FKB10_HUMAN - dbPTM
FKB10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FKB10_HUMAN
UniProt AC Q96AY3
Protein Name Peptidyl-prolyl cis-trans isomerase FKBP10
Gene Name FKBP10
Organism Homo sapiens (Human).
Sequence Length 582
Subcellular Localization Endoplasmic reticulum lumen .
Protein Description PPIases accelerate the folding of proteins during protein synthesis..
Protein Sequence MFPAGPPSHSLLRLPLLQLLLLVVQAVGRGLGRASPAGGPLEDVVIERYHIPRACPREVQMGDFVRYHYNGTFEDGKKFDSSYDRNTLVAIVVGVGRLITGMDRGLMGMCVNERRRLIVPPHLGYGSIGLAGLIPPDATLYFDVVLLDVWNKEDTVQVSTLLRPPHCPRMVQDGDFVRYHYNGTLLDGTSFDTSYSKGGTYDTYVGSGWLIKGMDQGLLGMCPGERRKIIIPPFLAYGEKGYGTVIPPQASLVFHVLLIDVHNPKDAVQLETLELPPGCVRRAGAGDFMRYHYNGSLMDGTLFDSSYSRNHTYNTYIGQGYIIPGMDQGLQGACMGERRRITIPPHLAYGENGTGDKIPGSAVLIFNVHVIDFHNPADVVEIRTLSRPSETCNETTKLGDFVRYHYNCSLLDGTQLFTSHDYGAPQEATLGANKVIEGLDTGLQGMCVGERRQLIVPPHLAHGESGARGVPGSAVLLFEVELVSREDGLPTGYLFVWHKDPPANLFEDMDLNKDGEVPPEEFSTFIKAQVSEGKGRLMPGQDPEKTIGDMFQNQDRNQDGKITVDELKLKSDEDEERVHEEL
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
10PhosphorylationPAGPPSHSLLRLPLL
CCCCCCCHHHHHHHH		33.1824719451
35PhosphorylationGRGLGRASPAGGPLE
HHCCCCCCCCCCCHH		17.5821406692
35O-linked_GlycosylationGRGLGRASPAGGPLE
HHCCCCCCCCCCCHH		17.5837820845
61SulfoxidationACPREVQMGDFVRYH
CCCCCEECCCEEEEE		7.2230846556
70N-linked_GlycosylationDFVRYHYNGTFEDGK
CEEEEEECCCCCCCC		29.71UniProtKB CARBOHYD
107SulfoxidationTGMDRGLMGMCVNER
HCCCCCHHHHCCCCC		3.4230846556
109SulfoxidationMDRGLMGMCVNERRR
CCCCHHHHCCCCCCE		1.1230846556
110GlutathionylationDRGLMGMCVNERRRL
CCCHHHHCCCCCCEE		2.1722555962
170SulfoxidationRPPHCPRMVQDGDFV
CCCCCCCCCCCCCEE		1.5930846556
182N-linked_GlycosylationDFVRYHYNGTLLDGT
CEEEEEECCEECCCC		24.5412754519
184PhosphorylationVRYHYNGTLLDGTSF
EEEEECCEECCCCEE		22.1019690332
193PhosphorylationLDGTSFDTSYSKGGT
CCCCEECCCCCCCCE		27.7919690332
204PhosphorylationKGGTYDTYVGSGWLI
CCCEEEEEECCCEEE		10.42-
214SulfoxidationSGWLIKGMDQGLLGM
CCEEEECCCCCCCCC		2.7130846556
221SulfoxidationMDQGLLGMCPGERRK
CCCCCCCCCCCCCCE		2.2230846556
222GlutathionylationDQGLLGMCPGERRKI
CCCCCCCCCCCCCEE		3.5722555962
228UbiquitinationMCPGERRKIIIPPFL
CCCCCCCEEEECCCH		44.47-
282MethylationLPPGCVRRAGAGDFM
CCCCCCEECCCCCCE		19.58-
294N-linked_GlycosylationDFMRYHYNGSLMDGT
CCEEEEECCCCCCCC		21.9212754519
294N-linked_GlycosylationDFMRYHYNGSLMDGT
CCEEEEECCCCCCCC		21.92UniProtKB CARBOHYD
310N-linked_GlycosylationFDSSYSRNHTYNTYI
CCCCCCCCCEECEEE		26.38UniProtKB CARBOHYD
352N-linked_GlycosylationPHLAYGENGTGDKIP
CHHCCCCCCCCCCCC		49.30UniProtKB CARBOHYD
393N-linked_GlycosylationSRPSETCNETTKLGD
CCCCCCCCCCCCHHH		58.00UniProtKB CARBOHYD
407N-linked_GlycosylationDFVRYHYNCSLLDGT
HHHHEEECCCCCCCC		8.7912754519
446SulfoxidationLDTGLQGMCVGERRQ
CCCCCCCCCCCCCEE		0.7830846556
493PhosphorylationEDGLPTGYLFVWHKD
CCCCCCEEEEEEECC		10.23-
509SulfoxidationPANLFEDMDLNKDGE
CCCCCCCCCCCCCCC		5.0630846556
527UbiquitinationEEFSTFIKAQVSEGK
HHHHHHHHHHHHCCC		28.68-
538SulfoxidationSEGKGRLMPGQDPEK
HCCCCCCCCCCCHHC		3.1830846556
545UbiquitinationMPGQDPEKTIGDMFQ
CCCCCHHCCHHHHHC		51.32-
550SulfoxidationPEKTIGDMFQNQDRN
HHCCHHHHHCCCCCC		2.9130846556
556MethylationDMFQNQDRNQDGKIT
HHHCCCCCCCCCCEE		32.71-
561UbiquitinationQDRNQDGKITVDELK
CCCCCCCCEEHHEEE		43.42-
568UbiquitinationKITVDELKLKSDEDE
CEEHHEEEECCCCCH		52.39-
5682-HydroxyisobutyrylationKITVDELKLKSDEDE
CEEHHEEEECCCCCH		52.39-
571PhosphorylationVDELKLKSDEDEERV
HHEEEECCCCCHHHH		57.5826462736
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 FKB10_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FKB10_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 FKB10_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARP3_HUMANACTR3physical
22863883
ARPC4_HUMANARPC4physical
22863883
DDX5_HUMANDDX5physical
22863883
EFL1_HUMANEFTUD1physical
22863883
DAAF5_HUMANDNAAF5physical
22863883
HPBP1_HUMANHSPBP1physical
22863883
P3H1_HUMANP3H1physical
22863883
LPP_HUMANLPPphysical
22863883
NPL4_HUMANNPLOC4physical
22863883
PPME1_HUMANPPME1physical
22863883
PP1R7_HUMANPPP1R7physical
22863883
TTL12_HUMANTTLL12physical
22863883
ZPR1_HUMANZPR1physical
22863883
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
610968Osteogenesis imperfecta 11 (OI11)
259450Bruck syndrome 1 (BRKS1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FKB10_HUMAN

loading...

Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-182, AND MASSSPECTROMETRY.
"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-182 AND ASN-407.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory