APOA1_HUMAN - dbPTM
APOA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID APOA1_HUMAN
UniProt AC P02647
Protein Name Apolipoprotein A-I
Gene Name APOA1
Organism Homo sapiens (Human).
Sequence Length 267
Subcellular Localization Secreted.
Protein Description Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility..
Protein Sequence MKAAVLTLAVLFLTGSQARHFWQQDEPPQSPWDRVKDLATVYVDVLKDSGRDYVSQFEGSALGKQLNLKLLDNWDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ
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
36GlycationQSPWDRVKDLATVYV
CCCCHHHHHHHHHHH
48.17-
40O-linked_GlycosylationDRVKDLATVYVDVLK
HHHHHHHHHHHHHHH
21.48OGP
42NitrationVKDLATVYVDVLKDS
HHHHHHHHHHHHHHC
6.13-
47GlycationTVYVDVLKDSGRDYV
HHHHHHHHHCCCCHH
50.09-
53PhosphorylationLKDSGRDYVSQFEGS
HHHCCCCHHHHHCCC
10.7123911959
53NitrationLKDSGRDYVSQFEGS
HHHCCCCHHHHHCCC
10.71-
55PhosphorylationDSGRDYVSQFEGSAL
HCCCCHHHHHCCCHH
23.9527130503
60PhosphorylationYVSQFEGSALGKQLN
HHHHHCCCHHHHHHC
17.0823911959
76O-linked_GlycosylationKLLDNWDSVTSTFSK
HHHCCCHHHHHHHHH
20.93OGP
78O-linked_GlycosylationLDNWDSVTSTFSKLR
HCCCHHHHHHHHHHH
26.46OGP
78PhosphorylationLDNWDSVTSTFSKLR
HCCCHHHHHHHHHHH
26.4627251275
79PhosphorylationDNWDSVTSTFSKLRE
CCCHHHHHHHHHHHH
25.8727251275
80PhosphorylationNWDSVTSTFSKLREQ
CCHHHHHHHHHHHHH
23.6727251275
82PhosphorylationDSVTSTFSKLREQLG
HHHHHHHHHHHHHHC
30.7627251275
110OxidationTEGLRQEMSKDLEEV
HHHHHHHHHHCHHHH
4.5812576517
110Methionine sulfoxideTEGLRQEMSKDLEEV
HHHHHHHHHHCHHHH
4.58-
112SulfoxidationGLRQEMSKDLEEVKA
HHHHHHHHCHHHHHH
66.0920133843
118AcetylationSKDLEEVKAKVQPYL
HHCHHHHHHHHHHHH
45.8527178108
120GlycationDLEEVKAKVQPYLDD
CHHHHHHHHHHHHHH
35.37-
124NitrationVKAKVQPYLDDFQKK
HHHHHHHHHHHHHHH
12.98-
130GlycationPYLDDFQKKWQEEME
HHHHHHHHHHHHHHH
56.84-
130AcetylationPYLDDFQKKWQEEME
HHHHHHHHHHHHHHH
56.8427178108
131GlycationYLDDFQKKWQEEMEL
HHHHHHHHHHHHHHH
43.24-
131AcetylationYLDDFQKKWQEEMEL
HHHHHHHHHHHHHHH
43.2427178108
136OxidationQKKWQEEMELYRQKV
HHHHHHHHHHHHHHH
4.1812576517
136Methionine sulfoxideQKKWQEEMELYRQKV
HHHHHHHHHHHHHHH
4.18-
139NitrationWQEEMELYRQKVEPL
HHHHHHHHHHHHHHH
9.55-
142UbiquitinationEMELYRQKVEPLRAE
HHHHHHHHHHHHHHH
39.30-
148SulfoxidationQKVEPLRAELQEGAR
HHHHHHHHHHHHHHH
29.5420133843
157GlycationLQEGARQKLHELQEK
HHHHHHHHHHHHHHH
46.38-
164GlycationKLHELQEKLSPLGEE
HHHHHHHHHCHHCHH
41.10-
164AcetylationKLHELQEKLSPLGEE
HHHHHHHHHCHHCHH
41.1027178108
166PhosphorylationHELQEKLSPLGEEMR
HHHHHHHCHHCHHHH
29.1919945452
185PhosphorylationAHVDALRTHLAPYSD
HHHHHHHHHCCCCCH
23.3019945452
190PhosphorylationLRTHLAPYSDELRQR
HHHHCCCCCHHHHHH
24.1323911959
190NitrationLRTHLAPYSDELRQR
HHHHCCCCCHHHHHH
24.13-
191PhosphorylationRTHLAPYSDELRQRL
HHHCCCCCHHHHHHH
24.4527130503
206GlycationAARLEALKENGGARL
HHHHHHHHHCCCHHH
57.06-
216PhosphorylationGGARLAEYHAKATEH
CCHHHHHHHHHHHHH
11.06-
216NitrationGGARLAEYHAKATEH
CCHHHHHHHHHHHHH
11.06-
219AcetylationRLAEYHAKATEHLST
HHHHHHHHHHHHHHH
42.397683359
219GlycationRLAEYHAKATEHLST
HHHHHHHHHHHHHHH
42.39-
221PhosphorylationAEYHAKATEHLSTLS
HHHHHHHHHHHHHHH
24.1919945452
221O-linked_GlycosylationAEYHAKATEHLSTLS
HHHHHHHHHHHHHHH
24.1923109999
225O-linked_GlycosylationAKATEHLSTLSEKAK
HHHHHHHHHHHHHHH
29.25OGP
225PhosphorylationAKATEHLSTLSEKAK
HHHHHHHHHHHHHHH
29.2527130503
226O-linked_GlycosylationKATEHLSTLSEKAKP
HHHHHHHHHHHHHHH
40.43OGP
226PhosphorylationKATEHLSTLSEKAKP
HHHHHHHHHHHHHHH
40.4327130503
228PhosphorylationTEHLSTLSEKAKPAL
HHHHHHHHHHHHHHH
36.8228857561
228O-linked_GlycosylationTEHLSTLSEKAKPAL
HHHHHHHHHHHHHHH
36.8255828079
232AcetylationSTLSEKAKPALEDLR
HHHHHHHHHHHHHHH
41.7227452117
252PhosphorylationVLESFKVSFLSALEE
HHHHHHHHHHHHHHH
22.5119945452
255PhosphorylationSFKVSFLSALEEYTK
HHHHHHHHHHHHHHH
28.8830087585
260NitrationFLSALEEYTKKLNTQ
HHHHHHHHHHHHCCC
17.93-
261O-linked_GlycosylationLSALEEYTKKLNTQ-
HHHHHHHHHHHCCC-
25.61OGP
262AcetylationSALEEYTKKLNTQ--
HHHHHHHHHHCCC--
55.1230586961
263N-linked_GlycosylationALEEYTKKLNTQ---
HHHHHHHHHCCC---
38.898261628
263GlycationALEEYTKKLNTQ---
HHHHHHHHHCCC---
38.89-

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 APOA1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of APOA1_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 APOA1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PDE1A_HUMANPDE1Aphysical
11991719
PLTP_HUMANPLTPphysical
9469594
ABCA1_HUMANABCA1physical
12084722
APOA1_HUMANAPOA1physical
9356442
LCAT_HUMANLCATphysical
1644835
APOC1_HUMANAPOC1physical
11991719
SAA2_HUMANSAA2physical
11991719
LCAT_HUMANLCATphysical
1587806
APOB_HUMANAPOBphysical
19164805
TERA_HUMANVCPphysical
19164805
A4_HUMANAPPphysical
21832049
ABCA6_HUMANABCA6physical
15174051
ASM3A_HUMANSMPDL3Aphysical
15174051
APOA1_HUMANAPOA1physical
15174051
APOC1_HUMANAPOC1physical
15174051
APOC3_HUMANAPOC3physical
15174051
SETX_HUMANSETXphysical
15174051
PDE4B_HUMANPDE4Bphysical
15174051
CATL1_HUMANCTSLphysical
15174051
CERU_HUMANCPphysical
15174051
CNMD_HUMANLECT1physical
15174051
CLUS_HUMANCLUphysical
15174051
C1QA_HUMANC1QAphysical
15174051
C1QC_HUMANC1QCphysical
15174051
DHPR_HUMANQDPRphysical
15174051
FA83C_HUMANFAM83Cphysical
15174051
TDT_HUMANDNTTphysical
15174051
FIBA_HUMANFGAphysical
15174051
FINC_HUMANFN1physical
15174051
HBA_HUMANHBA1physical
15174051
SRTD3_HUMANSERTAD3physical
15174051
SPEF2_HUMANSPEF2physical
15174051
ROBO3_HUMANROBO3physical
15174051
TENS3_HUMANTNS3physical
15174051
SAFB2_HUMANSAFB2physical
15174051
RRP1B_HUMANRRP1Bphysical
15174051
F169A_HUMANFAM169Aphysical
15174051
K1C16_HUMANKRT16physical
15174051
K1C9_HUMANKRT9physical
15174051
K2C1_HUMANKRT1physical
15174051
K0754_HUMANKIAA0754physical
15174051
NLRP1_HUMANNLRP1physical
15174051
PTN5_HUMANPTPN5physical
15174051
MOCOS_HUMANMOCOSphysical
15174051
TXND2_HUMANTXNDC2physical
15174051
TTHY_HUMANTTRphysical
15174051
APOA1_HUMANAPOA1physical
11744719
APOA2_HUMANAPOA2physical
10722751
LCAT_HUMANLCATphysical
3104518
DGAT1_HUMANDGAT1physical
3104518
APOA2_HUMANAPOA2physical
3104518
APOD_HUMANAPODphysical
3104518
APOB_MOUSEApobphysical
16204232
OSTP_HUMANSPP1physical
21988832
RPA12_HUMANZNRD1physical
21988832
FBLN1_HUMANFBLN1physical
21988832
JAK3_HUMANJAK3physical
21988832
CKLF5_HUMANCMTM5physical
25416956
FIBA_HUMANFGAphysical
25241761
APOA1_HUMANAPOA1physical
8810909
TMM43_HUMANTMEM43physical
28514442
ABCA1_HUMANABCA1physical
27017521
APOB_HUMANAPOBphysical
28183703

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
604091High density lipoprotein deficiency 2 (HDLD2)
205400High density lipoprotein deficiency 1 (HDLD1)
3142462 and PubMedNote=APOA1 mutations may be involved in the pathogenesis of amyloid polyneuropathy-nephropathy Iowa type, also known as amyloidosis van Allen type or familial amyloid polyneuropathy type III (PubMed
105200
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of APOA1_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"The preferential site of non-enzymatic glycation of humanapolipoprotein A-I in vivo.";
Calvo C., Ulloa N., Campos M., Verdugo C., Ayrault-Jarrier M.;
Clin. Chim. Acta 217:193-198(1993).
Cited for: GLYCATION AT LYS-263.
Phosphorylation
ReferencePubMed
"An initial characterization of the serum phosphoproteome.";
Zhou W., Ross M.M., Tessitore A., Ornstein D., Vanmeter A.,Liotta L.A., Petricoin E.F. III;
J. Proteome Res. 8:5523-5531(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191, TISSUE SPECIFICITY,AND MASS SPECTROMETRY.

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