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Protein

Pro-cathepsin H

Gene

CTSH

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

Functioni

Important for the overall degradation of proteins in lysosomes.

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei141By similarity1
Active sitei281By similarity1
Active sitei301By similarity1

GO - Molecular functioni

  • aminopeptidase activity Source: UniProtKB
  • cysteine-type endopeptidase activator activity involved in apoptotic process Source: UniProtKB
  • cysteine-type endopeptidase activity Source: BHF-UCL
  • cysteine-type peptidase activity Source: UniProtKB
  • endopeptidase activity Source: UniProtKB
  • HLA-A specific activating MHC class I receptor activity Source: UniProtKB
  • peptidase activity Source: UniProtKB
  • serine-type endopeptidase activity Source: UniProtKB
  • thyroid hormone binding Source: UniProtKB

GO - Biological processi

  • adaptive immune response Source: UniProtKB
  • antigen processing and presentation Source: UniProtKB
  • bradykinin catabolic process Source: UniProtKB
  • cellular protein metabolic process Source: Reactome
  • cellular response to thyroid hormone stimulus Source: UniProtKB
  • dichotomous subdivision of terminal units involved in lung branching Source: UniProtKB
  • ERK1 and ERK2 cascade Source: UniProtKB
  • immune response-regulating signaling pathway Source: UniProtKB
  • membrane protein proteolysis Source: UniProtKB
  • metanephros development Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • neuropeptide catabolic process Source: UniProtKB
  • neutrophil degranulation Source: Reactome
  • positive regulation of angiogenesis Source: UniProtKB
  • positive regulation of apoptotic signaling pathway Source: GO_Central
  • positive regulation of cell migration Source: UniProtKB
  • positive regulation of cell proliferation Source: UniProtKB
  • positive regulation of epithelial cell migration Source: UniProtKB
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of peptidase activity Source: UniProtKB
  • protein destabilization Source: UniProtKB
  • proteolysis Source: UniProtKB
  • proteolysis involved in cellular protein catabolic process Source: GO_Central
  • response to retinoic acid Source: UniProtKB
  • surfactant homeostasis Source: UniProtKB
  • T cell mediated cytotoxicity Source: UniProtKB
  • zymogen activation Source: UniProtKB

Keywordsi

Molecular functionHydrolase, Protease, Thiol protease

Enzyme and pathway databases

BRENDAi3.4.22.16 2681
ReactomeiR-HSA-2132295 MHC class II antigen presentation
R-HSA-5683826 Surfactant metabolism
R-HSA-6798695 Neutrophil degranulation
SABIO-RKiP09668

Protein family/group databases

MEROPSiC01.040

Names & Taxonomyi

Protein namesi
Recommended name:
Pro-cathepsin H
Cleaved into the following 4 chains:
Gene namesi
Name:CTSH
Synonyms:CPSB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

EuPathDBiHostDB:ENSG00000103811.15
HGNCiHGNC:2535 CTSH
MIMi116820 gene
neXtProtiNX_P09668

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Organism-specific databases

DisGeNETi1512
MalaCardsiCTSH
OpenTargetsiENSG00000103811
Orphaneti2073 Narcolepsy-cataplexy
PharmGKBiPA27033

Chemistry databases

ChEMBLiCHEMBL2225
DrugBankiDB08526 CARBOBENZYLOXY-(L)-LEUCINYL-(L)LEUCINYL METHOXYMETHYLKETONE
DB04126 N-[1-Hydroxycarboxyethyl-Carbonyl]Leucylamino-2-Methyl-Butane
DB02140 N1-(1-Dimethylcarbamoyl-2-Phenyl-Ethyl)-2-Oxo-N4-(2-Pyridin-2-Yl-Ethyl)-Succinamide
DB03120 Para-Toluene Sulfonate
GuidetoPHARMACOLOGYi2349

Polymorphism and mutation databases

BioMutaiCTSH
DMDMi288558851

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Add BLAST22
PropeptideiPRO_000002620623 – 97Activation peptide1 PublicationAdd BLAST75
PeptideiPRO_000002620798 – 105Cathepsin H mini chain8
PropeptideiPRO_0000026208106 – 1151 Publication10
ChainiPRO_0000026209116 – 335Cathepsin HAdd BLAST220
ChainiPRO_0000026210116 – 292Cathepsin H heavy chainAdd BLAST177
ChainiPRO_0000026211293 – 335Cathepsin H light chainAdd BLAST43

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi101N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi102 ↔ 327By similarity
Disulfide bondi138 ↔ 181By similarity
Disulfide bondi172 ↔ 214By similarity
Glycosylationi230N-linked (GlcNAc...) asparagine2 Publications1
Disulfide bondi272 ↔ 322By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

EPDiP09668
MaxQBiP09668
PaxDbiP09668
PeptideAtlasiP09668
PRIDEiP09668

PTM databases

iPTMnetiP09668
PhosphoSitePlusiP09668

Expressioni

Gene expression databases

BgeeiENSG00000103811
CleanExiHS_CTSH
ExpressionAtlasiP09668 baseline and differential
GenevisibleiP09668 HS

Organism-specific databases

HPAiCAB000458
HPA003524

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

BioGridi107892, 21 interactors
IntActiP09668, 1 interactor
STRINGi9606.ENSP00000220166

Chemistry databases

BindingDBiP09668

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BZNmodel-B116-335[»]
ProteinModelPortaliP09668
SMRiP09668
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1543 Eukaryota
COG4870 LUCA
GeneTreeiENSGT00900000140823
HOGENOMiHOG000230774
HOVERGENiHBG011513
InParanoidiP09668
KOiK01366
OMAiIMGEDTY
OrthoDBiEOG091G0AKT
PhylomeDBiP09668
TreeFamiTF328985

Family and domain databases

InterProiView protein in InterPro
IPR025661 Pept_asp_AS
IPR000169 Pept_cys_AS
IPR025660 Pept_his_AS
IPR013128 Peptidase_C1A
IPR000668 Peptidase_C1A_C
IPR013201 Prot_inhib_I29
PANTHERiPTHR12411 PTHR12411, 1 hit
PfamiView protein in Pfam
PF08246 Inhibitor_I29, 1 hit
PF00112 Peptidase_C1, 1 hit
PRINTSiPR00705 PAPAIN
SMARTiView protein in SMART
SM00848 Inhibitor_I29, 1 hit
SM00645 Pept_C1, 1 hit
PROSITEiView protein in PROSITE
PS00640 THIOL_PROTEASE_ASN, 1 hit
PS00139 THIOL_PROTEASE_CYS, 1 hit
PS00639 THIOL_PROTEASE_HIS, 1 hit

Sequencei

Sequence statusi: Complete.

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

P09668-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWATLPLLCA GAWLLGVPVC GAAELCVNSL EKFHFKSWMS KHRKTYSTEE
60 70 80 90 100
YHHRLQTFAS NWRKINAHNN GNHTFKMALN QFSDMSFAEI KHKYLWSEPQ
110 120 130 140 150
NCSATKSNYL RGTGPYPPSV DWRKKGNFVS PVKNQGACGS CWTFSTTGAL
160 170 180 190 200
ESAIAIATGK MLSLAEQQLV DCAQDFNNHG CQGGLPSQAF EYILYNKGIM
210 220 230 240 250
GEDTYPYQGK DGYCKFQPGK AIGFVKDVAN ITIYDEEAMV EAVALYNPVS
260 270 280 290 300
FAFEVTQDFM MYRTGIYSST SCHKTPDKVN HAVLAVGYGE KNGIPYWIVK
310 320 330
NSWGPQWGMN GYFLIERGKN MCGLAACASY PIPLV
Length:335
Mass (Da):37,394
Last modified:February 9, 2010 - v4
Checksum:iE2CF3A5EEA59C1D1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti306Q → E AA sequence (PubMed:3342889).Curated1
Sequence conflicti306Q → E AA sequence (Ref. 8) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05703811G → R. Corresponds to variant dbSNP:rs2289702Ensembl.1
Natural variantiVAR_05703923A → T. Corresponds to variant dbSNP:rs35001431Ensembl.1
Natural variantiVAR_06036826C → S3 PublicationsCorresponds to variant dbSNP:rs1036938Ensembl.1
Natural variantiVAR_036478126G → R in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_067717179H → Y3 PublicationsCorresponds to variant dbSNP:rs1130856Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
CCDSiCCDS10308.1
PIRiS12486 KHHUH
RefSeqiNP_004381.2, NM_004390.4
UniGeneiHs.148641

Genome annotation databases

EnsembliENST00000220166; ENSP00000220166; ENSG00000103811
GeneIDi1512
KEGGihsa:1512
UCSCiuc021srk.2 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiCATH_HUMAN
AccessioniPrimary (citable) accession number: P09668
Secondary accession number(s): B2RBK0, Q96NY6, Q9BUM7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: February 9, 2010
Last modified: February 28, 2018
This is version 189 of the entry and version 4 of the sequence. See 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, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health