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P02760

- AMBP_HUMAN

UniProt

P02760 - AMBP_HUMAN

Protein

Protein AMBP

Gene

AMBP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 180 (01 Oct 2014)
      Sequence version 1 (13 Aug 1987)
      Previous versions | rss
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    Functioni

    Inter-alpha-trypsin inhibitor inhibits trypsin, plasmin, and lysosomal granulocytic elastase. Inhibits calcium oxalate crystallization.1 Publication
    Trypstatin is a trypsin inhibitor.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei53 – 531Multimeric 3-hydroxykynurenine chromophore (covalent)
    Binding sitei111 – 1111Multimeric 3-hydroxykynurenine chromophore (covalent)
    Binding sitei137 – 1371Multimeric 3-hydroxykynurenine chromophore (covalent)
    Binding sitei149 – 1491Multimeric 3-hydroxykynurenine chromophore (covalent)
    Sitei241 – 2422Inhibitory (P1) (chymotrypsin, elastase)By similarity
    Sitei297 – 2982Inhibitory (P1) (trypsin)By similarity

    GO - Molecular functioni

    1. calcium channel inhibitor activity Source: UniProtKB
    2. calcium oxalate binding Source: UniProtKB
    3. heme binding Source: UniProtKB
    4. IgA binding Source: UniProtKB
    5. protein binding Source: IntAct
    6. protein homodimerization activity Source: UniProtKB
    7. serine-type endopeptidase inhibitor activity Source: UniProtKB
    8. small molecule binding Source: InterPro

    GO - Biological processi

    1. cell adhesion Source: UniProtKB
    2. female pregnancy Source: UniProtKB
    3. heme catabolic process Source: UniProtKB
    4. negative regulation of endopeptidase activity Source: GOC
    5. negative regulation of immune response Source: UniProtKB
    6. negative regulation of JNK cascade Source: UniProtKB
    7. protein catabolic process Source: Ensembl
    8. protein-chromophore linkage Source: UniProtKB-KW
    9. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Protease inhibitor, Serine protease inhibitor

    Keywords - Biological processi

    Host-virus interaction

    Keywords - Ligandi

    Chromophore

    Enzyme and pathway databases

    ReactomeiREACT_160163. Scavenging of heme from plasma.

    Protein family/group databases

    MEROPSiI02.005.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein AMBP
    Cleaved into the following 3 chains:
    Alpha-1-microglobulin
    Short name:
    Protein HC
    Alternative name(s):
    Alpha-1 microglycoprotein
    Complex-forming glycoprotein heterogeneous in charge
    Alternative name(s):
    Bikunin
    EDC1
    HI-30
    Uronic-acid-rich protein
    Gene namesi
    Name:AMBP
    Synonyms:HCP, ITIL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:453. AMBP.

    Subcellular locationi

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. cell surface Source: Ensembl
    3. extracellular region Source: UniProtKB
    4. extracellular space Source: UniProt
    5. extracellular vesicular exosome Source: UniProt
    6. intracellular membrane-bounded organelle Source: Ensembl
    7. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24759.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 19193 PublicationsAdd
    BLAST
    Chaini20 – 203184Alpha-1-microglobulinPRO_0000017886Add
    BLAST
    Chaini206 – 352147Inter-alpha-trypsin inhibitor light chainPRO_0000017887Add
    BLAST
    Chaini284 – 34461TrypstatinBy similarityPRO_0000318926Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi24 – 241O-linked (GalNAc...)1 PublicationCAR_000172
    Glycosylationi36 – 361N-linked (GlcNAc...) (complex)1 Publication
    Disulfide bondi91 ↔ 188
    Glycosylationi115 – 1151N-linked (GlcNAc...) (complex)2 Publications
    Glycosylationi215 – 2151O-linked (Xyl...) (chondroitin sulfate)3 Publications
    Disulfide bondi231 ↔ 281
    Disulfide bondi240 ↔ 264
    Glycosylationi250 – 2501N-linked (GlcNAc...) (complex)2 Publications
    Disulfide bondi256 ↔ 277
    Disulfide bondi287 ↔ 337
    Disulfide bondi296 ↔ 320
    Disulfide bondi312 ↔ 333

    Post-translational modificationi

    The precursor is proteolytically processed into separately functioning proteins.
    3-hydroxykynurenine, an oxidized tryptophan metabolite that is common in biological fluids, reacts with Cys-53, Lys-111, Lys-137, and Lys-149 to form heterogeneous polycyclic chromophores including hydroxanthommatin. The reaction by alpha-1-microglobulin is autocatalytic; the human protein forms chromophore even when expressed in insect and bacterial cells. The chromophore can react with accessible cysteines forming non-reducible thioether cross-links with other molecules of alpha-1-microglobulin or with other proteins such as Ig alpha-1 chain C region 'Cys-352'.
    Heavy chains are interlinked with bikunin via a chondroitin 4-sulfate bridge to the their C-terminal aspartate.By similarity
    N- and O-glycosylated. N-glycan heterogeneity at Asn-115: Hex5HexNAc4 (major), Hex6HexNAc5 (minor) and dHex1Hex6HexNAc5 (minor). N-glycan at Asn-250: Hex5HexNAc4. O-linkage of the glycosaminoglycan, chondroitin sulfate, at Ser-215 allows cross-linking between the three polypeptide chains.5 Publications

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP02760.
    PaxDbiP02760.
    PeptideAtlasiP02760.
    PRIDEiP02760.

    2D gel databases

    SWISS-2DPAGEP02760.

    PTM databases

    PhosphoSiteiP02760.
    UniCarbKBiP02760.

    Miscellaneous databases

    PMAP-CutDBP02760.

    Expressioni

    Tissue specificityi

    Expressed by the liver and secreted in plasma. Alpha-1-microglobulin occurs in many physiological fluids including plasma, urine, and cerebrospinal fluid. Inter-alpha-trypsin inhibitor is present in plasma and urine.

    Gene expression databases

    ArrayExpressiP02760.
    BgeeiP02760.
    CleanExiHS_AMBP.
    GenevestigatoriP02760.

    Organism-specific databases

    HPAiHPA001497.

    Interactioni

    Subunit structurei

    I-alpha-I plasma protease inhibitors are assembled from one or two heavy chains (H1, H2 or H3) and one light chain, bikunin. Inter-alpha-inhibitor (I-alpha-I) is composed of H1, H2 and bikunin, inter-alpha-like inhibitor (I-alpha-LI) of H2 and bikunin, and pre-alpha-inhibitor (P-alpha-I) of H3 and bikunin. Alpha-1-microglobulin occurs as a monomer and also in complexes with IgA and albumin. Alpha-1-microglobulin interacts with FN1. Trypstatin is a monomer and also occurs as a complex with tryptase in mast cells By similarity. Alpha-1-microglobulin and bikunin interact (via SH3 domain) with HEV ORF3 protein.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CTSBP078584EBI-2115136,EBI-715062

    Protein-protein interaction databases

    BioGridi106757. 12 interactions.
    IntActiP02760. 8 interactions.
    MINTiMINT-1367019.
    STRINGi9606.ENSP00000265132.

    Structurei

    Secondary structure

    1
    352
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi37 – 393
    Beta strandi42 – 5110
    Helixi54 – 596
    Helixi60 – 623
    Beta strandi66 – 727
    Beta strandi78 – 8710
    Beta strandi90 – 10011
    Beta strandi106 – 1116
    Turni112 – 1154
    Beta strandi116 – 12510
    Beta strandi127 – 14216
    Beta strandi145 – 15511
    Helixi159 – 17012
    Turni171 – 1733
    Helixi176 – 1783
    Beta strandi179 – 1813
    Beta strandi244 – 2507
    Turni251 – 2544
    Beta strandi255 – 2617
    Beta strandi263 – 2653
    Beta strandi271 – 2733
    Helixi274 – 2818
    Helixi284 – 2885
    Beta strandi300 – 3067
    Turni307 – 3104
    Beta strandi311 – 3177
    Beta strandi319 – 3213
    Beta strandi327 – 3293
    Helixi330 – 3378

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BIKX-ray2.50A206-352[»]
    3QKGX-ray2.30A20-202[»]
    4ES7X-ray2.00A27-193[»]
    ProteinModelPortaliP02760.
    SMRiP02760. Positions 28-193, 230-339.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02760.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini231 – 28151BPTI/Kunitz inhibitor 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini287 – 33751BPTI/Kunitz inhibitor 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni206 – 22621Glycopeptide (secretory piece)Add
    BLAST

    Sequence similaritiesi

    In the N-terminal section; belongs to the calycin superfamily. Lipocalin family.Curated
    Contains 2 BPTI/Kunitz inhibitor domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG328322.
    HOVERGENiHBG000225.
    InParanoidiP02760.
    OMAiGTSMACE.
    OrthoDBiEOG73FQKT.
    PhylomeDBiP02760.
    TreeFamiTF351222.

    Family and domain databases

    Gene3Di2.40.128.20. 1 hit.
    4.10.410.10. 2 hits.
    InterProiIPR002968. A1-microglobln.
    IPR012674. Calycin.
    IPR011038. Calycin-like.
    IPR002345. Lipocalin.
    IPR022272. Lipocalin_CS.
    IPR000566. Lipocln_cytosolic_FA-bd_dom.
    IPR002223. Prot_inh_Kunz-m.
    IPR020901. Prtase_inh_Kunz-CS.
    [Graphical view]
    PfamiPF00014. Kunitz_BPTI. 2 hits.
    PF00061. Lipocalin. 1 hit.
    [Graphical view]
    PRINTSiPR01215. A1MCGLOBULIN.
    PR00759. BASICPTASE.
    PR00179. LIPOCALIN.
    SMARTiSM00131. KU. 2 hits.
    [Graphical view]
    SUPFAMiSSF50814. SSF50814. 1 hit.
    SSF57362. SSF57362. 2 hits.
    PROSITEiPS00280. BPTI_KUNITZ_1. 2 hits.
    PS50279. BPTI_KUNITZ_2. 2 hits.
    PS00213. LIPOCALIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P02760-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRSLGALLLL LSACLAVSAG PVPTPPDNIQ VQENFNISRI YGKWYNLAIG    50
    STCPWLKKIM DRMTVSTLVL GEGATEAEIS MTSTRWRKGV CEETSGAYEK 100
    TDTDGKFLYH KSKWNITMES YVVHTNYDEY AIFLTKKFSR HHGPTITAKL 150
    YGRAPQLRET LLQDFRVVAQ GVGIPEDSIF TMADRGECVP GEQEPEPILI 200
    PRVRRAVLPQ EEEGSGGGQL VTEVTKKEDS CQLGYSAGPC MGMTSRYFYN 250
    GTSMACETFQ YGGCMGNGNN FVTEKECLQT CRTVAACNLP IVRGPCRAFI 300
    QLWAFDAVKG KCVLFPYGGC QGNGNKFYSE KECREYCGVP GDGDEELLRF 350
    SN 352
    Length:352
    Mass (Da):38,999
    Last modified:August 13, 1987 - v1
    Checksum:iBC001780094CBD06
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti48 – 5710Missing AA sequence (PubMed:6164372)Curated
    Sequence conflicti57 – 571Missing AA sequence (PubMed:6198962)Curated
    Sequence conflicti57 – 571Missing AA sequence 1 PublicationCurated
    Sequence conflicti137 – 1371Missing AA sequence (PubMed:6164372)Curated
    Sequence conflicti142 – 1421H → T AA sequence (PubMed:6164372)Curated
    Sequence conflicti145 – 1451Missing AA sequence (PubMed:6164372)Curated
    Sequence conflicti194 – 1941E → Q AA sequence (PubMed:6164372)Curated
    Sequence conflicti215 – 2151S → T AA sequence (PubMed:7676539)Curated
    Sequence conflicti218 – 2181G → T AA sequence (PubMed:7676539)Curated
    Sequence conflicti291 – 2922IV → VI AA sequence (PubMed:2408638)Curated
    Sequence conflicti291 – 2922IV → VI AA sequence (PubMed:1469060)Curated
    Sequence conflicti295 – 2951Missing AA sequence (PubMed:1469060)Curated
    Sequence conflicti343 – 3431G → E AA sequence (PubMed:2408638)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04225 mRNA. Translation: CAA27803.1.
    X04494 mRNA. Translation: CAA28182.1.
    X54816, X54817, X54818 Genomic DNA. Translation: CAA38585.1.
    X54817 Genomic DNA. Translation: CAA38586.1.
    X54818 Genomic DNA. Translation: CAA38587.1.
    M88249
    , M88165, M88243, M88244, M88246, M88247 Genomic DNA. Translation: AAA59196.1.
    AY544123 mRNA. Translation: AAT11154.1.
    AK290837 mRNA. Translation: BAF83526.1.
    AL137850 Genomic DNA. Translation: CAI15899.1.
    CH471090 Genomic DNA. Translation: EAW87404.1.
    BC041593 mRNA. Translation: AAH41593.1.
    CCDSiCCDS6800.1.
    PIRiS13433. HCHU.
    RefSeqiNP_001624.1. NM_001633.3.
    UniGeneiHs.436911.

    Genome annotation databases

    EnsembliENST00000265132; ENSP00000265132; ENSG00000106927.
    GeneIDi259.
    KEGGihsa:259.
    UCSCiuc004bie.4. human.

    Polymorphism databases

    DMDMi122801.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04225 mRNA. Translation: CAA27803.1 .
    X04494 mRNA. Translation: CAA28182.1 .
    X54816 , X54817 , X54818 Genomic DNA. Translation: CAA38585.1 .
    X54817 Genomic DNA. Translation: CAA38586.1 .
    X54818 Genomic DNA. Translation: CAA38587.1 .
    M88249
    , M88165 , M88243 , M88244 , M88246 , M88247 Genomic DNA. Translation: AAA59196.1 .
    AY544123 mRNA. Translation: AAT11154.1 .
    AK290837 mRNA. Translation: BAF83526.1 .
    AL137850 Genomic DNA. Translation: CAI15899.1 .
    CH471090 Genomic DNA. Translation: EAW87404.1 .
    BC041593 mRNA. Translation: AAH41593.1 .
    CCDSi CCDS6800.1.
    PIRi S13433. HCHU.
    RefSeqi NP_001624.1. NM_001633.3.
    UniGenei Hs.436911.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BIK X-ray 2.50 A 206-352 [» ]
    3QKG X-ray 2.30 A 20-202 [» ]
    4ES7 X-ray 2.00 A 27-193 [» ]
    ProteinModelPortali P02760.
    SMRi P02760. Positions 28-193, 230-339.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106757. 12 interactions.
    IntActi P02760. 8 interactions.
    MINTi MINT-1367019.
    STRINGi 9606.ENSP00000265132.

    Chemistry

    DrugBanki DB00062. Human Serum Albumin.
    DB00064. Serum albumin iodonated.

    Protein family/group databases

    MEROPSi I02.005.

    PTM databases

    PhosphoSitei P02760.
    UniCarbKBi P02760.

    Polymorphism databases

    DMDMi 122801.

    2D gel databases

    SWISS-2DPAGE P02760.

    Proteomic databases

    MaxQBi P02760.
    PaxDbi P02760.
    PeptideAtlasi P02760.
    PRIDEi P02760.

    Protocols and materials databases

    DNASUi 259.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265132 ; ENSP00000265132 ; ENSG00000106927 .
    GeneIDi 259.
    KEGGi hsa:259.
    UCSCi uc004bie.4. human.

    Organism-specific databases

    CTDi 259.
    GeneCardsi GC09M116823.
    HGNCi HGNC:453. AMBP.
    HPAi HPA001497.
    MIMi 176870. gene.
    neXtProti NX_P02760.
    PharmGKBi PA24759.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG328322.
    HOVERGENi HBG000225.
    InParanoidi P02760.
    OMAi GTSMACE.
    OrthoDBi EOG73FQKT.
    PhylomeDBi P02760.
    TreeFami TF351222.

    Enzyme and pathway databases

    Reactomei REACT_160163. Scavenging of heme from plasma.

    Miscellaneous databases

    ChiTaRSi AMBP. human.
    EvolutionaryTracei P02760.
    GeneWikii Alpha-1-microglobulin/bikunin_precursor.
    GenomeRNAii 259.
    NextBioi 1023.
    PMAP-CutDB P02760.
    PROi P02760.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P02760.
    Bgeei P02760.
    CleanExi HS_AMBP.
    Genevestigatori P02760.

    Family and domain databases

    Gene3Di 2.40.128.20. 1 hit.
    4.10.410.10. 2 hits.
    InterProi IPR002968. A1-microglobln.
    IPR012674. Calycin.
    IPR011038. Calycin-like.
    IPR002345. Lipocalin.
    IPR022272. Lipocalin_CS.
    IPR000566. Lipocln_cytosolic_FA-bd_dom.
    IPR002223. Prot_inh_Kunz-m.
    IPR020901. Prtase_inh_Kunz-CS.
    [Graphical view ]
    Pfami PF00014. Kunitz_BPTI. 2 hits.
    PF00061. Lipocalin. 1 hit.
    [Graphical view ]
    PRINTSi PR01215. A1MCGLOBULIN.
    PR00759. BASICPTASE.
    PR00179. LIPOCALIN.
    SMARTi SM00131. KU. 2 hits.
    [Graphical view ]
    SUPFAMi SSF50814. SSF50814. 1 hit.
    SSF57362. SSF57362. 2 hits.
    PROSITEi PS00280. BPTI_KUNITZ_1. 2 hits.
    PS50279. BPTI_KUNITZ_2. 2 hits.
    PS00213. LIPOCALIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence of a full length cDNA coding for human protein HC (alpha 1 microglobulin)."
      Traboni C., Cortese R.
      Nucleic Acids Res. 14:6340-6340(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The mRNA for a proteinase inhibitor related to the HI-30 domain of inter-alpha-trypsin inhibitor also encodes alpha-1-microglobulin (protein HC)."
      Kaumeyer J.F., Polazzi J.O., Kotick M.P.
      Nucleic Acids Res. 14:7839-7850(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    3. "Structure of the human alpha 1-microglobulin-bikunin gene."
      Vetr H., Gebhard W.
      Biol. Chem. Hoppe-Seyler 371:1185-1196(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Structural analysis of the human inter-alpha-trypsin inhibitor light-chain gene."
      Diarra-Mehrpour M., Bourguignon J., Sesboue R., Salier J.-P., Leveillard T., Martin J.-P.
      Eur. J. Biochem. 191:131-139(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Liver.
    5. "Identification of a human cell growth inhibition gene."
      Kim J.W.
      Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. "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.
    7. "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].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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. "The complete amino acid sequence of human complex-forming glycoprotein heterogeneous in charge (protein HC) from one individual."
      Lopez C., Grubb A.O., Mendez E.
      Arch. Biochem. Biophys. 228:544-554(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-202.
    11. "Complete amino acid sequence of human alpha 1-microglobulin."
      Takagi T., Takagi K., Kawai T.
      Biochem. Biophys. Res. Commun. 98:997-1001(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-198.
    12. "Human protein HC displays variability in its carboxyl-terminal amino acid sequence."
      Lopez C., Grubb A.O., Mendez E.
      FEBS Lett. 144:349-353(1982)
      Cited for: PROTEIN SEQUENCE OF 20-198.
    13. "Location of a novel type of interpolypeptide chain linkage in the human protein HC-IgA complex (HC-IgA) and identification of a heterogeneous chromophore associated with the complex."
      Calero M., Escribano J., Grubb A., Mendez E.
      J. Biol. Chem. 269:384-389(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 44-57, BINDING TO CHROMOPHORE.
    14. "Human inter-alpha-trypsin inhibitor: localization of the Kunitz-type domains in the N-terminal part of the molecule and their release by a trypsin-like proteinase."
      Reisinger P., Hochstrasser K., Albrecht G.J., Lempart K., Salier J.-P.
      Biol. Chem. Hoppe-Seyler 366:479-483(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 206-350.
    15. "Cancer-related urinary proteinase inhibitor, EDC1: a new method for its isolation and evidence for multiple forms."
      Chawla R.K., Lawson D.H., Ahmad M., Travis J.
      J. Cell. Biochem. 50:227-236(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 206-243 AND 275-303.
      Tissue: Urine.
    16. "Chondroitin 4-sulfate covalently cross-links the chains of the human blood protein pre-alpha-inhibitor."
      Enghild J.J., Salvesen G., Hefta S.A., Thoegersen I.B., Rutherfurd S., Pizzo S.V.
      J. Biol. Chem. 266:747-751(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 206-223, GLYCOSYLATION AT SER-215, CROSS-LINK SITE TO HC3.
    17. "Presence of the protein-glycosaminoglycan-protein covalent cross-link in the inter-alpha-inhibitor-related proteinase inhibitor heavy chain 2/bikunin."
      Enghild J.J., Salvesen G., Thoegersen I.B., Valnickova Z., Pizzo S.V., Hefta S.A.
      J. Biol. Chem. 268:8711-8716(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 206-223, GLYCOSYLATION AT SER-215, CROSS-LINK SITE TO HC2.
    18. "Characterization of uronic-acid-rich inhibitor of calcium oxalate crystallization isolated from rat urine."
      Atmani F., Khan S.R.
      Urol. Res. 23:95-101(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 206-223, FUNCTION.
      Tissue: Urine.
    19. "Chondroitin sulphate covalently cross-links the three polypeptide chains of inter-alpha-trypsin inhibitor."
      Morelle W., Capon C., Balduyck M., Sautiere P., Kouach M., Michalski C., Fournet B., Mizon J.
      Eur. J. Biochem. 221:881-888(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 206-219, COVALENT LINKAGE WITH CHONDROITIN SULFATE.
      Tissue: Plasma.
    20. "Kunitz-type proteinase inhibitors derived by limited proteolysis of the inter-alpha-trypsin inhibitor, V. Attachments of carbohydrates in the human urinary trypsin inhibitor isolated by affinity chromatography."
      Hochstrasser K., Schoenberger O.L., Rossmanith I., Wachter E.
      Hoppe-Seyler's Z. Physiol. Chem. 362:1357-1362(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT SER-215 AND ASN-250, STRUCTURE OF CARBOHYDRATES.
    21. "The reactive site of human inter-alpha-trypsin inhibitor is in the amino-terminal half of the protein."
      Morii M., Travis J.
      Biol. Chem. Hoppe-Seyler 366:19-21(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: INHIBITORY SITE.
    22. "Location and characterization of the three carbohydrate prosthetic groups of human protein HC."
      Escribano J., Lopex-Otin C., Hjerpe A., Grubb A.O., Mendez E.
      FEBS Lett. 266:167-170(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT THR-24; ASN-36 AND ASN-115, STRUCTURE OF CARBOHYDRATES.
    23. "The protein HC chromophore is linked to the cysteine residue at position 34 of the polypeptide chain by a reduction-resistant bond and causes the charge heterogeneity of protein HC."
      Escribano J., Grubb A.O., Calero M., Mendez E.
      J. Biol. Chem. 266:15758-15763(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: BINDING TO CHROMOPHORE.
      Tissue: Urine.
    24. "Alpha1-microglobulin chromophores are located to three lysine residues semiburied in the lipocalin pocket and associated with a novel lipophilic compound."
      Berggaard T., Cohen A., Persson P., Lindqvist A., Cedervall T., Silow M., Thoegersen I.B., Joensson J.A., Enghild J.J., Aakerstroem B.
      Protein Sci. 8:2611-2620(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: BINDING TO CHROMOPHORE.
    25. "Human alpha-1-microglobulin is covalently bound to kynurenine-derived chromophores."
      Sala A., Campagnoli M., Perani E., Romano A., Labo S., Monzani E., Minchiotti L., Galliano M.
      J. Biol. Chem. 279:51033-51041(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOPHORE CHARACTERIZATION.
    26. "The ORF3 protein of hepatitis E virus interacts with liver-specific alpha1-microglobulin and its precursor alpha1-microglobulin/bikunin precursor (AMBP) and expedites their export from the hepatocyte."
      Tyagi S., Surjit M., Roy A.K., Jameel S., Lal S.K.
      J. Biol. Chem. 279:29308-29319(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION OF ALPHA-1-MICROGLOBULIN WITH HEV ORF3 PROTEIN.
    27. "The 41-amino-acid C-terminal region of the hepatitis E virus ORF3 protein interacts with bikunin, a Kunitz-type serine protease inhibitor."
      Tyagi S., Surjit M., Lal S.K.
      J. Virol. 79:12081-12087(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION OF BIKUNIN WITH HEV ORF3 PROTEIN.
    28. "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-115 AND ASN-250, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
    29. "The crystal structure of bikunin from the inter-alpha-inhibitor complex: a serine protease inhibitor with two Kunitz domains."
      Xu Y., Carr P.D., Guss J.M., Ollis D.L.
      J. Mol. Biol. 276:955-966(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 230-339.
    30. "Alpha(1)-microglobulin: a yellow-brown lipocalin."
      Aakerstroem B., Loegdberg L., Berggaard T., Osmark P., Lindqvist A.
      Biochim. Biophys. Acta 1482:172-184(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.

    Entry informationi

    Entry nameiAMBP_HUMAN
    AccessioniPrimary (citable) accession number: P02760
    Secondary accession number(s): P00977
    , P02759, P78491, Q2TU33, Q5TBD7, Q9UC58, Q9UDI8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: August 13, 1987
    Last modified: October 1, 2014
    This is version 180 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

    Miscellaneous

    In vitro, the first twelve residues of the amino end of the inhibitor appear to have a reactive site capable of inhibiting the activity of a number of enzymes. Its in vivo function is not known.

    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. 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