FDFT_HUMAN - dbPTM
FDFT_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FDFT_HUMAN
UniProt AC P37268
Protein Name Squalene synthase
Gene Name FDFT1
Organism Homo sapiens (Human).
Sequence Length 417
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein.
Protein Description
Protein Sequence MEFVKCLGHPEEFYNLVRFRIGGKRKVMPKMDQDSLSSSLKTCYKYLNQTSRSFAAVIQALDGEMRNAVCIFYLVLRALDTLEDDMTISVEKKVPLLHNFHSFLYQPDWRFMESKEKDRQVLEDFPTISLEFRNLAEKYQTVIADICRRMGIGMAEFLDKHVTSEQEWDKYCHYVAGLVGIGLSRLFSASEFEDPLVGEDTERANSMGLFLQKTNIIRDYLEDQQGGREFWPQEVWSRYVKKLGDFAKPENIDLAVQCLNELITNALHHIPDVITYLSRLRNQSVFNFCAIPQVMAIATLAACYNNQQVFKGAVKIRKGQAVTLMMDATNMPAVKAIIYQYMEEIYHRIPDSDPSSSKTRQIISTIRTQNLPNCQLISRSHYSPIYLSFVMLLAALSWQYLTTLSQVTEDYVQTGEH
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
5Ubiquitination---MEFVKCLGHPEE
---CCCCCCCCCHHH		29.12-
5Ubiquitination---MEFVKCLGHPEE
---CCCCCCCCCHHH		29.12-
6S-nitrosocysteine--MEFVKCLGHPEEF
--CCCCCCCCCHHHH		4.65-
6S-nitrosylation--MEFVKCLGHPEEF
--CCCCCCCCCHHHH		4.6519483679
6Ubiquitination--MEFVKCLGHPEEF
--CCCCCCCCCHHHH		4.65-
7Ubiquitination-MEFVKCLGHPEEFY
-CCCCCCCCCHHHHH		6.1421890473
14PhosphorylationLGHPEEFYNLVRFRI
CCCHHHHHHHHHHEE		15.7428796482
27UbiquitinationRIGGKRKVMPKMDQD
EECCCCCCCCCCCHH		10.36-
30UbiquitinationGKRKVMPKMDQDSLS
CCCCCCCCCCHHHHH		36.69-
30UbiquitinationGKRKVMPKMDQDSLS
CCCCCCCCCCHHHHH		36.69-
35PhosphorylationMPKMDQDSLSSSLKT
CCCCCHHHHHHHHHH		25.2329083192
37PhosphorylationKMDQDSLSSSLKTCY
CCCHHHHHHHHHHHH		23.1029083192
38PhosphorylationMDQDSLSSSLKTCYK
CCHHHHHHHHHHHHH		45.0129083192
39PhosphorylationDQDSLSSSLKTCYKY
CHHHHHHHHHHHHHH		30.4329083192
41UbiquitinationDSLSSSLKTCYKYLN
HHHHHHHHHHHHHHH		38.20-
41UbiquitinationDSLSSSLKTCYKYLN
HHHHHHHHHHHHHHH		38.20-
42PhosphorylationSLSSSLKTCYKYLNQ
HHHHHHHHHHHHHHH		26.7629083192
44PhosphorylationSSSLKTCYKYLNQTS
HHHHHHHHHHHHHHH		14.1129083192
45UbiquitinationSSLKTCYKYLNQTSR
HHHHHHHHHHHHHHH		45.46-
45AcetylationSSLKTCYKYLNQTSR
HHHHHHHHHHHHHHH		45.4625953088
45UbiquitinationSSLKTCYKYLNQTSR
HHHHHHHHHHHHHHH		45.46-
45MalonylationSSLKTCYKYLNQTSR
HHHHHHHHHHHHHHH		45.4632601280
49UbiquitinationTCYKYLNQTSRSFAA
HHHHHHHHHHHHHHH		37.95-
53PhosphorylationYLNQTSRSFAAVIQA
HHHHHHHHHHHHHHH		21.0027499020
65SulfoxidationIQALDGEMRNAVCIF
HHHHCCHHHHHHHHH		4.9721406390
75UbiquitinationAVCIFYLVLRALDTL
HHHHHHHHHHHHHCC		2.0121890473
86SulfoxidationLDTLEDDMTISVEKK
HHCCCCCCEEEEEEC		5.7621406390
92UbiquitinationDMTISVEKKVPLLHN
CCEEEEEECCCCCCC		57.8421906983
92UbiquitinationDMTISVEKKVPLLHN
CCEEEEEECCCCCCC		57.84-
93UbiquitinationMTISVEKKVPLLHNF
CEEEEEECCCCCCCH		35.26-
93UbiquitinationMTISVEKKVPLLHNF
CEEEEEECCCCCCCH		35.26-
102UbiquitinationPLLHNFHSFLYQPDW
CCCCCHHHHHCCCCH		16.89-
115UbiquitinationDWRFMESKEKDRQVL
CHHHHCCHHHHHHHH		56.32-
115UbiquitinationDWRFMESKEKDRQVL
CHHHHCCHHHHHHHH		56.32-
117UbiquitinationRFMESKEKDRQVLED
HHHCCHHHHHHHHHH		63.05-
127PhosphorylationQVLEDFPTISLEFRN
HHHHHCCCCCHHHHH		24.16-
128UbiquitinationVLEDFPTISLEFRNL
HHHHCCCCCHHHHHH		4.5021890473
129PhosphorylationLEDFPTISLEFRNLA
HHHCCCCCHHHHHHH		25.07-
138UbiquitinationEFRNLAEKYQTVIAD
HHHHHHHHHHHHHHH		36.7321890473
149UbiquitinationVIADICRRMGIGMAE
HHHHHHHHCCCCHHH		24.2221890473
150SulfoxidationIADICRRMGIGMAEF
HHHHHHHCCCCHHHH		2.0721406390
160UbiquitinationGMAEFLDKHVTSEQE
CHHHHHHHHCCCHHH		41.9621906983
164PhosphorylationFLDKHVTSEQEWDKY
HHHHHCCCHHHHHHH		35.87-
170UbiquitinationTSEQEWDKYCHYVAG
CCHHHHHHHHHHHHH		51.3421890473
207SulfoxidationDTERANSMGLFLQKT
CCHHHHHHHHHHHHH		5.6221406390
207UbiquitinationDTERANSMGLFLQKT
CCHHHHHHHHHHHHH		5.62-
213UbiquitinationSMGLFLQKTNIIRDY
HHHHHHHHHHHHHHH		45.7621890473
213UbiquitinationSMGLFLQKTNIIRDY
HHHHHHHHHHHHHHH		45.7621890473
224UbiquitinationIRDYLEDQQGGREFW
HHHHHHHCCCCCCCC		34.15-
233UbiquitinationGGREFWPQEVWSRYV
CCCCCCCHHHHHHHH		48.7721890473
247UbiquitinationVKKLGDFAKPENIDL
HHHHCCCCCHHHHHH		31.10-
254UbiquitinationAKPENIDLAVQCLNE
CCHHHHHHHHHHHHH		4.4421890473
273UbiquitinationALHHIPDVITYLSRL
HHHHHHHHHHHHHHH		2.7121890473
294UbiquitinationNFCAIPQVMAIATLA
HCCHHHHHHHHHHHH		2.0421890473
318UbiquitinationKGAVKIRKGQAVTLM
CCCEEECCCCEEEEE		59.8721906983
335UbiquitinationATNMPAVKAIIYQYM
CCCCHHHHHHHHHHH		35.65-
346PhosphorylationYQYMEEIYHRIPDSD
HHHHHHHHHHCCCCC		6.58-
352PhosphorylationIYHRIPDSDPSSSKT
HHHHCCCCCCCCHHH		46.1720071362
358UbiquitinationDSDPSSSKTRQIIST
CCCCCCHHHHHHHHH		50.0721906983
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 FDFT_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FDFT_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 FDFT_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RUVB1_HUMANRUVBL1physical
17353931
UBP32_HUMANUSP32physical
28514442
UN93B_HUMANUNC93B1physical
28514442
CNNM1_HUMANCNNM1physical
28514442
POMT2_HUMANPOMT2physical
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
D00939 Alendronate sodium hydrate (JP16); Alendronate sodium (USAN); Binosto (TN); Fosamax (TN)
D00941 Pamidronate disodium hydrate (JAN); Pamidronate disodium (USAN); Pamidronate disodium pentahydrate;
D00942 Risedronate sodium (USP); Actonel (TN)
D01968 Zoledronic acid hydrate (JAN); Zoledronic acid (USAN); Zometa (TN)
D03234 Sodium risedronate hydrate (JP16); Sodium risedronate hemipentahydrate; Actonel (TN)
D04486 Ibandronate sodium hydrate (JAN); Ibandronate sodium (USAN); Ibandronate sodium monohydrate; Boniva
D06378 Zoledronate disodium (USAN); Zoledronate disodium hydrate
D06379 Zoledronate trisodium (USAN); Zoledronate trisodium hydrate
D07119 Alendronic acid (INN)
D07123 Incadronate disodium hydrate (JAN); Bisphonal (TN)
D07281 Pamidronic acid (INN); Ribodroat (TN)
D08056 Ibandronic acid (INN); Bondronat (TN)
D08073 Incadronic acid (INN)
D08484 Risedronic acid (INN); Ridron (TN)
D08689 Zoledronic acid (INN); Zometa (TN); Reclast (TN)
D09198 Minodronic acid hydrate (JAN); Bonoteo (TN); Recalbon (TN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FDFT_HUMAN

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