FKBP8_HUMAN - dbPTM
FKBP8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FKBP8_HUMAN
UniProt AC Q14318
Protein Name Peptidyl-prolyl cis-trans isomerase FKBP8
Gene Name FKBP8
Organism Homo sapiens (Human).
Sequence Length 412
Subcellular Localization Mitochondrion . Mitochondrion membrane
Single-pass membrane protein
Cytoplasmic side .
Isoform 1: Mitochondrion membrane
Single-pass membrane protein
Cytoplasmic side .
Isoform 3: Mitochondrion membrane
Single-pass membrane protein
Cytoplasmic
Protein Description Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis..
Protein Sequence MASCAEPSEPSAPLPAGVPPLEDFEVLDGVEDAEGEEEEEEEEEEEDDLSELPPLEDMGQPPAEEAEQPGALAREFLAAMEPEPAPAPAPEEWLDILGNGLLRKKTLVPGPPGSSRPVKGQVVTVHLQTSLENGTRVQEEPELVFTLGDCDVIQALDLSVPLMDVGETAMVTADSKYCYGPQGRSPYIPPHAALCLEVTLKTAVDGPDLEMLTGQERVALANRKRECGNAHYQRADFVLAANSYDLAIKAITSSAKVDMTFEEEAQLLQLKVKCLNNLAASQLKLDHYRAALRSCSLVLEHQPDNIKALFRKGKVLAQQGEYSEAIPILRAALKLEPSNKTIHAELSKLVKKHAAQRSTETALYRKMLGNPSRLPAKCPGKGAWSIPWKWLFGATAVALGGVALSVVIAARN
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
105UbiquitinationGNGLLRKKTLVPGPP
CCCCCCCCEECCCCC		40.43-
106PhosphorylationNGLLRKKTLVPGPPG
CCCCCCCEECCCCCC		35.7023312004
112UbiquitinationKTLVPGPPGSSRPVK
CEECCCCCCCCCCCC		62.3021890473
114UbiquitinationLVPGPPGSSRPVKGQ
ECCCCCCCCCCCCCC		29.02-
125UbiquitinationVKGQVVTVHLQTSLE
CCCCEEEEEEEEECC		2.61-
148UbiquitinationPELVFTLGDCDVIQA
CEEEEEECCCCHHHH		30.37-
155UbiquitinationGDCDVIQALDLSVPL
CCCCHHHHCCCCCEE		7.6021890473
175UbiquitinationTAMVTADSKYCYGPQ
EEEEECCCCCCCCCC		24.06-
181UbiquitinationDSKYCYGPQGRSPYI
CCCCCCCCCCCCCCC		13.64-
189UbiquitinationQGRSPYIPPHAALCL
CCCCCCCCHHHHHHH		14.58-
211SulfoxidationVDGPDLEMLTGQERV
CCCCCHHHHCCHHHH		5.4421406390
232PhosphorylationRECGNAHYQRADFVL
CCCCCCHHHHCCEEE		9.4028796482
249UbiquitinationNSYDLAIKAITSSAK
CCHHHHHHHHHCCCC		28.2921906983
249 (in isoform 1)Ubiquitination-28.2921890473
250 (in isoform 2)Ubiquitination-12.27-
259SulfoxidationTSSAKVDMTFEEEAQ
HCCCCCCCCHHHHHH		5.3221406390
265PhosphorylationDMTFEEEAQLLQLKV
CCCHHHHHHHHHHHH		14.4815592455
271AcetylationEAQLLQLKVKCLNNL
HHHHHHHHHHHHHHH		27.0426051181
271MethylationEAQLLQLKVKCLNNL
HHHHHHHHHHHHHHH		27.04-
271UbiquitinationEAQLLQLKVKCLNNL
HHHHHHHHHHHHHHH		27.0421890473
271 (in isoform 1)Ubiquitination-27.0421890473
272 (in isoform 2)Ubiquitination-7.8121890473
273MalonylationQLLQLKVKCLNNLAA
HHHHHHHHHHHHHHH		31.2726320211
273UbiquitinationQLLQLKVKCLNNLAA
HHHHHHHHHHHHHHH		31.2725621951
2732-HydroxyisobutyrylationQLLQLKVKCLNNLAA
HHHHHHHHHHHHHHH		31.27-
274 (in isoform 2)Ubiquitination-5.72-
278 (in isoform 2)Ubiquitination-4.0221890473
281PhosphorylationCLNNLAASQLKLDHY
HHHHHHHHHHCHHHH		30.3628857561
284UbiquitinationNLAASQLKLDHYRAA
HHHHHHHCHHHHHHH		44.2025621951
284AcetylationNLAASQLKLDHYRAA
HHHHHHHCHHHHHHH		44.2026051181
285 (in isoform 2)Ubiquitination-7.16-
288PhosphorylationSQLKLDHYRAALRSC
HHHCHHHHHHHHHHC		11.12-
294PhosphorylationHYRAALRSCSLVLEH
HHHHHHHHCCEEECC		14.6530266825
296PhosphorylationRAALRSCSLVLEHQP
HHHHHHCCEEECCCC		23.8223401153
297 (in isoform 2)Phosphorylation-6.3024719451
300 (in isoform 2)Ubiquitination-32.7521890473
307UbiquitinationEHQPDNIKALFRKGK
CCCCCCHHHHHHHCC		45.3421906983
3072-HydroxyisobutyrylationEHQPDNIKALFRKGK
CCCCCCHHHHHHHCC		45.34-
307AcetylationEHQPDNIKALFRKGK
CCCCCCHHHHHHHCC		45.3426051181
307 (in isoform 1)Ubiquitination-45.3421890473
308 (in isoform 2)Ubiquitination-14.24-
314 (in isoform 1)Ubiquitination-36.7921890473
314UbiquitinationKALFRKGKVLAQQGE
HHHHHHCCEEHHCCC		36.792189047
315 (in isoform 2)Ubiquitination-7.9421890473
322PhosphorylationVLAQQGEYSEAIPIL
EEHHCCCHHHHHHHH		20.7328796482
323PhosphorylationLAQQGEYSEAIPILR
EHHCCCHHHHHHHHH		19.0928796482
334MalonylationPILRAALKLEPSNKT
HHHHHHHCCCCCCCC		46.1826320211
334AcetylationPILRAALKLEPSNKT
HHHHHHHCCCCCCCC		46.1825953088
334UbiquitinationPILRAALKLEPSNKT
HHHHHHHCCCCCCCC		46.1825621951
335 (in isoform 2)Ubiquitination-14.06-
336 (in isoform 2)Ubiquitination-45.1321890473
340MalonylationLKLEPSNKTIHAELS
HCCCCCCCCHHHHHH		53.8726320211
340UbiquitinationLKLEPSNKTIHAELS
HCCCCCCCCHHHHHH		53.8725621951
341PhosphorylationKLEPSNKTIHAELSK
CCCCCCCCHHHHHHH		23.4223312004
341 (in isoform 2)Ubiquitination-23.42-
343 (in isoform 2)Ubiquitination-20.5521890473
347PhosphorylationKTIHAELSKLVKKHA
CCHHHHHHHHHHHHH		18.5630108239
348AcetylationTIHAELSKLVKKHAA
CHHHHHHHHHHHHHH		70.6725953088
348UbiquitinationTIHAELSKLVKKHAA
CHHHHHHHHHHHHHH		70.6719608861
348MalonylationTIHAELSKLVKKHAA
CHHHHHHHHHHHHHH		70.6726320211
348 (in isoform 2)Phosphorylation-70.6727251275
349AcetylationIHAELSKLVKKHAAQ
HHHHHHHHHHHHHHH		6.4919608861
349 (in isoform 2)Ubiquitination-6.49-
351UbiquitinationAELSKLVKKHAAQRS
HHHHHHHHHHHHHHH		49.6425621951
352UbiquitinationELSKLVKKHAAQRST
HHHHHHHHHHHHHHH		30.8825621951
358PhosphorylationKKHAAQRSTETALYR
HHHHHHHHHHHHHHH		20.6521815630
359PhosphorylationKHAAQRSTETALYRK
HHHHHHHHHHHHHHH		39.2730108239
361PhosphorylationAAQRSTETALYRKML
HHHHHHHHHHHHHHH		23.2728796482
364PhosphorylationRSTETALYRKMLGNP
HHHHHHHHHHHHCCH		13.0125884760
366UbiquitinationTETALYRKMLGNPSR
HHHHHHHHHHCCHHH		25.56-
372PhosphorylationRKMLGNPSRLPAKCP
HHHHCCHHHCCCCCC		50.9128857561
377UbiquitinationNPSRLPAKCPGKGAW
CHHHCCCCCCCCCCC		38.74-
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 FKBP8_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FKBP8_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 FKBP8_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HS90A_HUMANHSP90AA1physical
17379601
PRS4_HUMANPSMC1physical
17573772
PRS7_HUMANPSMC2physical
17573772
PRS6A_HUMANPSMC3physical
17573772
PRS6B_HUMANPSMC4physical
17573772
PRS8_HUMANPSMC5physical
17573772
PRS10_HUMANPSMC6physical
17573772
PSMD1_HUMANPSMD1physical
17573772
PSMD2_HUMANPSMD2physical
17573772
PSMD3_HUMANPSMD3physical
17573772
PSMD4_HUMANPSMD4physical
17573772
PSMD6_HUMANPSMD6physical
17573772
PSMD7_HUMANPSMD7physical
17573772
PSD11_HUMANPSMD11physical
17573772
PSD12_HUMANPSMD12physical
17573772
PSD13_HUMANPSMD13physical
17573772
PSDE_HUMANPSMD14physical
17573772
PSA1_HUMANPSMA1physical
17573772
PSA2_HUMANPSMA2physical
17573772
PSA3_HUMANPSMA3physical
17573772
PSA4_HUMANPSMA4physical
17573772
PSA5_HUMANPSMA5physical
17573772
PSA6_HUMANPSMA6physical
17573772
PSA7_HUMANPSMA7physical
17573772
PSB1_HUMANPSMB1physical
17573772
PSB2_HUMANPSMB2physical
17573772
PSB3_HUMANPSMB3physical
17573772
PSB5_HUMANPSMB5physical
17573772
PSB7_HUMANPSMB7physical
17573772
ADRM1_HUMANADRM1physical
17573772
PTPRK_HUMANPTPRKphysical
17573772
UBC_HUMANUBCphysical
17573772
EGLN1_HUMANEGLN1physical
19546213
PRS4_HUMANPSMC1physical
19546213
PSMD2_HUMANPSMD2physical
19546213
EGLN1_HUMANEGLN1physical
21559462
BCL2_HUMANBCL2physical
15733859
SURF1_HUMANSURF1physical
22939629
RM11_HUMANMRPL11physical
22939629
YMEL1_HUMANYME1L1physical
22939629
QCR1_HUMANUQCRC1physical
22939629
QCR2_HUMANUQCRC2physical
22939629
RM15_HUMANMRPL15physical
22939629
SSRA_HUMANSSR1physical
22939629
UCRI_HUMANUQCRFS1physical
22939629
PGRC1_HUMANPGRMC1physical
22939629
PYRD_HUMANDHODHphysical
22939629
NDUBA_HUMANNDUFB10physical
22939629
TOM22_HUMANTOMM22physical
22939629
MRP1_HUMANABCC1physical
22939629
NNTM_HUMANNNTphysical
22939629
KCNH2_HUMANKCNH2physical
17569659
BCL2_HUMANBCL2physical
15990872
FKBP8_HUMANFKBP8physical
17024179
HS90A_HUMANHSP90AA1physical
17024179
KCC2A_HUMANCAMK2Aphysical
15757646
PHLP_HUMANPDCLphysical
25036637
SGT1_HUMANSUGT1physical
25036637
TEBP_HUMANPTGES3physical
25036637
CYBP_HUMANCACYBPphysical
25036637
HPBP1_HUMANHSPBP1physical
25036637
RHEB_HUMANRHEBphysical
17991864
MTOR_HUMANMTORphysical
17991864
LST8_HUMANMLST8physical
17991864
RPTOR_HUMANRPTORphysical
17991864
RICTR_HUMANRICTORphysical
17991864
ABCB7_HUMANABCB7physical
26344197
EGLN1_HUMANEGLN1physical
17353276
EGLN1_HUMANEGLN1physical
23413029
EGLN1_HUMANEGLN1physical
24711448
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 FKBP8_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-348, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-322, AND MASSSPECTROMETRY.

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