SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P09668

- CATH_HUMAN

UniProt

P09668 - CATH_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Pro-cathepsin H

Gene
CTSH, CPSB
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei141 – 1411 By similarity
Active sitei281 – 2811 By similarity
Active sitei301 – 3011 By similarity

GO - Molecular functioni

  1. aminopeptidase activity Source: UniProtKB
  2. cysteine-type endopeptidase activator activity involved in apoptotic process Source: UniProtKB
  3. cysteine-type endopeptidase activity Source: UniProtKB
  4. cysteine-type peptidase activity Source: UniProtKB
  5. endopeptidase activity Source: UniProtKB
  6. HLA-A specific activating MHC class I receptor activity Source: UniProtKB
  7. peptidase activity Source: UniProtKB
  8. protein binding Source: UniProtKB
  9. serine-type endopeptidase activity Source: UniProtKB
  10. thyroid hormone binding Source: UniProtKB

GO - Biological processi

  1. adaptive immune response Source: UniProtKB
  2. antigen processing and presentation Source: UniProtKB
  3. bradykinin catabolic process Source: UniProtKB
  4. cellular response to thyroid hormone stimulus Source: UniProtKB
  5. dichotomous subdivision of terminal units involved in lung branching Source: UniProtKB
  6. ERK1 and ERK2 cascade Source: UniProtKB
  7. immune response-regulating signaling pathway Source: UniProtKB
  8. membrane protein proteolysis Source: UniProtKB
  9. metanephros development Source: UniProtKB
  10. negative regulation of apoptotic process Source: UniProtKB
  11. neuropeptide catabolic process Source: UniProtKB
  12. positive regulation of angiogenesis Source: UniProtKB
  13. positive regulation of apoptotic signaling pathway Source: Ensembl
  14. positive regulation of cell migration Source: UniProtKB
  15. positive regulation of cell proliferation Source: UniProtKB
  16. positive regulation of epithelial cell migration Source: UniProtKB
  17. positive regulation of gene expression Source: UniProtKB
  18. positive regulation of peptidase activity Source: UniProtKB
  19. protein destabilization Source: UniProtKB
  20. proteolysis Source: UniProtKB
  21. response to retinoic acid Source: UniProtKB
  22. spermatogenesis Source: Ensembl
  23. surfactant homeostasis Source: UniProtKB
  24. T cell mediated cytotoxicity Source: UniProtKB
  25. zymogen activation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

BRENDAi3.4.22.16. 2681.
ReactomeiREACT_121399. MHC class II antigen presentation.
SABIO-RKP09668.

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
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:2535. CTSH.

Subcellular locationi

GO - Cellular componenti

  1. acrosomal vesicle Source: Ensembl
  2. alveolar lamellar body Source: UniProtKB
  3. cytosol Source: UniProtKB
  4. extracellular space Source: UniProtKB
  5. extracellular vesicular exosome Source: UniProt
  6. lysosome Source: UniProtKB
  7. outer dense fiber Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Organism-specific databases

Orphaneti2073. Narcolepsy-cataplexy.
PharmGKBiPA27033.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Add
BLAST
Propeptidei23 – 9775Activation peptidePRO_0000026206Add
BLAST
Peptidei98 – 1058Cathepsin H mini chain1 PublicationPRO_0000026207
Propeptidei106 – 11510PRO_0000026208
Chaini116 – 335220Cathepsin HPRO_0000026209Add
BLAST
Chaini116 – 292177Cathepsin H heavy chainPRO_0000026210Add
BLAST
Chaini293 – 33543Cathepsin H light chainPRO_0000026211Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi101 – 1011N-linked (GlcNAc...)1 Publication
Disulfide bondi102 ↔ 327 By similarity
Disulfide bondi138 ↔ 181 By similarity
Disulfide bondi172 ↔ 214 By similarity
Glycosylationi230 – 2301N-linked (GlcNAc...)2 Publications
Disulfide bondi272 ↔ 322 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiP09668.
PaxDbiP09668.
PRIDEiP09668.

PTM databases

PhosphoSiteiP09668.

Expressioni

Gene expression databases

ArrayExpressiP09668.
BgeeiP09668.
CleanExiHS_CTSH.
GenevestigatoriP09668.

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. 4 interactions.
IntActiP09668. 1 interaction.
STRINGi9606.ENSP00000220166.

Structurei

Secondary structure

1
335
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi123 – 1264
Helixi141 – 15818
Helixi166 – 1727
Helixi180 – 1823
Turni186 – 1883
Helixi189 – 1968
Turni202 – 2043
Helixi237 – 2459
Beta strandi249 – 2524
Helixi258 – 2614
Beta strandi273 – 2753
Beta strandi283 – 2919
Beta strandi294 – 3007
Turni304 – 3107
Beta strandi326 – 3294

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BZNmodel-B116-335[»]
ProteinModelPortaliP09668.
SMRiP09668. Positions 34-335.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4870.
HOGENOMiHOG000230774.
HOVERGENiHBG011513.
InParanoidiP09668.
KOiK01366.
OMAiHKYLWSE.
OrthoDBiEOG70KGPX.
PhylomeDBiP09668.
TreeFamiTF328985.

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]

Sequencei

Sequence statusi: Complete.

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

P09668-1 [UniParc]FASTAAdd to Basket

« Hide

MWATLPLLCA GAWLLGVPVC GAAELCVNSL EKFHFKSWMS KHRKTYSTEE    50
YHHRLQTFAS NWRKINAHNN GNHTFKMALN QFSDMSFAEI KHKYLWSEPQ 100
NCSATKSNYL RGTGPYPPSV DWRKKGNFVS PVKNQGACGS CWTFSTTGAL 150
ESAIAIATGK MLSLAEQQLV DCAQDFNNHG CQGGLPSQAF EYILYNKGIM 200
GEDTYPYQGK DGYCKFQPGK AIGFVKDVAN ITIYDEEAMV EAVALYNPVS 250
FAFEVTQDFM MYRTGIYSST SCHKTPDKVN HAVLAVGYGE KNGIPYWIVK 300
NSWGPQWGMN GYFLIERGKN MCGLAACASY PIPLV 335
Length:335
Mass (Da):37,394
Last modified:February 9, 2010 - v4
Checksum:iE2CF3A5EEA59C1D1
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti11 – 111G → R.
Corresponds to variant rs2289702 [ dbSNP | Ensembl ].
VAR_057038
Natural varianti23 – 231A → T.
Corresponds to variant rs35001431 [ dbSNP | Ensembl ].
VAR_057039
Natural varianti26 – 261C → S.3 Publications
Corresponds to variant rs1036938 [ dbSNP | Ensembl ].
VAR_060368
Natural varianti126 – 1261G → R in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036478
Natural varianti179 – 1791H → Y.3 Publications
Corresponds to variant rs1130856 [ dbSNP | Ensembl ].
VAR_067717

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti306 – 3061Q → E AA sequence 1 Publication
Sequence conflicti306 – 3061Q → E AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_004390.3.
UniGeneiHs.148641.

Genome annotation databases

EnsembliENST00000220166; ENSP00000220166; ENSG00000103811.
GeneIDi1512.
KEGGihsa:1512.
UCSCiuc021srk.1. human.

Polymorphism databases

DMDMi288558851.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS10308.1.
PIRi S12486. KHHUH.
RefSeqi NP_004381.2. NM_004390.3.
UniGenei Hs.148641.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BZN model - B 116-335 [» ]
ProteinModelPortali P09668.
SMRi P09668. Positions 34-335.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107892. 4 interactions.
IntActi P09668. 1 interaction.
STRINGi 9606.ENSP00000220166.

Chemistry

ChEMBLi CHEMBL2111441.

Protein family/group databases

MEROPSi C01.040.

PTM databases

PhosphoSitei P09668.

Polymorphism databases

DMDMi 288558851.

Proteomic databases

MaxQBi P09668.
PaxDbi P09668.
PRIDEi P09668.

Protocols and materials databases

DNASUi 1512.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000220166 ; ENSP00000220166 ; ENSG00000103811 .
GeneIDi 1512.
KEGGi hsa:1512.
UCSCi uc021srk.1. human.

Organism-specific databases

CTDi 1512.
GeneCardsi GC15M079213.
H-InvDB HIX0012481.
HGNCi HGNC:2535. CTSH.
HPAi CAB000458.
HPA003524.
MIMi 116820. gene.
neXtProti NX_P09668.
Orphaneti 2073. Narcolepsy-cataplexy.
PharmGKBi PA27033.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG4870.
HOGENOMi HOG000230774.
HOVERGENi HBG011513.
InParanoidi P09668.
KOi K01366.
OMAi HKYLWSE.
OrthoDBi EOG70KGPX.
PhylomeDBi P09668.
TreeFami TF328985.

Enzyme and pathway databases

BRENDAi 3.4.22.16. 2681.
Reactomei REACT_121399. MHC class II antigen presentation.
SABIO-RK P09668.

Miscellaneous databases

GeneWikii Cathepsin_H.
GenomeRNAii 1512.
NextBioi 6261.
PROi P09668.
SOURCEi Search...

Gene expression databases

ArrayExpressi P09668.
Bgeei P09668.
CleanExi HS_CTSH.
Genevestigatori P09668.

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. "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.
    , 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.
    , 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-126.

Entry informationi

Entry nameiCATH_HUMAN
AccessioniPrimary (citable) accession number: P09668
Secondary accession number(s): B2RBK0, Q96NY6, Q9BUM7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: February 9, 2010
Last modified: September 3, 2014
This is version 159 of the entry and version 4 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: 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

Similar proteinsi