ABCA1_HUMAN - dbPTM
ABCA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ABCA1_HUMAN
UniProt AC O95477
Protein Name ATP-binding cassette sub-family A member 1
Gene Name ABCA1
Organism Homo sapiens (Human).
Sequence Length 2261
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description cAMP-dependent and sulfonylurea-sensitive anion transporter. Key gatekeeper influencing intracellular cholesterol transport..
Protein Sequence MACWPQLRLLLWKNLTFRRRQTCQLLLEVAWPLFIFLILISVRLSYPPYEQHECHFPNKAMPSAGTLPWVQGIICNANNPCFRYPTPGEAPGVVGNFNKSIVARLFSDARRLLLYSQKDTSMKDMRKVLRTLQQIKKSSSNLKLQDFLVDNETFSGFLYHNLSLPKSTVDKMLRADVILHKVFLQGYQLHLTSLCNGSKSEEMIQLGDQEVSELCGLPREKLAAAERVLRSNMDILKPILRTLNSTSPFPSKELAEATKTLLHSLGTLAQELFSMRSWSDMRQEVMFLTNVNSSSSSTQIYQAVSRIVCGHPEGGGLKIKSLNWYEDNNYKALFGGNGTEEDAETFYDNSTTPYCNDLMKNLESSPLSRIIWKALKPLLVGKILYTPDTPATRQVMAEVNKTFQELAVFHDLEGMWEELSPKIWTFMENSQEMDLVRMLLDSRDNDHFWEQQLDGLDWTAQDIVAFLAKHPEDVQSSNGSVYTWREAFNETNQAIRTISRFMECVNLNKLEPIATEVWLINKSMELLDERKFWAGIVFTGITPGSIELPHHVKYKIRMDIDNVERTNKIKDGYWDPGPRADPFEDMRYVWGGFAYLQDVVEQAIIRVLTGTEKKTGVYMQQMPYPCYVDDIFLRVMSRSMPLFMTLAWIYSVAVIIKGIVYEKEARLKETMRIMGLDNSILWFSWFISSLIPLLVSAGLLVVILKLGNLLPYSDPSVVFVFLSVFAVVTILQCFLISTLFSRANLAAACGGIIYFTLYLPYVLCVAWQDYVGFTLKIFASLLSPVAFGFGCEYFALFEEQGIGVQWDNLFESPVEEDGFNLTTSVSMMLFDTFLYGVMTWYIEAVFPGQYGIPRPWYFPCTKSYWFGEESDEKSHPGSNQKRISEICMEEEPTHLKLGVSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSSLFLKNQLGTGYYLTLVKKDVESSLSSCRNSSSTVSYLKKEDSVSQSSSDAGLGSDHESDTLTIDVSAISNLIRKHVSEARLVEDIGHELTYVLPYEAAKEGAFVELFHEIDDRLSDLGISSYGISETTLEEIFLKVAEESGVDAETSDGTLPARRNRRAFGDKQSCLRPFTEDDAADPNDSDIDPESRETDLLSGMDGKGSYQVKGWKLTQQQFVALLWKRLLIARRSRKGFFAQIVLPAVFVCIALVFSLIVPPFGKYPSLELQPWMYNEQYTFVSNDAPEDTGTLELLNALTKDPGFGTRCMEGNPIPDTPCQAGEEEWTTAPVPQTIMDLFQNGNWTMQNPSPACQCSSDKIKKMLPVCPPGAGGLPPPQRKQNTADILQDLTGRNISDYLVKTYVQIIAKSLKNKIWVNEFRYGGFSLGVSNTQALPPSQEVNDAIKQMKKHLKLAKDSSADRFLNSLGRFMTGLDTKNNVKVWFNNKGWHAISSFLNVINNAILRANLQKGENPSHYGITAFNHPLNLTKQQLSEVALMTTSVDVLVSICVIFAMSFVPASFVVFLIQERVSKAKHLQFISGVKPVIYWLSNFVWDMCNYVVPATLVIIIFICFQQKSYVSSTNLPVLALLLLLYGWSITPLMYPASFVFKIPSTAYVVLTSVNLFIGINGSVATFVLELFTDNKLNNINDILKSVFLIFPHFCLGRGLIDMVKNQAMADALERFGENRFVSPLSWDLVGRNLFAMAVEGVVFFLITVLIQYRFFIRPRPVNAKLSPLNDEDEDVRRERQRILDGGGQNDILEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNIHEVHQNMGYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNRFGDGYTIVVRIAGSNPDLKPVQDFFGLAFPGSVLKEKHRNMLQYQLPSSLSSLARIFSILSQSKKRLHIEDYSVSQTTLDQVFVNFAKDQSDDDHLKDLSLHKNQTVVDVAVLTSFLQDEKVKESYV
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
3S-palmitoyl cysteine-----MACWPQLRLL
-----CCHHHHHHHH
9.1919556522
23S-palmitoyl cysteineTFRRRQTCQLLLEVA
HHHCCCCHHHHHHHH
1.7119556522
98N-linked (GlcNAc)PGVVGNFNKSIVARL
CCCHHHHHHHHHHHC
40.9619159218
116PhosphoserineARRLLLYSQKDTSMK
HHHHHCCCCCHHHHH
30.62113303705
231PhosphoserineAAERVLRSNMDILKP
HHHHHHHHHCCHHHH
32.14108417611
244N-linked (GlcNAc)KPILRTLNSTSPFPS
HHHHHHHHCCCCHHH
42.5019159218
325PhosphotyrosineKIKSLNWYEDNNYKA
CCCCCCCCCCCCCCC
16.6059303065
884PhosphoserineGSNQKRISEICMEEE
CCCCCCCHHHHCCCC
25.5854885547
1031PhosphoserineSKLKSKTSQLSGGMQ
HHHCCCHHHCCCHHH
32.6268852465
1042PhosphoserineGGMQRKLSVALAFVG
CHHHHHHHHHHHHHC
14.3712196520
1110S-palmitoyl cysteineIISHGKLCCVGSSLF
EEECCEEEEECCHHH
1.6919556522
1111S-palmitoyl cysteineISHGKLCCVGSSLFL
EECCEEEEECCHHHH
5.8719556522
1145PhosphoserineSLSSCRNSSSTVSYL
HHHHHCCCCCCCCCE
13.309413855
1206PhosphotyrosineDIGHELTYVLPYEAA
ECCCEEEEEEECCCH
16.777436673
1242PhosphothreonineSSYGISETTLEEIFL
EEEECCCCCHHHHHH
29.8615218032
1243PhosphothreonineSYGISETTLEEIFLK
EEECCCCCHHHHHHH
28.2815218032
1255PhosphoserineFLKVAEESGVDAETS
HHHHHHHHCCCHHHH
35.3015218032
1262PhosphoserineSGVDAETSDGTLPAR
HCCCHHHHHCCHHHH
26.0868998007
1286PhosphothreonineQSCLRPFTEDDAADP
HHHHCCCCCCCCCCC
40.9812869555
1296PhosphoserineDAADPNDSDIDPESR
CCCCCCCCCCCCCCC
43.0193795
1305PhosphothreonineIDPESRETDLLSGMD
CCCCCCCCCCCCCCC
30.7312869555
1536PhosphoserineEFRYGGFSLGVSNTQ
CCCCCEEECCCCCCC
27.7322159673
1540PhosphoserineGGFSLGVSNTQALPP
CEEECCCCCCCCCCC
32.1522159681
1548PhosphoserineNTQALPPSQEVNDAI
CCCCCCCCHHHCCCH
36.71108935907
1582PhosphothreonineNSLGRFMTGLDTKNN
HHHHHHHHHCCHHHH
31.70113136027
1586PhosphothreonineRFMTGLDTKNNVKVW
HHHHHCCHHHHHEEE
40.49113136035
2050 N-acetyllysineGNYSGGNKRKLSTAM
HHCCCHHHHHHHHHH
54.9419826679
2054PhosphoserineGGNKRKLSTAMALIG
CHHHHHHHHHHHHHC
19.7012196520
2101PhosphoserineGRSVVLTSHSMEECE
CCEEEEEECCHHHHH
14.9246156249
2234PhosphoserineDDHLKDLSLHKNQTV
CHHHHHHHHHHHHCC
38.2635101185

Disease-associated PTM Sites based on nsSNP

* Distance = the distance between SNP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SNP Related Disease Reference
231Phosphorylation230 (1)RCrs9282541HDL cholesterol: high density lipoprotein cholesterol measurement23505323
244N-linked Glycosylation248 (4)PArs142625938--
884Phosphorylation883 (1)IMrs2066714--
1042Phosphorylation1046 (4)ADrs141021096--
1206Phosphorylation1216 (10)GVrs562403512--
1286Phosphorylation1289 (3)DNrs137854500--
1296Phosphorylation1289 (7)DNrs137854500--
1548Phosphorylation1555 (7)ITrs1997618--
1582Phosphorylation1587 (5)KRrs2230808--
1586Phosphorylation1587 (1)KRrs2230808--
2234Phosphorylation2244 (10)VIrs144588452--
2234Phosphorylation2243 (9)DErs34879708--

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FADD_HUMANFADDphysical
12235128
APOA1_HUMANAPOA1physical
12084722
SNTB2_HUMANSNTB2physical
12054535
UGPA_HUMANUGP2physical
12054535
SDHB_HUMANSDHBphysical
12054535
AOXA_HUMANAOX1physical
12054535
PRP8_HUMANPRPF8physical
12054535
HGS_HUMANHGSphysical
21520210
CSN5_HUMANCOPS5physical
19268428
STX12_HUMANSTX12physical
15469992
FLOT1_HUMANFLOT1physical
15469992
CDC42_HUMANCDC42physical
16443932
SPTC1_HUMANSPTLC1physical
18484747
TGM2_HUMANTGM2physical
21988832
NEMO_HUMANIKBKGphysical
21988832
NR1H2_HUMANNR1H2physical
20951680
NR1H2_HUMANNR1H2physical
25838426
APOA1_HUMANAPOA1physical
27017521
CSN2_HUMANCOPS2physical
27017521

Drug and Disease Associations
Kegg Disease
H00159 Tangier disease
H00930 Hypoalphalipoproteinemia
OMIM Disease
205400High density lipoprotein deficiency 1 (HDLD1)
604091High density lipoprotein deficiency 2 (HDLD2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-98 AND ASN-244, AND MASSSPECTROMETRY.
Palmitoylation
ReferencePubMed
"Palmitoylation of ATP-binding cassette transporter A1 is essentialfor its trafficking and function.";
Singaraja R.R., Kang M.H., Vaid K., Sanders S.S., Vilas G.L.,Arstikaitis P., Coutinho J., Drisdel R.C., El-Husseini Ael D.,Green W.N., Berthiaume L., Hayden M.R.;
Circ. Res. 105:138-147(2009).
Cited for: PALMITOYLATION AT CYS-3; CYS-23; CYS-1110 AND CYS-1111, ANDSUBCELLULAR LOCATION.
Phosphorylation
ReferencePubMed
"Protein kinase A site-specific phosphorylation regulates ATP-bindingcassette A1 (ABCA1)-mediated phospholipid efflux.";
See R.H., Caday-Malcolm R.A., Singaraja R.R., Zhou S., Silverston A.,Huber M.T., Moran J., James E.R., Janoo R., Savill J.M., Rigot V.,Zhang L.H., Wang M., Chimini G., Wellington C.L., Tafuri S.R.,Hayden M.R.;
J. Biol. Chem. 277:41835-41842(2002).
Cited for: PHOSPHORYLATION AT SER-1042 AND SER-2054.

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