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P06727 (APOA4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 163. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Apolipoprotein A-IV

Short name=Apo-AIV
Short name=ApoA-IV
Alternative name(s):
Apolipoprotein A4
Gene names
Name:APOA4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length396 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May have a role in chylomicrons and VLDL secretion and catabolism. Required for efficient activation of lipoprotein lipase by ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL and chylomicrons.

Subunit structure

Homodimer. Ref.14

Subcellular location

Secreted.

Tissue specificity

Synthesized primarily in the intestine and secreted in plasma.

Domain

Nine of the thirteen 22-amino acid tandem repeats (each 22-mer is actually a tandem array of two, A and B, related 11-mers) occurring in this sequence are predicted to be highly alpha-helical, and many of these helices are amphipathic. They may therefore serve as lipid-binding domains with lecithin:cholesterol acyltransferase (LCAT) activating abilities.

Post-translational modification

Phosphorylation sites are present in the extracellular medium.

Polymorphism

Eight alleles have been characterized (APOA-IV*0 to APOA-IV*7). APOA-IV*1 is the major allele (90%), APOA-IV*2 is also common (8%), the others are rare alleles. The sequence shown represents allele APOA-IV*1.

Sequence similarities

Belongs to the apolipoprotein A1/A4/E family.

Ontologies

Keywords
   Biological processLipid transport
Transport
   Cellular componentChylomicron
HDL
Secreted
   Coding sequence diversityPolymorphism
   DomainRepeat
Signal
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcholesterol efflux

Inferred from direct assay PubMed 11162594PubMed 1935934. Source: BHF-UCL

cholesterol homeostasis

Inferred from direct assay PubMed 1935934. Source: BHF-UCL

cholesterol metabolic process

Inferred from direct assay PubMed 1935934. Source: BHF-UCL

chylomicron assembly

Traceable author statement PubMed 16159879. Source: BHF-UCL

chylomicron remodeling

Inferred by curator PubMed 2307668. Source: BHF-UCL

high-density lipoprotein particle remodeling

Inferred by curator PubMed 1935934. Source: BHF-UCL

hydrogen peroxide catabolic process

Inferred from direct assay PubMed 16945374. Source: HGNC

innate immune response in mucosa

Inferred from direct assay PubMed 15254593. Source: BHF-UCL

leukocyte cell-cell adhesion

Inferred from direct assay PubMed 15254593. Source: BHF-UCL

lipid homeostasis

Inferred from direct assay PubMed 3095477. Source: BHF-UCL

lipid transport

Inferred from direct assay PubMed 1935934PubMed 3095477. Source: BHF-UCL

lipoprotein metabolic process

Traceable author statement. Source: Reactome

multicellular organismal lipid catabolic process

Inferred from direct assay PubMed 3095477. Source: BHF-UCL

negative regulation of plasma lipoprotein particle oxidation

Inferred from direct assay PubMed 16945374. Source: BHF-UCL

phosphatidylcholine metabolic process

Inferred from direct assay PubMed 1935934. 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 cholesterol esterification

Inferred from direct assay PubMed 1935934. Source: BHF-UCL

positive regulation of fatty acid biosynthetic process

Inferred from direct assay PubMed 2307668. Source: BHF-UCL

positive regulation of lipoprotein lipase activity

Inferred from direct assay PubMed 2307668. Source: BHF-UCL

positive regulation of triglyceride catabolic process

Inferred from direct assay PubMed 2307668. Source: BHF-UCL

protein-lipid complex assembly

Inferred from mutant phenotype PubMed 16159879. Source: BHF-UCL

regulation of cholesterol transport

Inferred from direct assay PubMed 11940599. Source: BHF-UCL

regulation of intestinal cholesterol absorption

Inferred from electronic annotation. Source: Ensembl

removal of superoxide radicals

Inferred from direct assay PubMed 16945374. Source: HGNC

response to lipid hydroperoxide

Inferred from direct assay PubMed 16945374. Source: HGNC

response to stilbenoid

Inferred from electronic annotation. Source: Ensembl

retinoid metabolic process

Traceable author statement. Source: Reactome

reverse cholesterol transport

Inferred from direct assay PubMed 3095477. Source: BHF-UCL

small molecule metabolic process

Traceable author statement. Source: Reactome

very-low-density lipoprotein particle remodeling

Inferred from direct assay PubMed 2307668. Source: BHF-UCL

   Cellular_componentblood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

chylomicron

Inferred from direct assay PubMed 3095477. 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 space

Inferred from direct assay PubMed 1935934PubMed 20551380. Source: BHF-UCL

high-density lipoprotein particle

Inferred from direct assay PubMed 3095477. Source: BHF-UCL

very-low-density lipoprotein particle

Inferred from direct assay PubMed 17154273PubMed 3095477. Source: BHF-UCL

   Molecular_functionantioxidant activity

Inferred from direct assay PubMed 16945374. Source: HGNC

cholesterol transporter activity

Inferred from direct assay PubMed 1935934. Source: BHF-UCL

copper ion binding

Inferred from direct assay PubMed 16945374. Source: HGNC

lipid binding

Inferred from mutant phenotype PubMed 16159879. Source: BHF-UCL

lipid transporter activity

Traceable author statement Ref.8. Source: ProtInc

phosphatidylcholine binding

Inferred from direct assay PubMed 11940599PubMed 1935934. Source: BHF-UCL

phosphatidylcholine-sterol O-acyltransferase activator activity

Inferred from direct assay PubMed 1935934. Source: BHF-UCL

protein homodimerization activity

Inferred from direct assay PubMed 1935934. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020
Chain21 – 396376Apolipoprotein A-IV
PRO_0000001975

Regions

Repeat33 – 54221
Repeat60 – 81222
Repeat82 – 103223
Repeat115 – 136224
Repeat137 – 158225
Repeat159 – 180226
Repeat181 – 202227
Repeat203 – 224228
Repeat225 – 246229
Repeat247 – 2682210
Repeat269 – 2861811
Repeat287 – 3082212
Repeat309 – 3302213
Region33 – 33029813 X 22 AA approximate tandem repeats
Compositional bias372 – 38918Gln/Glu-rich

Natural variations

Natural variant131V → M in allele APOA-IV*1D. Ref.5 Ref.18
VAR_000626
Natural variant441E → K in Budapest-2. Ref.21
VAR_000627
Natural variant741G → S.
Corresponds to variant rs5102 [ dbSNP | Ensembl ].
VAR_014610
Natural variant771Q → H. Ref.5
VAR_025444
Natural variant1471N → S in allele APOA-IV*1B. Ref.5 Ref.6 Ref.19
Corresponds to variant rs5104 [ dbSNP | Ensembl ].
VAR_000628
Natural variant1611A → S in Seattle-3. Ref.5 Ref.22
VAR_000629
Natural variant1781S → L in Seattle-1; may contribute to the development of familial combined hyperlipidemia. Ref.22
VAR_000630
Natural variant1851E → K in allele APOA-IV*3. Ref.16
VAR_000631
Natural variant1871K → E in allele APOA-IV*0A; associated with H-380. Ref.16
VAR_000632
Natural variant2501E → K in allele APOA-IV*3A. Ref.12
VAR_000633
Natural variant2641R → Q in Seattle-2; may contribute to the development of familial combined hyperlipidemia. Ref.22
Corresponds to variant rs2238008 [ dbSNP | Ensembl ].
VAR_000634
Natural variant2791R → K. Ref.1 Ref.2
Corresponds to variant rs1042372 [ dbSNP | Ensembl ].
VAR_025443
Natural variant3051R → C in Budapest-1. Ref.21
VAR_000635
Natural variant3071V → L.
Corresponds to variant rs5108 [ dbSNP | Ensembl ].
VAR_014611
Natural variant3671T → S in allele APOA-IV*1A and allele Budapest-1. Ref.5 Ref.16 Ref.21
Corresponds to variant rs675 [ dbSNP | Ensembl ].
VAR_000636
Natural variant3801Q → H in allele APOA-IV*2 and allele APOA-IV*0A; associated with E-187 in allele APOA-IV*0A. Ref.3 Ref.5 Ref.8 Ref.11 Ref.15 Ref.16 Ref.23
Corresponds to variant rs5110 [ dbSNP | Ensembl ].
VAR_000637
Natural variant3811Q → QEQQQ in allele APOA-IV*0 and allele APOA-IV*5; allele APOA-IV*5 is further defined by a silent nucleotide substitution.
VAR_000638

Experimental info

Sequence conflict158 – 1603TPY → DPL in AAA51744. Ref.1
Sequence conflict158 – 1603TPY → DPL in AAA51745. Ref.2
Sequence conflict3271Q → T in AAA96731. Ref.3
Sequence conflict3271Q → T in AAA51748. Ref.8

Secondary structure

.............. 396
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06727 [UniParc].

Last modified March 7, 2006. Version 3.
Checksum: 193753196CA2FA4A

FASTA39645,399
        10         20         30         40         50         60 
MFLKAVVLTL ALVAVAGARA EVSADQVATV MWDYFSQLSN NAKEAVEHLQ KSELTQQLNA 

        70         80         90        100        110        120 
LFQDKLGEVN TYAGDLQKKL VPFATELHER LAKDSEKLKE EIGKELEELR ARLLPHANEV 

       130        140        150        160        170        180 
SQKIGDNLRE LQQRLEPYAD QLRTQVNTQA EQLRRQLTPY AQRMERVLRE NADSLQASLR 

       190        200        210        220        230        240 
PHADELKAKI DQNVEELKGR LTPYADEFKV KIDQTVEELR RSLAPYAQDT QEKLNHQLEG 

       250        260        270        280        290        300 
LTFQMKKNAE ELKARISASA EELRQRLAPL AEDVRGNLRG NTEGLQKSLA ELGGHLDQQV 

       310        320        330        340        350        360 
EEFRRRVEPY GENFNKALVQ QMEQLRQKLG PHAGDVEGHL SFLEKDLRDK VNSFFSTFKE 

       370        380        390 
KESQDKTLSL PELEQQQEQQ QEQQQEQVQM LAPLES 

« Hide

References

« Hide 'large scale' references
[1]"Structure, evolution, and tissue-specific synthesis of human apolipoprotein AIV."
Karathanasis S.K., Yunis I.
Biochemistry 25:3962-3970(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LYS-279.
[2]"Structure, evolution, and polymorphisms of the human apolipoprotein A4 gene (APOA4)."
Karathanasis S.K., Oettgen P., Haddad I.A., Antonarakis S.E.
Proc. Natl. Acad. Sci. U.S.A. 83:8457-8461(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LYS-279.
[3]"Structure and expression of the human apolipoprotein A-IV gene."
Elshourbagy N.A., Walker D.W., Paik Y.K., Boguski M.S., Freeman M., Gordon J.I., Taylor J.M.
J. Biol. Chem. 262:7973-7981(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT APOA-IV*2 HIS-380.
[4]"The primary structure of human apolipoprotein A-IV."
Yang C., Gu Z.W., Xiong W., Rosseneu M., Yang H.X., Lee B.M., Gotto A.M. Jr., Chan L.
Biochim. Biophys. Acta 1002:231-237(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Intestine.
[5]"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], VARIANTS MET-13; HIS-77; SER-147; SER-161; SER-367 AND HIS-380.
[6]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT SER-147.
[7]"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 Colon.
[8]"The nucleotide and derived amino acid sequence of human apolipoprotein A-IV mRNA and the close linkage of its gene to the genes of apolipoproteins A-I and C-III."
Elshourbagy N.A., Walker D.W., Boguski M.S., Gordon J.I., Taylor J.M.
J. Biol. Chem. 261:1998-2002(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 21-396, VARIANT APOA-IV*2 HIS-380.
[9]"Biosynthesis of human preapolipoprotein A-IV."
Gordon J.I., Bisgaier C.L., Sims H.F., Sachdev O.P., Glickman R.M., Strauss A.W.
J. Biol. Chem. 259:468-474(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: SIGNAL SEQUENCE CLEAVAGE SITE.
[10]"Genetic polymorphism of apolipoprotein A-IV."
Lohse P., Brewer H.B. Jr.
Curr. Opin. Lipidol. 2:90-95(1991)
Cited for: REVIEW ON POLYMORPHISM.
[11]"Genetic polymorphism of human plasma apolipoprotein A-IV is due to nucleotide substitutions in the apolipoprotein A-IV gene."
Lohse P., Kindt M.R., Rader D.J., Brewer H.B. Jr.
J. Biol. Chem. 265:10061-10064(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: ALLELES APOA-IV*1 AND APOA-IV*2, VARIANT HIS-380.
[12]"Human plasma apolipoproteins A-IV-0 and A-IV-3. Molecular basis for two rare variants of apolipoprotein A-IV-1."
Lohse P., Kindt M.R., Rader D.J., Brewer H.B. Jr.
J. Biol. Chem. 265:12734-12739(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: ALLELES A-IV*0 AND A-IV*3, VARIANTS LYS-250 AND GLU-GLN-GLN-GLN-381 INS.
[13]"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].
[14]"The structure of dimeric apolipoprotein A-IV and its mechanism of self-association."
Deng X., Morris J., Dressmen J., Tubb M.R., Tso P., Jerome W.G., Davidson W.S., Thompson T.B.
Structure 20:767-779(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 84-355, SUBUNIT.
[15]"The mutation causing the common apolipoprotein A-IV polymorphism is a glutamine to histidine substitution of amino acid 360."
Tenkanen H., Lukka M., Jauhiainen M., Metso J., Baumann M., Peltonen L., Ehnholm C.
Arterioscler. Thromb. 11:851-856(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HIS-380.
[16]"Three genetic variants of human plasma apolipoprotein A-IV: apoA-IV-1(Thr-347-->Ser), apoA-IV-0(Lys-167-->Glu,Gln-360-->His), and apoA-IV-3(Glu-165-->Lys)."
Lohse P., Kindt M.R., Rader D.J., Brewer H.B. Jr.
J. Biol. Chem. 266:13513-13518(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: ALLELES A-IV*0; A-IV*1; A-IV*2 AND A-IV*3, VARIANTS LYS-185; GLU-187; SER-367 AND HIS-380.
[17]Erratum
Lohse P., Kindt M.R., Rader D.J., Brewer H.B. Jr.
J. Biol. Chem. 266:19866-19866(1991)
[18]"Nonsynonymous polymorphic sites in the apolipoprotein (apo) A-IV gene are associated with changes in the concentration of apo B- and apo A-I-containing lipoproteins in a normal population."
von Eckardstein A., Funke H., Schulte M., Erren M., Schulte H., Assmann G.
Am. J. Hum. Genet. 50:1115-1128(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MET-13.
[19]"A novel polymorphism of apolipoprotein A-IV is the result of an asparagine to serine substitution at residue 127."
Tenkanen H., Koskinen P., Metso J., Baumann M., Lukka M., Kauppinen-Makelin R., Kontula K., Taskinen M.R., Manttari M., Manninen V., Ehnholm C.
Biochim. Biophys. Acta 1138:27-33(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SER-147.
[20]"Molecular basis of a unique African variant (A-IV 5) of human apolipoprotein A-IV and its significance in lipid metabolism."
Kamboh M.I., Williams E.R., Law J.C., Aston C.E., Bunker C.H., Ferrell R.E., Pollitzer W.S.
Genet. Epidemiol. 9:379-388(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: ALLELE A-IV*5, VARIANT GLU-GLN-GLN-GLN-381 INS.
[21]"Apolipoprotein A-IV polymorphism in the Hungarian population: gene frequencies, effect on lipid levels, and sequence of two new variants."
Menzel H.J., Dieplinger H., Sandholzer C., Karadi I., Utermann G., Csaszar A.
Hum. Mutat. 5:58-65(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS BUDAPEST-2 LYS-44; BUDAPEST-1 CYS-305 AND SER-367.
[22]"Two novel apolipoprotein A-IV variants in individuals with familial combined hyperlipidemia and diminished levels of lipoprotein lipase activity."
Deeb S.S., Nevin D.N., Iwasaki L., Brunzell J.D.
Hum. Mutat. 8:319-325(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SEATTLE-3 SER-161; SEATTLE-1 LEU-178 AND SEATTLE-2 GLN-264.
[23]"Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis."
Halushka M.K., Fan J.-B., Bentley K., Hsie L., Shen N., Weder A., Cooper R., Lipshutz R., Chakravarti A.
Nat. Genet. 22:239-247(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HIS-380.
+Additional computationally mapped references.

Web resources

SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M13654 mRNA. Translation: AAA51744.1.
M14642 Genomic DNA. Translation: AAA51745.1.
J02758 Genomic DNA. Translation: AAA96731.1.
X13629 mRNA. Translation: CAA31955.1.
AY422950 Genomic DNA. Translation: AAQ91809.1.
AY555191 Genomic DNA. Translation: AAS68228.1.
AP006216 Genomic DNA. No translation available.
BC074764 mRNA. Translation: AAH74764.1.
BC113594 mRNA. Translation: AAI13595.1.
BC113596 mRNA. Translation: AAI13597.1.
M14566 mRNA. Translation: AAA51748.1.
CCDSCCDS31681.1.
PIRLPHUA4. A94137.
UniGeneHs.1247.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3S84X-ray2.40A/B84-355[»]
ProteinModelPortalP06727.
SMRP06727. Positions 25-389.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-38333N.
IntActP06727. 1 interaction.
STRING9606.ENSP00000350425.

PTM databases

PhosphoSiteP06727.

Polymorphism databases

DMDM93163358.

2D gel databases

DOSAC-COBS-2DPAGEP06727.
REPRODUCTION-2DPAGEIPI00304273.
SWISS-2DPAGEP06727.

Proteomic databases

MaxQBP06727.
PaxDbP06727.
PeptideAtlasP06727.
PRIDEP06727.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000357780; ENSP00000350425; ENSG00000110244.
UCSCuc001pps.1. human.

Organism-specific databases

GeneCardsGC11M116692.
HGNCHGNC:602. APOA4.
HPAHPA001352.
HPA002549.
MIM107690. gene.
neXtProtNX_P06727.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG42418.
HOGENOMHOG000037942.
HOVERGENHBG105707.
InParanoidP06727.
OrthoDBEOG7K9K48.
PhylomeDBP06727.
TreeFamTF334458.

Enzyme and pathway databases

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

Gene expression databases

BgeeP06727.
CleanExHS_APOA4.
GenevestigatorP06727.

Family and domain databases

InterProIPR000074. ApoA1_A4_E.
[Graphical view]
PfamPF01442. Apolipoprotein. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

PMAP-CutDBA8MSL6.
PROP06727.
SOURCESearch...

Entry information

Entry nameAPOA4_HUMAN
AccessionPrimary (citable) accession number: P06727
Secondary accession number(s): A8MSL6, Q14CW8, Q6Q787
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: March 7, 2006
Last modified: July 9, 2014
This is version 163 of the entry and version 3 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