Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Alpha-2-macroglobulin

Gene

A2M

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • calcium-dependent protein binding Source: AgBase
  • enzyme binding Source: UniProtKB
  • growth factor binding Source: UniProtKB
  • GTPase activator activity Source: Reactome
  • interleukin-1 binding Source: UniProtKB
  • interleukin-8 binding Source: UniProtKB
  • protease binding Source: BHF-UCL
  • receptor binding Source: AgBase
  • serine-type endopeptidase inhibitor activity Source: UniProtKB
  • tumor necrosis factor binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Enzyme and pathway databases

ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-140837. Intrinsic Pathway of Fibrin Clot Formation.
R-HSA-1474228. Degradation of the extracellular matrix.
R-HSA-194223. HDL-mediated lipid transport.
R-HSA-194840. Rho GTPase cycle.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:7. A2M.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: UniProtKB
  • platelet alpha granule lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi2.
MalaCardsiA2M.
OpenTargetsiENSG00000175899.
PharmGKBiPA24357.

Chemistry databases

DrugBankiDB00626. Bacitracin.
DB00102. Becaplermin.
DB08888. Ocriplasmin.

Polymorphism and mutation databases

BioMutaiA2M.
DMDMi308153640.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 231 PublicationAdd BLAST23
ChainiPRO_000000005524 – 1474Alpha-2-macroglobulin1 PublicationAdd BLAST1451

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi48 ↔ 861 Publication
Glycosylationi55N-linked (GlcNAc...) (complex)2 Publications1
Glycosylationi70N-linked (GlcNAc...)1 Publication1
Glycosylationi247N-linked (GlcNAc...)2 Publications1
Disulfide bondi251 ↔ 2991 Publication
Disulfide bondi269 ↔ 2871 Publication
Disulfide bondi278Interchain (with C-431)1 Publication
Glycosylationi396N-linked (GlcNAc...)3 Publications1
Glycosylationi410N-linked (GlcNAc...)2 Publications1
Disulfide bondi431Interchain (with C-278)1 Publication
Disulfide bondi470 ↔ 5631 Publication
Disulfide bondi595 ↔ 7712 Publications
Disulfide bondi642 ↔ 6891 Publication
Cross-linki693Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-? in other proteins)Sequence analysis
Cross-linki694Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-? in other proteins)Sequence analysis
Disulfide bondi821 ↔ 8491 Publication
Disulfide bondi847 ↔ 8831 Publication
Glycosylationi869N-linked (GlcNAc...)2 Publications1
Disulfide bondi921 ↔ 13211 Publication
Cross-linki972 ↔ 975Isoglutamyl cysteine thioester (Cys-Gln)1 Publication
Glycosylationi991N-linked (GlcNAc...)4 Publications1
Disulfide bondi1079 ↔ 11271 Publication
Disulfide bondi1352 ↔ 14671 Publication
Glycosylationi1424N-linked (GlcNAc...) (complex)4 Publications1

Keywords - PTMi

Disulfide bond, Glycoprotein, Isopeptide bond, Thioester bond

Proteomic databases

EPDiP01023.
MaxQBiP01023.
PaxDbiP01023.
PeptideAtlasiP01023.
PRIDEiP01023.

2D gel databases

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

PTM databases

iPTMnetiP01023.
PhosphoSitePlusiP01023.

Expressioni

Tissue specificityi

Secreted in plasma.1 Publication

Developmental stagei

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

Gene expression databases

BgeeiENSG00000175899.
CleanExiHS_A2M.
ExpressionAtlasiP01023. baseline and differential.
GenevisibleiP01023. HS.

Organism-specific databases

HPAiCAB017621.
HPA002265.

Interactioni

Subunit structurei

Homotetramer; disulfide-linked.2 Publications

GO - Molecular functioni

  • calcium-dependent protein binding Source: AgBase
  • enzyme binding Source: UniProtKB
  • growth factor binding Source: UniProtKB
  • interleukin-1 binding Source: UniProtKB
  • interleukin-8 binding Source: UniProtKB
  • protease binding Source: BHF-UCL
  • receptor binding Source: AgBase
  • tumor necrosis factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi106524. 108 interactors.
DIPiDIP-1118N.
IntActiP01023. 104 interactors.
MINTiMINT-122288.
STRINGi9606.ENSP00000323929.

Structurei

Secondary structure

11474
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi128 – 134Combined sources7
Beta strandi136 – 138Combined sources3
Beta strandi143 – 151Combined sources9
Helixi153 – 155Combined sources3
Beta strandi161 – 168Combined sources8
Beta strandi174 – 182Combined sources9
Beta strandi187 – 193Combined sources7
Beta strandi201 – 208Combined sources8
Beta strandi214 – 221Combined sources8
Beta strandi1341 – 1347Combined sources7
Helixi1355 – 1359Combined sources5
Beta strandi1360 – 1369Combined sources10
Beta strandi1379 – 1384Combined sources6
Beta strandi1389 – 1391Combined sources3
Helixi1393 – 1400Combined sources8
Turni1401 – 1403Combined sources3
Beta strandi1407 – 1410Combined sources4
Beta strandi1412 – 1419Combined sources8
Beta strandi1427 – 1434Combined sources8
Beta strandi1445 – 1450Combined sources6
Beta strandi1454 – 1456Combined sources3
Beta strandi1459 – 1463Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BV8NMR-A1337-1474[»]
2P9RX-ray2.30A/B126-227[»]
4ACQX-ray4.30A/B/C/D24-1474[»]
ProteinModelPortaliP01023.
SMRiP01023.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01023.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni690 – 728Bait regionAdd BLAST39
Regioni704 – 709Inhibitory6
Regioni719 – 723Inhibitory5
Regioni730 – 735Inhibitory6

Sequence similaritiesi

Keywords - Domaini

Bait region, Signal

Phylogenomic databases

eggNOGiKOG1366. Eukaryota.
ENOG410XRED. LUCA.
GeneTreeiENSGT00760000118982.
HOVERGENiHBG000039.
InParanoidiP01023.
KOiK03910.
OMAiNNDRINL.
OrthoDBiEOG091G00F5.
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]
SMARTiSM01360. A2M. 1 hit.
SM01359. A2M_N_2. 1 hit.
SM01361. A2M_recep. 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

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti63Missing AA sequence (PubMed:6203908).Curated1
Sequence conflicti82D → V in AAT02228 (Ref. 3) Curated1
Sequence conflicti350 – 353LSFV → ACCS in AAH26246 (PubMed:15489334).Curated4
Sequence conflicti563C → E AA sequence (PubMed:6203908).Curated1
Sequence conflicti844A → V in BAD92851 (PubMed:17974005).Curated1
Sequence conflicti872V → M in CAH18188 (PubMed:16541075).Curated1
Sequence conflicti1148A → D in AAA51552 (PubMed:2408344).Curated1
Sequence conflicti1195H → D in AAA51552 (PubMed:2408344).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_026820639N → D.5 PublicationsCorresponds to variant rs226405dbSNPEnsembl.1
Natural variantiVAR_000012704R → H.Corresponds to variant rs1800434dbSNPEnsembl.1
Natural variantiVAR_026821815L → Q.Corresponds to variant rs3180392dbSNPEnsembl.1
Natural variantiVAR_000013972C → Y Probably interferes with the activity. 1 PublicationCorresponds to variant rs1800433dbSNPEnsembl.1
Natural variantiVAR_0000141000I → V.5 PublicationsCorresponds to variant rs669dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
Hs.88556.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Alpha-2 macroglobulin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
Hs.88556.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BV8NMR-A1337-1474[»]
2P9RX-ray2.30A/B126-227[»]
4ACQX-ray4.30A/B/C/D24-1474[»]
ProteinModelPortaliP01023.
SMRiP01023.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106524. 108 interactors.
DIPiDIP-1118N.
IntActiP01023. 104 interactors.
MINTiMINT-122288.
STRINGi9606.ENSP00000323929.

Chemistry databases

DrugBankiDB00626. Bacitracin.
DB00102. Becaplermin.
DB08888. Ocriplasmin.

Protein family/group databases

MEROPSiI39.001.

PTM databases

iPTMnetiP01023.
PhosphoSitePlusiP01023.

Polymorphism and mutation databases

BioMutaiA2M.
DMDMi308153640.

2D gel databases

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

Proteomic databases

EPDiP01023.
MaxQBiP01023.
PaxDbiP01023.
PeptideAtlasiP01023.
PRIDEiP01023.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2.
DisGeNETi2.
GeneCardsiA2M.
H-InvDBHIX0026392.
HGNCiHGNC:7. A2M.
HPAiCAB017621.
HPA002265.
MalaCardsiA2M.
MIMi103950. gene.
neXtProtiNX_P01023.
OpenTargetsiENSG00000175899.
PharmGKBiPA24357.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1366. Eukaryota.
ENOG410XRED. LUCA.
GeneTreeiENSGT00760000118982.
HOVERGENiHBG000039.
InParanoidiP01023.
KOiK03910.
OMAiNNDRINL.
OrthoDBiEOG091G00F5.
PhylomeDBiP01023.
TreeFamiTF313285.

Enzyme and pathway databases

ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-140837. Intrinsic Pathway of Fibrin Clot Formation.
R-HSA-1474228. Degradation of the extracellular matrix.
R-HSA-194223. HDL-mediated lipid transport.
R-HSA-194840. Rho GTPase cycle.

Miscellaneous databases

ChiTaRSiA2M. human.
EvolutionaryTraceiP01023.
GenomeRNAii2.
PROiP01023.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000175899.
CleanExiHS_A2M.
ExpressionAtlasiP01023. baseline and differential.
GenevisibleiP01023. HS.

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]
SMARTiSM01360. A2M. 1 hit.
SM01359. A2M_N_2. 1 hit.
SM01361. A2M_recep. 1 hit.
[Graphical view]
SUPFAMiSSF48239. SSF48239. 1 hit.
SSF49410. SSF49410. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00477. ALPHA_2_MACROGLOBULIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 196 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.