Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P02763

- A1AG1_HUMAN

UniProt

P02763 - A1AG1_HUMAN

Protein

Alpha-1-acid glycoprotein 1

Gene

ORM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 164 (01 Oct 2014)
      Sequence version 1 (01 Jan 1988)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Functions as transport protein in the blood stream. Binds various ligands in the interior of its beta-barrel domain. Also binds synthetic drugs and influences their distribution and availability in the body. Appears to function in modulating the activity of the immune system during the acute-phase reaction.2 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

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

    Keywords - Biological processi

    Acute phase, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-1-acid glycoprotein 1
    Short name:
    AGP 1
    Alternative name(s):
    Orosomucoid-1
    Short name:
    OMD 1
    Gene namesi
    Name:ORM1
    Synonyms:AGP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:8498. ORM1.

    Subcellular locationi

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. extracellular region Source: UniProtKB
    3. extracellular space Source: UniProt
    4. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA260.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 18181 PublicationAdd
    BLAST
    Chaini19 – 201183Alpha-1-acid glycoprotein 1PRO_0000017860Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei19 – 191Pyrrolidone carboxylic acid1 Publication
    Disulfide bondi23 ↔ 1651 Publication
    Glycosylationi33 – 331N-linked (GlcNAc...) (complex)8 Publications
    Glycosylationi56 – 561N-linked (GlcNAc...)4 Publications
    Glycosylationi72 – 721N-linked (GlcNAc...) (complex)5 Publications
    Disulfide bondi90 ↔ 1831 Publication
    Glycosylationi93 – 931N-linked (GlcNAc...)8 Publications
    Glycosylationi103 – 1031N-linked (GlcNAc...)4 PublicationsCAR_000170

    Post-translational modificationi

    N-glycosylated. N-glycan heterogeneity at Asn-33: Hex5HexNAc4 (minor), Hex6HexNAc5 (major) and dHex1Hex6HexNAc5 (minor).10 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

    Proteomic databases

    MaxQBiP02763.
    PaxDbiP02763.
    PeptideAtlasiP02763.
    PRIDEiP02763.

    2D gel databases

    SWISS-2DPAGEP02763.

    PTM databases

    PhosphoSiteiP02763.
    UniCarbKBiP02763.

    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

    ArrayExpressiP02763.
    BgeeiP02763.
    CleanExiHS_ORM1.
    GenevestigatoriP02763.

    Organism-specific databases

    HPAiCAB006265.
    HPA046438.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SERPINE1P051214EBI-976767,EBI-953978

    Protein-protein interaction databases

    BioGridi111046. 7 interactions.
    IntActiP02763. 7 interactions.
    MINTiMINT-202382.
    STRINGi9606.ENSP00000259396.

    Structurei

    Secondary structure

    1
    201
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi24 – 263
    Helixi33 – 397
    Beta strandi41 – 5212
    Helixi53 – 597
    Beta strandi62 – 7211
    Turni73 – 764
    Beta strandi77 – 8610
    Beta strandi89 – 10012
    Turni101 – 1044
    Beta strandi105 – 1106
    Beta strandi113 – 1219
    Beta strandi127 – 1326
    Helixi137 – 1393
    Beta strandi141 – 1499
    Turni153 – 1564
    Helixi157 – 16610
    Helixi170 – 1723
    Helixi178 – 1803
    Helixi184 – 1929

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3KQ0X-ray1.80A19-201[»]
    ProteinModelPortaliP02763.
    SMRiP02763. Positions 19-193.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02763.

    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

    eggNOGiNOG41523.
    HOGENOMiHOG000125170.
    HOVERGENiHBG000035.
    InParanoidiP02763.
    KOiK17308.
    OrthoDBiEOG7B5WXT.
    PhylomeDBiP02763.
    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.

    P02763-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALSWVLTVL SLLPLLEAQI PLCANLVPVP ITNATLDQIT GKWFYIASAF    50
    RNEEYNKSVQ EIQATFFYFT PNKTEDTIFL REYQTRQDQC IYNTTYLNVQ 100
    RENGTISRYV GGQEHFAHLL ILRDTKTYML AFDVNDEKNW GLSVYADKPE 150
    TTKEQLGEFY EALDCLRIPK SDVVYTDWKK DKCEPLEKQH EKERKQEEGE 200
    S 201
    Length:201
    Mass (Da):23,512
    Last modified:January 1, 1988 - v1
    Checksum:i63292233AD6EAD8B
    GO

    Sequence cautioni

    The sequence CAA29229.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti170 – 1701K → R in AAI43315. (PubMed:15489334)Curated
    Sequence conflicti182 – 1821Missing AA sequence (PubMed:4561179)Curated
    Sequence conflicti193 – 1931Missing AA sequence (PubMed:4561179)Curated

    Polymorphismi

    Three common alleles of ORM1 are known. ORM1*F1 has Gln-38/Val-174; ORM1*F2 has Gln-38/Met-174 and ORM1*S has Arg-38/Val-174. The sequence shown is that of allele ORM1*F1.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti38 – 381Q → R in allele ORM1*S. 4 Publications
    VAR_013840
    Natural varianti167 – 1671R → C.1 Publication
    Corresponds to variant rs3182034 [ dbSNP | Ensembl ].
    VAR_056166
    Natural varianti174 – 1741V → M in allele ORM1*F2. 2 Publications
    Corresponds to variant rs1126801 [ dbSNP | Ensembl ].
    VAR_013841

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02544 mRNA. Translation: CAA26397.1.
    M13692 mRNA. Translation: AAA35515.1.
    X05779
    , X05780, X05781, X05782, X05783, X05784 Genomic DNA. Translation: CAA29229.1. Sequence problems.
    X06676 Genomic DNA. No translation available.
    X06680 Genomic DNA. No translation available.
    BT019790 mRNA. Translation: AAV38593.1.
    AK312035 mRNA. Translation: BAG34972.1.
    AL356796 Genomic DNA. Translation: CAI16859.1.
    CH471090 Genomic DNA. Translation: EAW87416.1.
    BC104818 mRNA. Translation: AAI04819.1.
    BC104820 mRNA. Translation: AAI04821.1.
    BC143313 mRNA. Translation: AAI43314.1.
    BC143314 mRNA. Translation: AAI43315.1.
    BC026238 mRNA. Translation: AAH26238.1.
    CCDSiCCDS6803.1.
    PIRiA28346. OMHU1.
    RefSeqiNP_000598.2. NM_000607.2.
    UniGeneiHs.522356.

    Genome annotation databases

    EnsembliENST00000259396; ENSP00000259396; ENSG00000229314.
    GeneIDi5004.
    KEGGihsa:5004.
    UCSCiuc004bik.4. human.

    Polymorphism databases

    DMDMi112877.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02544 mRNA. Translation: CAA26397.1 .
    M13692 mRNA. Translation: AAA35515.1 .
    X05779
    , X05780 , X05781 , X05782 , X05783 , X05784 Genomic DNA. Translation: CAA29229.1 . Sequence problems.
    X06676 Genomic DNA. No translation available.
    X06680 Genomic DNA. No translation available.
    BT019790 mRNA. Translation: AAV38593.1 .
    AK312035 mRNA. Translation: BAG34972.1 .
    AL356796 Genomic DNA. Translation: CAI16859.1 .
    CH471090 Genomic DNA. Translation: EAW87416.1 .
    BC104818 mRNA. Translation: AAI04819.1 .
    BC104820 mRNA. Translation: AAI04821.1 .
    BC143313 mRNA. Translation: AAI43314.1 .
    BC143314 mRNA. Translation: AAI43315.1 .
    BC026238 mRNA. Translation: AAH26238.1 .
    CCDSi CCDS6803.1.
    PIRi A28346. OMHU1.
    RefSeqi NP_000598.2. NM_000607.2.
    UniGenei Hs.522356.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3KQ0 X-ray 1.80 A 19-201 [» ]
    ProteinModelPortali P02763.
    SMRi P02763. Positions 19-193.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111046. 7 interactions.
    IntActi P02763. 7 interactions.
    MINTi MINT-202382.
    STRINGi 9606.ENSP00000259396.

    Chemistry

    BindingDBi P02763.
    ChEMBLi CHEMBL4285.
    DrugBanki DB01418. Acenocoumarol.
    DB00802. Alfentanil.
    DB01429. Aprindine.
    DB00280. Disopyramide.
    DB01359. Penbutolol.
    DB00946. Phenprocoumon.
    DB00908. Quinidine.
    DB00706. Tamsulosin.

    PTM databases

    PhosphoSitei P02763.
    UniCarbKBi P02763.

    Polymorphism databases

    DMDMi 112877.

    2D gel databases

    SWISS-2DPAGE P02763.

    Proteomic databases

    MaxQBi P02763.
    PaxDbi P02763.
    PeptideAtlasi P02763.
    PRIDEi P02763.

    Protocols and materials databases

    DNASUi 5004.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000259396 ; ENSP00000259396 ; ENSG00000229314 .
    GeneIDi 5004.
    KEGGi hsa:5004.
    UCSCi uc004bik.4. human.

    Organism-specific databases

    CTDi 5004.
    GeneCardsi GC09P117085.
    HGNCi HGNC:8498. ORM1.
    HPAi CAB006265.
    HPA046438.
    MIMi 138600. gene.
    neXtProti NX_P02763.
    PharmGKBi PA260.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG41523.
    HOGENOMi HOG000125170.
    HOVERGENi HBG000035.
    InParanoidi P02763.
    KOi K17308.
    OrthoDBi EOG7B5WXT.
    PhylomeDBi P02763.
    TreeFami TF343791.

    Miscellaneous databases

    ChiTaRSi ORM1. human.
    EvolutionaryTracei P02763.
    GeneWikii ORM1.
    GenomeRNAii 5004.
    NextBioi 19272.
    PROi P02763.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P02763.
    Bgeei P02763.
    CleanExi HS_ORM1.
    Genevestigatori P02763.

    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. "Molecular cloning and nucleotide sequence of human alpha 1 acid glycoprotein cDNA."
      Board P.G., Jones I.M., Bentley A.K.
      Gene 44:127-131(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Structure of the human alpha 1-acid glycoprotein gene: sequence homology with other human acute phase protein genes."
      Dente L., Ciliberto G., Cortese R.
      Nucleic Acids Res. 13:3941-3952(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "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].
    5. "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.
    6. "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], VARIANT ARG-38.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ARG-38.
    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], VARIANTS ARG-38; CYS-167 AND MET-174.
      Tissue: Liver.
    9. "Structure of alpha 1-acid glycoprotein. The complete amino acid sequence, multiple amino acid substitutions, and homology with the immunoglobulins."
      Schmid K., Kaufmann H., Isemura S., Bauer F., Emura J., Motoyama T., Ishiguro M., Nanno S.
      Biochemistry 12:2711-2724(1973) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 19-129, PYROGLUTAMATE FORMATION AT GLN-19.
    10. "Isolation and partial characterization of the cyanogen bromide fragments of alpha 1-acid glycoprotein and the elucidation of the amino acid sequence of the carboxyl-terminal cyanogen bromide fragment."
      Ikenaka T., Ishiguro M., Emura J., Kaufmann H., Isemura S., Bauer W., Schmid K.
      Biochemistry 11:3817-3829(1972) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 129-201.
    11. "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.
    12. "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.
    13. "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
      Zhang H., Li X.-J., Martin D.B., Aebersold R.
      Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-33.
    14. "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: GLYCOSYLATION AT ASN-33; ASN-72 AND ASN-93, IDENTIFICATION BY MASS SPECTROMETRY.
    15. Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33 AND ASN-93.
      Tissue: Bile.
    16. "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; ASN-93 AND ASN-103.
      Tissue: Plasma.
    17. "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.
    18. "Selective binding of imatinib to the genetic variants of human alpha1-acid glycoprotein."
      Fitos I., Visy J., Zsila F., Mady G., Simonyi M.
      Biochim. Biophys. Acta 1760:1704-1712(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    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-93.
      Tissue: Saliva.
    20. "The drug binding site of human alpha1-acid glycoprotein: insight from induced circular dichroism and electronic absorption spectra."
      Zsila F., Iwao Y.
      Biochim. Biophys. Acta 1770:797-809(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    21. "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-93 AND ASN-103.
      Tissue: Liver.
    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-33 AND ASN-72, STRUCTURE OF CARBOHYDRATES.
      Tissue: Cerebrospinal fluid.
    23. "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.
    24. "The 1.8-A crystal structure of alpha1-acid glycoprotein (Orosomucoid) solved by UV RIP reveals the broad drug-binding activity of this human plasma lipocalin."
      Schonfeld D.L., Ravelli R.B., Mueller U., Skerra A.
      J. Mol. Biol. 384:393-405(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 20-201, DOMAIN, DISULFIDE BONDS.
    25. "Human orosomucoid polymorphism: molecular basis of the three common ORM1 alleles, ORM1*F1, ORM1*F2, and ORM1*S."
      Yuasa I., Umetsu K., Vogt U., Nakamura H., Nanba E., Tamaki N., Irizawa Y.
      Hum. Genet. 99:393-398(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ARG-38 AND MET-174.

    Entry informationi

    Entry nameiA1AG1_HUMAN
    AccessioniPrimary (citable) accession number: P02763
    Secondary accession number(s): B7ZKQ5
    , Q5T539, Q5U067, Q8TC16
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 1, 1988
    Last modified: October 1, 2014
    This is version 164 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

    Keywords - Technical termi

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

    Dasty 3