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P09668 (CATH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 155. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pro-cathepsin H
Gene names
Name:CTSH
Synonyms:CPSB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length335 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Important for the overall degradation of proteins in lysosomes.

Catalytic activity

Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-|-Xaa bonds) as well as an endopeptidase.

Subunit structure

Composed of a mini chain and a large chain. The large chain may be split into heavy and light chain. All chains are held together by disulfide bonds.

Subcellular location

Lysosome.

Sequence similarities

Belongs to the peptidase C1 family.

Ontologies

Keywords
   Cellular componentLysosome
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionHydrolase
Protease
Thiol protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processERK1 and ERK2 cascade

Inferred from direct assay PubMed 21217776. Source: UniProtKB

T cell mediated cytotoxicity

Inferred from sequence or structural similarity. Source: UniProtKB

adaptive immune response

Inferred from expression pattern PubMed 15196205. Source: UniProtKB

antigen processing and presentation

Traceable author statement PubMed 15196205. Source: UniProtKB

bradykinin catabolic process

Inferred from direct assay PubMed 15127951. Source: UniProtKB

cellular response to thyroid hormone stimulus

Inferred from expression pattern PubMed 21217776. Source: UniProtKB

dichotomous subdivision of terminal units involved in lung branching

Inferred from sequence or structural similarity. Source: UniProtKB

immune response-regulating signaling pathway

Inferred from direct assay PubMed 16822283. Source: UniProtKB

membrane protein proteolysis

Inferred from direct assay PubMed 14766755. Source: UniProtKB

metanephros development

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

neuropeptide catabolic process

Inferred from direct assay PubMed 15127951. Source: UniProtKB

positive regulation of angiogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell migration

Inferred from direct assay PubMed 21217776. Source: UniProtKB

positive regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of epithelial cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of gene expression

Inferred from direct assay PubMed 21217776. Source: UniProtKB

positive regulation of peptidase activity

Inferred from direct assay PubMed 20435891. Source: UniProtKB

protein destabilization

Inferred from mutant phenotype PubMed 17500053. Source: UniProtKB

proteolysis

Inferred from direct assay PubMed 8811434. Source: UniProtKB

response to retinoic acid

Inferred from sequence or structural similarity. Source: UniProtKB

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

surfactant homeostasis

Inferred from direct assay PubMed 18216060. Source: UniProtKB

zymogen activation

Inferred from direct assay PubMed 20435891. Source: UniProtKB

   Cellular_componentacrosomal vesicle

Inferred from electronic annotation. Source: Ensembl

alveolar lamellar body

Inferred from direct assay PubMed 18216060. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 9050938. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 18216060PubMed 21217776PubMed 9050938. Source: UniProtKB

lysosome

Inferred from direct assay PubMed 15196205PubMed 16822283PubMed 1837142. Source: UniProtKB

outer dense fiber

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionHLA-A specific activating MHC class I receptor activity

Inferred from direct assay PubMed 16822283. Source: UniProtKB

aminopeptidase activity

Inferred from direct assay PubMed 15127951. Source: UniProtKB

cysteine-type endopeptidase activator activity involved in apoptotic process

Inferred from direct assay PubMed 20435891. Source: UniProtKB

cysteine-type endopeptidase activity

Traceable author statement Ref.6. Source: UniProtKB

cysteine-type peptidase activity

Inferred from direct assay PubMed 8811434. Source: UniProtKB

endopeptidase activity

Inferred from direct assay PubMed 14766755PubMed 15127951. Source: UniProtKB

peptidase activity

Inferred from direct assay PubMed 18216060. Source: UniProtKB

serine-type endopeptidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

thyroid hormone binding

Inferred from direct assay PubMed 21217776. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222
Propeptide23 – 9775Activation peptide
PRO_0000026206
Peptide98 – 1058Cathepsin H mini chain Ref.7
PRO_0000026207
Propeptide106 – 11510
PRO_0000026208
Chain116 – 335220Cathepsin H
PRO_0000026209
Chain116 – 292177Cathepsin H heavy chain
PRO_0000026210
Chain293 – 33543Cathepsin H light chain
PRO_0000026211

Sites

Active site1411 By similarity
Active site2811 By similarity
Active site3011 By similarity

Amino acid modifications

Glycosylation1011N-linked (GlcNAc...) Ref.7
Glycosylation2301N-linked (GlcNAc...) Ref.7 Ref.9
Disulfide bond102 ↔ 327 By similarity
Disulfide bond138 ↔ 181 By similarity
Disulfide bond172 ↔ 214 By similarity
Disulfide bond272 ↔ 322 By similarity

Natural variations

Natural variant111G → R.
Corresponds to variant rs2289702 [ dbSNP | Ensembl ].
VAR_057038
Natural variant231A → T.
Corresponds to variant rs35001431 [ dbSNP | Ensembl ].
VAR_057039
Natural variant261C → S. Ref.1 Ref.3 Ref.5
Corresponds to variant rs1036938 [ dbSNP | Ensembl ].
VAR_060368
Natural variant1261G → R in a colorectal cancer sample; somatic mutation. Ref.11
VAR_036478
Natural variant1791H → Y. Ref.1 Ref.2 Ref.6
Corresponds to variant rs1130856 [ dbSNP | Ensembl ].
VAR_067717

Experimental info

Sequence conflict3061Q → E AA sequence Ref.7
Sequence conflict3061Q → E AA sequence Ref.8

Secondary structure

.............................. 335
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09668 [UniParc].

Last modified February 9, 2010. Version 4.
Checksum: E2CF3A5EEA59C1D1

FASTA33537,394
        10         20         30         40         50         60 
MWATLPLLCA GAWLLGVPVC GAAELCVNSL EKFHFKSWMS KHRKTYSTEE YHHRLQTFAS 

        70         80         90        100        110        120 
NWRKINAHNN GNHTFKMALN QFSDMSFAEI KHKYLWSEPQ NCSATKSNYL RGTGPYPPSV 

       130        140        150        160        170        180 
DWRKKGNFVS PVKNQGACGS CWTFSTTGAL ESAIAIATGK MLSLAEQQLV DCAQDFNNHG 

       190        200        210        220        230        240 
CQGGLPSQAF EYILYNKGIM GEDTYPYQGK DGYCKFQPGK AIGFVKDVAN ITIYDEEAMV 

       250        260        270        280        290        300 
EAVALYNPVS FAFEVTQDFM MYRTGIYSST SCHKTPDKVN HAVLAVGYGE KNGIPYWIVK 

       310        320        330 
NSWGPQWGMN GYFLIERGKN MCGLAACASY PIPLV 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of human preprocathepsin H, a lysosomal cysteine proteinase."
Fuchs R., Gassen H.G.
Nucleic Acids Res. 17:9471-9471(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS SER-26 AND TYR-179.
Tissue: Liver.
[2]"Analysis of a truncated form of cathepsin H in human prostate tumor cells."
Waghray A., Keppler D., Sloane B.F., Schuger L., Chen Y.Q.
J. Biol. Chem. 277:11533-11538(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT TYR-179.
[3]"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], VARIANT SER-26.
Tissue: Lung.
[4]"Analysis of the DNA sequence and duplication history of human chromosome 15."
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. expand/collapse author list , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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], VARIANT SER-26.
Tissue: Eye.
[6]"Molecular cloning and sequencing of a cDNA coding for mature human kidney cathepsin H."
Fuchs R., Machleidt W., Gassen H.G.
Biol. Chem. Hoppe-Seyler 369:469-475(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 88-335, VARIANT TYR-179.
Tissue: Kidney.
[7]"Amino acid sequences of the human kidney cathepsins H and L."
Ritonja A., Popovic T., Kotnik M., Machleidt W., Turk V.
FEBS Lett. 228:341-345(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 98-105 AND 114-335, GLYCOSYLATION AT ASN-101 AND ASN-230.
Tissue: Kidney.
[8]"Human cathepsins B, H and L: characterization by amino acid sequences and some kinetics of inhibition by the kininogens."
Machleidt W., Ritonja A., Popovic T., Kotnik M., Brzin J., Turk V., Machleidt I., Mueller-Esterl W.
(In) Turk V. (eds.); Cysteine proteinases and their inhibitors, pp.3-18, Walter de Gruyter, Berlin and New York (1986)
Cited for: PROTEIN SEQUENCE OF 99-105; 116-159 AND 294-335.
[9]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-230.
Tissue: Liver.
[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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-126.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X16832 mRNA. Translation: CAA34734.1.
AF426247 mRNA. Translation: AAL23961.1.
AK314698 mRNA. Translation: BAG37247.1.
AC011944 Genomic DNA. No translation available.
BC002479 mRNA. Translation: AAH02479.1.
X07549 mRNA. Translation: CAA30428.1.
X07549 mRNA. Translation: CAA30429.1.
PIRKHHUH. S12486.
RefSeqNP_004381.2. NM_004390.3.
UniGeneHs.148641.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BZNmodel-B116-335[»]
ProteinModelPortalP09668.
SMRP09668. Positions 34-335.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107892. 4 interactions.
IntActP09668. 1 interaction.
STRING9606.ENSP00000220166.

Chemistry

ChEMBLCHEMBL2111441.

Protein family/group databases

MEROPSC01.040.

PTM databases

PhosphoSiteP09668.

Polymorphism databases

DMDM288558851.

Proteomic databases

PaxDbP09668.
PRIDEP09668.

Protocols and materials databases

DNASU1512.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000220166; ENSP00000220166; ENSG00000103811.
GeneID1512.
KEGGhsa:1512.
UCSCuc021srk.1. human.

Organism-specific databases

CTD1512.
GeneCardsGC15M079213.
H-InvDBHIX0012481.
HGNCHGNC:2535. CTSH.
HPACAB000458.
HPA003524.
MIM116820. gene.
neXtProtNX_P09668.
Orphanet2073. Narcolepsy-cataplexy.
PharmGKBPA27033.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4870.
HOGENOMHOG000230774.
HOVERGENHBG011513.
InParanoidP09668.
KOK01366.
OMASTSCHKT.
OrthoDBEOG70KGPX.
PhylomeDBP09668.
TreeFamTF328985.

Enzyme and pathway databases

BRENDA3.4.22.16. 2681.
ReactomeREACT_6900. Immune System.
SABIO-RKP09668.

Gene expression databases

ArrayExpressP09668.
BgeeP09668.
CleanExHS_CTSH.
GenevestigatorP09668.

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

GeneWikiCathepsin_H.
GenomeRNAi1512.
NextBio6261.
PROP09668.
SOURCESearch...

Entry information

Entry nameCATH_HUMAN
AccessionPrimary (citable) accession number: P09668
Secondary accession number(s): B2RBK0, Q96NY6, Q9BUM7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: February 9, 2010
Last modified: April 16, 2014
This is version 155 of the entry and version 4 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 15

Human chromosome 15: entries, gene names and cross-references to MIM