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

Proteasome subunit beta type-4

Gene

Psmb4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Mediates the lipopolysaccharide-induced signal macrophage proteasome. SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1 (By similarity).By similarity

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei46 – 461NucleophileBy similarity

GO - Molecular functioni

  1. lipopolysaccharide binding Source: UniProtKB
  2. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. negative regulation of inflammatory response to antigenic stimulus Source: UniProtKB
  2. proteolysis involved in cellular protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

ReactomeiREACT_197102. ER-Phagosome pathway.
REACT_198693. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_199105. ER-Phagosome pathway.
REACT_199114. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_199121. Activation of NF-kappaB in B cells.
REACT_203336. Degradation of beta-catenin by the destruction complex.
REACT_203517. SCF-beta-TrCP mediated degradation of Emi1.
REACT_203973. Asymmetric localization of PCP proteins.
REACT_207679. Separation of Sister Chromatids.
REACT_212633. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_218318. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_219129. degradation of AXIN.
REACT_219897. APC/C:Cdc20 mediated degradation of Securin.
REACT_220647. SCF(Skp2)-mediated degradation of p27/p21.
REACT_225686. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_226135. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_227429. degradation of DVL.
REACT_232069. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_232469. Hh ligand biogenesis disease.
REACT_233316. Hedgehog ligand biogenesis.
REACT_234963. Regulation of ornithine decarboxylase (ODC).
REACT_244558. CDT1 association with the CDC6:ORC:origin complex.
REACT_245230. Orc1 removal from chromatin.
REACT_249922. CDK-mediated phosphorylation and removal of Cdc6.
REACT_263467. Ubiquitin-dependent degradation of Cyclin D1.
REACT_268522. GLI3 is processed to GLI3R by the proteasome.
REACT_268705. Degradation of GLI1 by the proteasome.
REACT_270923. Degradation of GLI2 by the proteasome.

Protein family/group databases

MEROPSiT01.987.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-4 (EC:3.4.25.1)
Alternative name(s):
Low molecular mass protein 3
Macropain beta chain
Multicatalytic endopeptidase complex beta chain
Proteasome beta chain
Proteasome chain 3
Gene namesi
Name:Psmb4
Synonyms:Lmp3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:1098257. Psmb4.

Subcellular locationi

Cytoplasm PROSITE-ProRule annotation. Nucleus By similarity

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: MGI
  3. nucleus Source: MGI
  4. proteasome complex Source: MGI
  5. proteasome core complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 45452 PublicationsPRO_0000026581Add
BLAST
Chaini46 – 264219Proteasome subunit beta type-4PRO_0000026582Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei102 – 1021PhosphotyrosineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Zymogen

Proteomic databases

MaxQBiP99026.
PaxDbiP99026.
PRIDEiP99026.

2D gel databases

REPRODUCTION-2DPAGEP99026.
SWISS-2DPAGEP99026.

PTM databases

PhosphoSiteiP99026.

Expressioni

Tissue specificityi

Detected in liver (at protein level).1 Publication

Inductioni

Up-regulated in liver tumor tissues (at protein level).1 Publication

Gene expression databases

BgeeiP99026.
GenevestigatoriP99026.

Interactioni

Subunit structurei

The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. Interacts with bacterial lipopolysaccharide (LPS). Forms a ternary complex with SMAD1 and OAZ1 before PSMB4 is incorporated into the 20S proteasome. Interacts with PRPF19.3 Publications

Protein-protein interaction databases

BioGridi202420. 4 interactions.
IntActiP99026. 5 interactions.
MINTiMINT-1850556.

Structurei

Secondary structure

1
264
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi51 – 533Combined sources
Beta strandi56 – 616Combined sources
Beta strandi64 – 707Combined sources
Beta strandi73 – 753Combined sources
Beta strandi78 – 836Combined sources
Beta strandi87 – 893Combined sources
Beta strandi91 – 10111Combined sources
Helixi102 – 12221Combined sources
Helixi130 – 14617Combined sources
Beta strandi153 – 1619Combined sources
Beta strandi164 – 1707Combined sources
Beta strandi172 – 1743Combined sources
Beta strandi176 – 1783Combined sources
Beta strandi180 – 1834Combined sources
Helixi187 – 20115Combined sources
Helixi207 – 22418Combined sources
Beta strandi232 – 2376Combined sources
Beta strandi242 – 2487Combined sources
Helixi255 – 2573Combined sources
Turni258 – 2603Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UNBX-ray2.903/M/a/o46-264[»]
3UNEX-ray3.203/M/a/o46-264[»]
3UNFX-ray2.90M/a46-264[»]
3UNHX-ray3.20M/a46-264[»]
ProteinModelPortaliP99026.
SMRiP99026. Positions 46-261.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00390000000698.
HOVERGENiHBG018194.
InParanoidiP99026.
KOiK02736.
OMAiRIMRVND.
OrthoDBiEOG74FF1D.
PhylomeDBiP99026.
TreeFamiTF106220.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR016295. Proteasome_endopept_cplx_B.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PIRSFiPIRSF001213. Psome_endopept_beta. 1 hit.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P99026-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEAFWESRAG HWAGGPAPGQ FYRIPATPSG LMDPASAPCE GPITRTQNPM
60 70 80 90 100
VTGTSVLGVK FDGGVVIAAD MLGSYGSLAR FRNISRIMRV NDSTMLGASG
110 120 130 140 150
DYADFQYLKQ VLGQMVIDEE LLGDGHSYSP RAIHSWLTRA MYSRRSKMNP
160 170 180 190 200
LWNTMVIGGY ADGESFLGYV DMLGVAYEAP SLATGYGAYL AQPLLREVLE
210 220 230 240 250
KQPVLSQTEA RELVERCMRV LYYRDARSYN RFQIATVTEK GVEIEGPLSA
260
QTNWDIAHMI SGFE
Length:264
Mass (Da):29,116
Last modified:December 15, 1998 - v1
Checksum:i6B6B42B21DFA2B74
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261A → S in BAE33781. (PubMed:16141072)Curated
Sequence conflicti26 – 261A → S in AAH08241. (PubMed:15489334)Curated
Sequence conflicti27 – 271T → A in BAE33781. (PubMed:16141072)Curated
Sequence conflicti42 – 421P → H in BAE40213. (PubMed:16141072)Curated
Sequence conflicti215 – 2151E → G in BAE23215. (PubMed:16141072)Curated
Sequence conflicti224 – 2241R → K in BAC36805. (PubMed:16141072)Curated
Sequence conflicti234 – 2341I → V in BAE33781. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U65636 mRNA. Translation: AAC53263.1.
AK077448 mRNA. Translation: BAC36805.1.
AK137044 mRNA. Translation: BAE23215.1.
AK156624 mRNA. Translation: BAE33781.1.
AK168265 mRNA. Translation: BAE40213.1.
AK168340 mRNA. Translation: BAE40277.1.
BC008241 mRNA. Translation: AAH08241.1.
M74556 mRNA. Translation: AAA39863.1.
CCDSiCCDS17597.1.
RefSeqiNP_032971.2. NM_008945.3.
UniGeneiMm.368.

Genome annotation databases

EnsembliENSMUST00000005923; ENSMUSP00000005923; ENSMUSG00000005779.
GeneIDi19172.
KEGGimmu:19172.
UCSCiuc008qhe.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U65636 mRNA. Translation: AAC53263.1.
AK077448 mRNA. Translation: BAC36805.1.
AK137044 mRNA. Translation: BAE23215.1.
AK156624 mRNA. Translation: BAE33781.1.
AK168265 mRNA. Translation: BAE40213.1.
AK168340 mRNA. Translation: BAE40277.1.
BC008241 mRNA. Translation: AAH08241.1.
M74556 mRNA. Translation: AAA39863.1.
CCDSiCCDS17597.1.
RefSeqiNP_032971.2. NM_008945.3.
UniGeneiMm.368.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UNBX-ray2.903/M/a/o46-264[»]
3UNEX-ray3.203/M/a/o46-264[»]
3UNFX-ray2.90M/a46-264[»]
3UNHX-ray3.20M/a46-264[»]
ProteinModelPortaliP99026.
SMRiP99026. Positions 46-261.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202420. 4 interactions.
IntActiP99026. 5 interactions.
MINTiMINT-1850556.

Protein family/group databases

MEROPSiT01.987.

PTM databases

PhosphoSiteiP99026.

2D gel databases

REPRODUCTION-2DPAGEP99026.
SWISS-2DPAGEP99026.

Proteomic databases

MaxQBiP99026.
PaxDbiP99026.
PRIDEiP99026.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000005923; ENSMUSP00000005923; ENSMUSG00000005779.
GeneIDi19172.
KEGGimmu:19172.
UCSCiuc008qhe.2. mouse.

Organism-specific databases

CTDi5692.
MGIiMGI:1098257. Psmb4.

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00390000000698.
HOVERGENiHBG018194.
InParanoidiP99026.
KOiK02736.
OMAiRIMRVND.
OrthoDBiEOG74FF1D.
PhylomeDBiP99026.
TreeFamiTF106220.

Enzyme and pathway databases

ReactomeiREACT_197102. ER-Phagosome pathway.
REACT_198693. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_199105. ER-Phagosome pathway.
REACT_199114. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_199121. Activation of NF-kappaB in B cells.
REACT_203336. Degradation of beta-catenin by the destruction complex.
REACT_203517. SCF-beta-TrCP mediated degradation of Emi1.
REACT_203973. Asymmetric localization of PCP proteins.
REACT_207679. Separation of Sister Chromatids.
REACT_212633. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_218318. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_219129. degradation of AXIN.
REACT_219897. APC/C:Cdc20 mediated degradation of Securin.
REACT_220647. SCF(Skp2)-mediated degradation of p27/p21.
REACT_225686. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_226135. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_227429. degradation of DVL.
REACT_232069. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_232469. Hh ligand biogenesis disease.
REACT_233316. Hedgehog ligand biogenesis.
REACT_234963. Regulation of ornithine decarboxylase (ODC).
REACT_244558. CDT1 association with the CDC6:ORC:origin complex.
REACT_245230. Orc1 removal from chromatin.
REACT_249922. CDK-mediated phosphorylation and removal of Cdc6.
REACT_263467. Ubiquitin-dependent degradation of Cyclin D1.
REACT_268522. GLI3 is processed to GLI3R by the proteasome.
REACT_268705. Degradation of GLI1 by the proteasome.
REACT_270923. Degradation of GLI2 by the proteasome.

Miscellaneous databases

ChiTaRSiPsmb4. mouse.
NextBioi295846.
PROiP99026.
SOURCEiSearch...

Gene expression databases

BgeeiP99026.
GenevestigatoriP99026.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR016295. Proteasome_endopept_cplx_B.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PIRSFiPIRSF001213. Psome_endopept_beta. 1 hit.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of mouse Lmp3 cDNA, encoding a proteasome beta subunit."
    Cruz M., Nandi D., Hendil K.B., Monaco J.J.
    Gene 190:251-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: B10.A.
    Tissue: Macrophage.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: BALB/c, C57BL/6J and NOD.
    Tissue: Spleen.
  3. "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].
    Strain: NMRI.
    Tissue: Mammary tumor.
  4. Lubec G., Klug S., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 46-80; 110-131 AND 232-240, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain and Hippocampus.
  5. Cited for: PROTEIN SEQUENCE OF 46-51.
    Tissue: Liver.
  6. Wang B., Hunsperger J., Laib J., Fan D.
    Submitted (AUG-1991) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 95-112.
    Strain: C57BL/6.
  7. "The proteasome as a lipopolysaccharide-binding protein in macrophages: differential effects of proteasome inhibition on lipopolysaccharide-induced signaling events."
    Qureshi N., Perera P.-Y., Shen J., Zhang G., Lenschat A., Splitter G., Morrison D.C., Vogel S.N.
    J. Immunol. 171:1515-1525(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH LPS.
  8. "The up-regulation of proteasome subunits and lysosomal proteases in hepatocellular carcinomas of the HBx gene knockin transgenic mice."
    Cui F., Wang Y., Wang J., Wei K., Hu J., Liu F., Wang H., Zhao X., Zhang X., Yang X.
    Proteomics 6:498-504(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
  9. Cited for: IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX.
  10. "Immuno- and constitutive proteasome crystal structures reveal differences in substrate and inhibitor specificity."
    Huber E.M., Basler M., Schwab R., Heinemeyer W., Kirk C.J., Groettrup M., Groll M.
    Cell 148:727-738(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 20S IMMUNOPROTEASOME, SUBUNIT, FUNCTION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiPSB4_MOUSE
AccessioniPrimary (citable) accession number: P99026
Secondary accession number(s): Q3THC0
, Q3THI3, Q3U0S0, Q3UVQ4, Q62008, Q8BK27, Q91VV7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 15, 1998
Last modified: February 4, 2015
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. 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.