Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Alpha-2-macroglobulin  

UniProtKB / Swiss-Prot ID :  A2MG_HUMAN

Gene Name (Synonyms) : 
A2M, CPAMD5 FWP007  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Secreted. 

Protein 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. 

Protein Sequence MGKNKLLHPSLVLLLLVLLPTDASVSGKPQYMVLVPSLLHTETTEKGCVLLSYLNETVTVSASLESVRGN...
Predicted Secondary Structure CCCCCHHHHHHHHHHHHHCCCCCCCCCCCEEEEEECCEEECCCCEEEEEEEECCCCCEEEEEEEEECCCC...
Protein Variant
LocationDescription
639N -> D (in dbSNP:rs226405). VAR_026820
704R -> H (in dbSNP:rs1800434). VAR_000012
815L -> Q (in dbSNP:rs3180392). VAR_026821
972C -> Y (probably interferes with theactivity; dbSNP:rs1800433).
1000I -> V (in dbSNP:rs669). VAR_000014
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
55N-linked (GlcNAc...)LSYLNETVT
EECCCCCEE
34.36SysPTM
Link-
55N-linked (GlcNAc...).LSYLNETVT
EECCCCCEE
34.36UniProtKB
Link-
70N-linked (GlcNAc...)SVRGNRSLF
ECCCCEEEE
21.58SysPTM
Link-
70N-linked (GlcNAc...).SVRGNRSLF
ECCCCEEEE
21.58UniProtKB
Link-
247N-linked (GlcNAc...).EEEMNVSVC
CCCEEEEEE
26.62UniProtKB
Link-
396N-linked (GlcNAc...).NYYSNATTD
CCCCCEEEC
25.78UniProtKB
Link-
410N-linked (Glc...)QFSINTTNV
EEEEECCCC
39.39HPRD
Link-
410N-linked (GlcNAc...).QFSINTTNV
EEEEECCCC
39.39UniProtKB
Link-
497PhosphotyrosineLSFYYLIMA
EEEEEEEEE
6.42Phosphositeplus
Link-
679PhosphothreonineLKAFTNSKI
CEECCCCCC
43.36HPRD
Link-
679PhosphothreonineLKAFTNSKI
CEECCCCCC
43.36Phosphositeplus
Link-
693Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-...) (interchain with K-? in other proteiCPQLQQYEM
CCCHHHCCC
38.26UniProtKB
Link-
694Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-...) (interchain with K-? in other proteiPQLQQYEMH
CCHHHCCCC
44.75UniProtKB
Link-
695PhosphotyrosineQLQQYEMHG
CHHHCCCCC
11.40Phosphositeplus
Link-
702noneHGPEGLRVG
CCCHHHHHH
23.16HPRD
Link-
708PhosphotyrosineRVGFYESDV
HHHHCHHHH
14.48Phosphositeplus
Link-
719noneRGHARLVHV
HHHCCCCCC
31.41HPRD
Link-
834noneASPAFLAVP
ECCCEEECC
5.23HPRD
Link-
869N-linked (Glc...)LGNVNFTVS
CCCEEEEEE
30.76HPRD
Link-
869N-linked (GlcNAc...)LGNVNFTVS
CCCEEEEEE
30.76SysPTM
Link-
869N-linked (GlcNAc...).LGNVNFTVS
CCCEEEEEE
30.76UniProtKB
Link-
972Isoglutamyl cysteine thioester (Cys-Gln).MPYGCGEQN
CCCCHHHHH
4.47UniProtKB
Link-
991N-linked (Glc...)LDYLNETQQ
HHHHHHHHH
44.00HPRD
Link-
991N-linked (GlcNAc...).LDYLNETQQ
HHHHHHHHH
44.00UniProtKB
Link-
1424N-linked (Glc...)DKVSNQTLS
CCCCCCEEE
41.67HPRD
Link
1424N-linked (GlcNAc...)DKVSNQTLS
CCCCCCEEE
41.67SysPTM
Link
1424N-linked (GlcNAc...).DKVSNQTLS
CCCCCCEEE
41.67UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
TPP1_HUMANcolocalizationMINT-4054731MINT17174955
IL1B_HUMANphysical interactionMINT-16559MINT2466831
APOD_HUMANcolocalizationMINT-4054731MINT17174955
PERM_HUMANcolocalizationMINT-4054731MINT17174955
CH60_HUMANcolocalizationMINT-4054731MINT17174955
GRP78_HUMANcolocalizationMINT-4054731MINT17174955
BGAL_HUMANcolocalizationMINT-4054731MINT17174955
CAP7_HUMANcolocalizationMINT-4054731MINT17174955
VATB2_HUMANcolocalizationMINT-4054731MINT17174955
VDAC1_HUMANcolocalizationMINT-4054731MINT17174955
ASAH1_HUMANcolocalizationMINT-4054731MINT17174955
A4_HUMANphysical interaction
physical interaction
DIP:1300EDIP9501253
9501253
SHBG_HUMANyeast 2-hybridHPRD:00072HPRD15862967
SMAP_HUMANyeast 2-hybridHPRD:00072HPRD16169070
TGFB1_HUMANENSP00000323929STRING
PAI1_HUMANENSP00000323929STRING
IFNG_HUMANENSP00000323929STRING
PROC_HUMANENSP00000323929STRING
LRP1_HUMANENSP00000323929STRING
APOE_HUMANENSP00000323929STRING
IL6_HUMANENSP00000323929STRING
LYSC_HUMANENSP00000323929STRING
IL1A_HUMANENSP00000323929STRING
IL1B_HUMANENSP00000323929STRING
LRP2_HUMANENSP00000323929STRING
STAT3_HUMANENSP00000323929STRING
KLKB1_HUMANENSP00000323929STRING
AMBP_HUMANENSP00000323929STRING
AMBP_HUMANENSP00000323929STRING
EGF_HUMANENSP00000323929STRING
A4_HUMANENSP00000323929STRING
ELA1_HUMANENSP00000323929STRING
LIPL_HUMANENSP00000323929STRING
PROS_HUMANENSP00000323929STRING
B2MG_HUMANENSP00000323929STRING
CATB_HUMANENSP00000323929STRING
A1AT_HUMANENSP00000323929STRING
A1AT_HUMANENSP00000323929STRING
A1AT_HUMANENSP00000323929STRING
A1AT_HUMANENSP00000323929STRING
A1AT_HUMANENSP00000323929STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry.";
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
Nat. Biotechnol. 21:660-666(2003).
Cited for: GLYCOSYLATION AT ASN-991.
"Screening for N-glycosylated proteins by liquid chromatography massspectrometry.";
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
Proteomics 4:454-465(2004).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-869 AND ASN-1424, AND MASSSPECTROMETRY.
"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).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-55; ASN-247; ASN-396;ASN-410; ASN-869; ASN-991 AND ASN-1424, AND MASS SPECTROMETRY.
"Glycoproteomics analysis of human liver tissue by combination ofmultiple 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).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-396; ASN-991 AND ASN-1424,AND MASS SPECTROMETRY.
"Primary structure of human alpha 2-macroglobulin. V. The completestructure.";
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).
Cited for: PROTEIN SEQUENCE OF 24-1474, SUBUNIT, SUBCELLULAR LOCATION, TISSUESPECIFICITY, AND DISULFIDE BONDS.
Thioester bond
ReferencePubMed
"Primary structure of human alpha 2-macroglobulin. V. The completestructure.";
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).
Cited for: PROTEIN SEQUENCE OF 24-1474, SUBUNIT, SUBCELLULAR LOCATION, TISSUESPECIFICITY, AND DISULFIDE BONDS.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures