P14091 (CATE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cathepsin E
EC=3.4.23.34

Cleaved into the following 2 chains:

1. Cathepsin E form I
2. Cathepsin E form II

Gene names

Name:

CTSE

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	401 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May have a role in immune function. Probably involved in the processing of antigenic peptides during MHC class II-mediated antigen presentation. May play a role in activation-induced lymphocyte depletion in the thymus, and in neuronal degeneration and glial cell activation in the brain. Ref.12
Catalytic activity	Similar to cathepsin D, but slightly broader specificity. Ref.11 Ref.12
Subunit structure	Homodimer; disulfide-linked. Ref.11
Subcellular location	Endosome. Note: The proenzyme is localized to the endoplasmic reticulum and Golgi apparatus, while the mature enzyme is localized to the endosome. Ref.3
Tissue specificity	Expressed abundantly in the stomach, the Clara cells of the lung and activated B-lymphocytes, and at lower levels in lymph nodes, skin and spleen. Not expressed in resting B-lymphocytes. Ref.2 Ref.12 Ref.13
Post-translational modification	Glycosylated. The nature of the carbohydrate chain varies between cell types. In fibroblasts, the proenzyme contains a high mannose-type oligosaccharide, while the mature enzyme contains a complex-type oligosaccharide. In erythrocyte membranes, both the proenzyme and mature enzyme contain a complex-type oligosaccharide. Ref.3 Ref.9 Ref.10 Two forms are produced by autocatalytic cleavage, form I begins at Ile-54, form II begins at Thr-57.
Sequence similarities	Belongs to the peptidase A1 family.
Biophysicochemical properties	Kinetic parameters: KM=0.06 mM for hemoglobin KM=0.13 mM for Pro-Pro-Thr-Ile-Phe-Phe(4-NO2)-Arg-Leu KM=0.04 mM for Lys-Pro-Ile-Glu-Phe-Phe(4-NO2)-Arg-Leu

Ontologies

Keywords
Cellular component	Endosome
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal
Molecular function	Aspartyl protease Hydrolase Protease
PTM	Autocatalytic cleavage Disulfide bond Glycoprotein Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	antigen processing and presentation of exogenous peptide antigen via MHC class II Inferred from direct assay Ref.12. Source: UniProtKB digestion Traceable author statement Ref.1. Source: ProtInc protein autoprocessing Inferred from electronic annotation. Source: Compara proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	endosome Inferred from direct assay Ref.3. Source: UniProtKB
Molecular_function	aspartic-type endopeptidase activity Inferred from direct assay Ref.11. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 3 (identifier: P14091-3)

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.

Isoform 1 (identifier: P14091-1)

The sequence of this isoform differs from the canonical sequence as follows:
     155-159: Missing.

Isoform 2 (identifier: P14091-2)

The sequence of this isoform differs from the canonical sequence as follows:
     155-159: Missing.
     268-368: IQVGGTVMFC...GFQGLDIHPP → MLWSVPTLTS...CVCACLSDRP
     369-401: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

Ref.9

Propeptide

20 – 53

34

Activation peptide

PRO_0000025974

Chain

54 – 401

348

Cathepsin E form I

PRO_0000025975

Chain

57 – 401

345

Cathepsin E form II

PRO_0000354668

Sites

Active site

96

1

By similarity

Active site

286

1

By similarity

Amino acid modifications

Glycosylation

90

1

N-linked (GlcNAc...)

Disulfide bond

60

Interchain Ref.11

Disulfide bond

109 ↔ 114

By similarity

Disulfide bond

277 ↔ 281

By similarity

Disulfide bond

319 ↔ 356

By similarity

Natural variations

Alternative sequence

155 – 159

5

Missing in isoform 1 and isoform 2.

VSP_009729

Alternative sequence

268 – 368

101

IQVGG…DIHPP → MLWSVPTLTSCRMSPSPLTE SPIPSAQLPTPYWTSWMECS SAAVAFKDLTSTLQLGPSGS WGMSSFDSFTQSLTVGITVW DWPQQSPKEGPCVCACLSDR P in isoform 2.

VSP_009730

Alternative sequence

369 – 401

33

Missing in isoform 2.

VSP_009731

Natural variant

82

1

I → V.
Corresponds to variant rs57621203 [ dbSNP | Ensembl ].

VAR_061731

Natural variant

329

1

T → I.
Corresponds to variant rs6503 [ dbSNP | Ensembl ].

VAR_014572

Experimental info

Mutagenesis

60

1

C → A: Abolishes homodimerization. Ref.11

Secondary structure

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401

Helix Strand Turn

Details...

Beta strand

22 – 25

4

Helix

71 – 73

3

Beta strand

74 – 76

3

Beta strand

79 – 84

6

Turn

85 – 88

4

Beta strand

89 – 96

8

Beta strand

102 – 106

5

Helix

112 – 114

3

Helix

122 – 124

3

Beta strand

134 – 141

8

Beta strand

143 – 160

18

Beta strand

163 – 173

11

Helix

179 – 183

5

Beta strand

187 – 191

5

Helix

195 – 197

3

Helix

199 – 201

3

Helix

205 – 211

7

Beta strand

216 – 223

8

Beta strand

235 – 238

4

Helix

243 – 245

3

Beta strand

251 – 254

4

Turn

258 – 261

4

Beta strand

262 – 270

9

Beta strand

273 – 276

4

Beta strand

281 – 285

5

Beta strand

290 – 294

5

Helix

296 – 306

11

Beta strand

312 – 317

6

Helix

319 – 324

6

Beta strand

328 – 332

5

Beta strand

335 – 339

5

Turn

341 – 343

3

Beta strand

344 – 346

3

Beta strand

356 – 362

7

Turn

367 – 369

3

Beta strand

373 – 375

3

Helix

377 – 382

6

Beta strand

383 – 388

6

Turn

389 – 392

4

Beta strand

393 – 399

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 3 [UniParc]. Last modified March 29, 2004. Version 2. Checksum: 46A2BA35266032CB	FASTA	401	43,312
	10 20 30 40 50 60 MKTLLLLLLV LLELGEAQGS LHRVPLRRHP SLKKKLRARS QLSEFWKSHN LDMIQFTESC 70 80 90 100 110 120 SMDQSAKEPL INYLDMEYFG TISIGSPPQN FTVIFDTGSS NLWVPSVYCT SPACKTHSRF 130 140 150 160 170 180 QPSQSSTYSQ PGQSFSIQYG TGSLSGIIGA DQVSAFATQV EGLTVVGQQF GESVTEPGQT 190 200 210 220 230 240 FVDAEFDGIL GLGYPSLAVG GVTPVFDNMM AQNLVDLPMF SVYMSSNPEG GAGSELIFGG 250 260 270 280 290 300 YDHSHFSGSL NWVPVTKQAY WQIALDNIQV GGTVMFCSEG CQAIVDTGTS LITGPSDKIK 310 320 330 340 350 360 QLQNAIGAAP VDGEYAVECA NLNVMPDVTF TINGVPYTLS PTAYTLLDFV DGMQFCSSGF 370 380 390 400 QGLDIHPPAG PLWILGDVFI RQFYSVFDRG NNRVGLAPAV P
	Isoform 1 [UniParc]. Checksum: 40B643C5FB01521E	FASTA	396	42,794
	10 20 30 40 50 60 MKTLLLLLLV LLELGEAQGS LHRVPLRRHP SLKKKLRARS QLSEFWKSHN LDMIQFTESC 70 80 90 100 110 120 SMDQSAKEPL INYLDMEYFG TISIGSPPQN FTVIFDTGSS NLWVPSVYCT SPACKTHSRF 130 140 150 160 170 180 QPSQSSTYSQ PGQSFSIQYG TGSLSGIIGA DQVSVEGLTV VGQQFGESVT EPGQTFVDAE 190 200 210 220 230 240 FDGILGLGYP SLAVGGVTPV FDNMMAQNLV DLPMFSVYMS SNPEGGAGSE LIFGGYDHSH 250 260 270 280 290 300 FSGSLNWVPV TKQAYWQIAL DNIQVGGTVM FCSEGCQAIV DTGTSLITGP SDKIKQLQNA 310 320 330 340 350 360 IGAAPVDGEY AVECANLNVM PDVTFTINGV PYTLSPTAYT LLDFVDGMQF CSSGFQGLDI 370 380 390 HPPAGPLWIL GDVFIRQFYS VFDRGNNRVG LAPAVP
	Isoform 2 [UniParc]. Checksum: 4443819D6393C1FC	FASTA	363	39,553
	10 20 30 40 50 60 MKTLLLLLLV LLELGEAQGS LHRVPLRRHP SLKKKLRARS QLSEFWKSHN LDMIQFTESC 70 80 90 100 110 120 SMDQSAKEPL INYLDMEYFG TISIGSPPQN FTVIFDTGSS NLWVPSVYCT SPACKTHSRF 130 140 150 160 170 180 QPSQSSTYSQ PGQSFSIQYG TGSLSGIIGA DQVSVEGLTV VGQQFGESVT EPGQTFVDAE 190 200 210 220 230 240 FDGILGLGYP SLAVGGVTPV FDNMMAQNLV DLPMFSVYMS SNPEGGAGSE LIFGGYDHSH 250 260 270 280 290 300 FSGSLNWVPV TKQAYWQIAL DNMLWSVPTL TSCRMSPSPL TESPIPSAQL PTPYWTSWME 310 320 330 340 350 360 CSSAAVAFKD LTSTLQLGPS GSWGMSSFDS FTQSLTVGIT VWDWPQQSPK EGPCVCACLS DRP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human gastric cathepsin E. Predicted sequence, localization to chromosome 1, and sequence homology with other aspartic proteinases." Azuma T., Pals G., Mohandas T.K., Couvreur J.M., Taggart R.T. J. Biol. Chem. 264:16748-16753(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). Tissue: Gastric mucosa.
[2]	"Human gastric cathepsin E gene. Multiple transcripts result from alternative polyadenylation of the primary transcripts of a single gene locus at 1q31-q32." Azuma T., Liu W.G., Vander Laan D.J., Bowcock A.M., Taggart R.T. J. Biol. Chem. 267:1609-1614(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), TISSUE SPECIFICITY.
[3]	"Subcellular localization and targeting of cathepsin E." Finley E.M., Kornfeld S. J. Biol. Chem. 269:31259-31266(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), SUBCELLULAR LOCATION, GLYCOSYLATION. Tissue: Intestine.
[4]	"An alternatively spliced variant of cathepsin E in human gastric adenocarcinoma cells." Tatnell P.J., Cook M., Kay J. Biochim. Biophys. Acta 1625:203-206(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). Tissue: Gastric adenocarcinoma.
[5]	"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] (ISOFORM 1). Tissue: Stomach.
[6]	"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].
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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). Tissue: Brain.
[9]	"Isolation and biochemical characterization of procathepsin E from human erythrocyte membranes." Takeda-Ezaki M., Yamamoto K. Arch. Biochem. Biophys. 304:352-358(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-38 AND 54-76, BIOPHYSICOCHEMICAL PROTERTIES, AUTOCATALYTIC CLEAVAGE, GLYCOSYLATION. Tissue: Erythrocyte.
[10]	"Structural evidence for two isozymic forms and the carbohydrate attachment site of human gastric cathepsin E." Athauda S.B.P., Matsuzaki O., Kgeyama T., Takahashi K. Biochem. Biophys. Res. Commun. 168:878-885(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 54-68; 77-95; 141-154; 280-290 AND 394-401, GLYCOSYLATION. Tissue: Gastric mucosa.
[11]	"Monomeric human cathepsin E." Fowler S.D., Kay J., Dunn B.M., Tatnell P.J. FEBS Lett. 366:72-74(1995) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, SUBUNIT, DISULFIDE BONDS, MUTAGENESIS OF CYS-60.
[12]	"Regulation of cathepsin E expression during human B cell differentiation in vitro." Sealy L., Mota F., Rayment N., Tatnell P.J., Kay J., Chain B. Eur. J. Immunol. 26:1838-1843(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
[13]	"Regulation of human and mouse procathepsin E gene expression." Cook M., Caswell R.C., Richards R.J., Kay J., Tatnell P.J. Eur. J. Biochem. 268:2658-2668(2001) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J05036 mRNA. Translation: AAA52130.1.
M84424 , M84413, M84417, M84418, M84419, M84420, M84421, M84422 Genomic DNA. Translation: AAA52300.1.
AJ250716 mRNA. Translation: CAB82849.1.
AJ250717 mRNA. Translation: CAB82850.1.
AK292057 mRNA. Translation: BAF84746.1.
BX571818 Genomic DNA. Translation: CAH73264.1.
BX571818 Genomic DNA. Translation: CAH73265.1.
CH471067 Genomic DNA. Translation: EAW91592.1.
CH471067 Genomic DNA. Translation: EAW91593.1.
BC042537 mRNA. Translation: AAH42537.1.

IPI

IPI00020716.
IPI00025062.
IPI00409646.

PIR

A34401. A42038.

RefSeq

NP_001901.1. NM_001910.3.
NP_683865.1. NM_148964.2.

UniGene

Hs.644082.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LCG	model	-	A	1-401	[»]
1TZS	X-ray	2.35	A	54-401	[»]
			P	19-53	[»]

ProteinModelPortal

P14091.

ModBase

Search...

Protein-protein interaction databases

IntAct

P14091. 2 interactions.

MINT

MINT-1388890.

STRING

9606.ENSP00000350911.

Protein family/group databases

MEROPS

A01.010.

PTM databases

PhosphoSite

P14091.

Polymorphism databases

DMDM

46397366.

Proteomic databases

PaxDb

P14091.

PRIDE

P14091.

Protocols and materials databases

DNASU

1510.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000358184; ENSP00000350911; ENSG00000196188.
ENST00000360218; ENSP00000353350; ENSG00000196188.
ENST00000581049; ENSP00000463969; ENSG00000264606.
ENST00000583663; ENSP00000463953; ENSG00000264606.

GeneID

1510.

KEGG

hsa:1510.

UCSC

uc001hdu.3. human.
uc001hdv.3. human.

Organism-specific databases

CTD

1510.

GeneCards

GC01P206319.

HGNC

HGNC:2530. CTSE.

HPA

HPA008021.

MIM

116890. gene.

neXtProt

NX_P14091.

PharmGKB

PA27030.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG248684.

HOGENOM

HOG000197681.

HOVERGEN

HBG000482.

InParanoid

P14091.

KO

K01382.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

SABIO-RK

P14091.

Gene expression databases

ArrayExpress

P14091.

Bgee

P14091.

CleanEx

HS_CTSE.

Genevestigator

P14091.

GermOnline

ENSG00000196188. Homo sapiens.

Family and domain databases

Gene3D

2.40.70.10. 2 hits.

InterPro

IPR001461. Peptidase_A1.
IPR021109. Peptidase_aspartic.
IPR001969. Peptidase_aspartic_AS.
IPR012848. Propep_A1.
[Graphical view]

PANTHER

PTHR13683. PTHR13683. 1 hit.

Pfam

PF07966. A1_Propeptide. 1 hit.
PF00026. Asp. 1 hit.
[Graphical view]

PRINTS

PR00792. PEPSIN.

SUPFAM

SSF50630. Pept_Aspartic. 1 hit.

PROSITE

PS00141. ASP_PROTEASE. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P14091.

ChEMBL

CHEMBL3092.

EvolutionaryTrace

P14091.

GenomeRNAi

1510.

NextBio

6251.

PMAP-CutDB

P14091.

SOURCE

Search...

Entry information

Entry name

CATE_HUMAN

Accession

Primary (citable) accession number: P14091
Secondary accession number(s): Q5TZ01 , Q5TZ02, Q9NY58, Q9UCE3, Q9UCE4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	March 29, 2004
Last modified:	May 1, 2013
This is version 149 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.