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Q9UBR2

- CATZ_HUMAN

UniProt

Q9UBR2 - CATZ_HUMAN

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

Functioni

Exhibits carboxy-monopeptidase as well as carboxy-dipeptidase activity.

Catalytic activityi

Release of C-terminal amino acid residues with broad specificity, but lacks action on C-terminal proline. Shows weak endopeptidase activity.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei92 – 921
Active sitei241 – 2411
Active sitei261 – 2611

GO - Molecular functioni

  1. cysteine-type peptidase activity Source: ProtInc
Complete GO annotation...

GO - Biological processi

  1. angiotensin maturation Source: Reactome
  2. cellular protein metabolic process Source: Reactome
  3. epithelial tube branching involved in lung morphogenesis Source: Ensembl
  4. proteolysis Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

BRENDAi3.4.18.1. 2681.
ReactomeiREACT_147707. Metabolism of Angiotensinogen to Angiotensins.
REACT_19287. Lysosome Vesicle Biogenesis.

Protein family/group databases

MEROPSiC01.013.

Names & Taxonomyi

Protein namesi
Recommended name:
Cathepsin Z (EC:3.4.18.1)
Alternative name(s):
Cathepsin P
Cathepsin X
Gene namesi
Name:CTSZ
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:2547. CTSZ.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum Source: LIFEdb
  2. extracellular space Source: BHF-UCL
  3. extracellular vesicular exosome Source: UniProt
  4. intracellular membrane-bounded organelle Source: HPA
  5. lysosome Source: UniProtKB-SubCell
  6. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27043.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323 Reviewed prediction
Add
BLAST
Propeptidei24 – 6138Activation peptide
PRO_0000026285Add
BLAST
Chaini62 – 303242Cathepsin Z
PRO_0000026286Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi89 ↔ 132
Disulfide bondi126 ↔ 164
Disulfide bondi154 ↔ 170
Disulfide bondi173 ↔ 179
Glycosylationi184 – 1841N-linked (GlcNAc...)1 Publication
Disulfide bondi214 ↔ 296
Glycosylationi224 – 2241N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiQ9UBR2.
PaxDbiQ9UBR2.
PeptideAtlasiQ9UBR2.
PRIDEiQ9UBR2.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiQ9UBR2.
CleanExiHS_CTSZ.
GenevestigatoriQ9UBR2.

Organism-specific databases

HPAiCAB025114.
HPA049876.

Interactioni

Protein-protein interaction databases

BioGridi107902. 3 interactions.
IntActiQ9UBR2. 1 interaction.
MINTiMINT-3079312.
STRINGi9606.ENSP00000217131.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi40 – 423
Helixi59 – 613
Beta strandi85 – 873
Helixi92 – 10817
Turni109 – 1113
Helixi120 – 1267
Beta strandi127 – 1315
Beta strandi133 – 1353
Helixi137 – 14610
Beta strandi149 – 1513
Helixi152 – 1543
Helixi166 – 1694
Beta strandi170 – 1756
Beta strandi178 – 1814
Beta strandi190 – 1967
Helixi199 – 20911
Beta strandi212 – 2165
Helixi220 – 2234
Beta strandi227 – 2304
Beta strandi241 – 25111
Beta strandi254 – 2607
Beta strandi272 – 2765
Helixi280 – 2834
Helixi285 – 2873
Turni290 – 2934
Beta strandi296 – 3016

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DEUX-ray1.70A/B27-303[»]
1EF7X-ray2.67A/B62-303[»]
ProteinModelPortaliQ9UBR2.
SMRiQ9UBR2. Positions 29-303.

Miscellaneous databases

EvolutionaryTraceiQ9UBR2.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4870.
HOGENOMiHOG000264454.
HOVERGENiHBG004456.
InParanoidiQ9UBR2.
KOiK08568.
OMAiQCGTCTE.
OrthoDBiEOG751NFZ.
PhylomeDBiQ9UBR2.
TreeFamiTF313225.

Family and domain databases

InterProiIPR025661. Pept_asp_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PfamiPF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9UBR2-1 [UniParc]FASTAAdd to Basket

« Hide

MARRGPGWRP LLLLVLLAGA AQGGLYFRRG QTCYRPLRGD GLAPLGRSTY    50
PRPHEYLSPA DLPKSWDWRN VDGVNYASIT RNQHIPQYCG SCWAHASTSA 100
MADRINIKRK GAWPSTLLSV QNVIDCGNAG SCEGGNDLSV WDYAHQHGIP 150
DETCNNYQAK DQECDKFNQC GTCNEFKECH AIRNYTLWRV GDYGSLSGRE 200
KMMAEIYANG PISCGIMATE RLANYTGGIY AEYQDTTYIN HVVSVAGWGI 250
SDGTEYWIVR NSWGEPWGER GWLRIVTSTY KDGKGARYNL AIEEHCTFGD 300
PIV 303
Length:303
Mass (Da):33,868
Last modified:May 1, 2000 - v1
Checksum:i6274FD1974D0EBDC
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti36 – 361P → S.1 Publication
VAR_010254
Natural varianti129 – 1291A → R Requires 2 nucleotide substitutions. 1 Publication
VAR_010255
Natural varianti286 – 2861A → T.
Corresponds to variant rs34069356 [ dbSNP | Ensembl ].
VAR_033719

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 481S → T in AAC39839. 1 Publication
Sequence conflicti150 – 1501P → S in AAC61477. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF073890 mRNA. Translation: AAC61477.1.
AF032906 mRNA. Translation: AAC39839.1.
AF136273 mRNA. Translation: AAF13145.1.
AF136276, AF136274, AF136275 Genomic DNA. Translation: AAF13148.1.
AK314931 mRNA. Translation: BAG37437.1.
AL109840 Genomic DNA. Translation: CAC09370.1.
CH471077 Genomic DNA. Translation: EAW75448.1.
BC042168 mRNA. Translation: AAH42168.1.
AF009923 mRNA. Translation: AAC63141.1.
CCDSiCCDS13474.1.
RefSeqiNP_001327.2. NM_001336.3.
UniGeneiHs.252549.

Genome annotation databases

EnsembliENST00000217131; ENSP00000217131; ENSG00000101160.
GeneIDi1522.
KEGGihsa:1522.
UCSCiuc002yai.2. human.

Polymorphism databases

DMDMi12643324.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF073890 mRNA. Translation: AAC61477.1 .
AF032906 mRNA. Translation: AAC39839.1 .
AF136273 mRNA. Translation: AAF13145.1 .
AF136276 , AF136274 , AF136275 Genomic DNA. Translation: AAF13148.1 .
AK314931 mRNA. Translation: BAG37437.1 .
AL109840 Genomic DNA. Translation: CAC09370.1 .
CH471077 Genomic DNA. Translation: EAW75448.1 .
BC042168 mRNA. Translation: AAH42168.1 .
AF009923 mRNA. Translation: AAC63141.1 .
CCDSi CCDS13474.1.
RefSeqi NP_001327.2. NM_001336.3.
UniGenei Hs.252549.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DEU X-ray 1.70 A/B 27-303 [» ]
1EF7 X-ray 2.67 A/B 62-303 [» ]
ProteinModelPortali Q9UBR2.
SMRi Q9UBR2. Positions 29-303.
ModBasei Search...

Protein-protein interaction databases

BioGridi 107902. 3 interactions.
IntActi Q9UBR2. 1 interaction.
MINTi MINT-3079312.
STRINGi 9606.ENSP00000217131.

Chemistry

BindingDBi Q9UBR2.
ChEMBLi CHEMBL4160.

Protein family/group databases

MEROPSi C01.013.

Polymorphism databases

DMDMi 12643324.

Proteomic databases

MaxQBi Q9UBR2.
PaxDbi Q9UBR2.
PeptideAtlasi Q9UBR2.
PRIDEi Q9UBR2.

Protocols and materials databases

DNASUi 1522.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000217131 ; ENSP00000217131 ; ENSG00000101160 .
GeneIDi 1522.
KEGGi hsa:1522.
UCSCi uc002yai.2. human.

Organism-specific databases

CTDi 1522.
GeneCardsi GC20M057570.
HGNCi HGNC:2547. CTSZ.
HPAi CAB025114.
HPA049876.
MIMi 603169. gene.
neXtProti NX_Q9UBR2.
PharmGKBi PA27043.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG4870.
HOGENOMi HOG000264454.
HOVERGENi HBG004456.
InParanoidi Q9UBR2.
KOi K08568.
OMAi QCGTCTE.
OrthoDBi EOG751NFZ.
PhylomeDBi Q9UBR2.
TreeFami TF313225.

Enzyme and pathway databases

BRENDAi 3.4.18.1. 2681.
Reactomei REACT_147707. Metabolism of Angiotensinogen to Angiotensins.
REACT_19287. Lysosome Vesicle Biogenesis.

Miscellaneous databases

ChiTaRSi CTSZ. human.
EvolutionaryTracei Q9UBR2.
GeneWikii Cathepsin_Z.
GenomeRNAii 1522.
NextBioi 6299.
PROi Q9UBR2.
SOURCEi Search...

Gene expression databases

Bgeei Q9UBR2.
CleanExi HS_CTSZ.
Genevestigatori Q9UBR2.

Family and domain databases

InterProi IPR025661. Pept_asp_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
[Graphical view ]
PANTHERi PTHR12411. PTHR12411. 1 hit.
Pfami PF00112. Peptidase_C1. 1 hit.
[Graphical view ]
PRINTSi PR00705. PAPAIN.
SMARTi SM00645. Pept_C1. 1 hit.
[Graphical view ]
PROSITEi PS00640. THIOL_PROTEASE_ASN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human cathepsin X: a novel cysteine protease of the papain family with a very short proregion and unique insertions."
    Naegler D.K., Menard R.
    FEBS Lett. 434:135-139(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS SER-36 AND ARG-129.
    Tissue: Ovary.
  2. "Cathepsin Z, a novel human cysteine proteinase with a short propeptide domain and a unique chromosomal location."
    Santamaria I., Velasco G., Pendas A.M., Fueyo A., Lopez-Otin C.
    J. Biol. Chem. 273:16816-16823(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Prostate.
  3. "Murine and human cathepsin Z: cDNA-cloning, characterization of the genes and chromosomal localization."
    Deussing J., von Olshausen I., Peters C.
    Biochim. Biophys. Acta 1491:93-106(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Tissue: Blood and Colon tumor.
  4. "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].
    Tissue: Colon.
  5. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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].
    Tissue: Pancreas.
  8. "Identification and molecular cloning of cathepsin P, a novel human putative cysteine protease of the papain family."
    Pungercar J., Ivanovski G.
    Pflugers Arch. 439:R116-R118(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 11-303.
    Tissue: Ileum.
  9. "Human cathepsin X: a cysteine protease with unique carboxypeptidase activity."
    Naegler D.K., Zhang R., Tam W., Sulea T., Purisima E.O., Menard R.
    Biochemistry 38:12648-12654(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, CHARACTERIZATION.
  10. "Tissue expression and immunolocalization of a novel human cathepsin P."
    Pungercar J., Viyjak A., Ivanovski G., Krizaj I.
    Pflugers Arch. 439:R119-R121(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  11. "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-184.
    Tissue: Liver.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Crystal structure of cathepsin X: a flip-flop of the ring of His23 allows carboxy-monopeptidase and carboxy-dipeptidase activity of the protease."
    Guncar G., Klemencic I., Turk B., Turk V., Karaoglanovic-Carmona A., Juliano L., Turk D.
    Structure 8:305-313(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.67 ANGSTROMS).

Entry informationi

Entry nameiCATZ_HUMAN
AccessioniPrimary (citable) accession number: Q9UBR2
Secondary accession number(s): B2RC40
, O75331, Q9UQV5, Q9UQV6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: May 1, 2000
Last modified: September 3, 2014
This is version 138 of the entry and version 1 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 20
    Human chromosome 20: 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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