P02652 (APOA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Apolipoprotein A-II
Short name=Apo-AII
Short name=ApoA-II

Alternative name(s):
Apolipoprotein A2

Cleaved into the following chain:

1. Truncated apolipoprotein A-II
   Alternative name(s):
   Apolipoprotein A-II(1-76)

Gene names

Name:

APOA2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	100 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.14 Ref.15 Ref.18 Ref.22
Subcellular location	Secreted.
Tissue specificity	Plasma; synthesized in the liver and intestine.
Post-translational modification	Met-49 is oxidized to methionine sulfoxide. Phosphorylation sites are present in the extracellular medium. Apolipoprotein A-II is O-glycosylated. Ref.21
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.16 Molecular mass is 17269 Da from positions 24 - 100. Determined by ESI. Homodimer, with 1 methionine sulfoxide, oxidation at Met-49. Ref.16 Molecular mass is 8701.2 Da from positions 24 - 100. Determined by MALDI. Ref.17 Molecular mass is 8823.4 Da from positions 24 - 100. Determined by MALDI. Cysteinylated ApoA-II. Ref.17 Molecular mass is 17421.3 Da from positions 24 - 100. Determined by MALDI. Homodimer. Ref.17 Molecular mass is 17293.4 Da from positions 24 - 100. Determined by MALDI. Heterodimer with truncated apolipoprotein A-II. Ref.17 Molecular mass is 8578.3 Da from positions 24 - 99. Determined by MALDI. Ref.17 Molecular mass is 17166.2 Da from positions 24 - 99. Determined by MALDI. Homodimer. Ref.17

Ontologies

Keywords
Biological process	Host-virus interaction Lipid transport Transport
Cellular component	HDL Secreted
Domain	Signal
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Oxidation Phosphoprotein Pyrrolidone carboxylic acid
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	acute inflammatory response Inferred from electronic annotation. Source: Compara 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: Compara 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 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: Compara peptidyl-methionine modification Inferred from direct assay Ref.16. 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 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.16. Source: UniProtKB regulation of intestinal cholesterol absorption Inferred from electronic annotation. Source: Compara regulation of protein stability Inferred from direct assay PubMed 14967812. Source: BHF-UCL response to drug Inferred from electronic annotation. Source: Compara response to estrogen stimulus Inferred from electronic annotation. Source: Compara response to glucocorticoid stimulus Inferred from electronic annotation. Source: Compara response to glucose stimulus Inferred from direct assay PubMed 14988251. Source: BHF-UCL reverse cholesterol transport Inferred from direct assay PubMed 14967812. Source: BHF-UCL 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 virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	chylomicron Inferred from direct assay PubMed 8245722. Source: BHF-UCL endoplasmic reticulum 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 8245722. Source: BHF-UCL
Molecular_function	cholesterol binding Inferred from direct assay PubMed 218942. Source: BHF-UCL cholesterol transporter activity Inferred from electronic annotation. Source: Compara high-density lipoprotein particle binding Inferred from electronic annotation. Source: Compara lipase inhibitor activity 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 protein homodimerization activity Inferred from direct assay PubMed 17264082. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

18

Ref.3

Propeptide

19 – 23

5

PRO_0000002002

Chain

24 – 100

77

Apolipoprotein A-II

PRO_0000002003

Chain

24 – 99

76

Truncated apolipoprotein A-II

PRO_0000002004

Regions

Region

32 – 43

12

O-glycosylated at one site

Amino acid modifications

Modified residue

24

1

Pyrrolidone carboxylic acid Ref.12

Modified residue

49

1

Methionine sulfoxide

Modified residue

68

1

Phosphoserine Ref.19

Disulfide bond

29

Interchain (with C-136 in APOD); in heterodimeric form Ref.14 Ref.22

Disulfide bond

29

Interchain; in homodimeric form Ref.5 Ref.14 Ref.22

Experimental info

Sequence conflict

96

1

Q → H in CAA28583. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

100

Helix Strand Turn

Details...

Helix

31 – 56

26

Beta strand

58 – 60

3

Helix

63 – 69

7

Turn

70 – 72

3

Helix

74 – 77

4

Helix

79 – 82

4

Helix

88 – 95

8

Turn

96 – 98

3

Sequences

	Sequence		Length	Mass (Da)
	P02652 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: 1247868A25EC3AF2	FASTA	100	11,175
	10 20 30 40 50 60 MKLLAATVLL LTICSLEGAL VRRQAKEPCV ESLVSQYFQT VTDYGKDLME KVKSPELQAE 70 80 90 100 AKSYFEKSKE QLTPLIKKAG TELVNFLSYF VELGTQPATQ

References

	« Hide 'large scale' referencesShow '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. , 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.
[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]	"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.
[15]	"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.
[16]	"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.
[17]	"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.
[18]	"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.
[19]	"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, MASS SPECTROMETRY. Tissue: Serum.
[20]	"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].
[21]	"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, MASS SPECTROMETRY.
[22]	"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.

IPI

IPI00021854.

PIR

LPHUA2. A93586.

RefSeq

NP_001634.1. NM_001643.1.

UniGene

Hs.237658.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1L6L	X-ray	2.30	1/2/3/4/5/6/7/8/A/B/C/D/E/F/G/H/I/J/K/L/M/N/P/Q/S/T/U/V/W/X/Y/Z	24-100	[»]
2OU1	X-ray	2.00	A/B/C/D/E/F/G/H/I/J/K/L	24-100	[»]

ProteinModelPortal

P02652.

SMR

P02652. Positions 25-100.

ModBase

Search...

Protein-protein interaction databases

IntAct

P02652. 2 interactions.

STRING

9606.ENSP00000356969.

PTM databases

PhosphoSite

P02652.

Polymorphism databases

DMDM

114000.

2D gel databases

SWISS-2DPAGE

P02652.

Proteomic databases

PaxDb

P02652.

PeptideAtlas

P02652.

PRIDE

P02652.

Protocols and materials databases

DNASU

336.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000367990; ENSP00000356969; ENSG00000158874.

GeneID

336.

KEGG

hsa:336.

UCSC

uc001fzc.1. human.

Organism-specific databases

CTD

336.

GeneCards

GC01M161192.

HGNC

HGNC:601. APOA2.

HPA

CAB025885.

MIM

107670. gene.

neXtProt

NX_P02652.

Orphanet

238269. Familial renal amyloidosis due to Apolipoprotein AII variant.

PharmGKB

PA24886.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG40617.

HOGENOM

HOG000033999.

HOVERGEN

HBG050544.

InParanoid

P02652.

KO

K08758.

OMA

TICSLEG.

OrthoDB

EOG42NJ1Z.

PhylomeDB

P02652.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

Gene expression databases

Bgee

P02652.

CleanEx

HS_APOA2.

Genevestigator

P02652.

GermOnline

ENSG00000158874. Homo sapiens.

Family and domain databases

InterPro

IPR006801. ApoA-II.
[Graphical view]

PANTHER

PTHR11027. PTHR11027. 1 hit.

Pfam

PF04711. ApoA-II. 1 hit.
[Graphical view]

ProDom

PD010397. ApoA-II. 1 hit.
[Graphical view] [Entries sharing at least one domain]

ProtoNet

Search...

Other

ChiTaRS

APOA2. human.

EvolutionaryTrace

P02652.

GenomeRNAi

336.

NextBio

1391.

PMAP-CutDB

P02652.

SOURCE

Search...

Entry information

Entry name

APOA2_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 163 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.