FBX7_HUMAN - dbPTM
FBX7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FBX7_HUMAN
UniProt AC Q9Y3I1
Protein Name F-box only protein 7
Gene Name FBXO7
Organism Homo sapiens (Human).
Sequence Length 522
Subcellular Localization Cytoplasm. Nucleus. Mitochondrion. Cytoplasm, cytosol. Predominantly cytoplasmic. A minor proportion is detected in the nucleus. Relocates from the cytosol to depolarized mitochondria.
Protein Description Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes BIRC2 and DLGAP5. Plays a role downstream of PINK1 in the clearance of damaged mitochondria via selective autophagy (mitophagy) by targeting PRKN to dysfunctional depolarized mitochondria. Promotes MFN1 ubiquitination..
Protein Sequence MRLRVRLLKRTWPLEVPETEPTLGHLRSHLRQSLLCTWGYSSNTRFTITLNYKDPLTGDEETLASYGIVSGDLICLILQDDIPAPNIPSSTDSEHSSLQNNEQPSLATSSNQTSMQDEQPSDSFQGQAAQSGVWNDDSMLGPSQNFEAESIQDNAHMAEGTGFYPSEPMLCSESVEGQVPHSLETLYQSADCSDANDALIVLIHLLMLESGYIPQGTEAKALSMPEKWKLSGVYKLQYMHPLCEGSSATLTCVPLGNLIVVNATLKINNEIRSVKRLQLLPESFICKEKLGENVANIYKDLQKLSRLFKDQLVYPLLAFTRQALNLPDVFGLVVLPLELKLRIFRLLDVRSVLSLSAVCRDLFTASNDPLLWRFLYLRDFRDNTVRVQDTDWKELYRKRHIQRKESPKGRFVMLLPSSTHTIPFYPNPLHPRPFPSSRLPPGIIGGEYDQRPTLPYVGDPISSLIPGPGETPSQFPPLRPRFDPVGPLPGPNPILPGRGGPNDRFPFRPSRGRPTDGRLSFM
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
11PhosphorylationRVRLLKRTWPLEVPE
HHEHHHCCCCCCCCC		29.8226270265
28PhosphorylationPTLGHLRSHLRQSLL
CCHHHHHHHHHHHHH		32.9829759185
33PhosphorylationLRSHLRQSLLCTWGY
HHHHHHHHHHHCCCC		19.5125072903
37PhosphorylationLRQSLLCTWGYSSNT
HHHHHHHCCCCCCCC		23.1525072903
40PhosphorylationSLLCTWGYSSNTRFT
HHHHCCCCCCCCEEE		10.6525072903
41PhosphorylationLLCTWGYSSNTRFTI
HHHCCCCCCCCEEEE		17.1125072903
42PhosphorylationLCTWGYSSNTRFTIT
HHCCCCCCCCEEEEE		33.4625072903
44PhosphorylationTWGYSSNTRFTITLN
CCCCCCCCEEEEEEE		29.1625072903
113UbiquitinationLATSSNQTSMQDEQP
CCCCCCCCCCCCCCC		30.3429967540
148UbiquitinationGPSQNFEAESIQDNA
CCCCCCCCHHHHHCC		16.2329967540
153UbiquitinationFEAESIQDNAHMAEG
CCCHHHHHCCCCCCC		53.2521890473
173UbiquitinationSEPMLCSESVEGQVP
CCCCCCCCCCCCCCC		58.7829967540
175UbiquitinationPMLCSESVEGQVPHS
CCCCCCCCCCCCCCC		9.3429967540
195UbiquitinationQSADCSDANDALIVL
HCCCCCCHHHHHHHH		10.2521890473
208UbiquitinationVLIHLLMLESGYIPQ
HHHHHHHHHCCCCCC		4.8329967540
210UbiquitinationIHLLMLESGYIPQGT
HHHHHHHCCCCCCCC		32.7029967540
227UbiquitinationKALSMPEKWKLSGVY
HHCCCCCHHCCCCEE		43.7029967540
230UbiquitinationSMPEKWKLSGVYKLQ
CCCCHHCCCCEEEEE		5.3821890473
230UbiquitinationSMPEKWKLSGVYKLQ
CCCCHHCCCCEEEEE		5.3821890473
230UbiquitinationSMPEKWKLSGVYKLQ
CCCCHHCCCCEEEEE		5.3821890473
230UbiquitinationSMPEKWKLSGVYKLQ
CCCCHHCCCCEEEEE		5.3821890473
237UbiquitinationLSGVYKLQYMHPLCE
CCCEEEEEECCCCCC		29.3821890473
279UbiquitinationRSVKRLQLLPESFIC
HHCCEEEECCHHHCC		11.5921890473
283PhosphorylationRLQLLPESFICKEKL
EEEECCHHHCCHHHH		20.26-
286S-nitrosylationLLPESFICKEKLGEN
ECCHHHCCHHHHCCC		4.3619483679
286S-nitrosocysteineLLPESFICKEKLGEN
ECCHHHCCHHHHCCC		4.36-
287UbiquitinationLPESFICKEKLGENV
CCHHHCCHHHHCCCH		53.7429967540
289UbiquitinationESFICKEKLGENVAN
HHHCCHHHHCCCHHH		47.4929967540
289AcetylationESFICKEKLGENVAN
HHHCCHHHHCCCHHH		47.4925953088
305PhosphorylationYKDLQKLSRLFKDQL
HHHHHHHHHHHHHHC		33.6921955146
309UbiquitinationQKLSRLFKDQLVYPL
HHHHHHHHHHCHHHH		49.5121890473
314UbiquitinationLFKDQLVYPLLAFTR
HHHHHCHHHHHHHHH		9.2121890473
314UbiquitinationLFKDQLVYPLLAFTR
HHHHHCHHHHHHHHH		9.2121890473
314UbiquitinationLFKDQLVYPLLAFTR
HHHHHCHHHHHHHHH		9.2121890473
314UbiquitinationLFKDQLVYPLLAFTR
HHHHHCHHHHHHHHH		9.2121890473
384PhosphorylationLRDFRDNTVRVQDTD
HHHCCCCEEEEECCC		17.61-
393UbiquitinationRVQDTDWKELYRKRH
EEECCCHHHHHHHHH		40.4221906983
417O-linked_GlycosylationRFVMLLPSSTHTIPF
CEEEECCCCCCCCCC		48.0830059200
421O-linked_GlycosylationLLPSSTHTIPFYPNP
ECCCCCCCCCCCCCC		30.3630059200
432MethylationYPNPLHPRPFPSSRL
CCCCCCCCCCCHHCC		34.44-
451MethylationIGGEYDQRPTLPYVG
CCCCCCCCCCCCCCC		24.23-
479MethylationPSQFPPLRPRFDPVG
CCCCCCCCCCCCCCC		26.56-
481MethylationQFPPLRPRFDPVGPL
CCCCCCCCCCCCCCC		42.01-
498MethylationPNPILPGRGGPNDRF
CCCCCCCCCCCCCCC		44.98-
504MethylationGRGGPNDRFPFRPSR
CCCCCCCCCCCCCCC		48.02-
518MethylationRGRPTDGRLSFM---
CCCCCCCCCCCC---		29.93-
518Asymmetric dimethylarginineRGRPTDGRLSFM---
CCCCCCCCCCCC---		29.93-
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 FBX7_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FBX7_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 FBX7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CUL1_HUMANCUL1physical
10531035
SKP1_HUMANSKP1physical
10531035
PSMF1_HUMANPSMF1physical
18495667
CUL1_HUMANCUL1physical
18495667
DLGP5_HUMANDLGAP5physical
15145941
CUL1_HUMANCUL1physical
15145941
SKP1_HUMANSKP1physical
15145941
SKP1_HUMANSKP1physical
21378169
BIRC2_HUMANBIRC2physical
22212761
SKP1_HUMANSKP1physical
16278047
CUL1_HUMANCUL1physical
16278047
PINK1_HUMANPINK1physical
23933751
PRKN_HUMANPARK2physical
23933751
SC24C_HUMANSEC24Cphysical
21988832
MAGD1_HUMANMAGED1physical
24947323
SKP1_HUMANSKP1physical
24947323
TZAP_HUMANZBTB48physical
26496610
ANM1_HUMANPRMT1physical
26496610
CH60_HUMANHSPD1physical
26496610
PDE3A_HUMANPDE3Aphysical
26496610
PSA6_HUMANPSMA6physical
26496610
SKP1_HUMANSKP1physical
26496610
ELOC_HUMANTCEB1physical
26496610
CUL1_HUMANCUL1physical
26496610
GBF1_HUMANGBF1physical
26496610
PSMF1_HUMANPSMF1physical
26496610
ESPL1_HUMANESPL1physical
26496610
HPSE_HUMANHPSEphysical
26496610
XPOT_HUMANXPOTphysical
26496610
SIR1_HUMANSIRT1physical
26496610
PANX1_HUMANPANX1physical
26496610
NECT3_HUMANPVRL3physical
26496610
FBXW2_HUMANFBXW2physical
26496610
CRNL1_HUMANCRNKL1physical
26496610
ESF1_HUMANESF1physical
26496610
SRRT_HUMANSRRTphysical
26496610
NSF1C_HUMANNSFL1Cphysical
26496610
PAR10_HUMANPARP10physical
26496610
SKP1_HUMANSKP1physical
27497298
PSMF1_HUMANPSMF1physical
27497298
PSA2_HUMANPSMA2physical
27497298
CUL1_HUMANCUL1physical
27497298
RBX1_HUMANRBX1physical
27497298
PSB3_HUMANPSMB3physical
27497298
PSB4_HUMANPSMB4physical
27497298
PSB6_HUMANPSMB6physical
27497298
PSA6_HUMANPSMA6physical
27497298
PSME3_HUMANPSME3physical
27497298
PSME1_HUMANPSME1physical
27497298
PSB1_HUMANPSMB1physical
27497298
UB2R1_HUMANCDC34physical
27497298
UB2D3_HUMANUBE2D3physical
27497298
PSMF1_HUMANPSMF1physical
28514442
RN181_HUMANRNF181physical
28514442
CUL1_HUMANCUL1physical
28514442
FBXW2_HUMANFBXW2physical
28514442
CSN7B_HUMANCOPS7Bphysical
28514442
PSME2_HUMANPSME2physical
28514442
CSN7A_HUMANCOPS7Aphysical
28514442
PSME1_HUMANPSME1physical
28514442
CSN6_HUMANCOPS6physical
28514442
CSN5_HUMANCOPS5physical
28514442
CSN4_HUMANCOPS4physical
28514442
CSN3_HUMANCOPS3physical
28514442
TTC38_HUMANTTC38physical
28514442
SKP1_HUMANSKP1physical
28514442
CSN1_HUMANGPS1physical
28514442
PRS8_HUMANPSMC5physical
27497298
PSB5_HUMANPSMB5physical
27497298
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
260300Parkinson disease 15 (PARK15)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FBX7_HUMAN

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Related Literatures of Post-Translational Modification

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