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)

P01023

- A2MG_HUMAN

UniProt

P01023 - A2MG_HUMAN

Protein

Alpha-2-macroglobulin

Gene

A2M

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 174 (01 Oct 2014)
      Sequence version 3 (05 Oct 2010)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase.

    GO - Molecular functioni

    1. calcium-dependent protein binding Source: AgBase
    2. enzyme binding Source: UniProtKB
    3. growth factor binding Source: UniProtKB
    4. interleukin-1 binding Source: UniProtKB
    5. interleukin-8 binding Source: UniProtKB
    6. protease binding Source: BHF-UCL
    7. protein binding Source: UniProtKB
    8. receptor binding Source: AgBase
    9. serine-type endopeptidase inhibitor activity Source: UniProtKB
    10. tumor necrosis factor binding Source: UniProtKB

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. blood coagulation, intrinsic pathway Source: Reactome
    3. extracellular matrix disassembly Source: Reactome
    4. extracellular matrix organization Source: Reactome
    5. negative regulation of complement activation, lectin pathway Source: UniProtKB
    6. negative regulation of endopeptidase activity Source: GOC
    7. platelet activation Source: Reactome
    8. platelet degranulation Source: Reactome
    9. regulation of small GTPase mediated signal transduction Source: Reactome
    10. small GTPase mediated signal transduction Source: Reactome
    11. stem cell differentiation Source: Ensembl

    Keywords - Molecular functioni

    Protease inhibitor, Serine protease inhibitor

    Enzyme and pathway databases

    ReactomeiREACT_11051. Rho GTPase cycle.
    REACT_118572. Degradation of the extracellular matrix.
    REACT_13621. HDL-mediated lipid transport.
    REACT_326. Intrinsic Pathway.

    Protein family/group databases

    MEROPSiI39.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-2-macroglobulin
    Short name:
    Alpha-2-M
    Alternative name(s):
    C3 and PZP-like alpha-2-macroglobulin domain-containing protein 5
    Gene namesi
    Name:A2M
    Synonyms:CPAMD5
    ORF Names:FWP007
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:7. A2M.

    Subcellular locationi

    Secreted 1 Publication

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. cytosol Source: Reactome
    3. extracellular region Source: UniProtKB
    4. extracellular vesicular exosome Source: UniProtKB
    5. platelet alpha granule lumen Source: Reactome

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24357.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 23231 PublicationAdd
    BLAST
    Chaini24 – 14741451Alpha-2-macroglobulin1 PublicationPRO_0000000055Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi48 ↔ 861 Publication
    Glycosylationi55 – 551N-linked (GlcNAc...) (complex)2 Publications
    Glycosylationi70 – 701N-linked (GlcNAc...)1 Publication
    Glycosylationi247 – 2471N-linked (GlcNAc...)2 Publications
    Disulfide bondi251 ↔ 2991 Publication
    Disulfide bondi269 ↔ 2871 Publication
    Disulfide bondi278 – 278Interchain (with C-431)
    Glycosylationi396 – 3961N-linked (GlcNAc...)3 Publications
    Glycosylationi410 – 4101N-linked (GlcNAc...)2 Publications
    Disulfide bondi431 – 431Interchain (with C-278)
    Disulfide bondi470 ↔ 563
    Disulfide bondi595 ↔ 7711 Publication
    Disulfide bondi642 ↔ 6891 Publication
    Cross-linki693 – 693Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-? in other proteins)Sequence Analysis
    Cross-linki694 – 694Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-? in other proteins)Sequence Analysis
    Disulfide bondi821 ↔ 8491 Publication
    Disulfide bondi847 ↔ 8831 Publication
    Glycosylationi869 – 8691N-linked (GlcNAc...)2 Publications
    Disulfide bondi921 ↔ 13211 Publication
    Cross-linki972 ↔ 975Isoglutamyl cysteine thioester (Cys-Gln)1 Publication
    Glycosylationi991 – 9911N-linked (GlcNAc...)4 Publications
    Disulfide bondi1079 ↔ 11271 Publication
    Disulfide bondi1352 ↔ 14671 Publication
    Glycosylationi1424 – 14241N-linked (GlcNAc...) (complex)4 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Isopeptide bond, Thioester bond

    Proteomic databases

    MaxQBiP01023.
    PaxDbiP01023.
    PeptideAtlasiP01023.
    PRIDEiP01023.

    2D gel databases

    DOSAC-COBS-2DPAGEP01023.
    SWISS-2DPAGEP01023.

    PTM databases

    PhosphoSiteiP01023.

    Expressioni

    Tissue specificityi

    Secreted in plasma.1 Publication

    Developmental stagei

    Contrary to the rat protein, which is an acute phase protein, this protein is always present at high levels in circulation.

    Gene expression databases

    ArrayExpressiP01023.
    BgeeiP01023.
    CleanExiHS_A2M.
    GenevestigatoriP01023.

    Organism-specific databases

    HPAiCAB017621.
    HPA002265.

    Interactioni

    Subunit structurei

    Homotetramer; disulfide-linked.2 Publications

    Protein-protein interaction databases

    BioGridi106524. 89 interactions.
    DIPiDIP-1118N.
    IntActiP01023. 99 interactions.
    MINTiMINT-122288.
    STRINGi9606.ENSP00000323929.

    Structurei

    Secondary structure

    1
    1474
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi128 – 1347
    Beta strandi136 – 1383
    Beta strandi143 – 1519
    Helixi153 – 1553
    Beta strandi161 – 1688
    Beta strandi174 – 1829
    Beta strandi187 – 1937
    Beta strandi201 – 2088
    Beta strandi214 – 2218
    Beta strandi1341 – 13477
    Helixi1355 – 13595
    Beta strandi1360 – 136910
    Beta strandi1379 – 13846
    Beta strandi1389 – 13913
    Helixi1393 – 14008
    Turni1401 – 14033
    Beta strandi1407 – 14104
    Beta strandi1412 – 14198
    Beta strandi1427 – 14348
    Beta strandi1445 – 14506
    Beta strandi1454 – 14563
    Beta strandi1459 – 14635

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BV8NMR-A1337-1474[»]
    2P9RX-ray2.30A/B126-227[»]
    4ACQX-ray4.30A/B/C/D24-1474[»]
    ProteinModelPortaliP01023.
    SMRiP01023. Positions 126-227, 1338-1474.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP01023.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni690 – 72839Bait regionAdd
    BLAST
    Regioni704 – 7096Inhibitory
    Regioni719 – 7235Inhibitory
    Regioni730 – 7356Inhibitory

    Sequence similaritiesi

    Keywords - Domaini

    Bait region, Signal

    Phylogenomic databases

    eggNOGiCOG2373.
    HOVERGENiHBG000039.
    KOiK03910.
    OMAiQTVQAHY.
    OrthoDBiEOG7DJSKB.
    PhylomeDBiP01023.
    TreeFamiTF313285.

    Family and domain databases

    Gene3Di1.50.10.20. 1 hit.
    2.60.40.690. 1 hit.
    InterProiIPR009048. A-macroglobulin_rcpt-bd.
    IPR011626. A2M_comp.
    IPR002890. A2M_N.
    IPR011625. A2M_N_2.
    IPR014756. Ig_E-set.
    IPR001599. Macroglobln_a2.
    IPR019742. MacrogloblnA2_CS.
    IPR019565. MacrogloblnA2_thiol-ester-bond.
    IPR008930. Terpenoid_cyclase/PrenylTrfase.
    IPR010916. TonB_box_CS.
    [Graphical view]
    PfamiPF00207. A2M. 1 hit.
    PF07678. A2M_comp. 1 hit.
    PF01835. A2M_N. 1 hit.
    PF07703. A2M_N_2. 1 hit.
    PF07677. A2M_recep. 1 hit.
    PF10569. Thiol-ester_cl. 1 hit.
    [Graphical view]
    SUPFAMiSSF48239. SSF48239. 1 hit.
    SSF49410. SSF49410. 1 hit.
    SSF81296. SSF81296. 1 hit.
    PROSITEiPS00477. ALPHA_2_MACROGLOBULIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P01023-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGKNKLLHPS LVLLLLVLLP TDASVSGKPQ YMVLVPSLLH TETTEKGCVL     50
    LSYLNETVTV SASLESVRGN RSLFTDLEAE NDVLHCVAFA VPKSSSNEEV 100
    MFLTVQVKGP TQEFKKRTTV MVKNEDSLVF VQTDKSIYKP GQTVKFRVVS 150
    MDENFHPLNE LIPLVYIQDP KGNRIAQWQS FQLEGGLKQF SFPLSSEPFQ 200
    GSYKVVVQKK SGGRTEHPFT VEEFVLPKFE VQVTVPKIIT ILEEEMNVSV 250
    CGLYTYGKPV PGHVTVSICR KYSDASDCHG EDSQAFCEKF SGQLNSHGCF 300
    YQQVKTKVFQ LKRKEYEMKL HTEAQIQEEG TVVELTGRQS SEITRTITKL 350
    SFVKVDSHFR QGIPFFGQVR LVDGKGVPIP NKVIFIRGNE ANYYSNATTD 400
    EHGLVQFSIN TTNVMGTSLT VRVNYKDRSP CYGYQWVSEE HEEAHHTAYL 450
    VFSPSKSFVH LEPMSHELPC GHTQTVQAHY ILNGGTLLGL KKLSFYYLIM 500
    AKGGIVRTGT HGLLVKQEDM KGHFSISIPV KSDIAPVARL LIYAVLPTGD 550
    VIGDSAKYDV ENCLANKVDL SFSPSQSLPA SHAHLRVTAA PQSVCALRAV 600
    DQSVLLMKPD AELSASSVYN LLPEKDLTGF PGPLNDQDNE DCINRHNVYI 650
    NGITYTPVSS TNEKDMYSFL EDMGLKAFTN SKIRKPKMCP QLQQYEMHGP 700
    EGLRVGFYES DVMGRGHARL VHVEEPHTET VRKYFPETWI WDLVVVNSAG 750
    VAEVGVTVPD TITEWKAGAF CLSEDAGLGI SSTASLRAFQ PFFVELTMPY 800
    SVIRGEAFTL KATVLNYLPK CIRVSVQLEA SPAFLAVPVE KEQAPHCICA 850
    NGRQTVSWAV TPKSLGNVNF TVSAEALESQ ELCGTEVPSV PEHGRKDTVI 900
    KPLLVEPEGL EKETTFNSLL CPSGGEVSEE LSLKLPPNVV EESARASVSV 950
    LGDILGSAMQ NTQNLLQMPY GCGEQNMVLF APNIYVLDYL NETQQLTPEI 1000
    KSKAIGYLNT GYQRQLNYKH YDGSYSTFGE RYGRNQGNTW LTAFVLKTFA 1050
    QARAYIFIDE AHITQALIWL SQRQKDNGCF RSSGSLLNNA IKGGVEDEVT 1100
    LSAYITIALL EIPLTVTHPV VRNALFCLES AWKTAQEGDH GSHVYTKALL 1150
    AYAFALAGNQ DKRKEVLKSL NEEAVKKDNS VHWERPQKPK APVGHFYEPQ 1200
    APSAEVEMTS YVLLAYLTAQ PAPTSEDLTS ATNIVKWITK QQNAQGGFSS 1250
    TQDTVVALHA LSKYGAATFT RTGKAAQVTI QSSGTFSSKF QVDNNNRLLL 1300
    QQVSLPELPG EYSMKVTGEG CVYLQTSLKY NILPEKEEFP FALGVQTLPQ 1350
    TCDEPKAHTS FQISLSVSYT GSRSASNMAI VDVKMVSGFI PLKPTVKMLE 1400
    RSNHVSRTEV SSNHVLIYLD KVSNQTLSLF FTVLQDVPVR DLKPAIVKVY 1450
    DYYETDEFAI AEYNAPCSKD LGNA 1474
    Length:1,474
    Mass (Da):163,291
    Last modified:October 5, 2010 - v3
    Checksum:i0A46DF09EFD3CF40
    GO

    Sequence cautioni

    The sequence AAT02228.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAD92851.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti63 – 631Missing AA sequence (PubMed:6203908)Curated
    Sequence conflicti82 – 821D → V in AAT02228. 1 PublicationCurated
    Sequence conflicti350 – 3534LSFV → ACCS in AAH26246. (PubMed:15489334)Curated
    Sequence conflicti563 – 5631C → E AA sequence (PubMed:6203908)Curated
    Sequence conflicti844 – 8441A → V in BAD92851. (PubMed:17974005)Curated
    Sequence conflicti872 – 8721V → M in CAH18188. (PubMed:16541075)Curated
    Sequence conflicti1148 – 11481A → D in AAA51552. (PubMed:2408344)Curated
    Sequence conflicti1195 – 11951H → D in AAA51552. (PubMed:2408344)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti639 – 6391N → D.5 Publications
    Corresponds to variant rs226405 [ dbSNP | Ensembl ].
    VAR_026820
    Natural varianti704 – 7041R → H.
    Corresponds to variant rs1800434 [ dbSNP | Ensembl ].
    VAR_000012
    Natural varianti815 – 8151L → Q.
    Corresponds to variant rs3180392 [ dbSNP | Ensembl ].
    VAR_026821
    Natural varianti972 – 9721C → Y Probably interferes with the activity. 1 Publication
    Corresponds to variant rs1800433 [ dbSNP | Ensembl ].
    VAR_000013
    Natural varianti1000 – 10001I → V.5 Publications
    Corresponds to variant rs669 [ dbSNP | Ensembl ].
    VAR_000014

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M11313 mRNA. Translation: AAA51551.1.
    AY591530 mRNA. Translation: AAT02228.1. Different initiation.
    AB209614 mRNA. Translation: BAD92851.1. Different initiation.
    CR749334 mRNA. Translation: CAH18188.1.
    AC007436 Genomic DNA. No translation available.
    BC026246 mRNA. Translation: AAH26246.1.
    BC040071 mRNA. Translation: AAH40071.1.
    Z11711 Genomic DNA. Translation: CAA77774.1.
    X68728, X68729 Genomic DNA. Translation: CAA48670.1.
    M36501 mRNA. Translation: AAA51552.1.
    AF109189 mRNA. Translation: AAQ13498.1.
    CCDSiCCDS44827.1.
    PIRiA94033. MAHU.
    RefSeqiNP_000005.2. NM_000014.4.
    UniGeneiHs.212838.

    Genome annotation databases

    EnsembliENST00000318602; ENSP00000323929; ENSG00000175899.
    GeneIDi2.
    KEGGihsa:2.
    UCSCiuc001qvk.1. human.

    Polymorphism databases

    DMDMi308153640.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Alpha-2 macroglobulin entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M11313 mRNA. Translation: AAA51551.1 .
    AY591530 mRNA. Translation: AAT02228.1 . Different initiation.
    AB209614 mRNA. Translation: BAD92851.1 . Different initiation.
    CR749334 mRNA. Translation: CAH18188.1 .
    AC007436 Genomic DNA. No translation available.
    BC026246 mRNA. Translation: AAH26246.1 .
    BC040071 mRNA. Translation: AAH40071.1 .
    Z11711 Genomic DNA. Translation: CAA77774.1 .
    X68728 , X68729 Genomic DNA. Translation: CAA48670.1 .
    M36501 mRNA. Translation: AAA51552.1 .
    AF109189 mRNA. Translation: AAQ13498.1 .
    CCDSi CCDS44827.1.
    PIRi A94033. MAHU.
    RefSeqi NP_000005.2. NM_000014.4.
    UniGenei Hs.212838.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BV8 NMR - A 1337-1474 [» ]
    2P9R X-ray 2.30 A/B 126-227 [» ]
    4ACQ X-ray 4.30 A/B/C/D 24-1474 [» ]
    ProteinModelPortali P01023.
    SMRi P01023. Positions 126-227, 1338-1474.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106524. 89 interactions.
    DIPi DIP-1118N.
    IntActi P01023. 99 interactions.
    MINTi MINT-122288.
    STRINGi 9606.ENSP00000323929.

    Chemistry

    DrugBanki DB00626. Bacitracin.
    DB00102. Becaplermin.
    DB08888. Ocriplasmin.

    Protein family/group databases

    MEROPSi I39.001.

    PTM databases

    PhosphoSitei P01023.

    Polymorphism databases

    DMDMi 308153640.

    2D gel databases

    DOSAC-COBS-2DPAGE P01023.
    SWISS-2DPAGE P01023.

    Proteomic databases

    MaxQBi P01023.
    PaxDbi P01023.
    PeptideAtlasi P01023.
    PRIDEi P01023.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000318602 ; ENSP00000323929 ; ENSG00000175899 .
    GeneIDi 2.
    KEGGi hsa:2.
    UCSCi uc001qvk.1. human.

    Organism-specific databases

    CTDi 2.
    GeneCardsi GC12M009220.
    H-InvDB HIX0026392.
    HGNCi HGNC:7. A2M.
    HPAi CAB017621.
    HPA002265.
    MIMi 103950. gene.
    neXtProti NX_P01023.
    PharmGKBi PA24357.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2373.
    HOVERGENi HBG000039.
    KOi K03910.
    OMAi QTVQAHY.
    OrthoDBi EOG7DJSKB.
    PhylomeDBi P01023.
    TreeFami TF313285.

    Enzyme and pathway databases

    Reactomei REACT_11051. Rho GTPase cycle.
    REACT_118572. Degradation of the extracellular matrix.
    REACT_13621. HDL-mediated lipid transport.
    REACT_326. Intrinsic Pathway.

    Miscellaneous databases

    ChiTaRSi A2M. human.
    EvolutionaryTracei P01023.
    GenomeRNAii 2.
    NextBioi 5.
    PROi P01023.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P01023.
    Bgeei P01023.
    CleanExi HS_A2M.
    Genevestigatori P01023.

    Family and domain databases

    Gene3Di 1.50.10.20. 1 hit.
    2.60.40.690. 1 hit.
    InterProi IPR009048. A-macroglobulin_rcpt-bd.
    IPR011626. A2M_comp.
    IPR002890. A2M_N.
    IPR011625. A2M_N_2.
    IPR014756. Ig_E-set.
    IPR001599. Macroglobln_a2.
    IPR019742. MacrogloblnA2_CS.
    IPR019565. MacrogloblnA2_thiol-ester-bond.
    IPR008930. Terpenoid_cyclase/PrenylTrfase.
    IPR010916. TonB_box_CS.
    [Graphical view ]
    Pfami PF00207. A2M. 1 hit.
    PF07678. A2M_comp. 1 hit.
    PF01835. A2M_N. 1 hit.
    PF07703. A2M_N_2. 1 hit.
    PF07677. A2M_recep. 1 hit.
    PF10569. Thiol-ester_cl. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48239. SSF48239. 1 hit.
    SSF49410. SSF49410. 1 hit.
    SSF81296. SSF81296. 1 hit.
    PROSITEi PS00477. ALPHA_2_MACROGLOBULIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of cDNA encoding human alpha 2-macroglobulin and assignment of the chromosomal locus."
      Kan C.-C., Solomon E., Belt K.T., Chain A.C., Hiorns L.R., Fey G.H.
      Proc. Natl. Acad. Sci. U.S.A. 82:2282-2286(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ASP-639 AND VAL-1000.
    2. "Alpha(2) macroglobulin, a PSA-binding protein, is expressed in human prostate stroma."
      Lin V.K., Wang S.-Y., Boetticher N.C., Vazquez D.V., Saboorian H., McConnell J.D., Roehrborn C.G.
      Prostate 63:299-308(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ASP-639 AND VAL-1000.
      Tissue: Prostate.
    3. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASP-639.
      Tissue: Spleen.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ASP-639 AND VAL-1000.
      Tissue: Liver.
    5. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 ASP-639 AND VAL-1000.
      Tissue: Skin.
    7. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
      Tissue: Placenta.
    8. "Primary structure of human alpha 2-macroglobulin. V. The complete structure."
      Sottrup-Jensen L., Stepanik T.M., Kristensen T., Wierzbicki D.M., Jones C.M., Loenblad P.B., Magnusson S., Petersen T.E.
      J. Biol. Chem. 259:8318-8327(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 24-1474, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISULFIDE BONDS.
    9. "Primary structure of human alpha 2-macroglobulin. Complete disulfide bridge assignment and localization of two interchain bridges in the dimeric proteinase binding unit."
      Jensen P.E.H., Sottrup-Jensen L.
      J. Biol. Chem. 261:15863-15869(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 273-286 AND 426-436, DISULFIDE BONDS.
    10. "A genetic polymorphism in a functional domain of human pregnancy zone protein: the bait region. Genomic structure of the bait domains of human pregnancy zone protein and alpha 2 macroglobulin."
      Marynen P., Devriendt K., van den Berghe H., Cassiman J.-J.
      FEBS Lett. 262:349-352(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 672-747.
    11. "Cloning of the human alpha 2-macroglobulin gene and detection of mutations in two functional domains: the bait region and the thiolester site."
      Poller W., Faber J.-P., Klobeck G., Olek K.
      Hum. Genet. 88:313-319(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 672-746, VARIANT TYR-972.
    12. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 832-1474.
      Tissue: Liver.
    13. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1208-1474.
      Tissue: Aorta.
    14. "Proteolytic cleavage sites on alpha 2-macroglobulin resulting in proteinase binding are different for trypsin and Staphylococcus aureus V-8 proteinase."
      Hall P.K., Nelles L.P., Travis J., Roberts R.C.
      Biochem. Biophys. Res. Commun. 100:8-16(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: INHIBITORY SITE.
    15. "Primary structure of the 'bait' region for proteinases in alpha 2-macroglobulin. Nature of the complex."
      Sottrup-Jensen L., Loenblad P.B., Stepanik T.M., Petersen T.E., Magnusson S., Joernvall H.
      FEBS Lett. 127:167-173(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: INHIBITORY SITE.
    16. "Primary and secondary cleavage sites in the bait region of alpha 2-macroglobulin."
      Mortensen S.B., Sottrup-Jensen L., Hansen H.F., Petersen T.E., Magnusson S.
      FEBS Lett. 135:295-300(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: INHIBITORY SITE.
    17. "Human neutrophil elastase and cathepsin G cleavage sites in the bait region of alpha 2-macroglobulin. Proposed structural limits of the bait region."
      Virca G.D., Salvesen G.S., Travis J.
      Hoppe-Seyler's Z. Physiol. Chem. 364:1297-1302(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: INHIBITORY SITE.
    18. "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-991.
    19. "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-869 AND ASN-1424.
      Tissue: Plasma.
    20. "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-55; ASN-247; ASN-396; ASN-410; ASN-869; ASN-991 AND ASN-1424.
      Tissue: Plasma.
    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-396; ASN-991 AND ASN-1424.
      Tissue: Liver.
    22. Cited for: GLYCOSYLATION AT ASN-55 AND ASN-1424.
    23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "Localization of basic residues required for receptor binding to the single alpha-helix of the receptor binding domain of human alpha2-macroglobulin."
      Huang W., Dolmer K., Liao X., Gettins P.G.W.
      Protein Sci. 7:2602-2612(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1337-1474.
    25. "Human alpha2-macroglobulin is composed of multiple domains, as predicted by homology with complement component C3."
      Doan N., Gettins P.G.W.
      Biochem. J. 407:23-30(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 126-227, DOMAIN STRUCTURE.
    26. "Sequence polymorphism in the human alpha2-macroglobulin (A2M) gene."
      Poller W., Faber J.-P., Olek K.
      Nucleic Acids Res. 19:198-198(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VAL-1000.

    Entry informationi

    Entry nameiA2MG_HUMAN
    AccessioniPrimary (citable) accession number: P01023
    Secondary accession number(s): Q13677
    , Q59F47, Q5QTS0, Q68DN2, Q6PIY3, Q6PN97
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 174 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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