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Protein

Legumain

Gene

LGMN

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

Functioni

Has a strict specificity for hydrolysis of asparaginyl bonds. Can also cleave aspartyl bonds slowly, especially under acidic conditions. Required for normal lysosomal protein degradation in renal proximal tubules. Required for normal degradation of internalized EGFR. Plays a role in the regulation of cell proliferation via its role in EGFR degradation (By similarity). May be involved in the processing of proteins for MHC class II antigen presentation in the lysosomal/endosomal system.By similarity1 Publication

Catalytic activityi

Hydrolysis of proteins and small molecule substrates at -Asn-|-Xaa- bonds.1 Publication

pH dependencei

Optimum pH is 5.5 for the free enzyme, and pH 6 in the presence of bound integrins.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei148 – 14811 Publication
Active sitei189 – 1891Nucleophile1 Publication
Sitei323 – 3242Cleavage; by autolysis

GO - Molecular functioni

  • cysteine-type endopeptidase activity Source: UniProtKB
  • peptidase activity Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

BRENDAi3.4.22.34. 2681.
ReactomeiREACT_118632. Trafficking and processing of endosomal TLR.
REACT_121399. MHC class II antigen presentation.
REACT_13523. Vitamin D (calciferol) metabolism.
SABIO-RKQ99538.

Protein family/group databases

MEROPSiC13.004.

Names & Taxonomyi

Protein namesi
Recommended name:
Legumain (EC:3.4.22.34)
Alternative name(s):
Asparaginyl endopeptidase
Protease, cysteine 1
Gene namesi
Name:LGMN
Synonyms:PRSC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:9472. LGMN.

Subcellular locationi

GO - Cellular componenti

  • apical part of cell Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • late endosome Source: Ensembl
  • lysosomal lumen Source: Reactome
  • lysosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi190 – 1901E → K: Increases catalytic activity at pH 5.5. 1 Publication
Mutagenesisi323 – 3231N → D, Q or S: Loss of autoactivation.

Organism-specific databases

PharmGKBiPA30354.

Polymorphism and mutation databases

BioMutaiLGMN.
DMDMi2842759.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 17171 PublicationAdd
BLAST
Chaini18 – 323306LegumainPRO_0000026502Add
BLAST
Propeptidei324 – 433110PRO_0000026503Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi91 – 911N-linked (GlcNAc...)2 Publications
Glycosylationi167 – 1671N-linked (GlcNAc...)2 Publications
Glycosylationi263 – 2631N-linked (GlcNAc...)1 Publication
Glycosylationi272 – 2721N-linked (GlcNAc...)1 Publication
Disulfide bondi378 ↔ 412By similarity
Disulfide bondi390 ↔ 429By similarity

Post-translational modificationi

Glycosylated.2 Publications
Activated by autocatalytic processing at pH 4.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiQ99538.
PaxDbiQ99538.
PRIDEiQ99538.

PTM databases

PhosphoSiteiQ99538.

Miscellaneous databases

PMAP-CutDBQ99538.

Expressioni

Tissue specificityi

Ubiquitous. Particularly abundant in kidney, heart and placenta.

Gene expression databases

BgeeiQ99538.
CleanExiHS_LGMN.
ExpressionAtlasiQ99538. baseline and differential.
GenevisibleiQ99538. HS.

Organism-specific databases

HPAiHPA000799.
HPA001426.

Interactioni

Subunit structurei

Homodimer before autocatalytic removal of the propeptide (By similarity). Monomer after autocatalytic processing. May interact with integrins.By similarity1 Publication

Protein-protein interaction databases

BioGridi111624. 14 interactions.
IntActiQ99538. 4 interactions.
MINTiMINT-4537529.
STRINGi9606.ENSP00000334052.

Structurei

Secondary structure

1
433
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 358Combined sources
Helixi40 – 423Combined sources
Helixi43 – 5816Combined sources
Helixi63 – 653Combined sources
Beta strandi66 – 694Combined sources
Beta strandi87 – 893Combined sources
Helixi105 – 1073Combined sources
Helixi110 – 1189Combined sources
Turni121 – 1266Combined sources
Beta strandi140 – 1467Combined sources
Beta strandi153 – 1553Combined sources
Beta strandi157 – 1626Combined sources
Helixi163 – 17513Combined sources
Beta strandi180 – 1867Combined sources
Helixi191 – 1944Combined sources
Turni195 – 1973Combined sources
Beta strandi202 – 2109Combined sources
Beta strandi217 – 2226Combined sources
Turni223 – 2264Combined sources
Beta strandi227 – 2315Combined sources
Helixi232 – 24312Combined sources
Turni246 – 2483Combined sources
Helixi251 – 26111Combined sources
Beta strandi268 – 2714Combined sources
Helixi273 – 2775Combined sources
Helixi281 – 2844Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4AW9X-ray2.20A26-309[»]
4AWAX-ray2.50A26-309[»]
4AWBX-ray2.70A/B26-309[»]
4FGUX-ray3.90A/B18-433[»]
4N6NX-ray1.87A26-303[»]
4N6OX-ray1.80A26-303[»]
ProteinModelPortaliQ99538.
SMRiQ99538. Positions 28-433.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

In the zymogen form, the uncleaved propeptide blocks access to the active site.1 Publication

Sequence similaritiesi

Belongs to the peptidase C13 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5206.
GeneTreeiENSGT00530000063391.
HOGENOMiHOG000236335.
HOVERGENiHBG031304.
InParanoidiQ99538.
KOiK01369.
OMAiDRIKLSM.
OrthoDBiEOG779NXS.
PhylomeDBiQ99538.
TreeFamiTF313403.

Family and domain databases

InterProiIPR001096. Peptidase_C13.
[Graphical view]
PANTHERiPTHR12000. PTHR12000. 1 hit.
PfamiPF01650. Peptidase_C13. 1 hit.
[Graphical view]
PIRSFiPIRSF019663. Legumain. 1 hit.
PRINTSiPR00776. HEMOGLOBNASE.

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q99538-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVWKVAVFLS VALGIGAVPI DDPEDGGKHW VVIVAGSNGW YNYRHQADAC
60 70 80 90 100
HAYQIIHRNG IPDEQIVVMM YDDIAYSEDN PTPGIVINRP NGTDVYQGVP
110 120 130 140 150
KDYTGEDVTP QNFLAVLRGD AEAVKGIGSG KVLKSGPQDH VFIYFTDHGS
160 170 180 190 200
TGILVFPNED LHVKDLNETI HYMYKHKMYR KMVFYIEACE SGSMMNHLPD
210 220 230 240 250
NINVYATTAA NPRESSYACY YDEKRSTYLG DWYSVNWMED SDVEDLTKET
260 270 280 290 300
LHKQYHLVKS HTNTSHVMQY GNKTISTMKV MQFQGMKRKA SSPVPLPPVT
310 320 330 340 350
HLDLTPSPDV PLTIMKRKLM NTNDLEESRQ LTEEIQRHLD ARHLIEKSVR
360 370 380 390 400
KIVSLLAASE AEVEQLLSER APLTGHSCYP EALLHFRTHC FNWHSPTYEY
410 420 430
ALRHLYVLVN LCEKPYPLHR IKLSMDHVCL GHY
Length:433
Mass (Da):49,411
Last modified:May 1, 1997 - v1
Checksum:i081AD2D0D584E72A
GO
Isoform 2 (identifier: Q99538-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     341-397: Missing.

Note: No experimental confirmation available.
Show »
Length:376
Mass (Da):42,948
Checksum:i582E0D702B640C1F
GO
Isoform 3 (identifier: Q99538-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     341-372: ARHLIEKSVRKIVSLLAASEAEVEQLLSERAP → DKIVHGPRVPWSLLKSCLLEAFPSVSAPPTVC
     373-433: Missing.

Note: No experimental confirmation available.
Show »
Length:372
Mass (Da):42,008
Checksum:i915FFBB4216E8BF6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti31 – 311V → A in BAA09530 (PubMed:8893817).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti18 – 181V → I.1 Publication
Corresponds to variant rs2236264 [ dbSNP | Ensembl ].
VAR_024588

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei341 – 39757Missing in isoform 2. 1 PublicationVSP_056454Add
BLAST
Alternative sequencei341 – 37232ARHLI…SERAP → DKIVHGPRVPWSLLKSCLLE AFPSVSAPPTVC in isoform 3. 1 PublicationVSP_056455Add
BLAST
Alternative sequencei373 – 43361Missing in isoform 3. 1 PublicationVSP_056456Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y09862 mRNA. Translation: CAA70989.1.
D55696 mRNA. Translation: BAA09530.1.
BX161380 mRNA. Translation: CAD61872.1.
BX161422 mRNA. Translation: CAD61895.1.
AL132987 Genomic DNA. No translation available.
AL136332 Genomic DNA. No translation available.
BC003061 mRNA. Translation: AAH03061.1.
CCDSiCCDS9904.1. [Q99538-1]
RefSeqiNP_001008530.1. NM_001008530.2. [Q99538-1]
NP_005597.3. NM_005606.6. [Q99538-1]
XP_005267919.1. XM_005267862.3. [Q99538-2]
XP_005267920.1. XM_005267863.3. [Q99538-3]
UniGeneiHs.18069.

Genome annotation databases

EnsembliENST00000334869; ENSP00000334052; ENSG00000100600. [Q99538-1]
ENST00000393218; ENSP00000376911; ENSG00000100600. [Q99538-1]
ENST00000555699; ENSP00000451861; ENSG00000100600. [Q99538-3]
ENST00000557434; ENSP00000452572; ENSG00000100600. [Q99538-2]
GeneIDi5641.
KEGGihsa:5641.
UCSCiuc001yat.3. human.
uc001yau.3. human.
uc001yav.3. human. [Q99538-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y09862 mRNA. Translation: CAA70989.1.
D55696 mRNA. Translation: BAA09530.1.
BX161380 mRNA. Translation: CAD61872.1.
BX161422 mRNA. Translation: CAD61895.1.
AL132987 Genomic DNA. No translation available.
AL136332 Genomic DNA. No translation available.
BC003061 mRNA. Translation: AAH03061.1.
CCDSiCCDS9904.1. [Q99538-1]
RefSeqiNP_001008530.1. NM_001008530.2. [Q99538-1]
NP_005597.3. NM_005606.6. [Q99538-1]
XP_005267919.1. XM_005267862.3. [Q99538-2]
XP_005267920.1. XM_005267863.3. [Q99538-3]
UniGeneiHs.18069.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4AW9X-ray2.20A26-309[»]
4AWAX-ray2.50A26-309[»]
4AWBX-ray2.70A/B26-309[»]
4FGUX-ray3.90A/B18-433[»]
4N6NX-ray1.87A26-303[»]
4N6OX-ray1.80A26-303[»]
ProteinModelPortaliQ99538.
SMRiQ99538. Positions 28-433.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111624. 14 interactions.
IntActiQ99538. 4 interactions.
MINTiMINT-4537529.
STRINGi9606.ENSP00000334052.

Chemistry

BindingDBiQ99538.
ChEMBLiCHEMBL4244.

Protein family/group databases

MEROPSiC13.004.

PTM databases

PhosphoSiteiQ99538.

Polymorphism and mutation databases

BioMutaiLGMN.
DMDMi2842759.

Proteomic databases

MaxQBiQ99538.
PaxDbiQ99538.
PRIDEiQ99538.

Protocols and materials databases

DNASUi5641.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000334869; ENSP00000334052; ENSG00000100600. [Q99538-1]
ENST00000393218; ENSP00000376911; ENSG00000100600. [Q99538-1]
ENST00000555699; ENSP00000451861; ENSG00000100600. [Q99538-3]
ENST00000557434; ENSP00000452572; ENSG00000100600. [Q99538-2]
GeneIDi5641.
KEGGihsa:5641.
UCSCiuc001yat.3. human.
uc001yau.3. human.
uc001yav.3. human. [Q99538-1]

Organism-specific databases

CTDi5641.
GeneCardsiGC14M093170.
HGNCiHGNC:9472. LGMN.
HPAiHPA000799.
HPA001426.
MIMi602620. gene.
neXtProtiNX_Q99538.
PharmGKBiPA30354.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5206.
GeneTreeiENSGT00530000063391.
HOGENOMiHOG000236335.
HOVERGENiHBG031304.
InParanoidiQ99538.
KOiK01369.
OMAiDRIKLSM.
OrthoDBiEOG779NXS.
PhylomeDBiQ99538.
TreeFamiTF313403.

Enzyme and pathway databases

BRENDAi3.4.22.34. 2681.
ReactomeiREACT_118632. Trafficking and processing of endosomal TLR.
REACT_121399. MHC class II antigen presentation.
REACT_13523. Vitamin D (calciferol) metabolism.
SABIO-RKQ99538.

Miscellaneous databases

ChiTaRSiLGMN. human.
GeneWikiiLGMN.
GenomeRNAii5641.
NextBioi21918.
PMAP-CutDBQ99538.
PROiQ99538.
SOURCEiSearch...

Gene expression databases

BgeeiQ99538.
CleanExiHS_LGMN.
ExpressionAtlasiQ99538. baseline and differential.
GenevisibleiQ99538. HS.

Family and domain databases

InterProiIPR001096. Peptidase_C13.
[Graphical view]
PANTHERiPTHR12000. PTHR12000. 1 hit.
PfamiPF01650. Peptidase_C13. 1 hit.
[Graphical view]
PIRSFiPIRSF019663. Legumain. 1 hit.
PRINTSiPR00776. HEMOGLOBNASE.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, isolation, and characterization of mammalian legumain, an asparaginyl endopeptidase."
    Chen J.-M., Dando P.M., Rawlings N.D., Brown M.A., Young N.E., Stevens R.A.E., Hewitt E., Watts C., Barrett A.J.
    J. Biol. Chem. 272:8090-8098(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Placenta.
  2. "Molecular cloning of a human cDNA encoding putative cysteine protease (PRSC1) and its chromosome assignment to 14q32.1."
    Tanaka T., Inazawa J., Nakamura Y.
    Cytogenet. Cell Genet. 74:120-123(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Heart.
  3. "Full-length cDNA libraries and normalization."
    Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Tissue: Neuroblastoma and Placenta.
  4. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 1), VARIANT ILE-18.
    Tissue: Placenta.
  6. "Activation of human prolegumain by cleavage at a C-terminal asparagine residue."
    Chen J.-M., Fortunato M., Barrett A.J.
    Biochem. J. 352:327-334(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 18-24 AND 324-330, PROTEOLYTIC PROCESSING.
  7. "Autocatalytic activation of human legumain at aspartic acid residues."
    Halfon S., Patel S., Vega F., Zurawski S., Zurawski G.
    FEBS Lett. 438:114-118(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF ACTIVITY ON ASPARTATE BONDS, AUTOCATALYTIC CLEAVAGE.
  8. "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-91 AND ASN-167.
    Tissue: Liver.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "Mechanistic and structural studies on legumain explain its zymogenicity, distinct activation pathways, and regulation."
    Dall E., Brandstetter H.
    Proc. Natl. Acad. Sci. U.S.A. 110:10940-10945(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 26-309, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, PROPEPTIDE, GLYCOSYLATION AT ASN-91; ASN-167; ASN-263 AND ASN-272, SUBUNIT, DOMAIN, MUTAGENESIS OF GLU-190, AUTOCATALYTIC PROCESSING.

Entry informationi

Entry nameiLGMN_HUMAN
AccessioniPrimary (citable) accession number: Q99538
Secondary accession number(s): O00123
, Q86TV2, Q86TV3, Q9BTY1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: June 24, 2015
This is version 144 of the entry and version 1 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 14
    Human chromosome 14: 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. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.