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P02647 (APOA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 194. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Apolipoprotein A-I

Short name=Apo-AI
Short name=ApoA-I
Alternative name(s):
Apolipoprotein A1

Cleaved into the following 2 chains:

  1. Proapolipoprotein A-I
    Short name=ProapoA-I
  2. Truncated apolipoprotein A-I
    Alternative name(s):
    Apolipoprotein A-I(1-242)
Gene names
Name:APOA1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length267 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.20

Subunit structure

Interacts with APOA1BP and CLU. Component of a sperm activating protein complex (SPAP), consisting of APOA1, an immunoglobulin heavy chain, an immunoglobulin light chain and albumin. Interacts with NDRG1. Ref.20 Ref.25 Ref.31 Ref.34

Subcellular location

Secreted.

Tissue specificity

Major protein of plasma HDL, also found in chylomicrons. Synthesized in the liver and small intestine. The oxidized form at Met-110 and Met-136 is increased in individuals with increased risk for coronary artery disease, such as in carrier of the eNOSa/b genotype and exposure to cigarette smoking. It is also present in increased levels in aortic lesions relative to native ApoA-I and increased levels are seen with increasing severity of disease. Ref.32

Post-translational modification

Glycosylated By similarity.

Palmitoylated. Ref.28

Phosphorylation sites are present in the extracellular medium.

Polymorphism

Genetic variations in APOA1 can result in APOA1 deficiency and are associated with low levels of HDL cholesterol [MIM:107680].

Involvement in disease

High density lipoprotein deficiency 2 (HDLD2) [MIM:604091]: Inherited as autosomal dominant trait. It is characterized by moderately low HDL cholesterol, predilection toward premature coronary artery disease (CAD) and a reduction in cellular cholesterol efflux.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.38 Ref.39

High density lipoprotein deficiency 1 (HDLD1) [MIM:205400]: Recessive disorder characterized by absence of high density lipoprotein (HDL) cholesterol from plasma, accumulation of cholesteryl esters, premature coronary artery disease (CAD), hepatosplenomegaly, recurrent peripheral neuropathy and progressive muscle wasting and weakness.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.38 Ref.39

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 (Ref.44 and Ref.45). The clinical picture is dominated by neuropathy in the early stages of the disease and nephropathy late in the course. Death is due in most cases to renal amyloidosis. Ref.38 Ref.39

Amyloidosis 8 (AMYL8) [MIM:105200]: A hereditary generalized amyloidosis due to deposition of apolipoprotein A1, fibrinogen and lysozyme amyloids. Viscera are particularly affected. There is no involvement of the nervous system. Clinical features include renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.38 Ref.39 Ref.44 Ref.45 Ref.47 Ref.52

Sequence similarities

Belongs to the apolipoprotein A1/A4/E family.

Mass spectrometry

Molecular mass is 28081 Da from positions 25 - 267. Determined by ESI. Without methionine sulfoxide. Ref.32

Molecular mass is 28098 Da from positions 25 - 267. Determined by ESI. With 1 methionine sulfoxide, oxidation at Met-110. Ref.32

Molecular mass is 28095 Da from positions 25 - 267. Determined by ESI. With 1 methionine sulfoxide, oxidation at Met-136. Ref.32

Molecular mass is 28114 Da from positions 25 - 267. Determined by ESI. With 2 methionine sulfoxides, oxidation at Met-110 and Met-136. Ref.32

Ontologies

Keywords
   Biological processCholesterol metabolism
Lipid metabolism
Lipid transport
Steroid metabolism
Sterol metabolism
Transport
   Cellular componentAmyloid
HDL
Secreted
   Coding sequence diversityPolymorphism
   DiseaseAmyloidosis
Atherosclerosis
Disease mutation
Neuropathy
   DomainRepeat
Signal
   PTMGlycation
Glycoprotein
Lipoprotein
Oxidation
Palmitate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Inferred from direct assay PubMed 16443932. Source: BHF-UCL

adrenal gland development

Inferred from electronic annotation. Source: Ensembl

blood coagulation

Traceable author statement. Source: Reactome

blood vessel endothelial cell migration

Inferred from electronic annotation. Source: Ensembl

cellular lipid metabolic process

Traceable author statement. Source: Reactome

cholesterol biosynthetic process

Inferred from electronic annotation. Source: Ensembl

cholesterol efflux

Inferred from direct assay PubMed 11162594PubMed 14703508PubMed 15358760PubMed 16443932. Source: BHF-UCL

cholesterol homeostasis

Inferred from direct assay PubMed 21571275. Source: BHF-UCL

cholesterol import

Inferred from mutant phenotype PubMed 14718538. Source: BHF-UCL

cholesterol metabolic process

Inferred from mutant phenotype PubMed 15464323. Source: BHF-UCL

cholesterol transport

Inferred from direct assay PubMed 10559507. Source: MGI

endothelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

glucocorticoid metabolic process

Inferred from electronic annotation. Source: Ensembl

high-density lipoprotein particle assembly

Inferred from direct assay PubMed 190223. Source: BHF-UCL

high-density lipoprotein particle clearance

Inferred by curator PubMed 12651854. Source: BHF-UCL

high-density lipoprotein particle remodeling

Inferred by curator PubMed 4335615. Source: BHF-UCL

lipid storage

Inferred from electronic annotation. Source: Ensembl

lipoprotein biosynthetic process

Inferred from electronic annotation. Source: Ensembl

lipoprotein metabolic process

Traceable author statement. Source: Reactome

negative regulation of cell adhesion molecule production

Inferred from direct assay PubMed 21571275. Source: BHF-UCL

negative regulation of cytokine secretion involved in immune response

Inferred from direct assay PubMed 12458630. Source: BHF-UCL

negative regulation of heterotypic cell-cell adhesion

Inferred from direct assay PubMed 21571275. Source: BHF-UCL

negative regulation of inflammatory response

Inferred from direct assay PubMed 21571275. Source: BHF-UCL

negative regulation of interleukin-1 beta secretion

Inferred from direct assay PubMed 12458630. Source: BHF-UCL

negative regulation of lipase activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of response to cytokine stimulus

Inferred from direct assay PubMed 21571275. Source: BHF-UCL

negative regulation of tumor necrosis factor-mediated signaling pathway

Inferred from direct assay PubMed 21571275. Source: BHF-UCL

negative regulation of very-low-density lipoprotein particle remodeling

Inferred from direct assay PubMed 14967812. Source: BHF-UCL

organ regeneration

Inferred from electronic annotation. Source: Ensembl

peptidyl-methionine modification

Inferred from direct assay Ref.32. Source: UniProtKB

peripheral nervous system axon regeneration

Inferred from electronic annotation. Source: Ensembl

phosphatidylcholine biosynthetic process

Inferred from direct assay PubMed 4335615. Source: BHF-UCL

phospholipid efflux

Inferred from direct assay PubMed 11162594PubMed 14703508. Source: BHF-UCL

phospholipid homeostasis

Inferred from direct assay PubMed 21571275. Source: BHF-UCL

phototransduction, visible light

Traceable author statement. Source: Reactome

platelet activation

Traceable author statement. Source: Reactome

platelet degranulation

Traceable author statement. Source: Reactome

positive regulation of cholesterol esterification

Inferred from direct assay PubMed 4335615. Source: BHF-UCL

positive regulation of hydrolase activity

Inferred from direct assay PubMed 7638166. Source: BHF-UCL

positive regulation of transferase activity

Inferred from electronic annotation. Source: Ensembl

protein oxidation

Inferred from direct assay Ref.32. Source: UniProtKB

protein stabilization

Inferred from direct assay PubMed 17655203. Source: BHF-UCL

regulation of Cdc42 protein signal transduction

Inferred from direct assay PubMed 16443932. Source: BHF-UCL

regulation of intestinal cholesterol absorption

Inferred from electronic annotation. Source: Ensembl

regulation of protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to estrogen

Inferred from electronic annotation. Source: Ensembl

response to nutrient

Inferred from electronic annotation. Source: Ensembl

retinoid metabolic process

Traceable author statement. Source: Reactome

reverse cholesterol transport

Inferred from mutant phenotype PubMed 15464323. Source: BHF-UCL

small molecule metabolic process

Traceable author statement. Source: Reactome

transmembrane transport

Traceable author statement. Source: Reactome

triglyceride homeostasis

Inferred from direct assay PubMed 21571275. Source: BHF-UCL

   Cellular_componentblood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

cytoplasmic vesicle

Inferred from direct assay PubMed 14703508. Source: BHF-UCL

cytosol

Traceable author statement. Source: Reactome

early endosome

Traceable author statement. Source: Reactome

endocytic vesicle

Inferred from direct assay PubMed 14747463. Source: BHF-UCL

endocytic vesicle lumen

Traceable author statement. Source: Reactome

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 20551380. Source: BHF-UCL

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708PubMed 23376485. Source: UniProt

high-density lipoprotein particle

Inferred from direct assay PubMed 15464323PubMed 210174PubMed 21571275PubMed 3104518. Source: BHF-UCL

nucleus

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement. Source: Reactome

secretory granule lumen

Traceable author statement. Source: Reactome

spherical high-density lipoprotein particle

Inferred from direct assay PubMed 16682745. Source: BHF-UCL

very-low-density lipoprotein particle

Inferred from direct assay PubMed 17154273. Source: BHF-UCL

   Molecular_functionapolipoprotein A-I receptor binding

Inferred from physical interaction PubMed 16443932. Source: BHF-UCL

apolipoprotein receptor binding

Inferred from physical interaction PubMed 11162594. Source: BHF-UCL

beta-amyloid binding

Inferred from direct assay PubMed 11297421. Source: BHF-UCL

cholesterol binding

Inferred from direct assay PubMed 15464323. Source: BHF-UCL

cholesterol transporter activity

Inferred from mutant phenotype PubMed 15464323. Source: BHF-UCL

enzyme binding

Inferred from physical interaction PubMed 1587806. Source: BHF-UCL

high-density lipoprotein particle binding

Inferred from electronic annotation. Source: Ensembl

high-density lipoprotein particle receptor binding

Inferred from physical interaction PubMed 10764676PubMed 12651854. Source: BHF-UCL

identical protein binding

Inferred from physical interaction PubMed 22609356PubMed 24316228. Source: IntAct

lipase inhibitor activity

Inferred from electronic annotation. Source: Ensembl

phosphatidylcholine-sterol O-acyltransferase activator activity

Inferred from direct assay PubMed 4335615. Source: BHF-UCL

phospholipid binding

Inferred from direct assay PubMed 12810715. Source: BHF-UCL

phospholipid transporter activity

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction Ref.31PubMed 17786215. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.5 Ref.16
Chain19 – 267249Proapolipoprotein A-I
PRO_0000425323
Chain25 – 267243Apolipoprotein A-I
PRO_0000001939
Chain25 – 266242Truncated apolipoprotein A-I
PRO_0000001940

Regions

Repeat68 – 89221
Repeat90 – 111222
Repeat112 – 122113; half-length
Repeat123 – 144224
Repeat145 – 166225
Repeat167 – 188226
Repeat189 – 210227
Repeat211 – 232228
Repeat233 – 243119; half-length
Repeat244 – 2672410
Region68 – 26720010 X approximate tandem repeats

Amino acid modifications

Modified residue1101Methionine sulfoxide
Modified residue1361Methionine sulfoxide
Glycosylation2631N-linked (Glc) (glycation) Ref.30

Natural variations

Natural variant271P → H in Munster-3C.
Corresponds to variant rs121912720 [ dbSNP | Ensembl ].
VAR_000605
Natural variant271P → R. Ref.49
Corresponds to variant rs121912720 [ dbSNP | Ensembl ].
VAR_000606
Natural variant281P → R in Munster-3B. Ref.49
VAR_000607
Natural variant341R → L in Baltimore. Ref.48
Corresponds to variant rs28929476 [ dbSNP | Ensembl ].
VAR_000608
Natural variant501G → R in AMYL8; also found in a family with amyloid polyneuropathy-nephropathy Iowa. Ref.44 Ref.45 Ref.52
Corresponds to variant rs28931574 [ dbSNP | Ensembl ].
VAR_000609
Natural variant611A → T. Ref.10
Corresponds to variant rs12718465 [ dbSNP | Ensembl ].
VAR_025445
Natural variant841L → R in AMYL8. Ref.47
VAR_000610
Natural variant921T → I Polymorphism confirmed at protein level. Ref.55 Ref.56
VAR_017017
Natural variant1131D → E. Ref.50
VAR_000611
Natural variant1191A → D in Hita.
VAR_000612
Natural variant1261D → H.
Corresponds to variant rs5077 [ dbSNP | Ensembl ].
VAR_016189
Natural variant1271D → N in Munster-3A.
VAR_000613
Natural variant1311K → M. Ref.50
Corresponds to variant rs4882 [ dbSNP | Ensembl ].
VAR_000615
Natural variant1311Missing in Marburg/Munster-2.
VAR_000614
Natural variant1321W → R in Tsushima.
VAR_000616
Natural variant1341E → K in Fukuoka. Ref.46
VAR_000617
Natural variant1601E → K in Norway. Ref.43
VAR_000618
Natural variant1631E → G. Ref.50
VAR_000619
Natural variant1671P → R in Giessen. Ref.42
VAR_000620
Natural variant1681L → R in Zaragoza. Ref.54
VAR_000621
Natural variant1711E → V. Ref.50
VAR_000622
Natural variant1801V → E in Oita; 60% of normal apoA-I and normal HDL cholesterol levels. Rapidly cleared from plasma. Ref.53
VAR_021362
Natural variant1841R → P.
Corresponds to variant rs5078 [ dbSNP | Ensembl ].
VAR_014609
Natural variant1891P → R. Ref.49
VAR_000623
Natural variant1971R → C in Milano; associated with decreased HDL levels and moderate increases in triglycerides; no evidence of association with premature vascular disease. Ref.40
Corresponds to variant rs28931573 [ dbSNP | Ensembl ].
VAR_000624
Natural variant2221E → K in Munster-4. Ref.50
VAR_000625

Experimental info

Sequence conflict321W → P AA sequence Ref.25

Secondary structure

........................ 267
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02647 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 1A28B8366E620310

FASTA26730,778
        10         20         30         40         50         60 
MKAAVLTLAV LFLTGSQARH FWQQDEPPQS PWDRVKDLAT VYVDVLKDSG RDYVSQFEGS 

        70         80         90        100        110        120 
ALGKQLNLKL LDNWDSVTST FSKLREQLGP VTQEFWDNLE KETEGLRQEM SKDLEEVKAK 

       130        140        150        160        170        180 
VQPYLDDFQK KWQEEMELYR QKVEPLRAEL QEGARQKLHE LQEKLSPLGE EMRDRARAHV 

       190        200        210        220        230        240 
DALRTHLAPY SDELRQRLAA RLEALKENGG ARLAEYHAKA TEHLSTLSEK AKPALEDLRQ 

       250        260 
GLLPVLESFK VSFLSALEEY TKKLNTQ 

« Hide

References

« Hide 'large scale' references
[1]"Gene structure of human apolipoprotein A1."
Shoulders C.C., Kornblihtt A.R., Munro B.S., Baralle F.E.
Nucleic Acids Res. 11:2827-2837(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Nucleotide sequence of cloned cDNA of human apolipoprotein A-I."
Cheung P., Chan L.
Nucleic Acids Res. 11:3703-3715(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Isolation and characterization of the human apolipoprotein A-I gene."
Karathanasis S.K., Zannis V.I., Breslow J.L.
Proc. Natl. Acad. Sci. U.S.A. 80:6147-6151(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Isolation and DNA sequence of full-length cDNA and of the entire gene for human apolipoprotein AI -- discovery of a new genetic polymorphism in the apo AI gene."
Seilhamer J.J., Protter A.A., Frossard P., Levy-Wilson B.
DNA 3:309-317(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Human apolipoproteins AI, AII, CII and CIII. cDNA sequences and mRNA abundance."
Sharpe C.R., Sidoli A., Shelley C.S., Lucero M.A., Shoulders C.C., Baralle F.E.
Nucleic Acids Res. 12:3917-3932(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"Nucleotide sequence and the encoded amino acids of human apolipoprotein A-I mRNA."
Law S.W., Brewer H.B. Jr.
Proc. Natl. Acad. Sci. U.S.A. 81:66-70(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]"Tangier disease. The complete mRNA sequence encoding for preproapo-A-I."
Law S.W., Brewer H.B. Jr.
J. Biol. Chem. 260:12810-12814(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[8]"Sequence and expression of Tangier apoA-I gene."
Makrides S.C., Ruiz-Opazo N., Hayden M.R., Nussbaum A.L., Breslow J.L., Zannis V.I.
Eur. J. Biochem. 173:465-471(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (VARIANT TANGIER).
[9]"Production of human recombinant proapolipoprotein A-I in Escherichia coli: purification and biochemical characterization."
Moguilevsky N., Roobol C., Loriau R., Guillaume J.P., Jacobs P., Cravador A., Herzog A., Brouwers L., Scarso A., Gilles P., Holmquist L., Carlson L.A., Bollen A.
DNA 8:429-436(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[10]"The effects of scale: variation in the APOA1/C3/A4/A5 gene cluster."
Fullerton S.M., Buchanan A.V., Sonpar V.A., Taylor S.L., Smith J.D., Carlson C.S., Salomaa V., Stengaard J.H., Boerwinkle E., Clark A.G., Nickerson D.A., Weiss K.M.
Hum. Genet. 115:36-56(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-61.
[11]"Expression of human proapolipoprotein A-1."
Bollen A., Gobert J., Wuelfert E.
Patent number EP0293357, 30-NOV-1988
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[12]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[13]NHLBI resequencing and genotyping service (RS&G)
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[14]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[15]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain and Skeletal muscle.
[16]"Human plasma proapoA-I: isolation and amino-terminal sequence."
Brewer H.B. Jr., Fairwell T., Kay L., Meng M., Ronan R., Law S., Light J.A.
Biochem. Biophys. Res. Commun. 113:626-632(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-27.
[17]"The primary structure of human plasma high density apolipoprotein glutamine I (ApoA-I). II. The amino acid sequence and alignment of cyanogen bromide fragments IV, III, and I."
Baker H.N., Gotto A.M. Jr., Jackson R.L.
J. Biol. Chem. 250:2725-2738(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-267.
[18]"The amino acid sequence of human APOA-I, an apolipoprotein isolated from high density lipoproteins."
Brewer H.B. Jr., Fairwell T., Larue A., Ronan R., Houser A., Bronzert T.J.
Biochem. Biophys. Res. Commun. 80:623-630(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-267.
[19]"Serum prostacyclin stabilizing factor is identical to apolipoprotein A-I (Apo A-I). A novel function of Apo A-I."
Yui Y., Aoyama T., Morishita H., Takahashi M., Takatsu Y., Kawai C.
J. Clin. Invest. 82:803-807(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-56.
[20]"Identification of apolipoprotein A1 and immunoglobulin as components of a serum complex that mediates activation of human sperm motility."
Aakerloef E., Joernvall H., Slotte H., Pousette A.
Biochemistry 30:8986-8990(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-50, FUNCTION, IDENTIFICATION IN THE SPAP COMPLEX.
Tissue: Serum.
[21]"Apolipoprotein A-I binds to a family of bovine seminal plasma proteins."
Manjunath P., Marcel Y.L., Uma J., Seidah N.G., Chretien M., Chapdelaine A.
J. Biol. Chem. 264:16853-16857(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-48.
[22]"Similarity of cruzin, an inhibitor of Trypanosoma cruzi neuraminidase, to high-density lipoprotein."
Prioli R.P., Ordovas J.M., Rosenberg I., Schaeffer E.J., Pereira M.E.A.
Science 238:1417-1419(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-43.
[23]"The human myocardial two-dimensional gel protein database: update 1994."
Corbett J.M., Wheeler C.H., Baker C.S., Yacoub M.H., Dunn M.J.
Electrophoresis 15:1459-1465(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-42.
Tissue: Heart.
[24]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-34.
Tissue: Platelet.
[25]"The apolipoprotein A-I binding protein of placenta and the SP-40,40 protein of human blood are different proteins which both bind to apolipoprotein A-I."
Ehnholm C., Bozas S.E., Tenkanen H., Kirszbaum L., Metso J., Murphy B., Walker I.D.
Biochim. Biophys. Acta 1086:255-260(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-33, INTERACTION WITH APOA1BP AND CLU.
[26]Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 35-64; 70-101; 121-140; 165-173; 185-195 AND 240-263, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[27]"Isolation and characterization of cDNA clones for human apolipoprotein A-I."
Breslow J.L., Ross D., McPherson J., Williams H.W., Kurnit D., Nussbaum A.L., Karathanasis S.K., Zannis V.I.
Proc. Natl. Acad. Sci. U.S.A. 79:6861-6865(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 118-267.
[28]"Human apolipoprotein A-I. Post-translational modification by fatty acid acylation."
Hoeg J.M., Meng M.S., Ronan R., Fairwell T., Brewer H.B. Jr.
J. Biol. Chem. 261:3911-3914(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION.
[29]"Intracellular and extracellular processing of human apolipoprotein A-I: secreted apolipoprotein A-I isoprotein 2 is a propeptide."
Zannis V.I., Karathanasis S.K., Keutmann H.T., Goldberger G., Breslow J.L.
Proc. Natl. Acad. Sci. U.S.A. 80:2574-2578(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING.
[30]"The preferential site of non-enzymatic glycation of human apolipoprotein A-I in vivo."
Calvo C., Ulloa N., Campos M., Verdugo C., Ayrault-Jarrier M.
Clin. Chim. Acta 217:193-198(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCATION AT LYS-263.
[31]"Cloning and characterization of a novel apolipoprotein A-I-binding protein, AI-BP, secreted by cells of the kidney proximal tubules in response to HDL or ApoA-I."
Ritter M., Buechler C., Boettcher A., Barlage S., Schmitz-Madry A., Orso E., Bared S.M., Schmiedeknecht G., Baehr C.H., Fricker G., Schmitz G.
Genomics 79:693-702(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH APOA1BP.
[32]"Characterization of specifically oxidized apolipoproteins in mildly oxidized high density lipoprotein."
Pankhurst G., Wang X.L., Wilcken D.E., Baernthaler G., Panzenboeck U., Raftery M., Stocker R.
J. Lipid Res. 44:349-355(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: MASS SPECTROMETRY, OXIDATION AT MET-110 AND MET-136 TO METHIONINE SULFOXIDES, TISSUE SPECIFICITY.
[33]"Novel mass spectrometric immunoassays for the rapid structural characterization of plasma apolipoproteins."
Niederkofler E.E., Tubbs K.A., Kiernan U.A., Nedelkov D., Nelson R.W.
J. Lipid Res. 44:630-639(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
[34]"NDRG1 interacts with APO A-I and A-II and is a functional candidate for the HDL-C QTL on 8q24."
Hunter M., Angelicheva D., Tournev I., Ingley E., Chan D.C., Watts G.F., Kremensky I., Kalaydjieva L.
Biochem. Biophys. Res. Commun. 332:982-992(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NDRG1.
[35]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[36]"Conformation of human serum apolipoprotein A-I(166-185) in the presence of sodium dodecyl sulfate or dodecylphosphocholine by 1H-NMR and CD. Evidence for specific peptide-SDS interactions."
Wang G., Treleaven W.D., Cushley R.J.
Biochim. Biophys. Acta 1301:174-184(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 190-209.
[37]"Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation."
Borhani D.W., Rogers D.P., Engler J.A., Brouillette C.G.
Proc. Natl. Acad. Sci. U.S.A. 94:12291-12296(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 67-267.
[38]"Autosomal dominant hypoalphalipoproteinemia due to a completely defective apolipoprotein A-I gene."
Nakata K., Kobayashi K., Yanagi H., Shimakura Y., Tsuchiya S., Arinami T., Hamaguchi H.
Biochem. Biophys. Res. Commun. 196:950-955(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: DISEASE.
[39]"Apolipoprotein A-I Q[-2]X causing isolated apolipoprotein A-I deficiency in a family with analphalipoproteinemia."
Ng D.S., Leiter L.A., Vezina C., Connelly P.W., Hegele R.A.
J. Clin. Invest. 93:223-229(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: DISEASE.
[40]"Apolipoprotein A-IMilano. Detection of normal A-I in affected subjects and evidence for a cysteine for arginine substitution in the variant A-I."
Weisgraber K.H., Rall S.C. Jr., Bersot T.P., Mahley R.W., Franceschini G., Sirtori C.R.
J. Biol. Chem. 258:2508-2513(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MILANO CYS-197.
[41]"Tangier disease: defective recombination of a specific Tangier apolipoprotein A-I isoform (pro-apo A-I) with high density lipoproteins."
Schmitz G., Assmann G., Rall S.C. Jr., Mahley R.W.
Proc. Natl. Acad. Sci. U.S.A. 80:6081-6085(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT TANGIER.
[42]"Apolipoprotein A-IGiessen (Pro143-->Arg). A mutant that is defective in activating lecithin:cholesterol acyltransferase."
Utermann G., Haas J., Steinmetz A., Paetzold R., Rall S.C. Jr., Weisgraber K.H., Mahley R.W.
Eur. J. Biochem. 144:325-331(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GIESSEN ARG-167.
[43]"Abnormal lecithin:cholesterol acyltransferase activation by a human apolipoprotein A-I variant in which a single lysine residue is deleted."
Rall S.C. Jr., Weisgraber K.H., Mahley R.W., Ogawa Y., Fielding C.J., Utermann G., Haas J., Steinmetz A., Menzel H.J., Assmann G.
J. Biol. Chem. 259:10063-10070(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT NORWAY LYS-160.
[44]"Variant apolipoprotein AI as a major constituent of a human hereditary amyloid."
Nichols W.C., Dwulet F.E., Liepnieks J., Benson M.D.
Biochem. Biophys. Res. Commun. 156:762-768(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-107, VARIANT AMYL8 ARG-50.
[45]"A mutation in apolipoprotein A-I in the Iowa type of familial amyloidotic polyneuropathy."
Nichols W.C., Gregg R.E., Brewer H.B. Jr., Benson M.D.
Genomics 8:318-323(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL8 ARG-50.
[46]"Isolation and characterization of human apolipoprotein A-I Fukuoka (110 Glu-->Lys). A novel apolipoprotein variant."
Takada Y., Sasaki J., Ogata S., Nakanishi T., Ikehara Y., Arakawa K.
Biochim. Biophys. Acta 1043:169-176(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-267, VARIANT FUKUOKA LYS-134.
[47]"Apolipoprotein AI mutation Arg-60 causes autosomal dominant amyloidosis."
Soutar A.K., Hawkins P.N., Vigushin D.M., Tennent G.A., Booth S.E., Hutton T., Nguyen O., Totty N.F., Feest T.G., Hsuan J.J., Pepys M.B.
Proc. Natl. Acad. Sci. U.S.A. 89:7389-7393(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-112, VARIANT AMYL8 ARG-84.
[48]"Apolipoprotein A1 Baltimore (Arg-10-->Leu), a new ApoA1 variant."
Ladias J.A.A., Kwiterovich P.O. Jr., Smith H.H., Karathanasis S.K., Antonarakis S.E.
Hum. Genet. 84:439-445(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BALTIMORE LEU-34.
[49]"Apolipoprotein A-I variants. Naturally occurring substitutions of proline residues affect plasma concentration of apolipoprotein A-I."
von Eckardstein A., Funke H., Henke A., Altland K., Benninghoven A., Assmann G., Welp S., Roetrige A., Kock R.
J. Clin. Invest. 84:1722-1730(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ARG-27; ARG-28 AND ARG-189.
[50]"Structural analysis of human apolipoprotein A-I variants. Amino acid substitutions are nonrandomly distributed throughout the apolipoprotein A-I primary structure."
von Eckardstein A., Funke H., Walter M., Altland K., Benninghoven A., Assmann G.
J. Biol. Chem. 265:8610-8617(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLU-113; MET-131; GLY-163; VAL-171 AND LYS-222.
[51]"Characterization of two new human apolipoprotein A-I variants: apolipoprotein A-I Tsushima (Trp-108-->Arg) and A-I Hita (Ala-95-->Asp)."
Araki K., Sasaki J., Matsunaga A., Takada Y., Moriyama K., Hidaka K., Arakawa K.
Biochim. Biophys. Acta 1214:272-278(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HITA AND TSUSHIMA.
[52]"Familial nephropathic systemic amyloidosis caused by apolipoprotein AI variant Arg26."
Vigushin D.M., Gough J., Allan D., Alguacil A., Penner B., Pettigrew N.M., Quinonez G., Bernstein K., Booth S.E., Booth D.R., Soutar A.K., Hawkins P.N., Pepys M.B.
Q. J. Med. 87:149-154(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL8 ARG-50.
[53]"A novel homozygous missense mutation in the apo A-I gene with apo A-I deficiency."
Huang W., Sasaki J., Matsunaga A., Nanimatsu H., Moriyama K., Han H., Kugi M., Koga T., Yamaguchi K., Arakawa K.
Arterioscler. Thromb. Vasc. Biol. 18:389-396(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AOITA GLU-180.
[54]"Apo A-I Zaragoza(L144R): a novel mutation in the apolipoprotein A-I gene associated with familial hypoalphalipoproteinemia."
Recalde D., Cenarro A., Civeira F., Pocovi M.
Hum. Mutat. 11:416-416(1998)
Cited for: VARIANT ZARAGOZA ARG-168.
[55]"Association of extreme blood lipid profile phenotypic variation with 11 reverse cholesterol transport genes and 10 non-genetic cardiovascular disease risk factors."
Morabia A., Cayanis E., Costanza M.C., Ross B.M., Flaherty M.S., Alvin G.B., Das K., Gilliam T.C.
Hum. Mol. Genet. 12:2733-2743(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ILE-92.
[56]"Quantitative detection of single amino acid polymorphisms by targeted proteomics."
Su Z.D., Sun L., Yu D.X., Li R.X., Li H.X., Yu Z.J., Sheng Q.H., Lin X., Zeng R., Wu J.R.
J. Mol. Cell Biol. 3:309-315(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ILE-92, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Web resources

SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J00098 Genomic DNA. Translation: AAB59514.1.
X01038 Genomic DNA. Translation: CAA25519.1.
X02162 mRNA. Translation: CAA26097.1.
X00566 mRNA. Translation: CAA25232.1.
M11791 mRNA. Translation: AAA35545.1.
X07496 Genomic DNA. Translation: CAA30377.1.
M27875 mRNA. Translation: AAA62829.1.
M29068 mRNA. Translation: AAA51747.1.
AY422952 Genomic DNA. Translation: AAQ91811.1.
AY555191 Genomic DNA. Translation: AAS68227.1.
A14829 mRNA. Translation: CAA01198.1.
AK292231 mRNA. Translation: BAF84920.1.
EF444948 Genomic DNA. Translation: ACA05932.1.
EF444948 Genomic DNA. Translation: ACA05933.1.
EF444948 Genomic DNA. Translation: ACA05934.1.
EF444948 Genomic DNA. Translation: ACA05935.1.
EF444948 Genomic DNA. Translation: ACA05936.1.
CH471065 Genomic DNA. Translation: EAW67274.1.
BC005380 mRNA. Translation: AAH05380.1.
BC110286 mRNA. Translation: AAI10287.1.
CCDSCCDS8378.1.
PIRLPHUA1. A90947.
RefSeqNP_000030.1. NM_000039.1.
XP_005271596.1. XM_005271539.1.
XP_005271597.1. XM_005271540.1.
UniGeneHs.93194.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AV1X-ray4.00A/B/C/D68-267[»]
1GW3NMR-A166-211[»]
1GW4NMR-A166-211[»]
1ODPNMR-A190-209[»]
1ODQNMR-A190-209[»]
1ODRNMR-A190-209[»]
2A01X-ray2.40A/B/C25-267[»]
3J00electron microscopy-0/168-267[»]
3K2SX-ray-A/B25-267[»]
3R2PX-ray2.20A25-208[»]
DisProtDP00386.
ProteinModelPortalP02647.
SMRP02647. Positions 26-267.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106832. 73 interactions.
DIPDIP-29619N.
IntActP02647. 62 interactions.
MINTMINT-5000866.
STRING9606.ENSP00000236850.

Chemistry

ChEMBLCHEMBL5984.

PTM databases

PhosphoSiteP02647.

Polymorphism databases

DMDM113992.

2D gel databases

DOSAC-COBS-2DPAGEP02647.
OGPP02647.
REPRODUCTION-2DPAGEIPI00021841.
P02647.
SWISS-2DPAGEP02647.
UCD-2DPAGEP02647.

Proteomic databases

MaxQBP02647.
PaxDbP02647.
PeptideAtlasP02647.
PRIDEP02647.

Protocols and materials databases

DNASU335.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000236850; ENSP00000236850; ENSG00000118137.
ENST00000359492; ENSP00000352471; ENSG00000118137.
ENST00000375320; ENSP00000364469; ENSG00000118137.
ENST00000375323; ENSP00000364472; ENSG00000118137.
GeneID335.
KEGGhsa:335.
UCSCuc001ppv.1. human.

Organism-specific databases

CTD335.
GeneCardsGC11M116706.
HGNCHGNC:600. APOA1.
HPACAB016778.
HPA046715.
MIM105200. phenotype.
107680. gene+phenotype.
205400. phenotype.
604091. phenotype.
neXtProtNX_P02647.
Orphanet425. Apolipoprotein A-I deficiency.
93560. Familial renal amyloidosis due to Apolipoprotein AI variant.
314701. Primary systemic amyloidosis.
PharmGKBPA49.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG39720.
HOGENOMHOG000033998.
HOVERGENHBG105708.
InParanoidP02647.
KOK08757.
OMAYRQKVAP.
OrthoDBEOG7TBC3N.
PhylomeDBP02647.
TreeFamTF334458.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_116125. Disease.
REACT_15518. Transmembrane transport of small molecules.
REACT_160300. Binding and Uptake of Ligands by Scavenger Receptors.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP02647.
BgeeP02647.
CleanExHS_APOA1.
GenevestigatorP02647.

Family and domain databases

InterProIPR000074. ApoA1_A4_E.
[Graphical view]
PfamPF01442. Apolipoprotein. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAPOA1. human.
EvolutionaryTraceP02647.
GeneWikiApolipoprotein_A1.
GenomeRNAi335.
NextBio1387.
PMAP-CutDBP02647.
PROP02647.
SOURCESearch...

Entry information

Entry nameAPOA1_HUMAN
AccessionPrimary (citable) accession number: P02647
Secondary accession number(s): A8K866 expand/collapse secondary AC list , Q6LDN9, Q6Q785, Q9UCS8, Q9UCT8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 194 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM