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P02749 (APOH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 171. 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·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-2-glycoprotein 1
Alternative name(s):
APC inhibitor
Activated protein C-binding protein
Anticardiolipin cofactor
Apolipoprotein H
Short name=Apo-H
Beta-2-glycoprotein I
Short name=B2GPI
Short name=Beta(2)GPI
Gene names
Name:APOH
Synonyms:B2G1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length345 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds to various kinds of negatively charged substances such as heparin, phospholipids, and dextran sulfate. May prevent activation of the intrinsic blood coagulation cascade by binding to phospholipids on the surface of damaged cells.

Subcellular location

Secreted.

Tissue specificity

Expressed by the liver and secreted in plasma.

Post-translational modification

N- and O-glycosylated. Ref.10 also reports glycosylation on 'Asn-188' for their allele. Ref.10 Ref.15 Ref.21

Sequence similarities

Contains 4 Sushi (CCP/SCR) domains.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainRepeat
Signal
Sushi
   LigandHeparin-binding
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation, intrinsic pathway

Inferred from direct assay PubMed 4052628. Source: BHF-UCL

negative regulation of angiogenesis

Inferred from direct assay PubMed 17872974. Source: BHF-UCL

negative regulation of blood coagulation

Inferred from direct assay PubMed 4052628. Source: BHF-UCL

negative regulation of endothelial cell migration

Inferred from direct assay PubMed 17872974. Source: BHF-UCL

negative regulation of endothelial cell proliferation

Inferred from direct assay PubMed 17872974. Source: BHF-UCL

negative regulation of fibrinolysis

Inferred from direct assay PubMed 14726399. Source: BHF-UCL

negative regulation of myeloid cell apoptotic process

Inferred from direct assay PubMed 15534879. Source: BHF-UCL

negative regulation of smooth muscle cell apoptotic process

Inferred from direct assay PubMed 15534879. Source: BHF-UCL

plasminogen activation

Inferred from direct assay PubMed 16480936. Source: BHF-UCL

positive regulation of blood coagulation

Traceable author statement PubMed 16480936. Source: BHF-UCL

positive regulation of lipoprotein lipase activity

Inferred from direct assay PubMed 7417307. Source: BHF-UCL

regulation of fibrinolysis

Inferred from direct assay PubMed 16480936. Source: BHF-UCL

triglyceride metabolic process

Inferred from direct assay PubMed 7417307. Source: BHF-UCL

triglyceride transport

Inferred from sequence or structural similarity PubMed 7078428. Source: BHF-UCL

   Cellular_componentcell surface

Inferred from direct assay PubMed 16480936. Source: BHF-UCL

chylomicron

Inferred from direct assay PubMed 222615. Source: BHF-UCL

extracellular space

Inferred from direct assay PubMed 15486070PubMed 20551380. Source: BHF-UCL

high-density lipoprotein particle

Inferred from direct assay PubMed 222615. Source: BHF-UCL

very-low-density lipoprotein particle

Inferred from direct assay PubMed 222615. Source: BHF-UCL

   Molecular_functionglycoprotein binding

Inferred from physical interaction PubMed 9269765. Source: BHF-UCL

heparin binding

Inferred from electronic annotation. Source: UniProtKB-KW

identical protein binding

Inferred from physical interaction PubMed 18822289. Source: IntAct

lipid binding

Inferred from direct assay PubMed 222615. Source: BHF-UCL

lipoprotein lipase activator activity

Inferred from direct assay PubMed 7417307. Source: BHF-UCL

phospholipid binding

Inferred from direct assay PubMed 15486070. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 9269765. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-2114682,EBI-2114682
LPAP085194EBI-2114682,EBI-9232288

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.10 Ref.11 Ref.12 Ref.13
Chain20 – 345326Beta-2-glycoprotein 1
PRO_0000002059

Regions

Domain21 – 8161Sushi 1
Domain82 – 13958Sushi 2
Domain140 – 20263Sushi 3
Domain203 – 26260Sushi 4
Region263 – 34583Sushi-like

Amino acid modifications

Glycosylation1491O-linked (GalNAc...)
Glycosylation1621N-linked (GlcNAc...) (complex) Ref.10 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22
Glycosylation1831N-linked (GlcNAc...) Ref.10 Ref.17 Ref.18 Ref.20
Glycosylation1931N-linked (GlcNAc...) Ref.10 Ref.17 Ref.18 Ref.20
Glycosylation2531N-linked (GlcNAc...) Ref.10 Ref.16 Ref.18 Ref.19 Ref.20
Disulfide bond23 ↔ 66 Ref.10 Ref.14
Disulfide bond51 ↔ 79 Ref.10 Ref.14
Disulfide bond84 ↔ 124 Ref.10 Ref.14
Disulfide bond110 ↔ 137 Ref.10 Ref.14
Disulfide bond142 ↔ 188 Ref.10 Ref.14
Disulfide bond174 ↔ 200 Ref.10 Ref.14
Disulfide bond205 ↔ 248 Ref.10 Ref.14
Disulfide bond234 ↔ 260 Ref.10 Ref.14
Disulfide bond264 ↔ 315 Ref.10 Ref.14
Disulfide bond300 ↔ 325 Ref.10 Ref.14
Disulfide bond307 ↔ 345 Ref.10 Ref.14

Natural variations

Natural variant51V → A.
Corresponds to variant rs3826358 [ dbSNP | Ensembl ].
VAR_048316
Natural variant1071S → N in allele APOH*1. Ref.7 Ref.8 Ref.27
Corresponds to variant rs1801692 [ dbSNP | Ensembl ].
VAR_008169
Natural variant1541R → H. Ref.8
Corresponds to variant rs8178847 [ dbSNP | Ensembl ].
VAR_019155
Natural variant2661V → L in 23% of the population. Ref.8 Ref.26
Corresponds to variant rs4581 [ dbSNP | Ensembl ].
VAR_000673
Natural variant3251C → G Loss of phosphatidylserine-binding. Ref.28
Corresponds to variant rs1801689 [ dbSNP | Ensembl ].
VAR_008170
Natural variant3351W → S in allele APOH*3W; loss of phosphatidylserine-binding. Ref.8 Ref.28
Corresponds to variant rs1801690 [ dbSNP | Ensembl ].
VAR_008171

Experimental info

Sequence conflict1211S → C AA sequence Ref.10
Sequence conflict1881C → N AA sequence Ref.10

Secondary structure

....................................................................... 345
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02749 [UniParc].

Last modified June 1, 1994. Version 3.
Checksum: 63101704F8EDFE3F

FASTA34538,298
        10         20         30         40         50         60 
MISPVLILFS SFLCHVAIAG RTCPKPDDLP FSTVVPLKTF YEPGEEITYS CKPGYVSRGG 

        70         80         90        100        110        120 
MRKFICPLTG LWPINTLKCT PRVCPFAGIL ENGAVRYTTF EYPNTISFSC NTGFYLNGAD 

       130        140        150        160        170        180 
SAKCTEEGKW SPELPVCAPI ICPPPSIPTF ATLRVYKPSA GNNSLYRDTA VFECLPQHAM 

       190        200        210        220        230        240 
FGNDTITCTT HGNWTKLPEC REVKCPFPSR PDNGFVNYPA KPTLYYKDKA TFGCHDGYSL 

       250        260        270        280        290        300 
DGPEEIECTK LGNWSAMPSC KASCKVPVKK ATVVYQGERV KIQEKFKNGM LHGDKVSFFC 

       310        320        330        340 
KNKEKKCSYT EDAQCIDGTI EVPKCFKEHS SLAFWKTDAS DVKPC 

« Hide

References

« Hide 'large scale' references
[1]"Complete nucleotide and deduced amino acid sequence of human beta 2-glycoprotein I."
Steinkasserer A., Estaller C., Weiss E., Sim R.B., Day A.J.
Biochem. J. 277:387-391(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Molecular cloning and mammalian expression of human beta 2-glycoprotein I cDNA."
Kristensen T., Schousboe I., Boel E., Mulvihill E.M., Hansen R.R., Moeller K.B., Moeller N.P.H., Sottrup-Jensen L.
FEBS Lett. 289:183-186(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[3]"Nucleotide sequence and expression of the human gene encoding apolipoprotein H (beta 2-glycoprotein I)."
Mehdi H., Nunn M., Steel D.M., Whitehead A.S., Perez M., Walker L., Peeples M.E.
Gene 108:293-298(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[4]"Molecular cloning and sequence analysis of the cDNA encoding human apolipoprotein H (beta 2-glycoprotein I)."
Day J.R., O'Hara P.J., Grant F.J., Lofton-Day C.E., Berkaw M.N., Werner P., Arnaud P.
Int. J. Clin. Lab. Res. 21:256-263(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"Molecular definition of human beta 2-glycoprotein I (beta 2-GPI) by cDNA cloning and inter-species differences of beta 2-GPI in alternation of anticardiolipin binding."
Matsuura E., Igarashi M., Igarashi Y., Nagae H., Ichikawa K., Yasuda T., Koike T.
Int. Immunol. 3:1217-1221(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]"Structure of the human beta2-glycoprotein I (apolipoprotein H) gene."
Okkels H., Rasmussen T.E., Sanghera D.K., Kamboh M.I., Kristensen T.
Eur. J. Biochem. 259:435-440(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]"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], VARIANT ASN-107.
Tissue: Liver.
[8]SeattleSNPs variation discovery resource
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASN-107; HIS-154; LEU-266 AND SER-335.
[9]"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: Liver.
[10]"Complete amino acid sequence of human plasma beta 2-glycoprotein I."
Lozier J., Takahashi N., Putnam F.W.
Proc. Natl. Acad. Sci. U.S.A. 81:3640-3644(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-345, GLYCOSYLATION AT ASN-162; ASN-183; ASN-193 AND ASN-253, DISULFIDE BONDS.
[11]"Heterogeneity of anticardiolipin antibodies defined by the anticardiolipin cofactor."
Matsuura E., Igarashi Y., Fujimoto M., Ichikawa K., Suzuki T., Sumida T., Yasuda T., Koike T.
J. Immunol. 148:3885-3891(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-44.
[12]"Anti-phospholipid antibodies are directed against a complex antigen that includes a lipid-binding inhibitor of coagulation: beta 2-glycoprotein I (apolipoprotein H)."
McNeil H.P., Simpson R.J., Chesterman C.N., Krilis S.A.
Proc. Natl. Acad. Sci. U.S.A. 87:4120-4124(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-43.
[13]"Purification of apolipoprotein H (beta 2-glycoprotein I)-like protein from human follicular fluid."
Aleporou-Marinou V., Pappa H., Yalouris P., Patargias T.
Comp. Biochem. Physiol. 128B:537-542(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-38.
Tissue: Ovarian follicular fluid.
[14]"Activity, disulphide mapping and structural modelling of the fifth domain of human beta 2-glycoprotein I."
Steinkkasserer A., Barlow P.N., Willis A.C., Kertesz Z., Campbell I.D., Sim R.B., Norman D.G.
FEBS Lett. 313:193-197(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS IN C-TERMINAL DOMAIN.
[15]"Qualitative analysis of the carbohydrate composition of apolipoprotein H."
Gambino R., Ruiu G., Pagano G., Cassader M.
J. Protein Chem. 16:205-212(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE OF CARBOHYDRATES.
[16]"A proteomic analysis of human bile."
Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.
Mol. Cell. Proteomics 3:715-728(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162 AND ASN-253.
Tissue: Bile.
[17]"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-162; ASN-183 AND ASN-193.
Tissue: Plasma.
[18]"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-162; ASN-183; ASN-193 AND ASN-253.
Tissue: Plasma.
[19]"Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry."
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.
J. Proteome Res. 5:1493-1503(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162 AND ASN-253.
Tissue: Saliva.
[20]"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-162; ASN-183; ASN-193 AND ASN-253.
Tissue: Liver.
[21]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-162.
[22]"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-162, STRUCTURE OF CARBOHYDRATES.
Tissue: Cerebrospinal fluid.
[23]"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].
[24]"Adhesion mechanism of human beta(2)-glycoprotein I to phospholipids based on its crystal structure."
Bouma B., de Groot P.G., van Den Elsen J.M.H., Ravelli R.B.G., Schouten A., Simmelink M.J.A., Derksen R.H.W.M., Kroon J., Gros P.
EMBO J. 18:5166-5174(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
Tissue: Plasma.
[25]"Crystal structure of human beta2-glycoprotein I: implications for phospholipid binding and the antiphospholipid syndrome."
Schwarzenbacher R., Zeth K., Diederichs K., Gries A., Kostner G.M., Laggner P., Prassl R.
EMBO J. 18:6228-6239(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.87 ANGSTROMS).
[26]"Human beta 2-glycoprotein I: molecular analysis of DNA and amino acid polymorphism."
Steinkasserer A., Doerner C., Wuerzner R., Sim R.B.
Hum. Genet. 91:401-402(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LEU-266.
[27]"Molecular basis of the apolipoprotein H (beta 2-glycoprotein I) protein polymorphism."
Sanghera D.K., Kristensen T., Hamman R.F., Kamboh M.I.
Hum. Genet. 100:57-62(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ASN-107.
[28]"Identification of structural mutations in the fifth domain of apolipoprotein H (beta-2-glycoprotein I) which affect phospholipid binding."
Sanghera D.K., Wagenknecht D.R., McIntyre J.A., Kamboh M.I.
Hum. Mol. Genet. 6:311-316(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLY-325 AND SER-335.
+Additional computationally mapped references.

Web resources

SeattleSNPs
SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X58100 mRNA. Translation: CAA41113.1.
X53595 mRNA. Translation: CAA37664.1.
X57847 mRNA. Translation: CAA40977.1.
M62839 mRNA. Translation: AAA51766.1.
S80305 mRNA. Translation: AAB21330.1.
Y11493 expand/collapse EMBL AC list , Y11494, Y11495, X53595, Y11496, Y11497, Y11498 Genomic DNA. Translation: CAA72279.1.
Y17754 Genomic DNA. Translation: CAA76845.1.
AK313838 mRNA. Translation: BAG36570.1.
AY322156 Genomic DNA. Translation: AAP72014.1.
BC020703 mRNA. Translation: AAH20703.1.
BC026283 mRNA. Translation: AAH26283.1.
CCDSCCDS11663.1.
PIRNBHU. S17178.
RefSeqNP_000033.2. NM_000042.2.
UniGeneHs.445358.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1C1ZX-ray2.87A20-345[»]
1G4FNMR-A261-345[»]
1G4GNMR-A261-345[»]
1QUBX-ray2.70A20-345[»]
2KRINMR-A263-345[»]
3OP8X-ray1.90A/B263-345[»]
4JHSX-ray3.00A203-345[»]
ProteinModelPortalP02749.
SMRP02749. Positions 20-345.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106847. 11 interactions.
DIPDIP-46878N.
IntActP02749. 9 interactions.
MINTMINT-6743724.
STRING9606.ENSP00000205948.

Chemistry

BindingDBP02749.

PTM databases

PhosphoSiteP02749.

Polymorphism databases

DMDM543826.

Proteomic databases

MaxQBP02749.
PaxDbP02749.
PeptideAtlasP02749.
PRIDEP02749.

Protocols and materials databases

DNASU350.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000205948; ENSP00000205948; ENSG00000091583.
GeneID350.
KEGGhsa:350.
UCSCuc002jfn.4. human.

Organism-specific databases

CTD350.
GeneCardsGC17M064208.
HGNCHGNC:616. APOH.
HPACAB022214.
HPA001654.
HPA003732.
MIM138700. gene.
neXtProtNX_P02749.
PharmGKBPA24903.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG323950.
HOGENOMHOG000034008.
HOVERGENHBG004271.
InParanoidP02749.
KOK17305.
OMARFTCPLT.
OrthoDBEOG7K6PV8.
PhylomeDBP02749.
TreeFamTF334137.

Gene expression databases

ArrayExpressP02749.
BgeeP02749.
CleanExHS_APOH.
GenevestigatorP02749.

Family and domain databases

InterProIPR015104. Sushi_2.
IPR000436. Sushi_SCR_CCP.
[Graphical view]
PfamPF00084. Sushi. 4 hits.
PF09014. Sushi_2. 1 hit.
[Graphical view]
ProDomPD012422. Sushi_2. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00032. CCP. 4 hits.
[Graphical view]
SUPFAMSSF57535. SSF57535. 5 hits.
PROSITEPS50923. SUSHI. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAPOH. human.
EvolutionaryTraceP02749.
GeneWikiApolipoprotein_H.
GenomeRNAi350.
NextBio1441.
PMAP-CutDBP02749.
PROP02749.
SOURCESearch...

Entry information

Entry nameAPOH_HUMAN
AccessionPrimary (citable) accession number: P02749
Secondary accession number(s): B2R9M3, Q9UCN7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 1, 1994
Last modified: July 9, 2014
This is version 171 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 17

Human chromosome 17: entries, gene names and cross-references to MIM