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P02749

- APOH_HUMAN

UniProt

P02749 - APOH_HUMAN

Protein

Beta-2-glycoprotein 1

Gene

APOH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 173 (01 Oct 2014)
      Sequence version 3 (01 Jun 1994)
      Previous versions | rss
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    Functioni

    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.

    GO - Molecular functioni

    1. glycoprotein binding Source: BHF-UCL
    2. heparin binding Source: UniProtKB-KW
    3. identical protein binding Source: IntAct
    4. lipid binding Source: BHF-UCL
    5. lipoprotein lipase activator activity Source: BHF-UCL
    6. phospholipid binding Source: BHF-UCL
    7. protein binding Source: IntAct

    GO - Biological processi

    1. blood coagulation, intrinsic pathway Source: BHF-UCL
    2. negative regulation of angiogenesis Source: BHF-UCL
    3. negative regulation of blood coagulation Source: BHF-UCL
    4. negative regulation of endothelial cell migration Source: BHF-UCL
    5. negative regulation of endothelial cell proliferation Source: BHF-UCL
    6. negative regulation of fibrinolysis Source: BHF-UCL
    7. negative regulation of myeloid cell apoptotic process Source: BHF-UCL
    8. negative regulation of smooth muscle cell apoptotic process Source: BHF-UCL
    9. plasminogen activation Source: BHF-UCL
    10. positive regulation of blood coagulation Source: BHF-UCL
    11. positive regulation of lipoprotein lipase activity Source: BHF-UCL
    12. regulation of fibrinolysis Source: BHF-UCL
    13. triglyceride metabolic process Source: BHF-UCL
    14. triglyceride transport Source: BHF-UCL

    Keywords - Ligandi

    Heparin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:APOH
    Synonyms:B2G1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:616. APOH.

    Subcellular locationi

    GO - Cellular componenti

    1. cell surface Source: BHF-UCL
    2. chylomicron Source: BHF-UCL
    3. extracellular space Source: BHF-UCL
    4. extracellular vesicular exosome Source: UniProt
    5. high-density lipoprotein particle Source: BHF-UCL
    6. very-low-density lipoprotein particle Source: BHF-UCL

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24903.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 19194 PublicationsAdd
    BLAST
    Chaini20 – 345326Beta-2-glycoprotein 1PRO_0000002059Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi23 ↔ 66
    Disulfide bondi51 ↔ 79
    Disulfide bondi84 ↔ 124
    Disulfide bondi110 ↔ 137
    Disulfide bondi142 ↔ 188
    Glycosylationi149 – 1491O-linked (GalNAc...)
    Glycosylationi162 – 1621N-linked (GlcNAc...) (complex)8 Publications
    Disulfide bondi174 ↔ 200
    Glycosylationi183 – 1831N-linked (GlcNAc...)4 Publications
    Glycosylationi193 – 1931N-linked (GlcNAc...)4 Publications
    Disulfide bondi205 ↔ 248
    Disulfide bondi234 ↔ 260
    Glycosylationi253 – 2531N-linked (GlcNAc...)5 Publications
    Disulfide bondi264 ↔ 315
    Disulfide bondi300 ↔ 325
    Disulfide bondi307 ↔ 345

    Post-translational modificationi

    N- and O-glycosylated. PubMed:6587378 also reports glycosylation on 'Asn-188' for their allele.8 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP02749.
    PaxDbiP02749.
    PeptideAtlasiP02749.
    PRIDEiP02749.

    PTM databases

    PhosphoSiteiP02749.

    Miscellaneous databases

    PMAP-CutDBP02749.

    Expressioni

    Tissue specificityi

    Expressed by the liver and secreted in plasma.

    Gene expression databases

    ArrayExpressiP02749.
    BgeeiP02749.
    CleanExiHS_APOH.
    GenevestigatoriP02749.

    Organism-specific databases

    HPAiCAB022214.
    HPA001654.
    HPA003732.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-2114682,EBI-2114682
    LPAP085194EBI-2114682,EBI-9232288

    Protein-protein interaction databases

    BioGridi106847. 11 interactions.
    DIPiDIP-46878N.
    IntActiP02749. 9 interactions.
    MINTiMINT-6743724.
    STRINGi9606.ENSP00000205948.

    Structurei

    Secondary structure

    1
    345
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi22 – 243
    Beta strandi32 – 365
    Beta strandi39 – 413
    Beta strandi46 – 516
    Beta strandi55 – 573
    Beta strandi62 – 654
    Beta strandi79 – 813
    Beta strandi93 – 964
    Beta strandi105 – 1106
    Beta strandi114 – 1185
    Beta strandi120 – 1245
    Beta strandi130 – 1323
    Beta strandi136 – 1394
    Beta strandi151 – 1555
    Beta strandi163 – 1653
    Beta strandi169 – 1746
    Beta strandi178 – 1825
    Beta strandi184 – 1885
    Beta strandi192 – 1954
    Beta strandi199 – 2024
    Beta strandi214 – 2174
    Beta strandi222 – 2254
    Beta strandi229 – 2346
    Beta strandi238 – 2425
    Beta strandi244 – 2485
    Beta strandi252 – 2554
    Beta strandi260 – 2623
    Beta strandi267 – 2704
    Beta strandi272 – 2754
    Beta strandi278 – 2814
    Helixi282 – 2854
    Turni286 – 2883
    Beta strandi295 – 3028
    Turni303 – 3064
    Beta strandi307 – 31610
    Turni331 – 3333
    Helixi339 – 3413

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP02749.
    SMRiP02749. Positions 20-345.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02749.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini21 – 8161Sushi 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini82 – 13958Sushi 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini140 – 20263Sushi 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini203 – 26260Sushi 4PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni263 – 34583Sushi-likeAdd
    BLAST

    Sequence similaritiesi

    Contains 4 Sushi (CCP/SCR) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Sushi

    Phylogenomic databases

    eggNOGiNOG323950.
    HOGENOMiHOG000034008.
    HOVERGENiHBG004271.
    InParanoidiP02749.
    KOiK17305.
    OMAiRFTCPLT.
    OrthoDBiEOG7K6PV8.
    PhylomeDBiP02749.
    TreeFamiTF334137.

    Family and domain databases

    InterProiIPR015104. Sushi_2.
    IPR000436. Sushi_SCR_CCP.
    [Graphical view]
    PfamiPF00084. Sushi. 4 hits.
    PF09014. Sushi_2. 1 hit.
    [Graphical view]
    ProDomiPD012422. Sushi_2. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00032. CCP. 4 hits.
    [Graphical view]
    SUPFAMiSSF57535. SSF57535. 5 hits.
    PROSITEiPS50923. SUSHI. 4 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P02749-1 [UniParc]FASTAAdd to Basket

    « Hide

    MISPVLILFS SFLCHVAIAG RTCPKPDDLP FSTVVPLKTF YEPGEEITYS    50
    CKPGYVSRGG MRKFICPLTG LWPINTLKCT PRVCPFAGIL ENGAVRYTTF 100
    EYPNTISFSC NTGFYLNGAD SAKCTEEGKW SPELPVCAPI ICPPPSIPTF 150
    ATLRVYKPSA GNNSLYRDTA VFECLPQHAM FGNDTITCTT HGNWTKLPEC 200
    REVKCPFPSR PDNGFVNYPA KPTLYYKDKA TFGCHDGYSL DGPEEIECTK 250
    LGNWSAMPSC KASCKVPVKK ATVVYQGERV KIQEKFKNGM LHGDKVSFFC 300
    KNKEKKCSYT EDAQCIDGTI EVPKCFKEHS SLAFWKTDAS DVKPC 345
    Length:345
    Mass (Da):38,298
    Last modified:June 1, 1994 - v3
    Checksum:i63101704F8EDFE3F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti121 – 1211S → C AA sequence (PubMed:6587378)Curated
    Sequence conflicti188 – 1881C → N AA sequence (PubMed:6587378)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti5 – 51V → A.
    Corresponds to variant rs3826358 [ dbSNP | Ensembl ].
    VAR_048316
    Natural varianti107 – 1071S → N in allele APOH*1. 3 Publications
    Corresponds to variant rs1801692 [ dbSNP | Ensembl ].
    VAR_008169
    Natural varianti154 – 1541R → H.1 Publication
    Corresponds to variant rs8178847 [ dbSNP | Ensembl ].
    VAR_019155
    Natural varianti266 – 2661V → L in 23% of the population. 2 Publications
    Corresponds to variant rs4581 [ dbSNP | Ensembl ].
    VAR_000673
    Natural varianti325 – 3251C → G Loss of phosphatidylserine-binding. 1 Publication
    Corresponds to variant rs1801689 [ dbSNP | Ensembl ].
    VAR_008170
    Natural varianti335 – 3351W → S in allele APOH*3W; loss of phosphatidylserine-binding. 2 Publications
    Corresponds to variant rs1801690 [ dbSNP | Ensembl ].
    VAR_008171

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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
    , 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.
    CCDSiCCDS11663.1.
    PIRiS17178. NBHU.
    RefSeqiNP_000033.2. NM_000042.2.
    UniGeneiHs.445358.

    Genome annotation databases

    EnsembliENST00000205948; ENSP00000205948; ENSG00000091583.
    GeneIDi350.
    KEGGihsa:350.
    UCSCiuc002jfn.4. human.

    Polymorphism databases

    DMDMi543826.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs
    SHMPD

    The Singapore human mutation and polymorphism database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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
    , 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 .
    CCDSi CCDS11663.1.
    PIRi S17178. NBHU.
    RefSeqi NP_000033.2. NM_000042.2.
    UniGenei Hs.445358.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1C1Z X-ray 2.87 A 20-345 [» ]
    1G4F NMR - A 261-345 [» ]
    1G4G NMR - A 261-345 [» ]
    1QUB X-ray 2.70 A 20-345 [» ]
    2KRI NMR - A 263-345 [» ]
    3OP8 X-ray 1.90 A/B 263-345 [» ]
    4JHS X-ray 3.00 A 203-345 [» ]
    ProteinModelPortali P02749.
    SMRi P02749. Positions 20-345.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106847. 11 interactions.
    DIPi DIP-46878N.
    IntActi P02749. 9 interactions.
    MINTi MINT-6743724.
    STRINGi 9606.ENSP00000205948.

    Chemistry

    BindingDBi P02749.

    PTM databases

    PhosphoSitei P02749.

    Polymorphism databases

    DMDMi 543826.

    Proteomic databases

    MaxQBi P02749.
    PaxDbi P02749.
    PeptideAtlasi P02749.
    PRIDEi P02749.

    Protocols and materials databases

    DNASUi 350.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000205948 ; ENSP00000205948 ; ENSG00000091583 .
    GeneIDi 350.
    KEGGi hsa:350.
    UCSCi uc002jfn.4. human.

    Organism-specific databases

    CTDi 350.
    GeneCardsi GC17M064208.
    HGNCi HGNC:616. APOH.
    HPAi CAB022214.
    HPA001654.
    HPA003732.
    MIMi 138700. gene.
    neXtProti NX_P02749.
    PharmGKBi PA24903.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG323950.
    HOGENOMi HOG000034008.
    HOVERGENi HBG004271.
    InParanoidi P02749.
    KOi K17305.
    OMAi RFTCPLT.
    OrthoDBi EOG7K6PV8.
    PhylomeDBi P02749.
    TreeFami TF334137.

    Miscellaneous databases

    ChiTaRSi APOH. human.
    EvolutionaryTracei P02749.
    GeneWikii Apolipoprotein_H.
    GenomeRNAii 350.
    NextBioi 1441.
    PMAP-CutDB P02749.
    PROi P02749.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P02749.
    Bgeei P02749.
    CleanExi HS_APOH.
    Genevestigatori P02749.

    Family and domain databases

    InterProi IPR015104. Sushi_2.
    IPR000436. Sushi_SCR_CCP.
    [Graphical view ]
    Pfami PF00084. Sushi. 4 hits.
    PF09014. Sushi_2. 1 hit.
    [Graphical view ]
    ProDomi PD012422. Sushi_2. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00032. CCP. 4 hits.
    [Graphical view ]
    SUPFAMi SSF57535. SSF57535. 5 hits.
    PROSITEi PS50923. SUSHI. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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. 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.

    Entry informationi

    Entry nameiAPOH_HUMAN
    AccessioniPrimary (citable) accession number: P02749
    Secondary accession number(s): B2R9M3, Q9UCN7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 173 of the entry and version 3 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

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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