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P05090

- APOD_HUMAN

UniProt

P05090 - APOD_HUMAN

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Protein

Apolipoprotein D

Gene

APOD

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

Functioni

APOD occurs in the macromolecular complex with lecithin-cholesterol acyltransferase. It is probably involved in the transport and binding of bilin. Appears to be able to transport a variety of ligands in a number of different contexts.

GO - Molecular functioni

  1. cholesterol binding Source: UniProtKB
  2. lipid transporter activity Source: UniProtKB

GO - Biological processi

  1. aging Source: UniProtKB
  2. angiogenesis Source: UniProtKB
  3. brain development Source: UniProtKB
  4. glucose metabolic process Source: UniProtKB
  5. lipid metabolic process Source: UniProtKB
  6. lipid transport Source: GOC
  7. negative regulation of cytokine production involved in inflammatory response Source: UniProtKB
  8. negative regulation of focal adhesion assembly Source: UniProtKB
  9. negative regulation of lipoprotein lipid oxidation Source: UniProtKB
  10. negative regulation of monocyte chemotactic protein-1 production Source: UniProtKB
  11. negative regulation of platelet-derived growth factor receptor signaling pathway Source: UniProtKB
  12. negative regulation of protein import into nucleus Source: UniProtKB
  13. negative regulation of smooth muscle cell-matrix adhesion Source: UniProtKB
  14. negative regulation of smooth muscle cell proliferation Source: UniProtKB
  15. negative regulation of T cell migration Source: UniProtKB
  16. peripheral nervous system axon regeneration Source: UniProtKB
  17. response to axon injury Source: UniProtKB
  18. response to drug Source: UniProtKB
  19. response to reactive oxygen species Source: UniProtKB
  20. tissue regeneration Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Apolipoprotein D
Short name:
Apo-D
Short name:
ApoD
Gene namesi
Name:APOD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:612. APOD.

Subcellular locationi

GO - Cellular componenti

  1. cytosolic ribosome Source: UniProtKB
  2. dendrite Source: UniProtKB
  3. endoplasmic reticulum Source: UniProtKB
  4. extracellular region Source: UniProtKB
  5. extracellular space Source: UniProtKB
  6. extracellular vesicular exosome Source: UniProtKB
  7. neuronal cell body Source: UniProtKB
  8. perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24900.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20201 PublicationAdd
BLAST
Chaini21 – 189169Apolipoprotein DPRO_0000017872Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211Pyrrolidone carboxylic acid2 Publications
Disulfide bondi28 ↔ 1341 Publication
Disulfide bondi61 ↔ 1851 Publication
Glycosylationi65 – 651N-linked (GlcNAc...) (complex)4 Publications
Glycosylationi98 – 981N-linked (GlcNAc...) (complex)8 Publications
Disulfide bondi136 – 136Interchain (with C-29 in APOA2)1 Publication

Post-translational modificationi

N-glycosylatd. N-glycan heterogeneity at Asn-65: Hex5HexNAc4 (major) and Hex6HexNAc5 (minor); at Asn-98: Hex5HexNAc4 (minor), dHex1Hex5HexNAc4 (major), dHex1Hex6HexNAc5 (minor) and dHex1Hex7HexNAc6 (minor).8 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

MaxQBiP05090.
PaxDbiP05090.
PeptideAtlasiP05090.
PRIDEiP05090.

2D gel databases

SWISS-2DPAGEP05090.

PTM databases

PhosphoSiteiP05090.

Expressioni

Tissue specificityi

Expressed in liver, intestine, pancreas, kidney, placenta, adrenal, spleen, fetal brain tissue and tears.

Gene expression databases

BgeeiP05090.
CleanExiHS_APOD.
ExpressionAtlasiP05090. baseline and differential.
GenevestigatoriP05090.

Interactioni

Subunit structurei

Homodimer. In plasma, also exists as a disulfide-linked heterodimer with APOA2.1 Publication

Protein-protein interaction databases

BioGridi106844. 15 interactions.
IntActiP05090. 5 interactions.
MINTiMINT-1396020.
STRINGi9606.ENSP00000345179.

Structurei

Secondary structure

1
189
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi24 – 274
Helixi39 – 413
Beta strandi44 – 518
Beta strandi60 – 689
Beta strandi74 – 818
Beta strandi87 – 9711
Beta strandi104 – 1085
Beta strandi116 – 1238
Beta strandi125 – 13814
Beta strandi141 – 15313
Helixi157 – 16913
Beta strandi183 – 1853

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2APDmodel-A21-189[»]
2HZQX-ray1.80A23-189[»]
2HZRX-ray1.80A23-189[»]
ProteinModelPortaliP05090.
SMRiP05090. Positions 23-188.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05090.

Family & Domainsi

Sequence similaritiesi

Belongs to the calycin superfamily. Lipocalin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3040.
GeneTreeiENSGT00510000046981.
HOGENOMiHOG000061525.
HOVERGENiHBG018734.
InParanoidiP05090.
KOiK03098.
PhylomeDBiP05090.
TreeFamiTF324836.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR026222. ApoD_vertbrte.
IPR002969. ApolipopD.
IPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR022271. Lipocalin_ApoD.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PIRSFiPIRSF036893. Lipocalin_ApoD. 1 hit.
PRINTSiPR02058. APODVERTBRTE.
PR01219. APOLIPOPROTD.
PR00179. LIPOCALIN.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00213. LIPOCALIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P05090 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVMLLLLLSA LAGLFGAAEG QAFHLGKCPN PPVQENFDVN KYLGRWYEIE
60 70 80 90 100
KIPTTFENGR CIQANYSLME NGKIKVLNQE LRADGTVNQI EGEATPVNLT
110 120 130 140 150
EPAKLEVKFS WFMPSAPYWI LATDYENYAL VYSCTCIIQL FHVDFAWILA
160 170 180
RNPNLPPETV DSLKNILTSN NIDVKKMTVT DQVNCPKLS
Length:189
Mass (Da):21,276
Last modified:August 13, 1987 - v1
Checksum:i0EAA6DE03D5E71A8
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti15 – 151F → S.1 Publication
Corresponds to variant rs5952 [ dbSNP | Ensembl ].
VAR_011931
Natural varianti115 – 1151S → L.1 Publication
Corresponds to variant rs5954 [ dbSNP | Ensembl ].
VAR_011932
Natural varianti178 – 1781T → K.1 Publication
Corresponds to variant rs5955 [ dbSNP | Ensembl ].
VAR_011933

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02611 mRNA. Translation: AAB59517.1.
M16696 Genomic DNA. Translation: AAA51764.1.
BT019860 mRNA. Translation: AAV38663.1.
BT019861 mRNA. Translation: AAV38664.1.
CR456838 mRNA. Translation: CAG33119.1.
CR541773 mRNA. Translation: CAG46572.1.
AK312090 mRNA. Translation: BAG35026.1.
CH471052 Genomic DNA. Translation: EAW78023.1.
CH471052 Genomic DNA. Translation: EAW78024.1.
BC007402 mRNA. Translation: AAH07402.1.
S80440 mRNA. Translation: AAB35919.1.
CCDSiCCDS33925.1.
PIRiA26958. LPHUD.
RefSeqiNP_001638.1. NM_001647.3.
UniGeneiHs.522555.

Genome annotation databases

EnsembliENST00000343267; ENSP00000345179; ENSG00000189058.
GeneIDi347.
KEGGihsa:347.
UCSCiuc003fur.2. human.

Polymorphism databases

DMDMi114034.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02611 mRNA. Translation: AAB59517.1 .
M16696 Genomic DNA. Translation: AAA51764.1 .
BT019860 mRNA. Translation: AAV38663.1 .
BT019861 mRNA. Translation: AAV38664.1 .
CR456838 mRNA. Translation: CAG33119.1 .
CR541773 mRNA. Translation: CAG46572.1 .
AK312090 mRNA. Translation: BAG35026.1 .
CH471052 Genomic DNA. Translation: EAW78023.1 .
CH471052 Genomic DNA. Translation: EAW78024.1 .
BC007402 mRNA. Translation: AAH07402.1 .
S80440 mRNA. Translation: AAB35919.1 .
CCDSi CCDS33925.1.
PIRi A26958. LPHUD.
RefSeqi NP_001638.1. NM_001647.3.
UniGenei Hs.522555.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2APD model - A 21-189 [» ]
2HZQ X-ray 1.80 A 23-189 [» ]
2HZR X-ray 1.80 A 23-189 [» ]
ProteinModelPortali P05090.
SMRi P05090. Positions 23-188.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106844. 15 interactions.
IntActi P05090. 5 interactions.
MINTi MINT-1396020.
STRINGi 9606.ENSP00000345179.

PTM databases

PhosphoSitei P05090.

Polymorphism databases

DMDMi 114034.

2D gel databases

SWISS-2DPAGE P05090.

Proteomic databases

MaxQBi P05090.
PaxDbi P05090.
PeptideAtlasi P05090.
PRIDEi P05090.

Protocols and materials databases

DNASUi 347.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000343267 ; ENSP00000345179 ; ENSG00000189058 .
GeneIDi 347.
KEGGi hsa:347.
UCSCi uc003fur.2. human.

Organism-specific databases

CTDi 347.
GeneCardsi GC03M195295.
HGNCi HGNC:612. APOD.
MIMi 107740. gene.
neXtProti NX_P05090.
PharmGKBi PA24900.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG3040.
GeneTreei ENSGT00510000046981.
HOGENOMi HOG000061525.
HOVERGENi HBG018734.
InParanoidi P05090.
KOi K03098.
PhylomeDBi P05090.
TreeFami TF324836.

Miscellaneous databases

ChiTaRSi APOD. human.
EvolutionaryTracei P05090.
GeneWikii Apolipoprotein_D.
GenomeRNAii 347.
NextBioi 1431.
PROi P05090.
SOURCEi Search...

Gene expression databases

Bgeei P05090.
CleanExi HS_APOD.
ExpressionAtlasi P05090. baseline and differential.
Genevestigatori P05090.

Family and domain databases

Gene3Di 2.40.128.20. 1 hit.
InterProi IPR026222. ApoD_vertbrte.
IPR002969. ApolipopD.
IPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR022271. Lipocalin_ApoD.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view ]
Pfami PF00061. Lipocalin. 1 hit.
[Graphical view ]
PIRSFi PIRSF036893. Lipocalin_ApoD. 1 hit.
PRINTSi PR02058. APODVERTBRTE.
PR01219. APOLIPOPROTD.
PR00179. LIPOCALIN.
SUPFAMi SSF50814. SSF50814. 1 hit.
PROSITEi PS00213. LIPOCALIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of human apolipoprotein D cDNA."
    Drayna D.T., Fielding C., McLean J.W., Baer B., Castro G., Chen E., Comstock L., Henzel W., Kohr W., Rhee L., Wion K.L., Lawn R.M.
    J. Biol. Chem. 261:16535-16539(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Human apolipoprotein D gene: gene sequence, chromosome localization, and homology to the alpha 2u-globulin superfamily."
    Drayna D.T., McLean J.W., Wion K.L., Trent J.M., Drabkin H.A., Lawn R.M.
    DNA 6:199-204(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "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: Cerebellum.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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: Skin.
  9. "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: PROTEIN SEQUENCE OF 21-189, DISULFIDE BONDS, PYROGLUTAMATE FORMATION AT GLN-21, GLYCOSYLATION AT ASN-65 AND ASN-98.
    Tissue: Plasma.
  10. "The human lacrimal gland synthesizes apolipoprotein D mRNA in addition to tear prealbumin mRNA, both species encoding members of the lipocalin superfamily."
    Holzfeind P., Merschak P., Dieplinger H., Redl B.
    Exp. Eye Res. 61:495-500(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 92-189.
    Tissue: Lacrimal gland.
  11. "Apolipoprotein D is the major protein component in cyst fluid from women with human breast gross cystic disease."
    Balbin M., Freije J.M.P., Fueyo A., Sanchez L.M., Lopez-Otin C.
    Biochem. J. 271:803-807(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 128-187.
  12. "Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
    Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
    Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-98.
    Tissue: Plasma.
  13. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-98.
    Tissue: Plasma.
  14. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-65 AND ASN-98.
    Tissue: Liver.
  15. Cited for: GLYCOSYLATION AT ASN-98.
  16. "Enrichment of glycopeptides for glycan structure and attachment site identification."
    Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.
    Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-98, STRUCTURE OF CARBOHYDRATES.
    Tissue: Cerebrospinal fluid.
  17. "Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."
    Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.
    Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-65 AND ASN-98, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
  18. "Is apolipoprotein D a mammalian bilin-binding protein?"
    Peitsch M.C., Boguski M.S.
    New Biol. 2:197-206(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING, BILIN-BINDING.
  19. "Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion."
    Schindler P.A., Settineri C.A., Collet X., Fielding C.J., Burlingame A.L.
    Protein Sci. 4:791-803(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-65 AND ASN-98.
  20. Cited for: VARIANTS SER-15; LEU-115 AND LYS-178.

Entry informationi

Entry nameiAPOD_HUMAN
AccessioniPrimary (citable) accession number: P05090
Secondary accession number(s): B2R579, D3DNW6, Q6IBG6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: October 29, 2014
This is version 168 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

Miscellaneous

APOD is primarily localized in HDL (60-65%), with most of the remainder in VHDL and only trace amounts in VLDL and LDL.

Keywords - Technical termi

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

Documents

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

External Data

Dasty 3