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P25774

- CATS_HUMAN

UniProt

P25774 - CATS_HUMAN

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

Functioni

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 activityi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei139 – 1391 By similarity
Active sitei278 – 2781 By similarity
Active sitei298 – 2981 By similarity

GO - Molecular functioni

  1. collagen binding Source: BHF-UCL
  2. cysteine-type endopeptidase activity Source: BHF-UCL
  3. fibronectin binding Source: BHF-UCL
  4. laminin binding Source: BHF-UCL
  5. proteoglycan binding Source: BHF-UCL
Complete GO annotation...

GO - Biological processi

  1. adaptive immune response Source: UniProtKB
  2. antigen processing and presentation Source: UniProtKB
  3. antigen processing and presentation of exogenous peptide antigen via MHC class I Source: Reactome
  4. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent Source: Reactome
  5. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
  6. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
  7. basement membrane disassembly Source: BHF-UCL
  8. cellular response to thyroid hormone stimulus Source: UniProtKB
  9. collagen catabolic process Source: BHF-UCL
  10. extracellular matrix disassembly Source: Reactome
  11. extracellular matrix organization Source: Reactome
  12. immune response Source: ProtInc
  13. innate immune response Source: Reactome
  14. proteolysis Source: ProtInc
  15. proteolysis involved in cellular protein catabolic process Source: BHF-UCL
  16. toll-like receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

BRENDAi3.4.22.27. 2681.
ReactomeiREACT_111168. Endosomal/Vacuolar pathway.
REACT_118572. Degradation of the extracellular matrix.
REACT_118632. Trafficking and processing of endosomal TLR.
REACT_121399. MHC class II antigen presentation.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.

Protein family/group databases

MEROPSiC01.034.

Names & Taxonomyi

Protein namesi
Recommended name:
Cathepsin S (EC:3.4.22.27)
Gene namesi
Name:CTSS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:2545. CTSS.

Subcellular locationi

GO - Cellular componenti

  1. endolysosome lumen Source: Reactome
  2. extracellular region Source: UniProtKB
  3. extracellular space Source: BHF-UCL
  4. intracellular membrane-bounded organelle Source: HPA
  5. lysosomal lumen Source: Reactome
  6. lysosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27041.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616 Reviewed prediction
Add
BLAST
Propeptidei17 – 11498Activation peptide
PRO_0000026313Add
BLAST
Chaini115 – 331217Cathepsin S
PRO_0000026314Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi104 – 1041N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi126 ↔ 2241 Publication
Disulfide bondi136 ↔ 1801 Publication
Disulfide bondi170 ↔ 2131 Publication
Disulfide bondi272 ↔ 3201 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiP25774.
PaxDbiP25774.
PeptideAtlasiP25774.
PRIDEiP25774.

PTM databases

PhosphoSiteiP25774.

Miscellaneous databases

PMAP-CutDBP25774.

Expressioni

Gene expression databases

BgeeiP25774.
CleanExiHS_CTSS.
GenevestigatoriP25774.

Organism-specific databases

HPAiCAB000460.
HPA002988.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi107900. 2 interactions.
IntActiP25774. 2 interactions.
STRINGi9606.ENSP00000357981.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi22 – 243
Helixi25 – 3511
Helixi44 – 6724
Beta strandi72 – 754
Helixi79 – 824
Helixi85 – 917
Helixi100 – 1023
Helixi121 – 1244
Beta strandi135 – 1373
Helixi139 – 15618
Helixi164 – 1707
Helixi173 – 1753
Helixi179 – 1813
Helixi185 – 19511
Beta strandi198 – 2003
Turni201 – 2033
Helixi217 – 2193
Beta strandi220 – 2223
Beta strandi226 – 2294
Helixi235 – 24410
Beta strandi248 – 2525
Helixi257 – 2615
Beta strandi264 – 2674
Beta strandi278 – 28811
Beta strandi291 – 2977
Turni301 – 3033
Beta strandi309 – 3135
Beta strandi315 – 3184
Helixi319 – 3213
Turni322 – 3243
Beta strandi327 – 3304

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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/B114-331[»]
2FT2X-ray1.70A/B114-331[»]
2FUDX-ray1.95A/B114-331[»]
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[»]
ProteinModelPortaliP25774.
SMRiP25774. Positions 18-331.

Miscellaneous databases

EvolutionaryTraceiP25774.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4870.
HOGENOMiHOG000230774.
HOVERGENiHBG011513.
InParanoidiP25774.
KOiK01368.
OMAiMERTRVP.
OrthoDBiEOG786H3P.
PhylomeDBiP25774.
TreeFamiTF313739.

Family and domain databases

InterProiIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PfamiPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P25774-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MKRLVCVLLV CSSAVAQLHK DPTLDHHWHL WKKTYGKQYK EKNEEAVRRL    50
IWEKNLKFVM LHNLEHSMGM HSYDLGMNHL GDMTSEEVMS LMSSLRVPSQ 100
WQRNITYKSN PNRILPDSVD WREKGCVTEV KYQGSCGACW AFSAVGALEA 150
QLKLKTGKLV SLSAQNLVDC STEKYGNKGC NGGFMTTAFQ YIIDNKGIDS 200
DASYPYKAMD QKCQYDSKYR AATCSKYTEL PYGREDVLKE AVANKGPVSV 250
GVDARHPSFF LYRSGVYYEP SCTQNVNHGV LVVGYGDLNG KEYWLVKNSW 300
GHNFGEEGYI RMARNKGNHC GIASFPSYPE I 331
Length:331
Mass (Da):37,496
Last modified:February 21, 2006 - v3
Checksum:i86093619DB6F0269
GO
Isoform 2 (identifier: P25774-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     84-133: Missing.

Note: No experimental confirmation available.

Show »
Length:281
Mass (Da):31,626
Checksum:iC0445894FAD89713
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti113 – 1131R → W.3 Publications
Corresponds to variant rs2230061 [ dbSNP | Ensembl ].
VAR_025385
Natural varianti161 – 1611S → T.2 Publications
Corresponds to variant rs1059604 [ dbSNP | Ensembl ].
VAR_025386

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei84 – 13350Missing in isoform 2.
VSP_042712Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti92 – 921M → T1 Publication
Sequence conflicti92 – 921M → T1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S93414 mRNA. Translation: AAB22005.1.
M86553 mRNA. Translation: AAA35655.1.
M90696 mRNA. Translation: AAC37592.1.
U07374
, 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.
CCDSiCCDS55634.1. [P25774-2]
CCDS968.1. [P25774-1]
PIRiA42482.
RefSeqiNP_001186668.1. NM_001199739.1. [P25774-2]
NP_004070.3. NM_004079.4. [P25774-1]
UniGeneiHs.181301.

Genome annotation databases

EnsembliENST00000368985; ENSP00000357981; ENSG00000163131. [P25774-1]
ENST00000448301; ENSP00000408414; ENSG00000163131. [P25774-2]
GeneIDi1520.
KEGGihsa:1520.
UCSCiuc001evn.3. human. [P25774-1]
uc010pcj.2. human. [P25774-2]

Polymorphism databases

DMDMi88984046.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S93414 mRNA. Translation: AAB22005.1 .
M86553 mRNA. Translation: AAA35655.1 .
M90696 mRNA. Translation: AAC37592.1 .
U07374
, 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 .
CCDSi CCDS55634.1. [P25774-2 ]
CCDS968.1. [P25774-1 ]
PIRi A42482.
RefSeqi NP_001186668.1. NM_001199739.1. [P25774-2 ]
NP_004070.3. NM_004079.4. [P25774-1 ]
UniGenei Hs.181301.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BXF model - A 115-331 [» ]
1GLO X-ray 2.20 A 115-331 [» ]
1MS6 X-ray 1.90 A 115-331 [» ]
1NPZ X-ray 2.00 A/B 115-331 [» ]
1NQC X-ray 1.80 A 115-331 [» ]
2C0Y X-ray 2.10 A 17-331 [» ]
2F1G X-ray 1.90 A/B 112-331 [» ]
2FQ9 X-ray 1.65 A/B 114-331 [» ]
2FRA X-ray 1.90 A/B 114-330 [» ]
2FRQ X-ray 1.60 A/B 114-331 [» ]
2FT2 X-ray 1.70 A/B 114-331 [» ]
2FUD X-ray 1.95 A/B 114-331 [» ]
2FYE X-ray 2.20 A 115-331 [» ]
2G6D X-ray 2.50 A 115-331 [» ]
2G7Y X-ray 2.00 A/B 114-330 [» ]
2H7J X-ray 1.50 A/B 112-331 [» ]
2HH5 X-ray 1.80 A/B 112-331 [» ]
2HHN X-ray 1.55 A/B 112-331 [» ]
2HXZ X-ray 1.90 A/B/C 112-331 [» ]
2OP3 X-ray 1.60 A/B 112-331 [» ]
2R9M X-ray 1.97 A/B 115-331 [» ]
2R9N X-ray 2.00 A/B 115-331 [» ]
2R9O X-ray 2.00 A/B 115-331 [» ]
3IEJ X-ray 2.18 A/B 115-331 [» ]
3KWN X-ray 2.10 A/B 115-331 [» ]
3MPE X-ray 2.25 A/B 114-331 [» ]
3MPF X-ray 1.80 A/B 115-331 [» ]
3N3G X-ray 1.60 A/B 115-331 [» ]
3N4C X-ray 1.90 A/B 115-331 [» ]
3OVX X-ray 1.49 A/B 114-331 [» ]
ProteinModelPortali P25774.
SMRi P25774. Positions 18-331.
ModBasei Search...

Protein-protein interaction databases

BioGridi 107900. 2 interactions.
IntActi P25774. 2 interactions.
STRINGi 9606.ENSP00000357981.

Chemistry

BindingDBi P25774.
ChEMBLi CHEMBL2954.
GuidetoPHARMACOLOGYi 2353.

Protein family/group databases

MEROPSi C01.034.

PTM databases

PhosphoSitei P25774.

Polymorphism databases

DMDMi 88984046.

Proteomic databases

MaxQBi P25774.
PaxDbi P25774.
PeptideAtlasi P25774.
PRIDEi P25774.

Protocols and materials databases

DNASUi 1520.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000368985 ; ENSP00000357981 ; ENSG00000163131 . [P25774-1 ]
ENST00000448301 ; ENSP00000408414 ; ENSG00000163131 . [P25774-2 ]
GeneIDi 1520.
KEGGi hsa:1520.
UCSCi uc001evn.3. human. [P25774-1 ]
uc010pcj.2. human. [P25774-2 ]

Organism-specific databases

CTDi 1520.
GeneCardsi GC01M150702.
HGNCi HGNC:2545. CTSS.
HPAi CAB000460.
HPA002988.
MIMi 116845. gene.
neXtProti NX_P25774.
PharmGKBi PA27041.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG4870.
HOGENOMi HOG000230774.
HOVERGENi HBG011513.
InParanoidi P25774.
KOi K01368.
OMAi MERTRVP.
OrthoDBi EOG786H3P.
PhylomeDBi P25774.
TreeFami TF313739.

Enzyme and pathway databases

BRENDAi 3.4.22.27. 2681.
Reactomei REACT_111168. Endosomal/Vacuolar pathway.
REACT_118572. Degradation of the extracellular matrix.
REACT_118632. Trafficking and processing of endosomal TLR.
REACT_121399. MHC class II antigen presentation.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.

Miscellaneous databases

ChiTaRSi CTSS. human.
EvolutionaryTracei P25774.
GeneWikii Cathepsin_S.
GenomeRNAii 1520.
NextBioi 6291.
PMAP-CutDB P25774.
PROi P25774.
SOURCEi Search...

Gene expression databases

Bgeei P25774.
CleanExi HS_CTSS.
Genevestigatori P25774.

Family and domain databases

InterProi IPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view ]
PANTHERi PTHR12411. PTHR12411. 1 hit.
Pfami PF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view ]
PRINTSi PR00705. PAPAIN.
SMARTi SM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view ]
PROSITEi PS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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. 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.

Entry informationi

Entry nameiCATS_HUMAN
AccessioniPrimary (citable) accession number: P25774
Secondary accession number(s): B4DWC9
, D3DV05, Q5T5I0, Q6FHS5, Q9BUG3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: February 21, 2006
Last modified: September 3, 2014
This is version 155 of the entry and version 3 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, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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

External Data

Dasty 3

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