FKBP5_HUMAN - dbPTM
FKBP5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FKBP5_HUMAN
UniProt AC Q13451
Protein Name Peptidyl-prolyl cis-trans isomerase FKBP5
Gene Name FKBP5
Organism Homo sapiens (Human).
Sequence Length 457
Subcellular Localization Cytoplasm. Nucleus.
Protein Description Immunophilin protein with PPIase and co-chaperone activities. Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). Plays a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors maintaining the complex into the cytoplasm when unliganded..
Protein Sequence MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV
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
1Acetylation-------MTTDEGAK
-------CCCHHHHC		9.0919413330
2Phosphorylation------MTTDEGAKN
------CCCHHHHCC		42.8428450419
3Phosphorylation-----MTTDEGAKNN
-----CCCHHHHCCC		30.6528450419
13PhosphorylationGAKNNEESPTATVAE
HHCCCCCCCCCCHHC		22.7523927012
15PhosphorylationKNNEESPTATVAEQG
CCCCCCCCCCHHCCC		44.2130278072
17PhosphorylationNEESPTATVAEQGED
CCCCCCCCHHCCCCC		23.7923927012
26PhosphorylationAEQGEDITSKKDRGV
HCCCCCCCCHHHCCC		46.9823403867
27PhosphorylationEQGEDITSKKDRGVL
CCCCCCCCHHHCCCE		37.7323403867
28AcetylationQGEDITSKKDRGVLK
CCCCCCCHHHCCCEE		50.47126230419
28UbiquitinationQGEDITSKKDRGVLK
CCCCCCCHHHCCCEE		50.4721906983
48SulfoxidationGNGEETPMIGDKVYV
CCCCCCCCCCCEEEE		7.5521406390
54PhosphorylationPMIGDKVYVHYKGKL
CCCCCEEEEEEECCC		6.3028258704
57PhosphorylationGDKVYVHYKGKLSNG
CCEEEEEEECCCCCC		16.0528258704
58AcetylationDKVYVHYKGKLSNGK
CEEEEEEECCCCCCC		34.3925953088
66AcetylationGKLSNGKKFDSSHDR
CCCCCCCCCCCCCCC		56.6625953088
155AcetylationIIRRTKRKGEGYSNP
EEEEEEECCCCCCCC		63.9728147277
159PhosphorylationTKRKGEGYSNPNEGA
EEECCCCCCCCCCCC		10.8528152594
160PhosphorylationKRKGEGYSNPNEGAT
EECCCCCCCCCCCCE		57.5828152594
189PhosphorylationDCRDVAFTVGEGEDH
ECCEEEEEECCCCCC		20.1930387612
204UbiquitinationDIPIGIDKALEKMQR
CCCCCHHHHHHHHHH		53.61-
208UbiquitinationGIDKALEKMQREEQC
CHHHHHHHHHHHHCE		40.98-
215GlutathionylationKMQREEQCILYLGPR
HHHHHHCEEEEECCC		2.3422555962
218NitrationREEQCILYLGPRYGF
HHHCEEEEECCCCCC		6.95-
223PhosphorylationILYLGPRYGFGEAGK
EEEECCCCCCCCCCC		21.6828152594
236PhosphorylationGKPKFGIEPNAELIY
CCCCCCCCCCCEEEE		32.6424719451
243PhosphorylationEPNAELIYEVTLKSF
CCCCEEEEEEEHHHH		19.5727259358
248UbiquitinationLIYEVTLKSFEKAKE
EEEEEEHHHHHHHHH		43.67-
248AcetylationLIYEVTLKSFEKAKE
EEEEEEHHHHHHHHH		43.67126230423
274UbiquitinationQAAIVKEKGTVYFKG
HHHHHEECCEEEEEC		54.91-
284PhosphorylationVYFKGGKYMQAVIQY
EEEECCEEEEHHHHH		9.5720068231
291PhosphorylationYMQAVIQYGKIVSWL
EEEHHHHHHHHHHHH		14.8420068231
327PhosphorylationFLNLAMCYLKLREYT
HHHHHHHHHHHHHHH		8.1918083107
342AcetylationKAVECCDKALGLDSA
HHHHHHHHHHCCCCC		31.4326051181
342UbiquitinationKAVECCDKALGLDSA
HHHHHHHHHHCCCCC		31.43-
348PhosphorylationDKALGLDSANEKGLY
HHHHCCCCCCCCCCH		37.7327499020
352UbiquitinationGLDSANEKGLYRRGE
CCCCCCCCCCHHHHH		54.7621890473
352UbiquitinationGLDSANEKGLYRRGE
CCCCCCCCCCHHHHH		54.7621890473
355PhosphorylationSANEKGLYRRGEAQL
CCCCCCCHHHHHHHH		13.6125002506
357MethylationNEKGLYRRGEAQLLM
CCCCCHHHHHHHHHH		33.47-
364SulfoxidationRGEAQLLMNEFESAK
HHHHHHHHHHHHHCC		6.5021406390
376UbiquitinationSAKGDFEKVLEVNPQ
HCCCCHHHHHCCCCC		52.7121890473
376UbiquitinationSAKGDFEKVLEVNPQ
HCCCCHHHHHCCCCC		52.7121890473
385UbiquitinationLEVNPQNKAARLQIS
HCCCCCCHHHHHHHH		37.87-
392PhosphorylationKAARLQISMCQKKAK
HHHHHHHHHHHHHHH		10.6727080861
396AcetylationLQISMCQKKAKEHNE
HHHHHHHHHHHHHCH		50.1725953088
409PhosphorylationNERDRRIYANMFKKF
CHHHHHHHHHHHHHH		7.0728796482
414AcetylationRIYANMFKKFAEQDA
HHHHHHHHHHHHHHH		35.8925953088
415AcetylationIYANMFKKFAEQDAK
HHHHHHHHHHHHHHH		38.2430585551
422SumoylationKFAEQDAKEEANKAM
HHHHHHHHHHHHHHH		65.46-
422UbiquitinationKFAEQDAKEEANKAM
HHHHHHHHHHHHHHH		65.46-
422SumoylationKFAEQDAKEEANKAM
HHHHHHHHHHHHHHH		65.46-
433PhosphorylationNKAMGKKTSEGVTNE
HHHHCCCCCCCCCCC		35.1823927012
434PhosphorylationKAMGKKTSEGVTNEK
HHHCCCCCCCCCCCC		41.0323927012
438PhosphorylationKKTSEGVTNEKGTDS
CCCCCCCCCCCCCCC		48.8223927012
441UbiquitinationSEGVTNEKGTDSQAM
CCCCCCCCCCCCHHH		70.002190698
441AcetylationSEGVTNEKGTDSQAM
CCCCCCCCCCCCHHH		70.0026051181
443PhosphorylationGVTNEKGTDSQAMEE
CCCCCCCCCCHHHHH		43.4723401153
445PhosphorylationTNEKGTDSQAMEEEK
CCCCCCCCHHHHHCC		21.4829255136
448SulfoxidationKGTDSQAMEEEKPEG
CCCCCHHHHHCCCCC		5.3021406390
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 FKBP5_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FKBP5_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 FKBP5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PRGR_HUMANPGRphysical
12538866
HS90A_HUMANHSP90AA1physical
9001212
HS90A_HUMANHSP90AA1physical
21170051
STIP1_HUMANSTIP1physical
21170051
AKT1_HUMANAKT1physical
20605778
PRGR_HUMANPGRphysical
22891251
MAGAB_HUMANMAGEA11physical
22891251
A4_HUMANAPPphysical
21832049
HS90A_HUMANHSP90AA1physical
21235734
SGT1_HUMANSUGT1physical
25036637
NUDC3_HUMANNUDCD3physical
25036637
HS90B_HUMANHSP90AB1physical
25036637
ILK_HUMANILKphysical
25036637
NUDC_HUMANNUDCphysical
25036637
HS90A_HUMANHSP90AA1physical
25036637
AGO2_HUMANAGO2physical
25036637
CYBP_HUMANCACYBPphysical
25036637
GCR_HUMANNR3C1physical
25036637
IKKA_HUMANCHUKphysical
25036637
AURKB_HUMANAURKBphysical
25036637
ARAF_HUMANARAFphysical
25036637
TEBP_HUMANPTGES3physical
25036637
GLMN_HUMANGLMNphysical
25036637
CD37L_HUMANCDC37L1physical
25036637
TTC4_HUMANTTC4physical
25036637
CHRD1_HUMANCHORDC1physical
25036637
LRC40_HUMANLRRC40physical
25036637
NEMO_HUMANIKBKGphysical
25036637
KBP_HUMANKIAA1279physical
25036637
CDC37_HUMANCDC37physical
25036637
AHSA1_HUMANAHSA1physical
25036637
ANKY2_HUMANANKMY2physical
25036637
EGLN1_HUMANEGLN1physical
25036637
HGH1_HUMANHGH1physical
25036637
MCMBP_HUMANMCMBPphysical
25036637
PDCD2_HUMANPDCD2physical
25036637
CDK9_HUMANCDK9physical
25036637
CDK4_HUMANCDK4physical
25036637
CD11A_HUMANCDK11Aphysical
25036637
AGO1_HUMANAGO1physical
25036637
TBA1A_HUMANTUBA1Aphysical
25036637
PLPL2_HUMANPNPLA2physical
25036637
DNJB6_HUMANDNAJB6physical
25036637
CN080_HUMANC14orf80physical
25036637
CX057_HUMANCXorf57physical
25036637
PYGL_HUMANPYGLphysical
25036637
MCM4_HUMANMCM4physical
25036637
HS90A_HUMANHSP90AA1physical
10642522
DUT_HUMANDUTphysical
26344197
TLE3_HUMANTLE3physical
26344197
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 FKBP5_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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 MET-1, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-445, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND MASSSPECTROMETRY.

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