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P01023 (A2MG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 169. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-2-macroglobulin

Short name=Alpha-2-M
Alternative name(s):
C3 and PZP-like alpha-2-macroglobulin domain-containing protein 5
Gene names
Name:A2M
Synonyms:CPAMD5
ORF Names:FWP007
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1474 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

Homotetramer; disulfide-linked. Ref.8 Ref.10

Subcellular location

Secreted Ref.8.

Tissue specificity

Secreted in plasma. Ref.8

Developmental stage

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

Sequence similarities

Belongs to the protease inhibitor I39 (alpha-2-macroglobulin) family. [View classification]

Sequence caution

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.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainBait region
Signal
   Molecular functionProtease inhibitor
Serine protease inhibitor
   PTMDisulfide bond
Glycoprotein
Isopeptide bond
Thioester bond
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Traceable author statement. Source: Reactome

blood coagulation, intrinsic pathway

Traceable author statement. Source: Reactome

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

negative regulation of complement activation, lectin pathway

Inferred from direct assay PubMed 12538697. Source: UniProtKB

negative regulation of endopeptidase activity

Inferred from direct assay PubMed 12538697. Source: GOC

platelet activation

Traceable author statement. Source: Reactome

platelet degranulation

Traceable author statement. Source: Reactome

regulation of small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

stem cell differentiation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentblood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

cytosol

Traceable author statement. Source: Reactome

extracellular region

Non-traceable author statement PubMed 14718574. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 21362503. Source: UniProtKB

platelet alpha granule lumen

Traceable author statement. Source: Reactome

   Molecular_functionenzyme binding

Inferred from physical interaction PubMed 11435418. Source: UniProtKB

growth factor binding

Inferred from direct assay PubMed 9398211. Source: UniProtKB

interleukin-1 binding

Inferred from direct assay PubMed 9714181. Source: UniProtKB

interleukin-8 binding

Inferred from physical interaction PubMed 10880251. Source: UniProtKB

protease binding

Inferred from physical interaction PubMed 18485748. Source: BHF-UCL

serine-type endopeptidase inhibitor activity

Inferred from direct assay PubMed 12538697. Source: UniProtKB

tumor necrosis factor binding

Inferred from direct assay PubMed 9714181. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Ref.8
Chain24 – 14741451Alpha-2-macroglobulin Ref.8
PRO_0000000055

Regions

Region690 – 72839Bait region
Region704 – 7096Inhibitory
Region719 – 7235Inhibitory
Region730 – 7356Inhibitory

Amino acid modifications

Glycosylation551N-linked (GlcNAc...) (complex) Ref.21 Ref.23
Glycosylation701N-linked (GlcNAc...) Ref.8
Glycosylation2471N-linked (GlcNAc...) Ref.8 Ref.21
Glycosylation3961N-linked (GlcNAc...) Ref.8 Ref.21 Ref.22
Glycosylation4101N-linked (GlcNAc...) Ref.8 Ref.21
Glycosylation8691N-linked (GlcNAc...) Ref.20 Ref.21
Glycosylation9911N-linked (GlcNAc...) Ref.8 Ref.19 Ref.21 Ref.22
Glycosylation14241N-linked (GlcNAc...) (complex) Ref.20 Ref.21 Ref.22 Ref.23
Disulfide bond48 ↔ 86 Ref.8 Ref.10
Disulfide bond251 ↔ 299 Ref.8 Ref.10
Disulfide bond269 ↔ 287 Ref.8 Ref.10
Disulfide bond278Interchain (with C-431) Ref.8 Ref.10
Disulfide bond431Interchain (with C-278) Ref.8 Ref.10
Disulfide bond470 ↔ 563 Ref.8 Ref.10
Disulfide bond595 ↔ 771 Ref.8 Ref.10
Disulfide bond642 ↔ 689 Ref.8 Ref.10
Disulfide bond821 ↔ 849 Ref.8 Ref.10
Disulfide bond847 ↔ 883 Ref.8 Ref.10
Disulfide bond921 ↔ 1321 Ref.8 Ref.10
Disulfide bond1079 ↔ 1127 Ref.8 Ref.10
Disulfide bond1352 ↔ 1467 Ref.8 Ref.10
Cross-link693Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-? in other proteins) Potential
Cross-link694Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-? in other proteins) Potential
Cross-link972 ↔ 975Isoglutamyl cysteine thioester (Cys-Gln) Ref.8

Natural variations

Natural variant6391N → D. Ref.1 Ref.2 Ref.3 Ref.4 Ref.6
Corresponds to variant rs226405 [ dbSNP | Ensembl ].
VAR_026820
Natural variant7041R → H.
Corresponds to variant rs1800434 [ dbSNP | Ensembl ].
VAR_000012
Natural variant8151L → Q.
Corresponds to variant rs3180392 [ dbSNP | Ensembl ].
VAR_026821
Natural variant9721C → Y Probably interferes with the activity. Ref.12
Corresponds to variant rs1800433 [ dbSNP | Ensembl ].
VAR_000013
Natural variant10001I → V. Ref.1 Ref.2 Ref.4 Ref.6 Ref.27
Corresponds to variant rs669 [ dbSNP | Ensembl ].
VAR_000014

Experimental info

Sequence conflict631Missing AA sequence Ref.8
Sequence conflict821D → V in AAT02228. Ref.3
Sequence conflict350 – 3534LSFV → ACCS in AAH26246. Ref.6
Sequence conflict5631C → E AA sequence Ref.8
Sequence conflict8441A → V in BAD92851. Ref.4
Sequence conflict8721V → M in CAH18188. Ref.5
Sequence conflict11481A → D in AAA51552. Ref.13
Sequence conflict11951H → D in AAA51552. Ref.13

Secondary structure

........................................... 1474
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P01023 [UniParc].

Last modified October 5, 2010. Version 3.
Checksum: 0A46DF09EFD3CF40

FASTA1,474163,291
        10         20         30         40         50         60 
MGKNKLLHPS LVLLLLVLLP TDASVSGKPQ YMVLVPSLLH TETTEKGCVL LSYLNETVTV 

        70         80         90        100        110        120 
SASLESVRGN RSLFTDLEAE NDVLHCVAFA VPKSSSNEEV MFLTVQVKGP TQEFKKRTTV 

       130        140        150        160        170        180 
MVKNEDSLVF VQTDKSIYKP GQTVKFRVVS MDENFHPLNE LIPLVYIQDP KGNRIAQWQS 

       190        200        210        220        230        240 
FQLEGGLKQF SFPLSSEPFQ GSYKVVVQKK SGGRTEHPFT VEEFVLPKFE VQVTVPKIIT 

       250        260        270        280        290        300 
ILEEEMNVSV CGLYTYGKPV PGHVTVSICR KYSDASDCHG EDSQAFCEKF SGQLNSHGCF 

       310        320        330        340        350        360 
YQQVKTKVFQ LKRKEYEMKL HTEAQIQEEG TVVELTGRQS SEITRTITKL SFVKVDSHFR 

       370        380        390        400        410        420 
QGIPFFGQVR LVDGKGVPIP NKVIFIRGNE ANYYSNATTD EHGLVQFSIN TTNVMGTSLT 

       430        440        450        460        470        480 
VRVNYKDRSP CYGYQWVSEE HEEAHHTAYL VFSPSKSFVH LEPMSHELPC GHTQTVQAHY 

       490        500        510        520        530        540 
ILNGGTLLGL KKLSFYYLIM AKGGIVRTGT HGLLVKQEDM KGHFSISIPV KSDIAPVARL 

       550        560        570        580        590        600 
LIYAVLPTGD VIGDSAKYDV ENCLANKVDL SFSPSQSLPA SHAHLRVTAA PQSVCALRAV 

       610        620        630        640        650        660 
DQSVLLMKPD AELSASSVYN LLPEKDLTGF PGPLNDQDNE DCINRHNVYI NGITYTPVSS 

       670        680        690        700        710        720 
TNEKDMYSFL EDMGLKAFTN SKIRKPKMCP QLQQYEMHGP EGLRVGFYES DVMGRGHARL 

       730        740        750        760        770        780 
VHVEEPHTET VRKYFPETWI WDLVVVNSAG VAEVGVTVPD TITEWKAGAF CLSEDAGLGI 

       790        800        810        820        830        840 
SSTASLRAFQ PFFVELTMPY SVIRGEAFTL KATVLNYLPK CIRVSVQLEA SPAFLAVPVE 

       850        860        870        880        890        900 
KEQAPHCICA NGRQTVSWAV TPKSLGNVNF TVSAEALESQ ELCGTEVPSV PEHGRKDTVI 

       910        920        930        940        950        960 
KPLLVEPEGL EKETTFNSLL CPSGGEVSEE LSLKLPPNVV EESARASVSV LGDILGSAMQ 

       970        980        990       1000       1010       1020 
NTQNLLQMPY GCGEQNMVLF APNIYVLDYL NETQQLTPEI KSKAIGYLNT GYQRQLNYKH 

      1030       1040       1050       1060       1070       1080 
YDGSYSTFGE RYGRNQGNTW LTAFVLKTFA QARAYIFIDE AHITQALIWL SQRQKDNGCF 

      1090       1100       1110       1120       1130       1140 
RSSGSLLNNA IKGGVEDEVT LSAYITIALL EIPLTVTHPV VRNALFCLES AWKTAQEGDH 

      1150       1160       1170       1180       1190       1200 
GSHVYTKALL AYAFALAGNQ DKRKEVLKSL NEEAVKKDNS VHWERPQKPK APVGHFYEPQ 

      1210       1220       1230       1240       1250       1260 
APSAEVEMTS YVLLAYLTAQ PAPTSEDLTS ATNIVKWITK QQNAQGGFSS TQDTVVALHA 

      1270       1280       1290       1300       1310       1320 
LSKYGAATFT RTGKAAQVTI QSSGTFSSKF QVDNNNRLLL QQVSLPELPG EYSMKVTGEG 

      1330       1340       1350       1360       1370       1380 
CVYLQTSLKY NILPEKEEFP FALGVQTLPQ TCDEPKAHTS FQISLSVSYT GSRSASNMAI 

      1390       1400       1410       1420       1430       1440 
VDVKMVSGFI PLKPTVKMLE RSNHVSRTEV SSNHVLIYLD KVSNQTLSLF FTVLQDVPVR 

      1450       1460       1470 
DLKPAIVKVY DYYETDEFAI AEYNAPCSKD LGNA 

« Hide

References

« Hide 'large scale' references
[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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Structure of the human alpha-2 macroglobulin gene and its promotor."
Matthijs G., Devriendt K., Cassiman J.-J., van den Berghe H., Marynen P.
Biochem. Biophys. Res. Commun. 184:596-603(1992) [PubMed] [Europe PMC] [Abstract]
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]Erratum
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. 260:6500-6500(1985)
[10]"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.
[11]"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.
[12]"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.
[13]"Human alpha 2-macroglobulin gene is located on chromosome 12."
Bell G.I., Rall L.B., Sanchez-Pescador R., Merryweather J.P., Scott J., Eddy R.L., Shows T.B.
Somat. Cell Mol. Genet. 11:285-289(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 832-1474.
Tissue: Liver.
[14]Liu B., Zhao B., Wang X.Y., Xu Y.Y., Liu Y.Q., Song L., Ye J., Sheng H., Gao Y., Zhang C.L., Wei Y.J., Zhang J., Song L., Jiang Y.X., Zhao Z.W., Ding J.F., Liu L.S., Gao R.L. expand/collapse author list , Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S., Hui R.T.
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1208-1474.
Tissue: Aorta.
[15]"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.
[16]"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.
[17]"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.
[18]"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.
[19]"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.
[20]"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.
[21]"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.
[22]"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.
[23]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-55 AND ASN-1424.
[24]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"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.
[26]"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.
[27]"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.
+Additional computationally mapped references.

Web resources

Wikipedia

Alpha-2 macroglobulin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRMAHU. A94033.
RefSeqNP_000005.2. NM_000014.4.
UniGeneHs.212838.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BV8NMR-A1337-1474[»]
2P9RX-ray2.30A/B126-227[»]
4ACQX-ray4.30A/B/C/D24-1474[»]
ProteinModelPortalP01023.
SMRP01023. Positions 126-227, 1338-1474.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106524. 89 interactions.
DIPDIP-1118N.
IntActP01023. 95 interactions.
MINTMINT-122288.
STRING9606.ENSP00000323929.

Chemistry

DrugBankDB00626. Bacitracin.
DB00102. Becaplermin.

Protein family/group databases

MEROPSI39.001.

PTM databases

PhosphoSiteP01023.

Polymorphism databases

DMDM308153640.

2D gel databases

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

Proteomic databases

PaxDbP01023.
PeptideAtlasP01023.
PRIDEP01023.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000318602; ENSP00000323929; ENSG00000175899.
GeneID2.
KEGGhsa:2.
UCSCuc001qvk.1. human.

Organism-specific databases

CTD2.
GeneCardsGC12M009220.
H-InvDBHIX0026392.
HGNCHGNC:7. A2M.
HPACAB017621.
HPA002265.
MIM103950. gene.
neXtProtNX_P01023.
PharmGKBPA24357.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2373.
HOVERGENHBG000039.
KOK03910.
OMAQTVQAHY.
OrthoDBEOG7DJSKB.
PhylomeDBP01023.
TreeFamTF313285.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_118779. Extracellular matrix organization.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP01023.
BgeeP01023.
CleanExHS_A2M.
GenevestigatorP01023.

Family and domain databases

Gene3D1.50.10.20. 1 hit.
2.60.40.690. 1 hit.
InterProIPR009048. 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]
PfamPF00207. 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]
SUPFAMSSF48239. SSF48239. 1 hit.
SSF49410. SSF49410. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEPS00477. ALPHA_2_MACROGLOBULIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSA2M. human.
EvolutionaryTraceP01023.
GenomeRNAi2.
NextBio5.
PROP01023.
SOURCESearch...

Entry information

Entry nameA2MG_HUMAN
AccessionPrimary (citable) accession number: P01023
Secondary accession number(s): Q13677 expand/collapse secondary AC list , Q59F47, Q5QTS0, Q68DN2, Q6PIY3, Q6PN97
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 5, 2010
Last modified: April 16, 2014
This is version 169 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM