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Protein

Apolipoprotein A-II

Gene

APOA2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism.

GO - Molecular functioni

  • apolipoprotein receptor binding Source: BHF-UCL
  • cholesterol binding Source: BHF-UCL
  • cholesterol transporter activity Source: Ensembl
  • high-density lipoprotein particle binding Source: Ensembl
  • high-density lipoprotein particle receptor binding Source: BHF-UCL
  • lipase inhibitor activity Source: BHF-UCL
  • lipid binding Source: BHF-UCL
  • lipid transporter activity Source: BHF-UCL
  • phosphatidylcholine binding Source: BHF-UCL
  • phosphatidylcholine-sterol O-acyltransferase activator activity Source: BHF-UCL
  • phospholipid binding Source: BHF-UCL
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: BHF-UCL

GO - Biological processi

  • acute inflammatory response Source: Ensembl
  • cellular lipid metabolic process Source: Reactome
  • cholesterol efflux Source: BHF-UCL
  • cholesterol homeostasis Source: BHF-UCL
  • cholesterol metabolic process Source: Ensembl
  • diacylglycerol catabolic process Source: BHF-UCL
  • high-density lipoprotein particle assembly Source: BHF-UCL
  • high-density lipoprotein particle clearance Source: BHF-UCL
  • high-density lipoprotein particle remodeling Source: BHF-UCL
  • lipoprotein metabolic process Source: Reactome
  • low-density lipoprotein particle remodeling Source: BHF-UCL
  • negative regulation of cholesterol import Source: BHF-UCL
  • negative regulation of cholesterol transport Source: BHF-UCL
  • negative regulation of cholesterol transporter activity Source: BHF-UCL
  • negative regulation of cytokine secretion involved in immune response Source: BHF-UCL
  • negative regulation of lipase activity Source: BHF-UCL
  • negative regulation of lipid catabolic process Source: BHF-UCL
  • negative regulation of very-low-density lipoprotein particle remodeling Source: BHF-UCL
  • organ regeneration Source: Ensembl
  • peptidyl-methionine modification Source: UniProtKB
  • phosphatidylcholine biosynthetic process Source: BHF-UCL
  • phospholipid catabolic process Source: BHF-UCL
  • phospholipid efflux Source: BHF-UCL
  • phototransduction, visible light Source: Reactome
  • positive regulation of catalytic activity Source: GOC
  • positive regulation of cholesterol esterification Source: BHF-UCL
  • positive regulation of interleukin-8 biosynthetic process Source: UniProtKB
  • positive regulation of lipid catabolic process Source: BHF-UCL
  • protein folding Source: BHF-UCL
  • protein oxidation Source: UniProtKB
  • regulation of intestinal cholesterol absorption Source: Ensembl
  • regulation of protein stability Source: BHF-UCL
  • response to drug Source: Ensembl
  • response to estrogen Source: Ensembl
  • response to glucocorticoid Source: Ensembl
  • response to glucose Source: BHF-UCL
  • retinoid metabolic process Source: Reactome
  • reverse cholesterol transport Source: BHF-UCL
  • small molecule metabolic process Source: Reactome
  • triglyceride metabolic process Source: BHF-UCL
  • triglyceride-rich lipoprotein particle remodeling Source: BHF-UCL
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Lipid transport, Transport

Enzyme and pathway databases

ReactomeiREACT_116145. PPARA activates gene expression.
REACT_24968. Retinoid metabolism and transport.
REACT_6841. Chylomicron-mediated lipid transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Apolipoprotein A-II
Short name:
Apo-AII
Short name:
ApoA-II
Alternative name(s):
Apolipoprotein A2
Cleaved into the following 2 chains:
Proapolipoprotein A-II
Short name:
ProapoA-II
Alternative name(s):
Apolipoprotein A-II(1-76)
Gene namesi
Name:APOA2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:601. APOA2.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • chylomicron Source: BHF-UCL
  • cytosol Source: Reactome
  • early endosome Source: Reactome
  • endoplasmic reticulum lumen Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: UniProtKB
  • high-density lipoprotein particle Source: BHF-UCL
  • spherical high-density lipoprotein particle Source: BHF-UCL
  • very-low-density lipoprotein particle Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

HDL, Secreted

Pathology & Biotechi

Organism-specific databases

MIMi107670. gene+phenotype.
Orphaneti238269. Familial renal amyloidosis due to Apolipoprotein AII variant.
PharmGKBiPA24886.

Polymorphism and mutation databases

BioMutaiAPOA2.
DMDMi114000.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18181 PublicationAdd
BLAST
Chaini19 – 10082Proapolipoprotein A-IIPRO_0000425351Add
BLAST
Chaini24 – 10077Apolipoprotein A-IIPRO_0000002003Add
BLAST
Chaini24 – 9976Truncated apolipoprotein A-IIPRO_0000002004Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei24 – 241Pyrrolidone carboxylic acid1 Publication
Disulfide bondi29 – 29Interchain (with C-136 in APOD); in heterodimeric form1 Publication
Modified residuei49 – 491Methionine sulfoxide1 Publication
Modified residuei68 – 681Phosphoserine1 Publication

Post-translational modificationi

Phosphorylation sites are present in the extracellular medium.
Apolipoprotein A-II is O-glycosylated.1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Oxidation, Phosphoprotein, Pyrrolidone carboxylic acid

Proteomic databases

MaxQBiP02652.
PaxDbiP02652.
PeptideAtlasiP02652.
PRIDEiP02652.

2D gel databases

SWISS-2DPAGEP02652.

PTM databases

PhosphoSiteiP02652.

Miscellaneous databases

PMAP-CutDBP02652.

Expressioni

Tissue specificityi

Plasma; synthesized in the liver and intestine.

Gene expression databases

BgeeiP02652.
CleanExiHS_APOA2.
ExpressionAtlasiP02652. baseline and differential.
GenevisibleiP02652. HS.

Organism-specific databases

HPAiCAB025885.

Interactioni

Subunit structurei

Homodimer; disulfide-linked. Also forms a disulfide-linked heterodimer with APOD. Interacts with HCV core protein. Interacts with APOA1BP and NDRG1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CATSPER1Q8NEC53EBI-1171525,EBI-744545

Protein-protein interaction databases

BioGridi106833. 12 interactions.
IntActiP02652. 8 interactions.
MINTiMINT-106326.
STRINGi9606.ENSP00000356969.

Structurei

Secondary structure

1
100
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi31 – 5626Combined sources
Beta strandi58 – 603Combined sources
Helixi63 – 697Combined sources
Turni70 – 723Combined sources
Helixi74 – 774Combined sources
Helixi79 – 824Combined sources
Helixi88 – 958Combined sources
Turni96 – 983Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L6LX-ray2.301/2/3/4/5/6/7/8/A/B/C/D/E/F/G/H/I/J/K/L/M/N/P/Q/S/T/U/V/W/X/Y/Z24-100[»]
2OU1X-ray2.00A/B/C/D/E/F/G/H/I/J/K/L24-100[»]
ProteinModelPortaliP02652.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02652.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni32 – 4312O-glycosylated at one siteAdd
BLAST

Sequence similaritiesi

Belongs to the apolipoprotein A2 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG40617.
GeneTreeiENSGT00390000003306.
HOGENOMiHOG000033999.
HOVERGENiHBG050544.
InParanoidiP02652.
KOiK08758.
OrthoDBiEOG7G4QHG.
PhylomeDBiP02652.
TreeFamiTF338165.

Family and domain databases

InterProiIPR006801. ApoA-II.
[Graphical view]
PANTHERiPTHR11027. PTHR11027. 1 hit.
PfamiPF04711. ApoA-II. 1 hit.
[Graphical view]
ProDomiPD010397. ApoA-II. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P02652-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLLAATVLL LTICSLEGAL VRRQAKEPCV ESLVSQYFQT VTDYGKDLME
60 70 80 90 100
KVKSPELQAE AKSYFEKSKE QLTPLIKKAG TELVNFLSYF VELGTQPATQ
Length:100
Mass (Da):11,175
Last modified:August 13, 1987 - v1
Checksum:i1247868A25EC3AF2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti96 – 961Q → H in CAA28583 (PubMed:6428397).Curated

Mass spectrometryi

Molecular mass is 17252 Da from positions 24 - 100. Determined by ESI. Homodimer, without methionine sulfoxide.1 Publication
Molecular mass is 17269 Da from positions 24 - 100. Determined by ESI. Homodimer, with 1 methionine sulfoxide, oxidation at Met-49.1 Publication
Molecular mass is 8701.2 Da from positions 24 - 100. Determined by MALDI. 1 Publication
Molecular mass is 8823.4 Da from positions 24 - 100. Determined by MALDI. Cysteinylated ApoA-II.1 Publication
Molecular mass is 17421.3 Da from positions 24 - 100. Determined by MALDI. Homodimer.1 Publication
Molecular mass is 17293.4 Da from positions 24 - 100. Determined by MALDI. Heterodimer with truncated apolipoprotein A-II.1 Publication
Molecular mass is 8578.3 Da from positions 24 - 99. Determined by MALDI. 1 Publication
Molecular mass is 17166.2 Da from positions 24 - 99. Determined by MALDI. Homodimer.1 Publication

Polymorphismi

A homozygous transition at position 1 of intron 3 of APOA2 results in deficiency of apolipoprotein A-II, without significant influence either on lipid and lipoprotein profiles or on the occurrence of coronary artery disease [MIMi:107670].

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04898 Genomic DNA. Translation: CAA28583.1.
X00955 mRNA. Translation: CAA25467.1.
X02905 Genomic DNA. Translation: CAA26665.1.
X02619 Genomic DNA. Translation: CAA26474.1.
M29882 mRNA. Translation: AAA51701.1.
AY100524 Genomic DNA. Translation: AAM49807.1.
AK312034 mRNA. Translation: BAG34971.1.
BT006786 mRNA. Translation: AAP35432.1.
AL590714 Genomic DNA. Translation: CAH72151.1.
BC005282 mRNA. Translation: AAH05282.1.
CCDSiCCDS1226.1.
PIRiA93586. LPHUA2.
RefSeqiNP_001634.1. NM_001643.1.
UniGeneiHs.237658.

Genome annotation databases

EnsembliENST00000367990; ENSP00000356969; ENSG00000158874.
GeneIDi336.
KEGGihsa:336.
UCSCiuc001fzc.1. human.

Cross-referencesi

Web resourcesi

SHMPD

The Singapore human mutation and polymorphism database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04898 Genomic DNA. Translation: CAA28583.1.
X00955 mRNA. Translation: CAA25467.1.
X02905 Genomic DNA. Translation: CAA26665.1.
X02619 Genomic DNA. Translation: CAA26474.1.
M29882 mRNA. Translation: AAA51701.1.
AY100524 Genomic DNA. Translation: AAM49807.1.
AK312034 mRNA. Translation: BAG34971.1.
BT006786 mRNA. Translation: AAP35432.1.
AL590714 Genomic DNA. Translation: CAH72151.1.
BC005282 mRNA. Translation: AAH05282.1.
CCDSiCCDS1226.1.
PIRiA93586. LPHUA2.
RefSeqiNP_001634.1. NM_001643.1.
UniGeneiHs.237658.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L6LX-ray2.301/2/3/4/5/6/7/8/A/B/C/D/E/F/G/H/I/J/K/L/M/N/P/Q/S/T/U/V/W/X/Y/Z24-100[»]
2OU1X-ray2.00A/B/C/D/E/F/G/H/I/J/K/L24-100[»]
ProteinModelPortaliP02652.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106833. 12 interactions.
IntActiP02652. 8 interactions.
MINTiMINT-106326.
STRINGi9606.ENSP00000356969.

PTM databases

PhosphoSiteiP02652.

Polymorphism and mutation databases

BioMutaiAPOA2.
DMDMi114000.

2D gel databases

SWISS-2DPAGEP02652.

Proteomic databases

MaxQBiP02652.
PaxDbiP02652.
PeptideAtlasiP02652.
PRIDEiP02652.

Protocols and materials databases

DNASUi336.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367990; ENSP00000356969; ENSG00000158874.
GeneIDi336.
KEGGihsa:336.
UCSCiuc001fzc.1. human.

Organism-specific databases

CTDi336.
GeneCardsiGC01M161192.
HGNCiHGNC:601. APOA2.
HPAiCAB025885.
MIMi107670. gene+phenotype.
neXtProtiNX_P02652.
Orphaneti238269. Familial renal amyloidosis due to Apolipoprotein AII variant.
PharmGKBiPA24886.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG40617.
GeneTreeiENSGT00390000003306.
HOGENOMiHOG000033999.
HOVERGENiHBG050544.
InParanoidiP02652.
KOiK08758.
OrthoDBiEOG7G4QHG.
PhylomeDBiP02652.
TreeFamiTF338165.

Enzyme and pathway databases

ReactomeiREACT_116145. PPARA activates gene expression.
REACT_24968. Retinoid metabolism and transport.
REACT_6841. Chylomicron-mediated lipid transport.

Miscellaneous databases

ChiTaRSiAPOA2. human.
EvolutionaryTraceiP02652.
GeneWikiiAPOA2.
GenomeRNAii336.
NextBioi1391.
PMAP-CutDBP02652.
PROiP02652.
SOURCEiSearch...

Gene expression databases

BgeeiP02652.
CleanExiHS_APOA2.
ExpressionAtlasiP02652. baseline and differential.
GenevisibleiP02652. HS.

Family and domain databases

InterProiIPR006801. ApoA-II.
[Graphical view]
PANTHERiPTHR11027. PTHR11027. 1 hit.
PfamiPF04711. ApoA-II. 1 hit.
[Graphical view]
ProDomiPD010397. ApoA-II. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterisation of a cDNA encoding the precursor for human apolipoprotein AII."
    Knott T.J., Priestley L.M., Urdea M., Scott J.
    Biochem. Biophys. Res. Commun. 120:734-740(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Human apolipoprotein A-II: nucleotide sequence of a cloned cDNA, and localization of its structural gene on human chromosome 1."
    Moore M.N., Kao F.-T., Tsao Y.-K., Chan L.
    Biochem. Biophys. Res. Commun. 123:1-7(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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 [MRNA].
  4. "The human apolipoprotein A-II gene: complete nucleic acid sequence and genomic organization."
    Lackner K.J., Law S.W., Brewer H.B. Jr.
    Nucleic Acids Res. 13:4597-4608(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "The human apolipoprotein AII gene: structural organization and sites of expression."
    Knott T.J., Wallis S.C., Robertson M.E., Priestley L.M., Urdea M., Rall L.B., Scott J.
    Nucleic Acids Res. 13:6387-6398(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. "Molecular cloning and sequence analysis of human apolipoprotein A-II cDNA."
    Chan L., Moore M.N., Tsao Y.-K.
    Methods Enzymol. 128:745-752(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  7. "Sequence polymorphism at the human apolipoprotein AII gene (APOA2): unexpected deficit of variation in an African-American sample."
    Fullerton S.M., Clark A.G., Weiss K.M., Taylor S.L., Stengard J.H., Salomaa V., Boerwinkle E., Nickerson D.A.
    Hum. Genet. 111:75-87(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  8. "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.
    , 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: Liver.
  9. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  10. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. "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: Skeletal muscle.
  12. "Isolation and characterization of the tryptic and cyanogen bromide peptides of apoLp-Gln-II (apoA-II), plasma high density apolipoprotein."
    Lux S.E., John K.M., Ronan R., Brewer H.B. Jr.
    J. Biol. Chem. 247:7519-7527(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 24-100, PYROGLUTAMATE FORMATION AT GLN-24.
  13. "Cell-free translation of human liver apolipoprotein AI and AII mRNA. Processing of primary translation products."
    Stoffel W., Krueger E., Deutzmann R.
    Hoppe-Seyler's Z. Physiol. Chem. 364:227-237(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE OF 1-29.
  14. "A splice-junction mutation responsible for familial apolipoprotein A-II deficiency."
    Deeb S.S., Takata K., Peng R.L., Kajiyama G., Albers J.J.
    Am. J. Hum. Genet. 46:822-827(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: POLYMORPHISM.
  15. "Structure of human apolipoprotein D: locations of the intermolecular and intramolecular disulfide links."
    Yang C.-Y., Gu Z.-W., Blanco-Vaca F., Gaskell S.J., Yang M., Massey J.B., Gotto A.M. Jr., Pownall H.J.
    Biochemistry 33:12451-12455(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERCHAIN DISULFIDE BOND WITH APOD.
    Tissue: Plasma.
  16. "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.
  17. "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-49.
  18. "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: MASS SPECTROMETRY.
  19. "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.
  20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Serum.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins."
    Halim A., Ruetschi U., Larson G., Nilsson J.
    J. Proteome Res. 12:573-584(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION, IDENTIFICATION BY MASS SPECTROMETRY.
  23. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  24. "Structures of apolipoprotein A-II and a lipid-surrogate complex provide insights into apolipoprotein-lipid interactions."
    Kumar M.S., Carson M., Hussain M.M., Murthy H.M.
    Biochemistry 41:11681-11691(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 24-100, SUBUNIT, DISULFIDE BOND.

Entry informationi

Entry nameiAPOA2_HUMAN
AccessioniPrimary (citable) accession number: P02652
Secondary accession number(s): B2R524
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 13, 1987
Last modified: June 24, 2015
This is version 185 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.