SOAT1_HUMAN - dbPTM
SOAT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SOAT1_HUMAN
UniProt AC P35610
Protein Name Sterol O-acyltransferase 1
Gene Name SOAT1
Organism Homo sapiens (Human).
Sequence Length 550
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein .
Protein Description Catalyzes the formation of fatty acid-cholesterol esters, which are less soluble in membranes than cholesterol. Plays a role in lipoprotein assembly and dietary cholesterol absorption. In addition to its acyltransferase activity, it may act as a ligase..
Protein Sequence MVGEEKMSLRNRLSKSRENPEEDEDQRNPAKESLETPSNGRIDIKQLIAKKIKLTAEAEELKPFFMKEVGSHFDDFVTNLIEKSASLDNGGCALTTFSVLEGEKNNHRAKDLRAPPEQGKIFIARRSLLDELLEVDHIRTIYHMFIALLILFILSTLVVDYIDEGRLVLEFSLLSYAFGKFPTVVWTWWIMFLSTFSVPYFLFQHWATGYSKSSHPLIRSLFHGFLFMIFQIGVLGFGPTYVVLAYTLPPASRFIIIFEQIRFVMKAHSFVRENVPRVLNSAKEKSSTVPIPTVNQYLYFLFAPTLIYRDSYPRNPTVRWGYVAMKFAQVFGCFFYVYYIFERLCAPLFRNIKQEPFSARVLVLCVFNSILPGVLILFLTFFAFLHCWLNAFAEMLRFGDRMFYKDWWNSTSYSNYYRTWNVVVHDWLYYYAYKDFLWFFSKRFKSAAMLAVFAVSAVVHEYALAVCLSFFYPVLFVLFMFFGMAFNFIVNDSRKKPIWNVLMWTSLFLGNGVLLCFYSQEWYARQHCPLKNPTFLDYVRPRSWTCRYVF
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-------MVGEEKMS
-------CCCHHHHH
8.6822814378
6Ubiquitination--MVGEEKMSLRNRL
--CCCHHHHHHHHHH
29.5024816145
8PhosphorylationMVGEEKMSLRNRLSK
CCCHHHHHHHHHHHH
34.9323401153
14PhosphorylationMSLRNRLSKSRENPE
HHHHHHHHHCCCCCC
25.9125159151
16PhosphorylationLRNRLSKSRENPEED
HHHHHHHCCCCCCCC
41.2629255136
18UbiquitinationNRLSKSRENPEEDED
HHHHHCCCCCCCCCC
81.7429967540
25UbiquitinationENPEEDEDQRNPAKE
CCCCCCCCCCCCCHH
66.1329967540
31UbiquitinationEDQRNPAKESLETPS
CCCCCCCHHHCCCCC
49.4424816145
33PhosphorylationQRNPAKESLETPSNG
CCCCCHHHCCCCCCC
30.6929255136
36PhosphorylationPAKESLETPSNGRID
CCHHHCCCCCCCCCC
36.9929255136
36O-linked_GlycosylationPAKESLETPSNGRID
CCHHHCCCCCCCCCC
36.9928510447
38PhosphorylationKESLETPSNGRIDIK
HHHCCCCCCCCCCHH
60.3725850435
38O-linked_GlycosylationKESLETPSNGRIDIK
HHHCCCCCCCCCCHH
60.3728510447
39UbiquitinationESLETPSNGRIDIKQ
HHCCCCCCCCCCHHH
44.9929967540
45UbiquitinationSNGRIDIKQLIAKKI
CCCCCCHHHHHHHHC
34.9921890473
45UbiquitinationSNGRIDIKQLIAKKI
CCCCCCHHHHHHHHC
34.9921890473
45AcetylationSNGRIDIKQLIAKKI
CCCCCCHHHHHHHHC
34.9926051181
45UbiquitinationSNGRIDIKQLIAKKI
CCCCCCHHHHHHHHC
34.9923000965
46UbiquitinationNGRIDIKQLIAKKIK
CCCCCHHHHHHHHCC
38.1329967540
50UbiquitinationDIKQLIAKKIKLTAE
CHHHHHHHHCCCCCC
48.3023000965
51UbiquitinationIKQLIAKKIKLTAEA
HHHHHHHHCCCCCCH
35.7323000965
53AcetylationQLIAKKIKLTAEAEE
HHHHHHCCCCCCHHH
48.9825953088
55UbiquitinationIAKKIKLTAEAEELK
HHHHCCCCCCHHHHH
19.9027667366
62AcetylationTAEAEELKPFFMKEV
CCCHHHHHHHHHHHH
42.9626051181
62UbiquitinationTAEAEELKPFFMKEV
CCCHHHHHHHHHHHH
42.9627667366
67UbiquitinationELKPFFMKEVGSHFD
HHHHHHHHHHHHCHH
44.0529967540
71PhosphorylationFFMKEVGSHFDDFVT
HHHHHHHHCHHHHHH
26.59-
83UbiquitinationFVTNLIEKSASLDNG
HHHHHHHHHCCCCCC
44.3129967540
84PhosphorylationVTNLIEKSASLDNGG
HHHHHHHHCCCCCCC
15.4225159151
86PhosphorylationNLIEKSASLDNGGCA
HHHHHHCCCCCCCEE
43.2625159151
104MalonylationFSVLEGEKNNHRAKD
EEEHHCCCCCCCCCC
74.1126320211
104UbiquitinationFSVLEGEKNNHRAKD
EEEHHCCCCCCCCCC
74.1129967540
104AcetylationFSVLEGEKNNHRAKD
EEEHHCCCCCCCCCC
74.1126051181
120UbiquitinationRAPPEQGKIFIARRS
CCCHHHCCEEEEEHH
33.8521906983
1202-HydroxyisobutyrylationRAPPEQGKIFIARRS
CCCHHHCCEEEEEHH
33.85-
218UbiquitinationSKSSHPLIRSLFHGF
CCCCCHHHHHHHHHH
3.1127667366
225UbiquitinationIRSLFHGFLFMIFQI
HHHHHHHHHHHHHHH
3.4027667366
283UbiquitinationPRVLNSAKEKSSTVP
HHHHHCCCCCCCCCC
66.5527667366
2832-HydroxyisobutyrylationPRVLNSAKEKSSTVP
HHHHHCCCCCCCCCC
66.55-
288UbiquitinationSAKEKSSTVPIPTVN
CCCCCCCCCCCCCHH
37.0722817900
295UbiquitinationTVPIPTVNQYLYFLF
CCCCCCHHHHHHHHH
27.5322817900
353AcetylationAPLFRNIKQEPFSAR
HHHHCCCCCCCCCHH
52.7526051181
353UbiquitinationAPLFRNIKQEPFSAR
HHHHCCCCCCCCCHH
52.7521906983
410PhosphorylationFYKDWWNSTSYSNYY
CCCCCCCCCCCCCHH
12.6624043423
411PhosphorylationYKDWWNSTSYSNYYR
CCCCCCCCCCCCHHH
28.5924043423
412PhosphorylationKDWWNSTSYSNYYRT
CCCCCCCCCCCHHHH
26.7824043423
413PhosphorylationDWWNSTSYSNYYRTW
CCCCCCCCCCHHHHH
10.8724043423
414PhosphorylationWWNSTSYSNYYRTWN
CCCCCCCCCHHHHHH
20.3724043423
416PhosphorylationNSTSYSNYYRTWNVV
CCCCCCCHHHHHHHE
6.5924043423
417PhosphorylationSTSYSNYYRTWNVVV
CCCCCCHHHHHHHEH
13.0524043423
466UbiquitinationVHEYALAVCLSFFYP
HHHHHHHHHHHHHHH
3.3421890473
473UbiquitinationVCLSFFYPVLFVLFM
HHHHHHHHHHHHHHH
15.9221890473
531UbiquitinationARQHCPLKNPTFLDY
HHHCCCCCCCCHHHH
46.1322817900
531UbiquitinationARQHCPLKNPTFLDY
HHHCCCCCCCCHHHH
46.1321890473
531UbiquitinationARQHCPLKNPTFLDY
HHHCCCCCCCCHHHH
46.1321890473
545PhosphorylationYVRPRSWTCRYVF--
HCCCCCCCCEECC--
6.5822210691

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 SOAT1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SOAT1_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 SOAT1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBIA1_HUMANUBIAD1physical
23169578
CARME_HUMANC9orf41physical
28514442
ACAP2_HUMANACAP2physical
27173435
MBOA7_HUMANMBOAT7physical
27173435
EHBP1_HUMANEHBP1physical
27173435
GDIA_HUMANGDI1physical
27173435
STOM_HUMANSTOMphysical
27173435
MKLN1_HUMANMKLN1physical
27173435
DCD_HUMANDCDphysical
29128334
THIO_HUMANTXNphysical
29128334
FLOT2_HUMANFLOT2physical
29128334
ANXA2_HUMANANXA2physical
29128334
THOC4_HUMANALYREFphysical
29128334
CH10_HUMANHSPE1physical
29128334
PPM1B_HUMANPPM1Bphysical
29128334
CHM4B_HUMANCHMP4Bphysical
29128334
DESP_HUMANDSPphysical
29128334
ADT1_HUMANSLC25A4physical
29128334
PROF1_HUMANPFN1physical
29128334
DSG1_HUMANDSG1physical
29128334
ADT2_HUMANSLC25A5physical
29128334
VDAC1_HUMANVDAC1physical
29128334
VDAC2_HUMANVDAC2physical
29128334
ARF1_HUMANARF1physical
29128334
PPIA_HUMANPPIAphysical
29128334
BAF_HUMANBANF1physical
29128334
RL27_HUMANRPL27physical
29128334
H1X_HUMANH1FXphysical
29128334
TPIS_HUMANTPI1physical
29128334
EMD_HUMANEMDphysical
29128334
SCYL2_HUMANSCYL2physical
29128334
ILF2_HUMANILF2physical
29128334
GFAP_HUMANGFAPphysical
29128334
PAIRB_HUMANSERBP1physical
29128334
CX7A2_HUMANCOX7A2physical
29128334
MDHM_HUMANMDH2physical
29128334
TOM22_HUMANTOMM22physical
29128334
MOB2_HUMANMOB2physical
29128334
CHTOP_HUMANCHTOPphysical
29128334
MPCP_HUMANSLC25A3physical
29128334
ATD3A_HUMANATAD3Aphysical
29128334
1433Z_HUMANYWHAZphysical
29128334
VDAC3_HUMANVDAC3physical
29128334
ODPB_HUMANPDHBphysical
29128334
PRDX3_HUMANPRDX3physical
29128334
PLAK_HUMANJUPphysical
29128334
STML2_HUMANSTOML2physical
29128334
PPM1A_HUMANPPM1Aphysical
29128334
COX2_HUMANCOX2physical
29128334
FBRL_HUMANFBLphysical
29128334
IF5A1_HUMANEIF5Aphysical
29128334
HORN_HUMANHRNRphysical
29128334
TPM1_HUMANTPM1physical
29128334
1433E_HUMANYWHAEphysical
29128334
1433B_HUMANYWHABphysical
29128334
RM12_HUMANMRPL12physical
29128334
COX41_HUMANCOX4I1physical
29128334
TRAP1_HUMANTRAP1physical
29128334
RL28_HUMANRPL28physical
29128334
LDHB_HUMANLDHBphysical
29128334
ATPG_HUMANATP5C1physical
29128334
QCR2_HUMANUQCRC2physical
29128334
NDUA5_HUMANNDUFA5physical
29128334
FILA2_HUMANFLG2physical
29128334
CALX_HUMANCANXphysical
29128334
PRDX6_HUMANPRDX6physical
29128334
ATPK_HUMANATP5J2physical
29128334
PAL4A_HUMANPPIAL4Bphysical
29128334
ADT3_HUMANSLC25A6physical
29128334
LDHA_HUMANLDHAphysical
29128334
BASI_HUMANBSGphysical
29128334
SFXN1_HUMANSFXN1physical
29128334
RMXL2_HUMANRBMXL2physical
29128334
NDUS3_HUMANNDUFS3physical
29128334
SET_HUMANSETphysical
29128334
GLYM_HUMANSHMT2physical
29128334
PI51C_HUMANPIP5K1Cphysical
29128334
ERLN2_HUMANERLIN2physical
29128334
NDKA_HUMANNME1physical
29128334
SYIC_HUMANIARSphysical
29128334
NDUAA_HUMANNDUFA10physical
29128334
ALDOA_HUMANALDOAphysical
29128334
MOT1_HUMANSLC16A1physical
29128334
SYEP_HUMANEPRSphysical
29128334
1433T_HUMANYWHAQphysical
29128334
KCRB_HUMANCKBphysical
29128334
P5CR1_HUMANPYCR1physical
29128334
DKC1_HUMANDKC1physical
29128334
MRP_HUMANMARCKSL1physical
29128334
MCA3_HUMANEEF1E1physical
29128334
ETFA_HUMANETFAphysical
29128334
ENPL_HUMANHSP90B1physical
29128334
NP1L1_HUMANNAP1L1physical
29128334
CMC2_HUMANSLC25A13physical
29128334
RANG_HUMANRANBP1physical
29128334
4F2_HUMANSLC3A2physical
29128334
QCR1_HUMANUQCRC1physical
29128334
EF1G_HUMANEEF1Gphysical
29128334
OAT_HUMANOATphysical
29128334
DLDH_HUMANDLDphysical
29128334
AIFM1_HUMANAIFM1physical
29128334
EF2_HUMANEEF2physical
29128334
TKT_HUMANTKTphysical
29128334
SYRC_HUMANRARSphysical
29128334
NDUS1_HUMANNDUFS1physical
29128334
ATD3B_HUMANATAD3Bphysical
29128334
IDHP_HUMANIDH2physical
29128334
TECR_HUMANTECRphysical
29128334
RTCB_HUMANRTCBphysical
29128334
PDC6I_HUMANPDCD6IPphysical
29128334
MYH11_HUMANMYH11physical
29128334
RPN2_HUMANRPN2physical
29128334
GANAB_HUMANGANABphysical
29128334
PDIA3_HUMANPDIA3physical
29128334
IMB1_HUMANKPNB1physical
29128334
PUR2_HUMANGARTphysical
29128334
BOLA2_HUMANBOLA2physical
29128334

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
D03012 Avasimibe (USAN/INN)
D03734 Eldacimibe (USAN/INN)
D03735 Lecimibide (USAN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SOAT1_HUMAN

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Related Literatures of Post-Translational Modification

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