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Protein

Proteasome subunit alpha type-2

Gene

PSMA2

Organism
Homo sapiens (Human)
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. PSMA2 may have a potential regulatory effect on another component(s) of the proteasome complex through tyrosine phosphorylation.

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

BioCyciZFISH:HS02926-MONOMER.
ReactomeiR-HSA-1169091. Activation of NF-kappaB in B cells.
R-HSA-1234176. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
R-HSA-1236974. ER-Phagosome pathway.
R-HSA-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-HSA-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-HSA-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-HSA-174154. APC/C:Cdc20 mediated degradation of Securin.
R-HSA-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-HSA-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-HSA-180534. Vpu mediated degradation of CD4.
R-HSA-180585. Vif-mediated degradation of APOBEC3G.
R-HSA-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-HSA-195253. Degradation of beta-catenin by the destruction complex.
R-HSA-202424. Downstream TCR signaling.
R-HSA-211733. Regulation of activated PAK-2p34 by proteasome mediated degradation.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-HSA-350562. Regulation of ornithine decarboxylase (ODC).
R-HSA-382556. ABC-family proteins mediated transport.
R-HSA-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-HSA-4608870. Asymmetric localization of PCP proteins.
R-HSA-4641257. Degradation of AXIN.
R-HSA-4641258. Degradation of DVL.
R-HSA-5358346. Hedgehog ligand biogenesis.
R-HSA-5362768. Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
R-HSA-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-HSA-5607764. CLEC7A (Dectin-1) signaling.
R-HSA-5610780. Degradation of GLI1 by the proteasome.
R-HSA-5610783. Degradation of GLI2 by the proteasome.
R-HSA-5610785. GLI3 is processed to GLI3R by the proteasome.
R-HSA-5632684. Hedgehog 'on' state.
R-HSA-5658442. Regulation of RAS by GAPs.
R-HSA-5668541. TNFR2 non-canonical NF-kB pathway.
R-HSA-5676590. NIK-->noncanonical NF-kB signaling.
R-HSA-5678895. Defective CFTR causes cystic fibrosis.
R-HSA-5687128. MAPK6/MAPK4 signaling.
R-HSA-5689603. UCH proteinases.
R-HSA-5689880. Ub-specific processing proteases.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-68827. CDT1 association with the CDC6:ORC:origin complex.
R-HSA-68949. Orc1 removal from chromatin.
R-HSA-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-HSA-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-HSA-69481. G2/M Checkpoints.
R-HSA-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-HSA-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-HSA-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Protein family/group databases

MEROPSiT01.972.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-2 (EC:3.4.25.1)
Alternative name(s):
Macropain subunit C3
Multicatalytic endopeptidase complex subunit C3
Proteasome component C3
Gene namesi
Name:PSMA2
Synonyms:HC3, PSC3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:9531. PSMA2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic mRNA processing body Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • proteasome complex Source: UniProtKB
  • proteasome core complex Source: UniProtKB
  • proteasome core complex, alpha-subunit complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Organism-specific databases

DisGeNETi5683.
OpenTargetsiENSG00000106588.
ENSG00000256646.
PharmGKBiPA33876.

Chemistry databases

ChEMBLiCHEMBL2364701.
DrugBankiDB00188. Bortezomib.

Polymorphism and mutation databases

BioMutaiPSMA2.
DMDMi130850.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001240772 – 234Proteasome subunit alpha type-2Add BLAST233

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei6PhosphotyrosineBy similarity1
Modified residuei7PhosphoserineCombined sources1
Modified residuei14PhosphoserineCombined sources1
Modified residuei16PhosphoserineCombined sources1
Modified residuei24PhosphotyrosineCombined sources1
Modified residuei70N6-acetyllysineCombined sources1
Modified residuei76PhosphotyrosineCombined sources1
Modified residuei171N6-acetyllysineCombined sources1

Post-translational modificationi

Phosphorylated on tyrosine residues; which may be important for nuclear import.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP25787.
MaxQBiP25787.
PaxDbiP25787.
PeptideAtlasiP25787.
PRIDEiP25787.
TopDownProteomicsiP25787.

2D gel databases

OGPiP25787.
REPRODUCTION-2DPAGEIPI00219622.

PTM databases

iPTMnetiP25787.
PhosphoSitePlusiP25787.
SwissPalmiP25787.

Expressioni

Inductioni

Down-regulated by antioxidants BO-653 and probucol. Down-regulated in response to enterovirus 71 (EV71) infection (at protein level).2 Publications

Gene expression databases

BgeeiENSG00000106588.
CleanExiHS_PSMA2.
ExpressionAtlasiP25787. baseline and differential.
GenevisibleiP25787. HS.

Organism-specific databases

HPAiHPA008188.

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
PSMA1P257865EBI-603262,EBI-359352
PSMA4P257897EBI-603262,EBI-359310
PSMA6P609005EBI-603262,EBI-357793
PSMA7O148185EBI-603262,EBI-603272

Protein-protein interaction databases

BioGridi111656. 132 interactors.
DIPiDIP-29364N.
IntActiP25787. 31 interactors.
MINTiMINT-1178435.
STRINGi9606.ENSP00000455744.

Chemistry databases

BindingDBiP25787.

Structurei

Secondary structure

1234
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 10Combined sources3
Helixi20 – 30Combined sources11
Beta strandi35 – 39Combined sources5
Beta strandi44 – 49Combined sources6
Beta strandi53 – 57Combined sources5
Helixi59 – 61Combined sources3
Beta strandi64 – 69Combined sources6
Beta strandi72 – 78Combined sources7
Helixi80 – 101Combined sources22
Helixi107 – 120Combined sources14
Turni121 – 123Combined sources3
Beta strandi131 – 140Combined sources10
Beta strandi143 – 149Combined sources7
Beta strandi155 – 164Combined sources10
Helixi167 – 177Combined sources11
Helixi184 – 196Combined sources13
Beta strandi207 – 214Combined sources8
Beta strandi217 – 220Combined sources4
Helixi223 – 231Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4R3OX-ray2.60B/P2-234[»]
4R67X-ray2.89B/P/d/r2-234[»]
5A0Qelectron microscopy3.50B/P1-234[»]
5GJQelectron microscopy4.50C/i1-234[»]
5GJRelectron microscopy3.50C/i1-234[»]
5L4Gelectron microscopy4.02B/O1-234[»]
5LE5X-ray1.80A/O1-234[»]
5LEXX-ray2.20A/O1-234[»]
5LEYX-ray1.90A/O1-234[»]
5LEZX-ray2.19A/O1-234[»]
5LF0X-ray2.41A/O1-234[»]
5LF1X-ray2.00A/O1-234[»]
5LF3X-ray2.10A/O1-234[»]
5LF4X-ray1.99A/O1-234[»]
5LF6X-ray2.07A/O1-234[»]
5LF7X-ray2.00A/O1-234[»]
5T0Celectron microscopy3.80AH/BH2-234[»]
5T0Gelectron microscopy4.40H2-234[»]
5T0Helectron microscopy6.80H2-234[»]
5T0Ielectron microscopy8.00H2-234[»]
5T0Jelectron microscopy8.00H2-234[»]
ProteinModelPortaliP25787.
SMRiP25787.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0181. Eukaryota.
ENOG410XPQ8. LUCA.
GeneTreeiENSGT00550000074870.
HOGENOMiHOG000091085.
HOVERGENiHBG003005.
InParanoidiP25787.
KOiK02726.
OMAiWKATALG.
OrthoDBiEOG091G0GX6.
PhylomeDBiP25787.
TreeFamiTF106207.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTiSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P25787-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAERGYSFSL TTFSPSGKLV QIEYALAAVA GGAPSVGIKA ANGVVLATEK
60 70 80 90 100
KQKSILYDER SVHKVEPITK HIGLVYSGMG PDYRVLVHRA RKLAQQYYLV
110 120 130 140 150
YQEPIPTAQL VQRVASVMQE YTQSGGVRPF GVSLLICGWN EGRPYLFQSD
160 170 180 190 200
PSGAYFAWKA TAMGKNYVNG KTFLEKRYNE DLELEDAIHT AILTLKESFE
210 220 230
GQMTEDNIEV GICNEAGFRR LTPTEVKDYL AAIA
Length:234
Mass (Da):25,899
Last modified:January 23, 2007 - v2
Checksum:i63CB56A233583836
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_036278110L → V in a colorectal cancer sample; somatic mutation. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00760 mRNA. Translation: BAA00657.1.
AK290654 mRNA. Translation: BAF83343.1.
CR450317 mRNA. Translation: CAG29313.1.
CH236951 Genomic DNA. Translation: EAL24005.1.
CH471073 Genomic DNA. Translation: EAW94152.1.
BC002900 mRNA. Translation: AAH02900.2.
BC047697 mRNA. Translation: AAH47697.1.
CCDSiCCDS5467.1.
PIRiS15970. SNHUC3.
RefSeqiNP_002778.1. NM_002787.4.
UniGeneiHs.333786.

Genome annotation databases

EnsembliENST00000223321; ENSP00000223321; ENSG00000106588.
GeneIDi5683.
KEGGihsa:5683.
UCSCiuc003thy.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00760 mRNA. Translation: BAA00657.1.
AK290654 mRNA. Translation: BAF83343.1.
CR450317 mRNA. Translation: CAG29313.1.
CH236951 Genomic DNA. Translation: EAL24005.1.
CH471073 Genomic DNA. Translation: EAW94152.1.
BC002900 mRNA. Translation: AAH02900.2.
BC047697 mRNA. Translation: AAH47697.1.
CCDSiCCDS5467.1.
PIRiS15970. SNHUC3.
RefSeqiNP_002778.1. NM_002787.4.
UniGeneiHs.333786.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4R3OX-ray2.60B/P2-234[»]
4R67X-ray2.89B/P/d/r2-234[»]
5A0Qelectron microscopy3.50B/P1-234[»]
5GJQelectron microscopy4.50C/i1-234[»]
5GJRelectron microscopy3.50C/i1-234[»]
5L4Gelectron microscopy4.02B/O1-234[»]
5LE5X-ray1.80A/O1-234[»]
5LEXX-ray2.20A/O1-234[»]
5LEYX-ray1.90A/O1-234[»]
5LEZX-ray2.19A/O1-234[»]
5LF0X-ray2.41A/O1-234[»]
5LF1X-ray2.00A/O1-234[»]
5LF3X-ray2.10A/O1-234[»]
5LF4X-ray1.99A/O1-234[»]
5LF6X-ray2.07A/O1-234[»]
5LF7X-ray2.00A/O1-234[»]
5T0Celectron microscopy3.80AH/BH2-234[»]
5T0Gelectron microscopy4.40H2-234[»]
5T0Helectron microscopy6.80H2-234[»]
5T0Ielectron microscopy8.00H2-234[»]
5T0Jelectron microscopy8.00H2-234[»]
ProteinModelPortaliP25787.
SMRiP25787.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111656. 132 interactors.
DIPiDIP-29364N.
IntActiP25787. 31 interactors.
MINTiMINT-1178435.
STRINGi9606.ENSP00000455744.

Chemistry databases

BindingDBiP25787.
ChEMBLiCHEMBL2364701.
DrugBankiDB00188. Bortezomib.

Protein family/group databases

MEROPSiT01.972.

PTM databases

iPTMnetiP25787.
PhosphoSitePlusiP25787.
SwissPalmiP25787.

Polymorphism and mutation databases

BioMutaiPSMA2.
DMDMi130850.

2D gel databases

OGPiP25787.
REPRODUCTION-2DPAGEIPI00219622.

Proteomic databases

EPDiP25787.
MaxQBiP25787.
PaxDbiP25787.
PeptideAtlasiP25787.
PRIDEiP25787.
TopDownProteomicsiP25787.

Protocols and materials databases

DNASUi5683.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000223321; ENSP00000223321; ENSG00000106588.
GeneIDi5683.
KEGGihsa:5683.
UCSCiuc003thy.5. human.

Organism-specific databases

CTDi5683.
DisGeNETi5683.
GeneCardsiPSMA2.
HGNCiHGNC:9531. PSMA2.
HPAiHPA008188.
MIMi176842. gene.
neXtProtiNX_P25787.
OpenTargetsiENSG00000106588.
ENSG00000256646.
PharmGKBiPA33876.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0181. Eukaryota.
ENOG410XPQ8. LUCA.
GeneTreeiENSGT00550000074870.
HOGENOMiHOG000091085.
HOVERGENiHBG003005.
InParanoidiP25787.
KOiK02726.
OMAiWKATALG.
OrthoDBiEOG091G0GX6.
PhylomeDBiP25787.
TreeFamiTF106207.

Enzyme and pathway databases

BioCyciZFISH:HS02926-MONOMER.
ReactomeiR-HSA-1169091. Activation of NF-kappaB in B cells.
R-HSA-1234176. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
R-HSA-1236974. ER-Phagosome pathway.
R-HSA-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-HSA-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-HSA-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-HSA-174154. APC/C:Cdc20 mediated degradation of Securin.
R-HSA-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-HSA-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-HSA-180534. Vpu mediated degradation of CD4.
R-HSA-180585. Vif-mediated degradation of APOBEC3G.
R-HSA-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-HSA-195253. Degradation of beta-catenin by the destruction complex.
R-HSA-202424. Downstream TCR signaling.
R-HSA-211733. Regulation of activated PAK-2p34 by proteasome mediated degradation.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-HSA-350562. Regulation of ornithine decarboxylase (ODC).
R-HSA-382556. ABC-family proteins mediated transport.
R-HSA-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-HSA-4608870. Asymmetric localization of PCP proteins.
R-HSA-4641257. Degradation of AXIN.
R-HSA-4641258. Degradation of DVL.
R-HSA-5358346. Hedgehog ligand biogenesis.
R-HSA-5362768. Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
R-HSA-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-HSA-5607764. CLEC7A (Dectin-1) signaling.
R-HSA-5610780. Degradation of GLI1 by the proteasome.
R-HSA-5610783. Degradation of GLI2 by the proteasome.
R-HSA-5610785. GLI3 is processed to GLI3R by the proteasome.
R-HSA-5632684. Hedgehog 'on' state.
R-HSA-5658442. Regulation of RAS by GAPs.
R-HSA-5668541. TNFR2 non-canonical NF-kB pathway.
R-HSA-5676590. NIK-->noncanonical NF-kB signaling.
R-HSA-5678895. Defective CFTR causes cystic fibrosis.
R-HSA-5687128. MAPK6/MAPK4 signaling.
R-HSA-5689603. UCH proteinases.
R-HSA-5689880. Ub-specific processing proteases.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-68827. CDT1 association with the CDC6:ORC:origin complex.
R-HSA-68949. Orc1 removal from chromatin.
R-HSA-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-HSA-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-HSA-69481. G2/M Checkpoints.
R-HSA-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-HSA-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-HSA-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

GeneWikiiPSMA2.
GenomeRNAii5683.
PROiP25787.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000106588.
CleanExiHS_PSMA2.
ExpressionAtlasiP25787. baseline and differential.
GenevisibleiP25787. HS.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTiSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPSA2_HUMAN
AccessioniPrimary (citable) accession number: P25787
Secondary accession number(s): Q6ICS6, Q9BU45
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 182 of the entry and version 2 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 7
    Human chromosome 7: 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

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.