FKBP9_HUMAN - dbPTM
FKBP9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FKBP9_HUMAN
UniProt AC O95302
Protein Name Peptidyl-prolyl cis-trans isomerase FKBP9
Gene Name FKBP9
Organism Homo sapiens (Human).
Sequence Length 570
Subcellular Localization Endoplasmic reticulum .
Protein Description PPIases accelerate the folding of proteins during protein synthesis..
Protein Sequence MAFRGWRPPPPPLLLLLLWVTGQAAPVAGLGSDAELQIERRFVPDECPRTVRSGDFVRYHYVGTFPDGQKFDSSYDRDSTFNVFVGKGQLITGMDQALVGMCVNERRFVKIPPKLAYGNEGVSGVIPPNSVLHFDVLLMDIWNSEDQVQIHTYFKPPSCPRTIQVSDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGIGWLIPGMDKGLLGMCVGEKRIITIPPFLAYGEDGDGKDIPGQASLVFDVALLDLHNPKDSISIENKVVPENCERISQSGDFLRYHYNGTLLDGTLFDSSYSRNRTFDTYIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEEGRGNIPGSAVLVFDIHVIDFHNPSDSISITSHYKPPDCSVLSKKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSGQVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDGEVPGSAVLVFDIELLELVAGLPEGYMFIWNGEVSPNLFEEIDKDGNGEVLLEEFSEYIHAQVASGKGKLAPGFDAELIVKNMFTNQDRNGDGKVTAEEFKLKDQEAKHDEL
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
47GlutathionylationRRFVPDECPRTVRSG
EECCCCCCCCCEECC		3.4422555962
59PhosphorylationRSGDFVRYHYVGTFP
ECCCEEEEEEEEECC		7.6922210691
64PhosphorylationVRYHYVGTFPDGQKF
EEEEEEEECCCCCCC		23.1922210691
94SulfoxidationKGQLITGMDQALVGM
CCCEEECCCHHHHHH		2.3030846556
98 (in isoform 3)Phosphorylation-2.5825159151
101SulfoxidationMDQALVGMCVNERRF
CCHHHHHHCCCCCEE		1.4730846556
174N-linked_GlycosylationDFVRYHYNGTFLDGT
CCEEEEECCEEECCE		29.7112754519
174N-linked_GlycosylationDFVRYHYNGTFLDGT
CCEEEEECCEEECCE		29.7112754519
206SulfoxidationIGWLIPGMDKGLLGM
CCHHCCCCCCCCCCE		3.9530846556
213SulfoxidationMDKGLLGMCVGEKRI
CCCCCCCEECCCCEE		1.3630846556
265UbiquitinationDSISIENKVVPENCE
CCCCEECCCCCCCCE		31.64-
286N-linked_GlycosylationDFLRYHYNGTLLDGT
CEEEEEECCEEECCE		24.5412754519
286N-linked_GlycosylationDFLRYHYNGTLLDGT
CEEEEEECCEEECCE		24.5412754519
293PhosphorylationNGTLLDGTLFDSSYS
CCEEECCEECCCCCC		24.7425587033
295UbiquitinationTLLDGTLFDSSYSRN
EEECCEECCCCCCCC		9.57-
297PhosphorylationLDGTLFDSSYSRNRT
ECCEECCCCCCCCCE		24.6825587033
298PhosphorylationDGTLFDSSYSRNRTF
CCEECCCCCCCCCEE		29.0425587033
299PhosphorylationGTLFDSSYSRNRTFD
CEECCCCCCCCCEEC		18.6625587033
300PhosphorylationTLFDSSYSRNRTFDT
EECCCCCCCCCEECE		25.6525587033
302N-linked_GlycosylationFDSSYSRNRTFDTYI
CCCCCCCCCEECEEE		41.21UniProtKB CARBOHYD
386PhosphorylationPPDCSVLSKKGDYLK
CCCCEECCCCCCCEE		30.1129978859
391PhosphorylationVLSKKGDYLKYHYNA
ECCCCCCCEEEEECC		17.4829978859
397N-linked_GlycosylationDYLKYHYNASLLDGT
CCEEEEECCHHCCCC		15.1112754519
525UbiquitinationHAQVASGKGKLAPGF
HHHHHCCCCCCCCCC		50.83-
527UbiquitinationQVASGKGKLAPGFDA
HHHCCCCCCCCCCCC		44.9821906983
539UbiquitinationFDAELIVKNMFTNQD
CCCEEEEEECCCCCC		35.38-
541SulfoxidationAELIVKNMFTNQDRN
CEEEEEECCCCCCCC		3.4830846556
580Ubiquitination-----------------
-----------------		21906983
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 FKBP9_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FKBP9_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 FKBP9_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
API5_HUMANAPI5physical
22863883
EHD1_HUMANEHD1physical
22863883
EZRI_HUMANEZRphysical
22863883
TF3C4_HUMANGTF3C4physical
22863883
HERC4_HUMANHERC4physical
22863883
HEXA_HUMANHEXAphysical
22863883
HXK1_HUMANHK1physical
22863883
LIMD1_HUMANLIMD1physical
22863883
NOL3_HUMANNOL3physical
22863883
NUBP1_HUMANNUBP1physical
22863883
NUBP2_HUMANNUBP2physical
22863883
PDC10_HUMANPDCD10physical
22863883
RD23A_HUMANRAD23Aphysical
22863883
STK39_HUMANSTK39physical
22863883
SYWC_HUMANWARSphysical
22863883
XPP1_HUMANXPNPEP1physical
22863883
CTF8_HUMANCHTF8physical
28514442
TCF20_HUMANTCF20physical
28514442
RAVR1_HUMANRAVER1physical
28514442
CBY1_HUMANCBY1physical
28514442
TFE2_HUMANTCF3physical
28514442
CO4A6_HUMANCOL4A6physical
28514442
CO2A1_HUMANCOL2A1physical
28514442
PTPRS_HUMANPTPRSphysical
28514442
CO4A2_HUMANCOL4A2physical
28514442
DAG1_HUMANDAG1physical
28514442
FINC_HUMANFN1physical
28514442
PRCC_HUMANPRCCphysical
28514442
RL23_HUMANRPL23physical
28514442
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
There are no disease associations of PTM sites.
Regulatory Network of FKBP9_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry.";
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
Nat. Biotechnol. 21:660-666(2003).
Cited for: GLYCOSYLATION AT ASN-174; ASN-286 AND ASN-397.

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