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O00487

- PSDE_HUMAN

UniProt

O00487 - PSDE_HUMAN

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Protein

26S proteasome non-ATPase regulatory subunit 14

Gene

PSMD14

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

Functioni

Metalloprotease component of the 26S proteasome that specifically cleaves 'Lys-63'-linked polyubiquitin chains. The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. Plays a role in response to double-strand breaks (DSBs): acts as a regulator of non-homologous end joining (NHEJ) by cleaving 'Lys-63'-linked polyubiquitin, thereby promoting retention of JMJD2A/KDM4A on chromatin and restricting TP53BP1 accumulation. Also involved in homologous recombination repair by promoting RAD51 loading.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi113 – 1131Zinc; catalyticCurated
Metal bindingi115 – 1151Zinc; catalyticCurated
Metal bindingi126 – 1261Zinc; catalyticBy similarity

GO - Molecular functioni

  1. endopeptidase activator activity Source: UniProtKB
  2. metal ion binding Source: UniProtKB-KW
  3. metallopeptidase activity Source: UniProtKB
  4. proteasome binding Source: UniProtKB
  5. ubiquitin thiolesterase activity Source: UniProtKB

GO - Biological processi

  1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
  2. antigen processing and presentation of exogenous peptide antigen via MHC class I Source: Reactome
  3. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
  4. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
  5. apoptotic process Source: Reactome
  6. cellular nitrogen compound metabolic process Source: Reactome
  7. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
  8. double-strand break repair via homologous recombination Source: UniProtKB
  9. double-strand break repair via nonhomologous end joining Source: UniProtKB
  10. G1/S transition of mitotic cell cycle Source: Reactome
  11. gene expression Source: Reactome
  12. mitotic cell cycle Source: Reactome
  13. mRNA metabolic process Source: Reactome
  14. negative regulation of apoptotic process Source: Reactome
  15. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  16. positive regulation of endopeptidase activity Source: GOC
  17. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  18. protein K63-linked deubiquitination Source: UniProtKB
  19. protein polyubiquitination Source: Reactome
  20. regulation of apoptotic process Source: Reactome
  21. regulation of cellular amino acid metabolic process Source: Reactome
  22. regulation of proteasomal protein catabolic process Source: UniProtKB
  23. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  24. RNA metabolic process Source: Reactome
  25. small molecule metabolic process Source: Reactome
  26. ubiquitin-dependent protein catabolic process Source: UniProtKB
  27. viral process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

DNA damage, DNA repair, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_111178. ER-Phagosome pathway.
REACT_1156. Orc1 removal from chromatin.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_13565. Regulation of ornithine decarboxylase (ODC).
REACT_150471. Separation of Sister Chromatids.
REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_172638. Asymmetric localization of PCP proteins.
REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
REACT_200766. degradation of AXIN.
REACT_200841. degradation of DVL.
REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9031. Vpu mediated degradation of CD4.
REACT_9453. Vif-mediated degradation of APOBEC3G.

Protein family/group databases

MEROPSiM67.A11.

Names & Taxonomyi

Protein namesi
Recommended name:
26S proteasome non-ATPase regulatory subunit 14 (EC:3.4.19.-)
Alternative name(s):
26S proteasome regulatory subunit RPN11
26S proteasome-associated PAD1 homolog 1
Gene namesi
Name:PSMD14
Synonyms:POH1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:16889. PSMD14.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProt
  5. proteasome accessory complex Source: UniProtKB
  6. proteasome complex Source: UniProtKB
  7. proteasome regulatory particle, lid subcomplex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Proteasome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi113 – 1153HSH → ASA: Abolishes ubiquitin thioesterase activity, leading to prevent maintenance of JMJD2A/KDM4A on chromatin. 1 Publication

Organism-specific databases

PharmGKBiPA134957776.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 31031026S proteasome non-ATPase regulatory subunit 14PRO_0000213952Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei150 – 1501Phosphoserine1 Publication
Modified residuei224 – 2241Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO00487.
PaxDbiO00487.
PeptideAtlasiO00487.
PRIDEiO00487.

2D gel databases

OGPiO00487.
REPRODUCTION-2DPAGEIPI00024821.

PTM databases

PhosphoSiteiO00487.

Expressioni

Tissue specificityi

Widely expressed. Highest levels in heart and skeletal muscle.1 Publication

Gene expression databases

BgeeiO00487.
CleanExiHS_PSMD14.
ExpressionAtlasiO00487. baseline and differential.
GenevestigatoriO00487.

Organism-specific databases

HPAiHPA002114.

Interactioni

Subunit structurei

Component of the lid subcomplex of the 19S proteasome regulatory particle complex (also named PA700 complex). The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. Interacts with TXNL1.3 Publications

Protein-protein interaction databases

BioGridi115508. 68 interactions.
IntActiO00487. 23 interactions.
MINTiMINT-5003743.
STRINGi9606.ENSP00000386541.

Structurei

3D structure databases

ProteinModelPortaliO00487.
SMRiO00487. Positions 27-302.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 139114MPNAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi113 – 12614JAMM motifAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase M67A family. PSMD14 subfamily.Curated
Contains 1 MPN (JAB/Mov34) domain.Curated

Phylogenomic databases

eggNOGiCOG1310.
GeneTreeiENSGT00730000111116.
HOGENOMiHOG000183690.
HOVERGENiHBG053742.
InParanoidiO00487.
KOiK03030.
OMAiQDPKKHL.
OrthoDBiEOG7T7GTF.
PhylomeDBiO00487.
TreeFamiTF105748.

Family and domain databases

InterProiIPR000555. JAMM/MPN+_dom.
IPR024969. Rpn11/EIF3F_C.
[Graphical view]
PfamiPF01398. JAB. 1 hit.
PF13012. MitMem_reg. 1 hit.
[Graphical view]
SMARTiSM00232. JAB_MPN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O00487-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDRLLRLGGG MPGLGQGPPT DAPAVDTAEQ VYISSLALLK MLKHGRAGVP
60 70 80 90 100
MEVMGLMLGE FVDDYTVRVI DVFAMPQSGT GVSVEAVDPV FQAKMLDMLK
110 120 130 140 150
QTGRPEMVVG WYHSHPGFGC WLSGVDINTQ QSFEALSERA VAVVVDPIQS
160 170 180 190 200
VKGKVVIDAF RLINANMMVL GHEPRQTTSN LGHLNKPSIQ ALIHGLNRHY
210 220 230 240 250
YSITINYRKN ELEQKMLLNL HKKSWMEGLT LQDYSEHCKH NESVVKEMLE
260 270 280 290 300
LAKNYNKAVE EEDKMTPEQL AIKNVGKQDP KRHLEEHVDV LMTSNIVQCL
310
AAMLDTVVFK
Length:310
Mass (Da):34,577
Last modified:July 1, 1997 - v1
Checksum:i18ACE876C7682039
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U86782 mRNA. Translation: AAC51866.1.
AK055128 mRNA. Translation: BAG51474.1.
CH471058 Genomic DNA. Translation: EAX11370.1.
BC066336 mRNA. Translation: AAH66336.1.
CCDSiCCDS46437.1.
RefSeqiNP_005796.1. NM_005805.5.
UniGeneiHs.740477.

Genome annotation databases

EnsembliENST00000409682; ENSP00000386541; ENSG00000115233.
GeneIDi10213.
KEGGihsa:10213.
UCSCiuc002ubu.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U86782 mRNA. Translation: AAC51866.1 .
AK055128 mRNA. Translation: BAG51474.1 .
CH471058 Genomic DNA. Translation: EAX11370.1 .
BC066336 mRNA. Translation: AAH66336.1 .
CCDSi CCDS46437.1.
RefSeqi NP_005796.1. NM_005805.5.
UniGenei Hs.740477.

3D structure databases

ProteinModelPortali O00487.
SMRi O00487. Positions 27-302.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115508. 68 interactions.
IntActi O00487. 23 interactions.
MINTi MINT-5003743.
STRINGi 9606.ENSP00000386541.

Chemistry

BindingDBi O00487.
ChEMBLi CHEMBL2007629.

Protein family/group databases

MEROPSi M67.A11.

PTM databases

PhosphoSitei O00487.

2D gel databases

OGPi O00487.
REPRODUCTION-2DPAGE IPI00024821.

Proteomic databases

MaxQBi O00487.
PaxDbi O00487.
PeptideAtlasi O00487.
PRIDEi O00487.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000409682 ; ENSP00000386541 ; ENSG00000115233 .
GeneIDi 10213.
KEGGi hsa:10213.
UCSCi uc002ubu.3. human.

Organism-specific databases

CTDi 10213.
GeneCardsi GC02P162164.
HGNCi HGNC:16889. PSMD14.
HPAi HPA002114.
MIMi 607173. gene.
neXtProti NX_O00487.
PharmGKBi PA134957776.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1310.
GeneTreei ENSGT00730000111116.
HOGENOMi HOG000183690.
HOVERGENi HBG053742.
InParanoidi O00487.
KOi K03030.
OMAi QDPKKHL.
OrthoDBi EOG7T7GTF.
PhylomeDBi O00487.
TreeFami TF105748.

Enzyme and pathway databases

Reactomei REACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_111178. ER-Phagosome pathway.
REACT_1156. Orc1 removal from chromatin.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_13565. Regulation of ornithine decarboxylase (ODC).
REACT_150471. Separation of Sister Chromatids.
REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_172638. Asymmetric localization of PCP proteins.
REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
REACT_200766. degradation of AXIN.
REACT_200841. degradation of DVL.
REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9031. Vpu mediated degradation of CD4.
REACT_9453. Vif-mediated degradation of APOBEC3G.

Miscellaneous databases

GeneWikii PSMD14.
GenomeRNAii 10213.
NextBioi 38668.
PROi O00487.
SOURCEi Search...

Gene expression databases

Bgeei O00487.
CleanExi HS_PSMD14.
ExpressionAtlasi O00487. baseline and differential.
Genevestigatori O00487.

Family and domain databases

InterProi IPR000555. JAMM/MPN+_dom.
IPR024969. Rpn11/EIF3F_C.
[Graphical view ]
Pfami PF01398. JAB. 1 hit.
PF13012. MitMem_reg. 1 hit.
[Graphical view ]
SMARTi SM00232. JAB_MPN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Resistance to diverse drugs and ultraviolet light conferred by overexpression of a novel human 26 S proteasome subunit."
    Spataro V., Toda T., Craig R., Seeger M., Dubiel W., Harris A.L., Norbury C.
    J. Biol. Chem. 272:30470-30475(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Tissue: Lung.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Tissue: Testis.
  5. Lubec G., Afjehi-Sadat L.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 199-208, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Cajal-Retzius cell.
  6. "Mass spectrometric characterization of the affinity-purified human 26S proteasome complex."
    Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.
    Biochemistry 46:3553-3565(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  7. "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
    Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
    Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  8. "K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-associated Brcc36 and proteasomal Poh1."
    Cooper E.M., Cutcliffe C., Kristiansen T.Z., Pandey A., Pickart C.M., Cohen R.E.
    EMBO J. 28:621-631(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROBABLE FUNCTION, IDENTIFICATION IN THE PROTEASOME.
  9. "Thioredoxin Txnl1/TRP32 is a redox-active cofactor of the 26 S proteasome."
    Andersen K.M., Madsen L., Prag S., Johnsen A.H., Semple C.A., Hendil K.B., Hartmann-Petersen R.
    J. Biol. Chem. 284:15246-15254(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TXNL1.
  10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "The proteasomal de-ubiquitinating enzyme POH1 promotes the double-strand DNA break response."
    Butler L.R., Densham R.M., Jia J., Garvin A.J., Stone H.R., Shah V., Weekes D., Festy F., Beesley J., Morris J.R.
    EMBO J. 31:3918-3934(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE PROTEASOME, MUTAGENESIS OF 113-HIS--HIS-115.

Entry informationi

Entry nameiPSDE_HUMAN
AccessioniPrimary (citable) accession number: O00487
Secondary accession number(s): B3KNW2, O00176
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: July 1, 1997
Last modified: October 29, 2014
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
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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3