGDGRTF
CCEEEEECCCCCCCC		30.1923401153
15PhosphorylationISPGDGRTFPKRGQT
ECCCCCCCCCCCCCE		50.2329514088
19MethylationDGRTFPKRGQTCVVH
CCCCCCCCCCEEEEE		42.56-
22PhosphorylationTFPKRGQTCVVHYTG
CCCCCCCEEEEEEEE		15.3023312004
23GlutathionylationFPKRGQTCVVHYTGM
CCCCCCEEEEEEEEE		2.0122555962
30SulfoxidationCVVHYTGMLEDGKKF
EEEEEEEEECCCCCC		2.6030846556
35AcetylationTGMLEDGKKFDSSRD
EEEECCCCCCCCCCC		63.6925953088
35UbiquitinationTGMLEDGKKFDSSRD
EEEECCCCCCCCCCC		63.69-
36AcetylationGMLEDGKKFDSSRDR
EEECCCCCCCCCCCC		60.99155799
36UbiquitinationGMLEDGKKFDSSRDR
EEECCCCCCCCCCCC		60.99-
48MalonylationRDRNKPFKFMLGKQE
CCCCCCEEEEECCHH		38.0926320211
48AcetylationRDRNKPFKFMLGKQE
CCCCCCEEEEECCHH		38.0923749302
48UbiquitinationRDRNKPFKFMLGKQE
CCCCCCEEEEECCHH		38.09-
53MalonylationPFKFMLGKQEVIRGW
CEEEEECCHHHHCCH		39.0526320211
53SuccinylationPFKFMLGKQEVIRGW
CEEEEECCHHHHCCH		39.05-
53SuccinylationPFKFMLGKQEVIRGW
CEEEEECCHHHHCCH		39.05-
53AcetylationPFKFMLGKQEVIRGW
CEEEEECCHHHHCCH		39.0523954790
53UbiquitinationPFKFMLGKQEVIRGW
CEEEEECCHHHHCCH		39.052189047
58MethylationLGKQEVIRGWEEGVA
ECCHHHHCCHHHHCE		49.72-
67SulfoxidationWEEGVAQMSVGQRAK
HHHHCEEEECCCCEE		2.2430846556
74UbiquitinationMSVGQRAKLTISPDY
EECCCCEEEEECCCC		48.64-
81PhosphorylationKLTISPDYAYGATGH
EEEECCCCCCCCCCC		12.7125884760
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of FKB1A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FKB1A_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of FKB1A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TGFR1_HUMANTGFBR1physical
7518616
MTOR_HUMANMTORphysical
15467718
RPTOR_HUMANRPTORphysical
15467718
TGFR1_HUMANTGFBR1physical
7791754
MTOR_HUMANMTORphysical
15268862
RPTOR_HUMANRPTORphysical
15268862
DYR_HUMANDHFRphysical
12812497
FKB1A_HUMANFKBP1Aphysical
10852943
RYR1_HUMANRYR1physical
11171121
RYR3_HUMANRYR3physical
11171121
MTOR_HUMANMTORphysical
8662507
MTOR_HUMANMTORphysical
7822316
MTOR_RATMtorphysical
14679009
GLMN_HUMANGLMNphysical
8955134
FKB1A_HUMANFKBP1Aphysical
9871618
GLMN_HUMANGLMNphysical
11164950
SMAD7_HUMANSMAD7physical
16720724
A4_HUMANAPPphysical
21832049
ZPR1_HUMANZPR1physical
22939629
MTOR_HUMANMTORphysical
10089303
TRI18_HUMANMID1physical
25416956
SF3B4_HUMANSF3B4physical
25416956
AHSP_HUMANAHSPphysical
25416956
CTBP1_HUMANCTBP1physical
26344197
GSTT1_HUMANGSTT1physical
26344197
HCD2_HUMANHSD17B10physical
26344197
CH10_HUMANHSPE1physical
26344197
NMRL1_HUMANNMRAL1physical
26344197
PPIF_HUMANPPIFphysical
26344197
P4R3A_HUMANSMEK1physical
26344197
THIO_HUMANTXNphysical
26344197
MDM2_HUMANMDM2physical
27617579
RYR3_HUMANRYR3physical
11598113
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00337Pimecrolimus
DB00877Sirolimus
DB00864Tacrolimus
Regulatory Network of FKB1A_HUMAN

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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-53, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND MASSSPECTROMETRY.

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