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P01023

- A2MG_HUMAN

UniProt

P01023 - A2MG_HUMAN

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Protein

Alpha-2-macroglobulin

Gene

A2M

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. receptor binding Source: AgBase
  8. serine-type endopeptidase inhibitor activity Source: UniProtKB
  9. 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiP01023.
CleanExiHS_A2M.
ExpressionAtlasiP01023. baseline and differential.
GenevestigatoriP01023.

Organism-specific databases

HPAiCAB017621.
HPA002265.

Interactioni

Subunit structurei

Homotetramer; disulfide-linked.2 Publications

Protein-protein interaction databases

BioGridi106524. 90 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.
GeneTreeiENSGT00760000118982.
HOVERGENiHBG000039.
InParanoidiP01023.
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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGKNKLLHPS LVLLLLVLLP TDASVSGKPQ YMVLVPSLLH TETTEKGCVL
60 70 80 90 100
LSYLNETVTV SASLESVRGN RSLFTDLEAE NDVLHCVAFA VPKSSSNEEV
110 120 130 140 150
MFLTVQVKGP TQEFKKRTTV MVKNEDSLVF VQTDKSIYKP GQTVKFRVVS
160 170 180 190 200
MDENFHPLNE LIPLVYIQDP KGNRIAQWQS FQLEGGLKQF SFPLSSEPFQ
210 220 230 240 250
GSYKVVVQKK SGGRTEHPFT VEEFVLPKFE VQVTVPKIIT ILEEEMNVSV
260 270 280 290 300
CGLYTYGKPV PGHVTVSICR KYSDASDCHG EDSQAFCEKF SGQLNSHGCF
310 320 330 340 350
YQQVKTKVFQ LKRKEYEMKL HTEAQIQEEG TVVELTGRQS SEITRTITKL
360 370 380 390 400
SFVKVDSHFR QGIPFFGQVR LVDGKGVPIP NKVIFIRGNE ANYYSNATTD
410 420 430 440 450
EHGLVQFSIN TTNVMGTSLT VRVNYKDRSP CYGYQWVSEE HEEAHHTAYL
460 470 480 490 500
VFSPSKSFVH LEPMSHELPC GHTQTVQAHY ILNGGTLLGL KKLSFYYLIM
510 520 530 540 550
AKGGIVRTGT HGLLVKQEDM KGHFSISIPV KSDIAPVARL LIYAVLPTGD
560 570 580 590 600
VIGDSAKYDV ENCLANKVDL SFSPSQSLPA SHAHLRVTAA PQSVCALRAV
610 620 630 640 650
DQSVLLMKPD AELSASSVYN LLPEKDLTGF PGPLNDQDNE DCINRHNVYI
660 670 680 690 700
NGITYTPVSS TNEKDMYSFL EDMGLKAFTN SKIRKPKMCP QLQQYEMHGP
710 720 730 740 750
EGLRVGFYES DVMGRGHARL VHVEEPHTET VRKYFPETWI WDLVVVNSAG
760 770 780 790 800
VAEVGVTVPD TITEWKAGAF CLSEDAGLGI SSTASLRAFQ PFFVELTMPY
810 820 830 840 850
SVIRGEAFTL KATVLNYLPK CIRVSVQLEA SPAFLAVPVE KEQAPHCICA
860 870 880 890 900
NGRQTVSWAV TPKSLGNVNF TVSAEALESQ ELCGTEVPSV PEHGRKDTVI
910 920 930 940 950
KPLLVEPEGL EKETTFNSLL CPSGGEVSEE LSLKLPPNVV EESARASVSV
960 970 980 990 1000
LGDILGSAMQ NTQNLLQMPY GCGEQNMVLF APNIYVLDYL NETQQLTPEI
1010 1020 1030 1040 1050
KSKAIGYLNT GYQRQLNYKH YDGSYSTFGE RYGRNQGNTW LTAFVLKTFA
1060 1070 1080 1090 1100
QARAYIFIDE AHITQALIWL SQRQKDNGCF RSSGSLLNNA IKGGVEDEVT
1110 1120 1130 1140 1150
LSAYITIALL EIPLTVTHPV VRNALFCLES AWKTAQEGDH GSHVYTKALL
1160 1170 1180 1190 1200
AYAFALAGNQ DKRKEVLKSL NEEAVKKDNS VHWERPQKPK APVGHFYEPQ
1210 1220 1230 1240 1250
APSAEVEMTS YVLLAYLTAQ PAPTSEDLTS ATNIVKWITK QQNAQGGFSS
1260 1270 1280 1290 1300
TQDTVVALHA LSKYGAATFT RTGKAAQVTI QSSGTFSSKF QVDNNNRLLL
1310 1320 1330 1340 1350
QQVSLPELPG EYSMKVTGEG CVYLQTSLKY NILPEKEEFP FALGVQTLPQ
1360 1370 1380 1390 1400
TCDEPKAHTS FQISLSVSYT GSRSASNMAI VDVKMVSGFI PLKPTVKMLE
1410 1420 1430 1440 1450
RSNHVSRTEV SSNHVLIYLD KVSNQTLSLF FTVLQDVPVR DLKPAIVKVY
1460 1470
DYYETDEFAI AEYNAPCSKD LGNA
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. 90 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.
GeneTreei ENSGT00760000118982.
HOVERGENi HBG000039.
InParanoidi P01023.
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

Bgeei P01023.
CleanExi HS_A2M.
ExpressionAtlasi P01023. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 175 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