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P25311

- ZA2G_HUMAN

UniProt

P25311 - ZA2G_HUMAN

Protein

Zinc-alpha-2-glycoprotein

Gene

AZGP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 2 (23 Mar 2010)
      Previous versions | rss
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    Functioni

    Stimulates lipid degradation in adipocytes and causes the extensive fat losses associated with some advanced cancers. May bind polyunsaturated fatty acids.

    GO - Molecular functioni

    1. glycoprotein binding Source: UniProt
    2. peptide antigen binding Source: InterPro
    3. protein transmembrane transporter activity Source: UniProtKB
    4. ribonuclease activity Source: UniProtKB

    GO - Biological processi

    1. antigen processing and presentation of peptide antigen via MHC class I Source: InterPro
    2. cell adhesion Source: UniProtKB
    3. detection of chemical stimulus involved in sensory perception of bitter taste Source: UniProt
    4. immune response Source: InterPro
    5. negative regulation of cell proliferation Source: UniProtKB
    6. positive regulation of T cell mediated cytotoxicity Source: InterPro
    7. protein transmembrane transport Source: GOC
    8. retina homeostasis Source: UniProt
    9. RNA phosphodiester bond hydrolysis Source: GOC

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Zinc-alpha-2-glycoprotein
    Short name:
    Zn-alpha-2-GP
    Short name:
    Zn-alpha-2-glycoprotein
    Gene namesi
    Name:AZGP1
    Synonyms:ZAG, ZNGP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:910. AZGP1.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB
    2. extracellular space Source: UniProt
    3. extracellular vesicular exosome Source: UniProt
    4. MHC class I protein complex Source: InterPro
    5. nucleus Source: UniProt

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25203.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 20202 PublicationsAdd
    BLAST
    Chaini21 – 298278Zinc-alpha-2-glycoproteinPRO_0000019012Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei21 – 211Pyrrolidone carboxylic acid1 Publication
    Glycosylationi109 – 1091N-linked (GlcNAc...) (complex)5 Publications
    Glycosylationi112 – 1121N-linked (GlcNAc...)5 Publications
    Disulfide bondi123 ↔ 186
    Glycosylationi128 – 1281N-linked (GlcNAc...) (complex)9 Publications
    Disulfide bondi225 ↔ 280
    Glycosylationi259 – 2591N-linked (GlcNAc...)3 Publications

    Post-translational modificationi

    N-glycosylated. N-glycan at Asn-128: Hex5HexNAc4.11 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

    Proteomic databases

    MaxQBiP25311.
    PaxDbiP25311.
    PRIDEiP25311.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00166729.
    SWISS-2DPAGEP25311.

    PTM databases

    PhosphoSiteiP25311.

    Expressioni

    Tissue specificityi

    Blood plasma, seminal plasma, urine, saliva, sweat, epithelial cells of various human glands, liver.

    Gene expression databases

    ArrayExpressiP25311.
    BgeeiP25311.
    CleanExiHS_AZGP1.
    GenevestigatoriP25311.

    Organism-specific databases

    HPAiCAB016087.
    HPA012582.

    Interactioni

    Subunit structurei

    Interacts with PIP.1 Publication

    Protein-protein interaction databases

    BioGridi107040. 9 interactions.
    IntActiP25311. 9 interactions.
    STRINGi9606.ENSP00000292401.

    Structurei

    Secondary structure

    1
    298
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi27 – 3913
    Beta strandi42 – 443
    Beta strandi46 – 538
    Beta strandi56 – 627
    Turni63 – 653
    Helixi72 – 765
    Beta strandi79 – 813
    Helixi83 – 10725
    Beta strandi116 – 12611
    Beta strandi129 – 13911
    Beta strandi142 – 1487
    Turni149 – 1524
    Beta strandi153 – 1564
    Helixi159 – 16810
    Helixi173 – 18311
    Helixi185 – 19612
    Helixi198 – 2014
    Beta strandi208 – 2158
    Beta strandi217 – 2193
    Beta strandi221 – 23313
    Beta strandi235 – 2417
    Beta strandi244 – 2463
    Beta strandi249 – 2568
    Turni257 – 2604
    Beta strandi261 – 27010
    Beta strandi278 – 2847
    Beta strandi291 – 2944

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1T7VX-ray1.95A21-298[»]
    1T7WX-ray2.70A21-298[»]
    1T7XX-ray3.10A21-298[»]
    1T7YX-ray2.80A21-298[»]
    1T7ZX-ray3.00A21-298[»]
    1T80X-ray2.10A21-298[»]
    1ZAGX-ray2.80A/B/C/D25-298[»]
    3ES6X-ray3.23A21-298[»]
    ProteinModelPortaliP25311.
    SMRiP25311. Positions 25-298.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP25311.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini207 – 29286Ig-like C1-typeAdd
    BLAST

    Sequence similaritiesi

    Belongs to the MHC class I family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG25830.
    HOGENOMiHOG000296917.
    HOVERGENiHBG016709.
    InParanoidiP25311.
    OMAiNILDRQD.
    OrthoDBiEOG7JT6WQ.
    PhylomeDBiP25311.
    TreeFamiTF336617.

    Family and domain databases

    Gene3Di2.60.40.10. 1 hit.
    3.30.500.10. 1 hit.
    InterProiIPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003006. Ig/MHC_CS.
    IPR003597. Ig_C1-set.
    IPR011161. MHC_I-like_Ag-recog.
    IPR011162. MHC_I/II-like_Ag-recog.
    IPR027648. MHC_I_a.
    IPR001039. MHC_I_a_a1/a2.
    [Graphical view]
    PfamiPF07654. C1-set. 1 hit.
    PF00129. MHC_I. 1 hit.
    [Graphical view]
    PRINTSiPR01638. MHCCLASSI.
    SMARTiSM00407. IGc1. 1 hit.
    [Graphical view]
    SUPFAMiSSF54452. SSF54452. 1 hit.
    PROSITEiPS50835. IG_LIKE. 1 hit.
    PS00290. IG_MHC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P25311-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVRMVPVLLS LLLLLGPAVP QENQDGRYSL TYIYTGLSKH VEDVPAFQAL    50
    GSLNDLQFFR YNSKDRKSQP MGLWRQVEGM EDWKQDSQLQ KAREDIFMET 100
    LKDIVEYYND SNGSHVLQGR FGCEIENNRS SGAFWKYYYD GKDYIEFNKE 150
    IPAWVPFDPA AQITKQKWEA EPVYVQRAKA YLEEECPATL RKYLKYSKNI 200
    LDRQDPPSVV VTSHQAPGEK KKLKCLAYDF YPGKIDVHWT RAGEVQEPEL 250
    RGDVLHNGNG TYQSWVVVAV PPQDTAPYSC HVQHSSLAQP LVVPWEAS 298
    Length:298
    Mass (Da):34,259
    Last modified:March 23, 2010 - v2
    Checksum:i006A153A8E32A0B1
    GO

    Sequence cautioni

    The sequence AAA61311.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAA03123.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAA14417.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAA42438.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21V → S in CAA42438. (PubMed:1915885)Curated
    Sequence conflicti5 – 51V → L in CAA42438. (PubMed:1915885)Curated
    Sequence conflicti33 – 331I → V in AAH05306. (PubMed:15489334)Curated
    Sequence conflicti85 – 851Q → E AA sequence (PubMed:3422450)Curated
    Sequence conflicti96 – 972Missing AA sequence (PubMed:3422450)Curated
    Sequence conflicti244 – 2441E → Q AA sequence (PubMed:3422450)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59766 mRNA. Translation: CAA42438.1. Different initiation.
    D14034 Genomic DNA. Translation: BAA03123.1. Different initiation.
    X69953 Genomic DNA. Translation: CAA49574.1.
    AC004522 Genomic DNA. No translation available.
    CH236956 Genomic DNA. Translation: EAL23862.1.
    CH471091 Genomic DNA. Translation: EAW76621.1.
    CH471091 Genomic DNA. Translation: EAW76622.1.
    BC005306 mRNA. Translation: AAH05306.1.
    BC033830 mRNA. Translation: AAH33830.1.
    D90427 mRNA. Translation: BAA14417.1. Different initiation.
    M76707 mRNA. Translation: AAA61311.1. Different initiation.
    CCDSiCCDS5680.1.
    PIRiA54175.
    RefSeqiNP_001176.1. NM_001185.3.
    UniGeneiHs.546239.

    Genome annotation databases

    EnsembliENST00000292401; ENSP00000292401; ENSG00000160862.
    GeneIDi563.
    KEGGihsa:563.
    UCSCiuc003ush.3. human.

    Polymorphism databases

    DMDMi292495049.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59766 mRNA. Translation: CAA42438.1 . Different initiation.
    D14034 Genomic DNA. Translation: BAA03123.1 . Different initiation.
    X69953 Genomic DNA. Translation: CAA49574.1 .
    AC004522 Genomic DNA. No translation available.
    CH236956 Genomic DNA. Translation: EAL23862.1 .
    CH471091 Genomic DNA. Translation: EAW76621.1 .
    CH471091 Genomic DNA. Translation: EAW76622.1 .
    BC005306 mRNA. Translation: AAH05306.1 .
    BC033830 mRNA. Translation: AAH33830.1 .
    D90427 mRNA. Translation: BAA14417.1 . Different initiation.
    M76707 mRNA. Translation: AAA61311.1 . Different initiation.
    CCDSi CCDS5680.1.
    PIRi A54175.
    RefSeqi NP_001176.1. NM_001185.3.
    UniGenei Hs.546239.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1T7V X-ray 1.95 A 21-298 [» ]
    1T7W X-ray 2.70 A 21-298 [» ]
    1T7X X-ray 3.10 A 21-298 [» ]
    1T7Y X-ray 2.80 A 21-298 [» ]
    1T7Z X-ray 3.00 A 21-298 [» ]
    1T80 X-ray 2.10 A 21-298 [» ]
    1ZAG X-ray 2.80 A/B/C/D 25-298 [» ]
    3ES6 X-ray 3.23 A 21-298 [» ]
    ProteinModelPortali P25311.
    SMRi P25311. Positions 25-298.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107040. 9 interactions.
    IntActi P25311. 9 interactions.
    STRINGi 9606.ENSP00000292401.

    PTM databases

    PhosphoSitei P25311.

    Polymorphism databases

    DMDMi 292495049.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00166729.
    SWISS-2DPAGE P25311.

    Proteomic databases

    MaxQBi P25311.
    PaxDbi P25311.
    PRIDEi P25311.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000292401 ; ENSP00000292401 ; ENSG00000160862 .
    GeneIDi 563.
    KEGGi hsa:563.
    UCSCi uc003ush.3. human.

    Organism-specific databases

    CTDi 563.
    GeneCardsi GC07M099564.
    HGNCi HGNC:910. AZGP1.
    HPAi CAB016087.
    HPA012582.
    MIMi 194460. gene.
    neXtProti NX_P25311.
    PharmGKBi PA25203.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG25830.
    HOGENOMi HOG000296917.
    HOVERGENi HBG016709.
    InParanoidi P25311.
    OMAi NILDRQD.
    OrthoDBi EOG7JT6WQ.
    PhylomeDBi P25311.
    TreeFami TF336617.

    Miscellaneous databases

    ChiTaRSi AZGP1. human.
    EvolutionaryTracei P25311.
    GeneWikii AZGP1.
    GenomeRNAii 563.
    NextBioi 2301.
    PROi P25311.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P25311.
    Bgeei P25311.
    CleanExi HS_AZGP1.
    Genevestigatori P25311.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    3.30.500.10. 1 hit.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003006. Ig/MHC_CS.
    IPR003597. Ig_C1-set.
    IPR011161. MHC_I-like_Ag-recog.
    IPR011162. MHC_I/II-like_Ag-recog.
    IPR027648. MHC_I_a.
    IPR001039. MHC_I_a_a1/a2.
    [Graphical view ]
    Pfami PF07654. C1-set. 1 hit.
    PF00129. MHC_I. 1 hit.
    [Graphical view ]
    PRINTSi PR01638. MHCCLASSI.
    SMARTi SM00407. IGc1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54452. SSF54452. 1 hit.
    PROSITEi PS50835. IG_LIKE. 1 hit.
    PS00290. IG_MHC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human Zn-alpha 2-glycoprotein cDNA cloning and expression analysis in benign and malignant breast tissues."
      Freije J.P., Fueyo A., Uria J., Lopez-Otin C.
      FEBS Lett. 290:247-249(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Mammary gland.
    2. "Molecular cloning and chromosomal assignment of the gene for human Zn-alpha 2-glycoprotein."
      Ueyama H., Deng H.X., Ohkubo I.
      Biochemistry 32:12968-12976(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Human Zn-alpha 2-glycoprotein: complete genomic sequence, identification of a related pseudogene and relationship to class I major histocompatibility complex genes."
      Freije J.P., Fueyo A., Uria J.A., Velasco G., Sanchez L.M., Lopez-Boado Y.S., Lopez-Otin C.
      Genomics 18:575-587(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Leukocyte.
    4. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [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: Colon and Prostate.
    8. "Cloning and nucleotide sequence of a human Zn-alpha 2-glycoprotein cDNA and chromosomal assignment of its gene."
      Ueyama H., Niwa M., Tada T., Sasaki M., Ohkubo I.
      Biochem. Biophys. Res. Commun. 177:696-703(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-298.
      Tissue: Liver and Prostate.
    9. "Complete amino acid sequence of human plasma Zn-alpha 2-glycoprotein and its homology to histocompatibility antigens."
      Araki T., Gejyo F., Takagaki K., Haupt H., Schwick H.G., Buergi W., Marti T., Schaller J., Rickli E., Brossmer R., Atkinson P.H., Putnam F.W., Schmid K.
      Proc. Natl. Acad. Sci. U.S.A. 85:679-683(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 21-298, PYROGLUTAMATE FORMATION AT GLN-21.
      Tissue: Plasma.
    10. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
      Zhang Z., Henzel W.J.
      Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 21-35.
    11. "Biochemical characterization and crystallization of human Zn-alpha2-glycoprotein, a soluble class I major histocompatibility complex homolog."
      Sanchez L.M., Lopez-Otin C., Bjorkman P.J.
      Proc. Natl. Acad. Sci. U.S.A. 94:4626-4630(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, CRYSTALLIZATION.
    12. "Hydrophobic ligand binding by Zn-alpha 2-glycoprotein, a soluble fat-depleting factor related to major histocompatibility complex proteins."
      Kennedy M.W., Heikema A.P., Cooper A., Bjorkman P.J., Sanchez L.M.
      J. Biol. Chem. 276:35008-35013(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IN VITRO BINDING OF FATTY ACID.
    13. Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-128.
      Tissue: Bile.
    14. "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-112 AND ASN-128.
      Tissue: Plasma.
    15. "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-112.
      Tissue: Plasma.
    16. "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-109; ASN-112 AND ASN-128.
      Tissue: Saliva.
    17. "Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry."
      Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.
      Proteomics 8:3833-3847(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-109; ASN-112 AND ASN-128.
      Tissue: Milk.
    18. "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-109; ASN-112 AND ASN-128.
      Tissue: Liver.
    19. Cited for: GLYCOSYLATION AT ASN-109 AND ASN-128.
    20. "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-128, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
    21. "Crystal structure of human ZAG, a fat-depleting factor related to MHC molecules."
      Sanchez L.M., Chirino A.J., Bjorkman P.J.
      Science 283:1914-1919(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), DISULFIDE BONDS, GLYCOSYLATION AT ASN-109; ASN-128 AND ASN-259.
    22. "Crystallographic studies of ligand binding by Zn-alpha2-glycoprotein."
      Delker S.L., West A.P. Jr., McDermott L., Kennedy M.W., Bjorkman P.J.
      J. Struct. Biol. 148:205-213(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 21-298, DISULFIDE BONDS, GLYCOSYLATION AT ASN-128 AND ASN-259.
    23. "Crystal structure of the novel complex formed between zinc alpha2-glycoprotein (ZAG) and prolactin-inducible protein (PIP) from human seminal plasma."
      Hassan M.I., Bilgrami S., Kumar V., Singh N., Yadav S., Kaur P., Singh T.P.
      J. Mol. Biol. 384:663-672(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 32-149 IN COMPLEX WITH PIP, DISULFIDE BONDS, GLYCOSYLATION AT ASN-259.

    Entry informationi

    Entry nameiZA2G_HUMAN
    AccessioniPrimary (citable) accession number: P25311
    Secondary accession number(s): D6W5T8
    , O60386, Q5XKQ4, Q8N4N0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: March 23, 2010
    Last modified: October 1, 2014
    This is version 154 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

    Caution

    It is uncertain whether Met-1 or Met-4 is the initiator.Curated

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3