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P25774 (CATS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cathepsin S

EC=3.4.22.27
Gene names
Name:CTSS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length331 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N.

Catalytic activity

Similar to cathepsin L, but with much less activity on Z-Phe-Arg-|-NHMec, and more activity on the Z-Val-Val-Arg-|-Xaa compound.

Subunit structure

Monomer.

Subcellular location

Lysosome.

Sequence similarities

Belongs to the peptidase C1 family.

Ontologies

Keywords
   Cellular componentLysosome
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal
   Molecular functionHydrolase
Protease
Thiol protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadaptive immune response

Inferred from expression pattern PubMed 15196205. Source: UniProtKB

antigen processing and presentation

Traceable author statement PubMed 15196205. Source: UniProtKB

antigen processing and presentation of exogenous peptide antigen via MHC class I

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class II

Traceable author statement. Source: Reactome

antigen processing and presentation of peptide antigen via MHC class I

Traceable author statement. Source: Reactome

basement membrane disassembly

Inferred from direct assay PubMed 22952693. Source: BHF-UCL

cellular response to thyroid hormone stimulus

Inferred from expression pattern PubMed 21217776. Source: UniProtKB

collagen catabolic process

Inferred from direct assay PubMed 22952693. Source: BHF-UCL

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

immune response

Traceable author statement Ref.4. Source: ProtInc

innate immune response

Traceable author statement. Source: Reactome

proteolysis

Traceable author statement Ref.1. Source: ProtInc

proteolysis involved in cellular protein catabolic process

Inferred from direct assay PubMed 22952693. Source: BHF-UCL

toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentendolysosome lumen

Traceable author statement. Source: Reactome

extracellular region

Non-traceable author statement PubMed 14718574. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 22952693. Source: BHF-UCL

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

lysosomal lumen

Traceable author statement. Source: Reactome

lysosome

Inferred from direct assay PubMed 15196205. Source: UniProtKB

   Molecular_functioncollagen binding

Inferred from direct assay PubMed 22952693. Source: BHF-UCL

cysteine-type endopeptidase activity

Inferred from direct assay PubMed 22952693. Source: BHF-UCL

fibronectin binding

Inferred from physical interaction PubMed 22952693. Source: BHF-UCL

laminin binding

Inferred from direct assay PubMed 22952693. Source: BHF-UCL

proteoglycan binding

Inferred from physical interaction PubMed 22952693. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P25774-1)

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.
Isoform 2 (identifier: P25774-2)

The sequence of this isoform differs from the canonical sequence as follows:
     84-133: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Propeptide17 – 11498Activation peptide
PRO_0000026313
Chain115 – 331217Cathepsin S
PRO_0000026314

Sites

Active site1391 By similarity
Active site2781 By similarity
Active site2981 By similarity

Amino acid modifications

Glycosylation1041N-linked (GlcNAc...) Potential
Disulfide bond126 ↔ 224 Ref.13
Disulfide bond136 ↔ 180 Ref.13
Disulfide bond170 ↔ 213 Ref.13
Disulfide bond272 ↔ 320 Ref.13

Natural variations

Alternative sequence84 – 13350Missing in isoform 2.
VSP_042712
Natural variant1131R → W. Ref.5 Ref.6 Ref.9
Corresponds to variant rs2230061 [ dbSNP | Ensembl ].
VAR_025385
Natural variant1611S → T. Ref.1 Ref.4
Corresponds to variant rs1059604 [ dbSNP | Ensembl ].
VAR_025386

Experimental info

Sequence conflict921M → T Ref.1
Sequence conflict921M → T Ref.4

Secondary structure

.......................................................... 331
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 21, 2006. Version 3.
Checksum: 86093619DB6F0269

FASTA33137,496
        10         20         30         40         50         60 
MKRLVCVLLV CSSAVAQLHK DPTLDHHWHL WKKTYGKQYK EKNEEAVRRL IWEKNLKFVM 

        70         80         90        100        110        120 
LHNLEHSMGM HSYDLGMNHL GDMTSEEVMS LMSSLRVPSQ WQRNITYKSN PNRILPDSVD 

       130        140        150        160        170        180 
WREKGCVTEV KYQGSCGACW AFSAVGALEA QLKLKTGKLV SLSAQNLVDC STEKYGNKGC 

       190        200        210        220        230        240 
NGGFMTTAFQ YIIDNKGIDS DASYPYKAMD QKCQYDSKYR AATCSKYTEL PYGREDVLKE 

       250        260        270        280        290        300 
AVANKGPVSV GVDARHPSFF LYRSGVYYEP SCTQNVNHGV LVVGYGDLNG KEYWLVKNSW 

       310        320        330 
GHNFGEEGYI RMARNKGNHC GIASFPSYPE I 

« Hide

Isoform 2 [UniParc].

Checksum: C0445894FAD89713
Show »

FASTA28131,626

References

« Hide 'large scale' references
[1]"Molecular cloning and expression of human alveolar macrophage cathepsin S, an elastinolytic cysteine protease."
Shi G.-P., Munger J.S., Meara J.P., Rich D.H., Chapman H.A.
J. Biol. Chem. 267:7258-7262(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-161.
Tissue: Alveolar macrophage.
[2]"Phylogenetic conservation of cysteine proteinases. Cloning and expression of a cDNA coding for human cathepsin S."
Wiederanders B., Broemme D., Kirschke H., von Figura K., Schmidt B., Peters C.
J. Biol. Chem. 267:13708-13713(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Testis.
[3]Wiederanders B., Broemme D., Kirschke H., von Figura K., Schmidt B., Peters C.
Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 211.
[4]"Human cathepsin S: chromosomal localization, gene structure, and tissue distribution."
Shi G.-P., Webb A.C., Foster K.E., Knoll J.H.M., Lemere C.A., Munger J.S., Chapman H.A.
J. Biol. Chem. 269:11530-11536(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-161.
[5]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT TRP-113.
[6]"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. expand/collapse author list , 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] (ISOFORMS 1 AND 2), VARIANT TRP-113.
Tissue: Placenta and Synovium.
[7]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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 TRP-113.
Tissue: Pancreas.
[10]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Three-dimensional structures of the cysteine proteases cathepsins K and S deduced by knowledge-based modelling and active site characteristics."
Fengler A., Brandt W.
Protein Eng. 11:1007-1013(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING OF 115-331.
[12]"Structure of a Cys25-->Ser mutant of human cathepsin S."
Turkenburg J.P., Lamers M.B., Brzozowski A.M., Wright L.M., Hubbard R.E., Sturt S.L., Williams D.H.
Acta Crystallogr. D 58:451-455(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 115-331.
[13]"Characterization and optimization of selective, nonpeptidic inhibitors of cathepsin S with an unprecedented binding mode."
Inagaki H., Tsuruoka H., Hornsby M., Lesley S.A., Spraggon G., Ellman J.A.
J. Med. Chem. 50:2693-2699(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 112-331 IN COMPLEX WITH INHIBITOR, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S93414 mRNA. Translation: AAB22005.1.
M86553 mRNA. Translation: AAA35655.1.
M90696 mRNA. Translation: AAC37592.1.
U07374 expand/collapse EMBL AC list , U07370, U07371, U07372, U07373 Genomic DNA. Translation: AAB60643.2.
CR541676 mRNA. Translation: CAG46477.1.
AK301472 mRNA. Translation: BAG62991.1.
AK314482 mRNA. Translation: BAG37086.1.
AL356292 Genomic DNA. Translation: CAI13657.1.
CH471121 Genomic DNA. Translation: EAW53518.1.
CH471121 Genomic DNA. Translation: EAW53519.1.
BC002642 mRNA. Translation: AAH02642.1.
PIRA42482.
RefSeqNP_001186668.1. NM_001199739.1.
NP_004070.3. NM_004079.4.
UniGeneHs.181301.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BXFmodel-A115-331[»]
1GLOX-ray2.20A115-331[»]
1MS6X-ray1.90A115-331[»]
1NPZX-ray2.00A/B115-331[»]
1NQCX-ray1.80A115-331[»]
2C0YX-ray2.10A17-331[»]
2F1GX-ray1.90A/B112-331[»]
2FQ9X-ray1.65A/B114-331[»]
2FRAX-ray1.90A/B114-330[»]
2FRQX-ray1.60A/B115-331[»]
2FT2X-ray1.70A/B114-331[»]
2FUDX-ray1.95A/B115-331[»]
2FYEX-ray2.20A115-331[»]
2G6DX-ray2.50A115-331[»]
2G7YX-ray2.00A/B114-330[»]
2H7JX-ray1.50A/B112-331[»]
2HH5X-ray1.80A/B112-331[»]
2HHNX-ray1.55A/B112-331[»]
2HXZX-ray1.90A/B/C112-331[»]
2OP3X-ray1.60A/B112-331[»]
2R9MX-ray1.97A/B115-331[»]
2R9NX-ray2.00A/B115-331[»]
2R9OX-ray2.00A/B115-331[»]
3IEJX-ray2.18A/B115-331[»]
3KWNX-ray2.10A/B115-331[»]
3MPEX-ray2.25A/B114-331[»]
3MPFX-ray1.80A/B115-331[»]
3N3GX-ray1.60A/B115-331[»]
3N4CX-ray1.90A/B115-331[»]
3OVXX-ray1.49A/B114-331[»]
ProteinModelPortalP25774.
SMRP25774. Positions 18-331.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107900. 2 interactions.
IntActP25774. 2 interactions.
STRING9606.ENSP00000357981.

Chemistry

BindingDBP25774.
ChEMBLCHEMBL2954.
GuidetoPHARMACOLOGY2353.

Protein family/group databases

MEROPSC01.034.

PTM databases

PhosphoSiteP25774.

Polymorphism databases

DMDM88984046.

Proteomic databases

PaxDbP25774.
PeptideAtlasP25774.
PRIDEP25774.

Protocols and materials databases

DNASU1520.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368985; ENSP00000357981; ENSG00000163131. [P25774-1]
ENST00000448301; ENSP00000408414; ENSG00000163131. [P25774-2]
GeneID1520.
KEGGhsa:1520.
UCSCuc001evn.3. human. [P25774-1]
uc010pcj.2. human. [P25774-2]

Organism-specific databases

CTD1520.
GeneCardsGC01M150702.
HGNCHGNC:2545. CTSS.
HPACAB000460.
HPA002988.
MIM116845. gene.
neXtProtNX_P25774.
PharmGKBPA27041.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4870.
HOGENOMHOG000230774.
HOVERGENHBG011513.
InParanoidP25774.
KOK01368.
OMAKAMDQKC.
OrthoDBEOG786H3P.
PhylomeDBP25774.
TreeFamTF313739.

Enzyme and pathway databases

BRENDA3.4.22.27. 2681.
ReactomeREACT_118779. Extracellular matrix organization.
REACT_6900. Immune System.

Gene expression databases

BgeeP25774.
CleanExHS_CTSS.
GenevestigatorP25774.

Family and domain databases

InterProIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERPTHR12411. PTHR12411. 1 hit.
PfamPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSPR00705. PAPAIN.
SMARTSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCTSS. human.
EvolutionaryTraceP25774.
GeneWikiCathepsin_S.
GenomeRNAi1520.
NextBio6291.
PMAP-CutDBP25774.
PROP25774.
SOURCESearch...

Entry information

Entry nameCATS_HUMAN
AccessionPrimary (citable) accession number: P25774
Secondary accession number(s): B4DWC9 expand/collapse secondary AC list , D3DV05, Q5T5I0, Q6FHS5, Q9BUG3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: February 21, 2006
Last modified: April 16, 2014
This is version 151 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM