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P02652 (APOA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 172. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Apolipoprotein A-II

Short name=Apo-AII
Short name=ApoA-II
Alternative name(s):
Apolipoprotein A2

Cleaved into the following 2 chains:

  1. Proapolipoprotein A-II
    Short name=ProapoA-II
  2. Truncated apolipoprotein A-II
    Alternative name(s):
    Apolipoprotein A-II(1-76)
Gene names
Name:APOA2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length100 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

Homodimer; disulfide-linked. Also forms a disulfide-linked heterodimer with APOD. Interacts with HCV core protein. Interacts with APOA1BP and NDRG1. Ref.15 Ref.16 Ref.19 Ref.23

Subcellular location

Secreted.

Tissue specificity

Plasma; synthesized in the liver and intestine.

Post-translational modification

Phosphorylation sites are present in the extracellular medium.

Apolipoprotein A-II is O-glycosylated. Ref.22

Polymorphism

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 [MIM:107670].

Sequence similarities

Belongs to the apolipoprotein A2 family.

Mass spectrometry

Molecular mass is 17252 Da from positions 24 - 100. Determined by ESI. Homodimer, without methionine sulfoxide. Ref.17

Molecular mass is 17269 Da from positions 24 - 100. Determined by ESI. Homodimer, with 1 methionine sulfoxide, oxidation at Met-49. Ref.17

Molecular mass is 8701.2 Da from positions 24 - 100. Determined by MALDI. Ref.18

Molecular mass is 8823.4 Da from positions 24 - 100. Determined by MALDI. Cysteinylated ApoA-II. Ref.18

Molecular mass is 17421.3 Da from positions 24 - 100. Determined by MALDI. Homodimer. Ref.18

Molecular mass is 17293.4 Da from positions 24 - 100. Determined by MALDI. Heterodimer with truncated apolipoprotein A-II. Ref.18

Molecular mass is 8578.3 Da from positions 24 - 99. Determined by MALDI. Ref.18

Molecular mass is 17166.2 Da from positions 24 - 99. Determined by MALDI. Homodimer. Ref.18

Ontologies

Keywords
   Biological processHost-virus interaction
Lipid transport
Transport
   Cellular componentHDL
Secreted
   DomainSignal
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Oxidation
Phosphoprotein
Pyrrolidone carboxylic acid
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processacute inflammatory response

Inferred from electronic annotation. Source: Ensembl

cellular lipid metabolic process

Traceable author statement. Source: Reactome

cholesterol efflux

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

cholesterol homeostasis

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

cholesterol metabolic process

Inferred from electronic annotation. Source: Ensembl

diacylglycerol catabolic process

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

high-density lipoprotein particle assembly

Inferred from direct assay PubMed 218942. Source: BHF-UCL

high-density lipoprotein particle clearance

Inferred from direct assay PubMed 10764676. Source: BHF-UCL

high-density lipoprotein particle remodeling

Inferred from direct assay PubMed 14967812PubMed 8106353. Source: BHF-UCL

lipoprotein metabolic process

Traceable author statement. Source: Reactome

low-density lipoprotein particle remodeling

Inferred from direct assay PubMed 8106353. Source: BHF-UCL

negative regulation of cholesterol import

Inferred from direct assay PubMed 10764676. Source: BHF-UCL

negative regulation of cholesterol transport

Inferred from mutant phenotype PubMed 8636092. Source: BHF-UCL

negative regulation of cholesterol transporter activity

Inferred from direct assay PubMed 8106353. Source: BHF-UCL

negative regulation of cytokine secretion involved in immune response

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

negative regulation of lipase activity

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

negative regulation of lipid catabolic process

Inferred from direct assay PubMed 14967812. 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.17. Source: UniProtKB

phosphatidylcholine biosynthetic process

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

phospholipid catabolic process

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

phospholipid efflux

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

phototransduction, visible light

Traceable author statement. Source: Reactome

positive regulation of catalytic activity

Inferred from direct assay PubMed 14967812. Source: GOC

positive regulation of cholesterol esterification

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

positive regulation of interleukin-8 biosynthetic process

Inferred from direct assay PubMed 11591715. Source: UniProtKB

positive regulation of lipid catabolic process

Inferred from direct assay PubMed 8640403. Source: BHF-UCL

protein folding

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

protein oxidation

Inferred from direct assay Ref.17. Source: UniProtKB

regulation of intestinal cholesterol absorption

Inferred from electronic annotation. Source: Ensembl

regulation of protein stability

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

response to drug

Inferred from electronic annotation. Source: Ensembl

response to estrogen

Inferred from electronic annotation. Source: Ensembl

response to glucocorticoid

Inferred from electronic annotation. Source: Ensembl

response to glucose

Inferred from direct assay PubMed 14988251. Source: BHF-UCL

retinoid metabolic process

Traceable author statement. Source: Reactome

reverse cholesterol transport

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

small molecule metabolic process

Traceable author statement. Source: Reactome

triglyceride metabolic process

Traceable author statement PubMed 11551871. Source: BHF-UCL

triglyceride-rich lipoprotein particle remodeling

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

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentblood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

chylomicron

Inferred from direct assay PubMed 8245722. Source: BHF-UCL

cytosol

Traceable author statement. Source: Reactome

early endosome

Traceable author statement. Source: Reactome

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

extracellular region

Non-traceable author statement PubMed 14718574. Source: UniProtKB

extracellular vesicular exosome

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

high-density lipoprotein particle

Inferred from direct assay PubMed 17264082PubMed 210174PubMed 3104518. Source: BHF-UCL

spherical high-density lipoprotein particle

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

very-low-density lipoprotein particle

Inferred from direct assay PubMed 8245722. Source: BHF-UCL

   Molecular_functionapolipoprotein receptor binding

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

cholesterol binding

Inferred from direct assay PubMed 218942. Source: BHF-UCL

cholesterol transporter activity

Inferred from electronic annotation. Source: Ensembl

high-density lipoprotein particle binding

Inferred from electronic annotation. Source: Ensembl

high-density lipoprotein particle receptor binding

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

lipase inhibitor activity

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

lipid binding

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

lipid transporter activity

Inferred from direct assay PubMed 1606170. Source: BHF-UCL

phosphatidylcholine binding

Inferred from direct assay PubMed 17264082. Source: BHF-UCL

phosphatidylcholine-sterol O-acyltransferase activator activity

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

phospholipid binding

Inferred from direct assay PubMed 218942. Source: BHF-UCL

protein heterodimerization activity

Inferred from physical interaction Ref.15. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay PubMed 17264082. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.3
Chain19 – 10082Proapolipoprotein A-II
PRO_0000425351
Chain24 – 10077Apolipoprotein A-II
PRO_0000002003
Chain24 – 9976Truncated apolipoprotein A-II
PRO_0000002004

Regions

Region32 – 4312O-glycosylated at one site

Amino acid modifications

Modified residue241Pyrrolidone carboxylic acid Ref.12
Modified residue491Methionine sulfoxide
Modified residue681Phosphoserine Ref.20
Disulfide bond29Interchain (with C-136 in APOD); in heterodimeric form Ref.15 Ref.23

Experimental info

Sequence conflict961Q → H in CAA28583. Ref.1

Secondary structure

............... 100
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02652 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 1247868A25EC3AF2

FASTA10011,175
        10         20         30         40         50         60 
MKLLAATVLL LTICSLEGAL VRRQAKEPCV ESLVSQYFQT VTDYGKDLME KVKSPELQAE 

        70         80         90        100 
AKSYFEKSKE QLTPLIKKAG TELVNFLSYF VELGTQPATQ 

« Hide

References

« Hide 'large scale' references
[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. 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: 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. expand/collapse author list , 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 TO METHIONINE SULFOXIDE.
[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]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Serum.
[21]"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].
[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]"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.
+Additional computationally mapped references.

Web resources

SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRLPHUA2. A93586.
RefSeqNP_001634.1. NM_001643.1.
UniGeneHs.237658.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP02652.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106833. 10 interactions.
IntActP02652. 7 interactions.
MINTMINT-106326.
STRING9606.ENSP00000356969.

PTM databases

PhosphoSiteP02652.

Polymorphism databases

DMDM114000.

2D gel databases

SWISS-2DPAGEP02652.

Proteomic databases

PaxDbP02652.
PeptideAtlasP02652.
PRIDEP02652.

Protocols and materials databases

DNASU336.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367990; ENSP00000356969; ENSG00000158874.
GeneID336.
KEGGhsa:336.
UCSCuc001fzc.1. human.

Organism-specific databases

CTD336.
GeneCardsGC01M161192.
HGNCHGNC:601. APOA2.
HPACAB025885.
MIM107670. gene+phenotype.
neXtProtNX_P02652.
Orphanet238269. Familial renal amyloidosis due to Apolipoprotein AII variant.
PharmGKBPA24886.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG40617.
HOGENOMHOG000033999.
HOVERGENHBG050544.
InParanoidP02652.
KOK08758.
OMAAYFEKTQ.
OrthoDBEOG7G4QHG.
PhylomeDBP02652.
TreeFamTF338165.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_116125. Disease.

Gene expression databases

BgeeP02652.
CleanExHS_APOA2.
GenevestigatorP02652.

Family and domain databases

InterProIPR006801. ApoA-II.
[Graphical view]
PANTHERPTHR11027. PTHR11027. 1 hit.
PfamPF04711. ApoA-II. 1 hit.
[Graphical view]
ProDomPD010397. ApoA-II. 1 hit.
[Graphical view] [Entries sharing at least one domain]
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Other

ChiTaRSAPOA2. human.
EvolutionaryTraceP02652.
GeneWikiAPOA2.
GenomeRNAi336.
NextBio1391.
PMAP-CutDBP02652.
PROP02652.
SOURCESearch...

Entry information

Entry nameAPOA2_HUMAN
AccessionPrimary (citable) accession number: P02652
Secondary accession number(s): B2R524
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 13, 1987
Last modified: April 16, 2014
This is version 172 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 chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM