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Q9H4L4

- SENP3_HUMAN

UniProt

Q9H4L4 - SENP3_HUMAN

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Protein

Sentrin-specific protease 3

Gene

SENP3

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

Functioni

Protease that releases SUMO2 and SUMO3 monomers from sumoylated substrates, but has only weak activity against SUMO1 conjugates. Deconjugates SUMO2 from MEF2D, which increases its transcriptional activation capability. Deconjugates SUMO2 and SUMO3 from CDCA8. Redox sensor that, when redistributed into nucleoplasm, can act as an effector to enhance HIF1A transcriptional activity by desumoylating EP300. Required for rRNA processing through deconjugation of SUMO2 and SUMO3 from nucleophosmin, NPM1. Plays a role in the regulation of sumoylation status of ZNF148. Functions as a component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes.7 Publications

Catalytic activityi

Hydrolysis of the alpha-linked peptide bond in the sequence Gly-Gly-|-Ala-Thr-Tyr at the C-terminal end of the small ubiquitin-like modifier (SUMO) propeptide, Smt3, leading to the mature form of the protein. A second reaction involves the cleavage of an epsilon-linked peptide bond between the C-terminal glycine of the mature SUMO and the lysine epsilon-amino group of the target protein.

Enzyme regulationi

On oxidative stress, SENP3 degradation is blocked by inhibition of its ubiquitination, which stabilizes it as it accumulates in the nucleoplasm.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei465 – 4651By similarity
Active sitei482 – 4821By similarity
Active sitei532 – 5321By similarity

GO - Molecular functioni

  1. cysteine-type peptidase activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

BRENDAi3.4.22.68. 2681.

Protein family/group databases

MEROPSiC48.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Sentrin-specific protease 3 (EC:3.4.22.68)
Alternative name(s):
SUMO-1-specific protease 3
Sentrin/SUMO-specific protease SENP3
Gene namesi
Name:SENP3
Synonyms:SSP3, SUSP3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:17862. SENP3.

Subcellular locationi

Cytoplasm By similarity. Nucleusnucleolus. Nucleusnucleoplasm
Note: Mainly found in the nucleoplasm, with low levels detected in the cytoplasmic and chromatin fractions (By similarity). Redistributes between the nucleolus and the nucleoplasm in response to mild oxidative stress.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. MLL1 complex Source: UniProtKB
  3. nucleolus Source: LIFEdb
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi532 – 5321C → S: Loss of enzymatic activity. 1 Publication

Organism-specific databases

PharmGKBiPA134933213.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 574574Sentrin-specific protease 3PRO_0000101721Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei169 – 1691Phosphoserine3 Publications
Modified residuei181 – 1811Phosphoserine1 Publication
Modified residuei212 – 2121Phosphoserine2 Publications
Modified residuei232 – 2321Phosphoserine3 Publications
Modified residuei353 – 3531Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9H4L4.
PaxDbiQ9H4L4.
PRIDEiQ9H4L4.

PTM databases

PhosphoSiteiQ9H4L4.

Expressioni

Gene expression databases

BgeeiQ9H4L4.
CleanExiHS_SENP3.
ExpressionAtlasiQ9H4L4. baseline.
GenevestigatoriQ9H4L4.

Organism-specific databases

HPAiHPA060290.

Interactioni

Subunit structurei

Binds to SUMO1 and SUMO3 (By similarity). Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with EP300, NPM1 and CDCA8. Component of the 5FMC complex, at least composed of PELP1, LAS1L, TEX10, WDR18 and SENP3; the complex interacts with methylated CHTOP and ZNF148. Interacts with NOL9.By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NPM1P067486EBI-2880236,EBI-78579
PELP1Q8IZL85EBI-2880236,EBI-716449
TEX10Q9NXF12EBI-2880236,EBI-2371062
UBCP0CG482EBI-2880236,EBI-3390054
WDR18Q9BV383EBI-2880236,EBI-727429

Protein-protein interaction databases

BioGridi117594. 45 interactions.
DIPiDIP-47511N.
IntActiQ9H4L4. 22 interactions.
MINTiMINT-1200849.
STRINGi9606.ENSP00000314029.

Structurei

3D structure databases

ProteinModelPortaliQ9H4L4.
SMRiQ9H4L4. Positions 360-572.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni386 – 543158ProteaseAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi125 – 1284Nuclear localization signalSequence Analysis
Motifi153 – 1597Nuclear localization signalSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi13 – 6856Pro-richAdd
BLAST
Compositional biasi76 – 9217Glu-richAdd
BLAST
Compositional biasi192 – 1954Poly-Pro

Sequence similaritiesi

Belongs to the peptidase C48 family.Curated

Phylogenomic databases

eggNOGiCOG5160.
GeneTreeiENSGT00530000062941.
HOGENOMiHOG000154287.
HOVERGENiHBG059450.
InParanoidiQ9H4L4.
KOiK08593.
OMAiRLPPRWG.
PhylomeDBiQ9H4L4.
TreeFamiTF316289.

Family and domain databases

InterProiIPR003653. Peptidase_C48.
[Graphical view]
PfamiPF02902. Peptidase_C48. 1 hit.
[Graphical view]
PROSITEiPS50600. ULP_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9H4L4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKETIQGTGS WGPEPPGPGI PPAYSSPRRE RLRWPPPPKP RLKSGGGFGP
60 70 80 90 100
DPGSGTTVPA RRLPVPRPSF DASASEEEEE EEEEEDEDEE EEVAAWRLPP
110 120 130 140 150
RWSQLGTSQR PRPSRPTHRK TCSQRRRRAM RAFRMLLYSK STSLTFHWKL
160 170 180 190 200
WGRHRGRRRG LAHPKNHLSP QQGGATPQVP SPCCRFDSPR GPPPPRLGLL
210 220 230 240 250
GALMAEDGVR GSPPVPSGPP MEEDGLRWTP KSPLDPDSGL LSCTLPNGFG
260 270 280 290 300
GQSGPEGERS LAPPDASILI SNVCSIGDHV AQELFQGSDL GMAEEAERPG
310 320 330 340 350
EKAGQHSPLR EEHVTCVQSI LDEFLQTYGS LIPLSTDEVV EKLEDIFQQE
360 370 380 390 400
FSTPSRKGLV LQLIQSYQRM PGNAMVRGFR VAYKRHVLTM DDLGTLYGQN
410 420 430 440 450
WLNDQVMNMY GDLVMDTVPE KVHFFNSFFY DKLRTKGYDG VKRWTKNVDI
460 470 480 490 500
FNKELLLIPI HLEVHWSLIS VDVRRRTITY FDSQRTLNRR CPKHIAKYLQ
510 520 530 540 550
AEAVKKDRLD FHQGWKGYFK MNVARQNNDS DCGAFVLQYC KHLALSQPFS
560 570
FTQQDMPKLR RQIYKELCHC KLTV
Length:574
Mass (Da):65,010
Last modified:December 12, 2006 - v2
Checksum:iE495137EE7500741
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 312ER → DG in AAG33252. (PubMed:10806345)Curated
Sequence conflicti60 – 601A → T in AAG33252. (PubMed:10806345)Curated
Sequence conflicti65 – 651V → A in AAG33252. (PubMed:10806345)Curated
Sequence conflicti113 – 1142PS → AL in AAG33252. (PubMed:10806345)Curated
Sequence conflicti117 – 1171T → S in AAG33252. (PubMed:10806345)Curated
Sequence conflicti134 – 1341R → Q in AAG33252. (PubMed:10806345)Curated
Sequence conflicti161 – 1611L → S in AAH48306. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti515 – 5151W → R.
Corresponds to variant rs9972914 [ dbSNP | Ensembl ].
VAR_051544

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY008763 mRNA. Translation: AAG33252.1.
AF199459 mRNA. Translation: AAL25652.1.
AL050283 mRNA. Translation: CAB43384.2.
AL834294 mRNA. Translation: CAD38967.1.
BC048306 mRNA. Translation: AAH48306.1.
BC080658 mRNA. Translation: AAH80658.1.
CCDSiCCDS73958.1.
PIRiT08759.
RefSeqiNP_056485.2. NM_015670.5.
UniGeneiHs.513926.
Hs.733104.

Genome annotation databases

EnsembliENST00000321337; ENSP00000314029; ENSG00000161956.
ENST00000429205; ENSP00000403712; ENSG00000161956.
GeneIDi26168.
KEGGihsa:26168.
UCSCiuc002ghm.3. human.

Polymorphism databases

DMDMi119370525.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY008763 mRNA. Translation: AAG33252.1 .
AF199459 mRNA. Translation: AAL25652.1 .
AL050283 mRNA. Translation: CAB43384.2 .
AL834294 mRNA. Translation: CAD38967.1 .
BC048306 mRNA. Translation: AAH48306.1 .
BC080658 mRNA. Translation: AAH80658.1 .
CCDSi CCDS73958.1.
PIRi T08759.
RefSeqi NP_056485.2. NM_015670.5.
UniGenei Hs.513926.
Hs.733104.

3D structure databases

ProteinModelPortali Q9H4L4.
SMRi Q9H4L4. Positions 360-572.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117594. 45 interactions.
DIPi DIP-47511N.
IntActi Q9H4L4. 22 interactions.
MINTi MINT-1200849.
STRINGi 9606.ENSP00000314029.

Protein family/group databases

MEROPSi C48.003.

PTM databases

PhosphoSitei Q9H4L4.

Polymorphism databases

DMDMi 119370525.

Proteomic databases

MaxQBi Q9H4L4.
PaxDbi Q9H4L4.
PRIDEi Q9H4L4.

Protocols and materials databases

DNASUi 26168.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000321337 ; ENSP00000314029 ; ENSG00000161956 .
ENST00000429205 ; ENSP00000403712 ; ENSG00000161956 .
GeneIDi 26168.
KEGGi hsa:26168.
UCSCi uc002ghm.3. human.

Organism-specific databases

CTDi 26168.
GeneCardsi GC17P007467.
H-InvDB HIX0013501.
HGNCi HGNC:17862. SENP3.
HPAi HPA060290.
MIMi 612844. gene.
neXtProti NX_Q9H4L4.
PharmGKBi PA134933213.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5160.
GeneTreei ENSGT00530000062941.
HOGENOMi HOG000154287.
HOVERGENi HBG059450.
InParanoidi Q9H4L4.
KOi K08593.
OMAi RLPPRWG.
PhylomeDBi Q9H4L4.
TreeFami TF316289.

Enzyme and pathway databases

BRENDAi 3.4.22.68. 2681.

Miscellaneous databases

ChiTaRSi SENP3. human.
GeneWikii SENP3.
GenomeRNAii 26168.
NextBioi 48279.
PROi Q9H4L4.
SOURCEi Search...

Gene expression databases

Bgeei Q9H4L4.
CleanExi HS_SENP3.
ExpressionAtlasi Q9H4L4. baseline.
Genevestigatori Q9H4L4.

Family and domain databases

InterProi IPR003653. Peptidase_C48.
[Graphical view ]
Pfami PF02902. Peptidase_C48. 1 hit.
[Graphical view ]
PROSITEi PS50600. ULP_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Ubiquitin-like proteins: new wines in new bottles."
    Yeh E.T.H., Gong L., Kamitani T.
    Gene 248:1-14(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Choi S.J., Jeon Y.-J., Kim K.I., Nishimori S., Suzuki T., Uchida S., Shimbara N., Tanaka K., Chung C.H.
    Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Melanoma and Uterus.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  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].
    Tissue: Lymph and Uterus.
  6. "Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF."
    Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J., Allis C.D., Chait B.T., Hess J.L., Roeder R.G.
    Cell 121:873-885(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MLL1/MLL COMPLEX.
  7. "Association with class IIa histone deacetylases upregulates the sumoylation of MEF2 transcription factors."
    Gregoire S., Yang X.-J.
    Mol. Cell. Biol. 25:2273-2287(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Characterization of a family of nucleolar SUMO-specific proteases with preference for SUMO-2 or SUMO-3."
    Gong L., Yeh E.T.H.
    J. Biol. Chem. 281:15869-15877(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "The nucleolar SUMO-specific protease SENP3 reverses SUMO modification of nucleophosmin and is required for rRNA processing."
    Haindl M., Harasim T., Eick D., Muller S.
    EMBO Rep. 9:273-279(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF CYS-532, INTERACTION WITH NPM1.
  11. "Nucleolar protein B23/nucleophosmin regulates the vertebrate SUMO pathway through SENP3 and SENP5 proteases."
    Yun C., Wang Y., Mukhopadhyay D., Backlund P., Kolli N., Yergey A., Wilkinson K.D., Dasso M.
    J. Cell Biol. 183:589-595(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH NPM1.
  12. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169 AND SER-181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169 AND SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212 AND THR-353, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "SENP3 is responsible for HIF-1 transactivation under mild oxidative stress via p300 de-SUMOylation."
    Huang C., Han Y., Wang Y., Sun X., Yan S., Yeh E.T.H., Chen Y., Cang H., Li H., Shi G., Cheng J., Tang X., Yi J.
    EMBO J. 28:2748-2762(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH EP300.
  16. "RanBP2 and SENP3 function in a mitotic SUMO2/3 conjugation-deconjugation cycle on Borealin."
    Klein U.R., Haindl M., Nigg E.A., Muller S.
    Mol. Biol. Cell 20:410-418(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CDCA8.
  17. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Five friends of methylated chromatin target of protein-arginine-methyltransferase[prmt]-1 (chtop), a complex linking arginine methylation to desumoylation."
    Fanis P., Gillemans N., Aghajanirefah A., Pourfarzad F., Demmers J., Esteghamat F., Vadlamudi R.K., Grosveld F., Philipsen S., van Dijk T.B.
    Mol. Cell. Proteomics 11:1263-1273(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE 5FMC COMPLEX.

Entry informationi

Entry nameiSENP3_HUMAN
AccessioniPrimary (citable) accession number: Q9H4L4
Secondary accession number(s): Q66K15
, Q86VS7, Q96PS4, Q9Y3W9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2002
Last sequence update: December 12, 2006
Last modified: October 29, 2014
This is version 117 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3