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P19652

- A1AG2_HUMAN

UniProt

P19652 - A1AG2_HUMAN

Protein

Alpha-1-acid glycoprotein 2

Gene

ORM2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 2 (01 Apr 1993)
      Previous versions | rss
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    Functioni

    Functions as transport protein in the blood stream. Binds various hydrophobic ligands in the interior of its beta-barrel domain. Also binds synthetic drugs and influences their distribution and availability. Appears to function in modulating the activity of the immune system during the acute-phase reaction.1 Publication

    GO - Biological processi

    1. acute-phase response Source: ProtInc
    2. regulation of immune system process Source: InterPro
    3. transport Source: UniProtKB-KW

    Keywords - Biological processi

    Acute phase, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-1-acid glycoprotein 2
    Short name:
    AGP 2
    Alternative name(s):
    Orosomucoid-2
    Short name:
    OMD 2
    Gene namesi
    Name:ORM2
    Synonyms:AGP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:8499. ORM2.

    Subcellular locationi

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. extracellular space Source: UniProt

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA32818.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Add
    BLAST
    Chaini19 – 201183Alpha-1-acid glycoprotein 2PRO_0000017861Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei19 – 191Pyrrolidone carboxylic acid1 Publication
    Disulfide bondi23 ↔ 165
    Glycosylationi33 – 331N-linked (GlcNAc...) (complex)8 Publications
    Glycosylationi56 – 561N-linked (GlcNAc...)4 Publications
    Glycosylationi72 – 721N-linked (GlcNAc...)3 Publications
    Disulfide bondi90 ↔ 183
    Glycosylationi93 – 931N-linked (GlcNAc...)5 Publications
    Glycosylationi103 – 1031N-linked (GlcNAc...)3 PublicationsCAR_000171

    Post-translational modificationi

    N-glycosylated. N-glycan heterogeneity at Asn-33: Hex5HexNAc4 (minor), Hex6HexNAc5 (major) and dHex1Hex6HexNAc5 (minor).8 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

    Proteomic databases

    MaxQBiP19652.
    PeptideAtlasiP19652.
    PRIDEiP19652.

    2D gel databases

    DOSAC-COBS-2DPAGEP19652.
    SWISS-2DPAGEP19652.

    PTM databases

    PhosphoSiteiP19652.
    UniCarbKBiP19652.

    Expressioni

    Tissue specificityi

    Expressed by the liver and secreted in plasma.

    Inductioni

    Synthesis is controlled by glucocorticoids, interleukin-1 and interleukin-6, It increases 5- to 50-fold upon inflammation.

    Gene expression databases

    ArrayExpressiP19652.
    BgeeiP19652.
    GenevestigatoriP19652.

    Organism-specific databases

    HPAiHPA046438.

    Interactioni

    Protein-protein interaction databases

    BioGridi111047. 3 interactions.
    IntActiP19652. 3 interactions.
    STRINGi9606.ENSP00000394936.

    Structurei

    Secondary structure

    1
    201
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni20 – 234
    Helixi24 – 263
    Helixi33 – 397
    Beta strandi41 – 5111
    Helixi53 – 608
    Beta strandi62 – 7211
    Turni73 – 764
    Beta strandi77 – 8610
    Beta strandi89 – 10012
    Turni101 – 1044
    Beta strandi105 – 1106
    Beta strandi113 – 1208
    Beta strandi127 – 1337
    Turni137 – 1393
    Beta strandi141 – 15010
    Helixi153 – 16513
    Helixi170 – 1723
    Helixi178 – 1803
    Helixi184 – 1918

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3APUX-ray2.10A/B19-201[»]
    3APVX-ray2.15A/B19-201[»]
    3APWX-ray2.20A/B19-201[»]
    3APXX-ray2.20A19-201[»]
    ProteinModelPortaliP19652.
    SMRiP19652. Positions 19-196.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19652.

    Family & Domainsi

    Domaini

    Contains a beta-barrel that binds various ligands in its interior.1 Publication

    Sequence similaritiesi

    Belongs to the calycin superfamily. Lipocalin family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOGENOMiHOG000125170.
    HOVERGENiHBG000035.
    InParanoidiP19652.
    KOiK17308.
    OMAiSKEHMEE.
    OrthoDBiEOG7B5WXT.
    PhylomeDBiP19652.
    TreeFamiTF343791.

    Family and domain databases

    Gene3Di2.40.128.20. 1 hit.
    InterProiIPR001500. A1A_glycop.
    IPR012674. Calycin.
    IPR011038. Calycin-like.
    IPR000566. Lipocln_cytosolic_FA-bd_dom.
    [Graphical view]
    PANTHERiPTHR11967. PTHR11967. 1 hit.
    PfamiPF00061. Lipocalin. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036899. AGP. 1 hit.
    PRINTSiPR00708. A1AGLPROTEIN.
    SUPFAMiSSF50814. SSF50814. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P19652-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALSWVLTVL SLLPLLEAQI PLCANLVPVP ITNATLDRIT GKWFYIASAF    50
    RNEEYNKSVQ EIQATFFYFT PNKTEDTIFL REYQTRQNQC FYNSSYLNVQ 100
    RENGTVSRYE GGREHVAHLL FLRDTKTLMF GSYLDDEKNW GLSFYADKPE 150
    TTKEQLGEFY EALDCLCIPR SDVMYTDWKK DKCEPLEKQH EKERKQEEGE 200
    S 201
    Length:201
    Mass (Da):23,603
    Last modified:April 1, 1993 - v2
    Checksum:i49167ABCC22933B9
    GO

    Sequence cautioni

    The sequence CAA29873.2 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAA29874.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti32 – 321T → I in CAG33211. 1 PublicationCurated
    Sequence conflicti102 – 1021E → D in BAG35159. (PubMed:14702039)Curated
    Sequence conflicti125 – 1251T → I in BAG35159. (PubMed:14702039)Curated
    Sequence conflicti162 – 1621A → V in BAG35159. (PubMed:14702039)Curated
    Sequence conflicti189 – 1891Q → H in BAG35159. (PubMed:14702039)Curated

    Polymorphismi

    Many different variants of ORM2 are known.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti38 – 381R → Q.
    Corresponds to variant rs17650 [ dbSNP | Ensembl ].
    VAR_014667
    Natural varianti99 – 991V → A.
    Corresponds to variant rs2636889 [ dbSNP | Ensembl ].
    VAR_050172
    Natural varianti141 – 1411G → R.
    Corresponds to variant rs12685968 [ dbSNP | Ensembl ].
    VAR_050173
    Natural varianti167 – 1671C → R.
    Corresponds to variant rs1126777 [ dbSNP | Ensembl ].
    VAR_050174
    Natural varianti174 – 1741M → V.
    Corresponds to variant rs2636890 [ dbSNP | Ensembl ].
    VAR_050175

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06675 Genomic DNA. Translation: CAA29874.1. Sequence problems.
    X05780 Genomic DNA. No translation available.
    X06674
    , X06676, X06677, X06678, X06679, X06680 Genomic DNA. Translation: CAA29873.2. Sequence problems.
    X05784 Genomic DNA. No translation available.
    M21540 Genomic DNA. Translation: AAA51549.1.
    AK312226 mRNA. Translation: BAG35159.1.
    CR456930 mRNA. Translation: CAG33211.1.
    AL356796 Genomic DNA. Translation: CAI16860.1.
    CH471090 Genomic DNA. Translation: EAW87417.1.
    BC015964 mRNA. Translation: AAH15964.1.
    BC056239 mRNA. Translation: AAH56239.1.
    CCDSiCCDS6804.1.
    PIRiJT0326. OMHU2.
    RefSeqiNP_000599.1. NM_000608.2.
    UniGeneiHs.719954.

    Genome annotation databases

    EnsembliENST00000431067; ENSP00000394936; ENSG00000228278.
    GeneIDi5005.
    KEGGihsa:5005.
    UCSCiuc004bil.3. human.

    Polymorphism databases

    DMDMi231458.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06675 Genomic DNA. Translation: CAA29874.1 . Sequence problems.
    X05780 Genomic DNA. No translation available.
    X06674
    , X06676 , X06677 , X06678 , X06679 , X06680 Genomic DNA. Translation: CAA29873.2 . Sequence problems.
    X05784 Genomic DNA. No translation available.
    M21540 Genomic DNA. Translation: AAA51549.1 .
    AK312226 mRNA. Translation: BAG35159.1 .
    CR456930 mRNA. Translation: CAG33211.1 .
    AL356796 Genomic DNA. Translation: CAI16860.1 .
    CH471090 Genomic DNA. Translation: EAW87417.1 .
    BC015964 mRNA. Translation: AAH15964.1 .
    BC056239 mRNA. Translation: AAH56239.1 .
    CCDSi CCDS6804.1.
    PIRi JT0326. OMHU2.
    RefSeqi NP_000599.1. NM_000608.2.
    UniGenei Hs.719954.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3APU X-ray 2.10 A/B 19-201 [» ]
    3APV X-ray 2.15 A/B 19-201 [» ]
    3APW X-ray 2.20 A/B 19-201 [» ]
    3APX X-ray 2.20 A 19-201 [» ]
    ProteinModelPortali P19652.
    SMRi P19652. Positions 19-196.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111047. 3 interactions.
    IntActi P19652. 3 interactions.
    STRINGi 9606.ENSP00000394936.

    Chemistry

    ChEMBLi CHEMBL5958.

    PTM databases

    PhosphoSitei P19652.
    UniCarbKBi P19652.

    Polymorphism databases

    DMDMi 231458.

    2D gel databases

    DOSAC-COBS-2DPAGE P19652.
    SWISS-2DPAGE P19652.

    Proteomic databases

    MaxQBi P19652.
    PeptideAtlasi P19652.
    PRIDEi P19652.

    Protocols and materials databases

    DNASUi 5005.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000431067 ; ENSP00000394936 ; ENSG00000228278 .
    GeneIDi 5005.
    KEGGi hsa:5005.
    UCSCi uc004bil.3. human.

    Organism-specific databases

    CTDi 5005.
    GeneCardsi GC09P117092.
    HGNCi HGNC:8499. ORM2.
    HPAi HPA046438.
    MIMi 138610. gene.
    neXtProti NX_P19652.
    PharmGKBi PA32818.
    GenAtlasi Search...

    Phylogenomic databases

    HOGENOMi HOG000125170.
    HOVERGENi HBG000035.
    InParanoidi P19652.
    KOi K17308.
    OMAi SKEHMEE.
    OrthoDBi EOG7B5WXT.
    PhylomeDBi P19652.
    TreeFami TF343791.

    Miscellaneous databases

    EvolutionaryTracei P19652.
    GenomeRNAii 5005.
    NextBioi 19276.
    PROi P19652.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P19652.
    Bgeei P19652.
    Genevestigatori P19652.

    Family and domain databases

    Gene3Di 2.40.128.20. 1 hit.
    InterProi IPR001500. A1A_glycop.
    IPR012674. Calycin.
    IPR011038. Calycin-like.
    IPR000566. Lipocln_cytosolic_FA-bd_dom.
    [Graphical view ]
    PANTHERi PTHR11967. PTHR11967. 1 hit.
    Pfami PF00061. Lipocalin. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036899. AGP. 1 hit.
    PRINTSi PR00708. A1AGLPROTEIN.
    SUPFAMi SSF50814. SSF50814. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Structure and expression of the genes coding for human alpha 1-acid glycoprotein."
      Dente L., Pizza M.G., Metspalu A., Cortese R.
      EMBO J. 6:2289-2296(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Structure and characterisation of a duplicated human alpha 1 acid glycoprotein gene."
      Merritt C.M., Board P.G.
      Gene 66:97-106(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "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.
    4. "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].
    5. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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: Skeletal muscle.
    8. "The disulfide bonds of alpha1-acid glycoprotein."
      Schmid K., Buergi W., Collins J.H., Nanno S.
      Biochemistry 13:2694-2697(1974) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BONDS.
    9. "Analysis of the five glycosylation sites of human alpha 1-acid glycoprotein."
      Treuheit M.J., Costello C.E., Halsall H.B.
      Biochem. J. 283:105-112(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-33; ASN-56; ASN-72; ASN-93 AND ASN-103.
    10. "A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation."
      Hagglund P., Bunkenborg J., Elortza F., Jensen O.N., Roepstorff P.
      J. Proteome Res. 3:556-566(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PYROGLUTAMATE FORMATION AT GLN-19, GLYCOSYLATION AT ASN-33 AND ASN-93, IDENTIFICATION BY MASS SPECTROMETRY.
    11. Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33.
      Tissue: Bile.
    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-33; ASN-56; ASN-72 AND ASN-93.
      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-33; ASN-56; ASN-72; ASN-93 AND ASN-103.
      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-33; ASN-56; ASN-93 AND ASN-103.
      Tissue: Liver.
    15. "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-33, STRUCTURE OF CARBOHYDRATES.
      Tissue: Cerebrospinal fluid.
    16. "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-33, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
    17. "Structural insights into differences in drug-binding selectivity between two forms of human {alpha}1-acid glycoprotein genetic variants, the A and F1*S forms."
      Nishi K., Ono T., Nakamura T., Fukunaga N., Izumi M., Watanabe H., Suenaga A., Maruyama T., Yamagata Y., Curry S., Otagiri M.
      J. Biol. Chem. 286:14427-14434(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 19-201 OF VARIANT ARG-167 IN COMPLEXES WITH DISOPYRAMIDE; AMITRIPTYLINE AND CHLORPROMAZINE, FUNCTION, DISULFIDE BONDS, DOMAIN.

    Entry informationi

    Entry nameiA1AG2_HUMAN
    AccessioniPrimary (citable) accession number: P19652
    Secondary accession number(s): B2R5L2
    , Q16571, Q5T538, Q6IB74
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: April 1, 1993
    Last modified: October 1, 2014
    This is version 153 of the entry and version 2 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, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: 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

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