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Protein

Cathepsin L1

Gene

CTSL

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

Functioni

Important for the overall degradation of proteins in lysosomes.

Catalytic activityi

Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei138 – 1381
Active sitei276 – 2761
Active sitei300 – 3001

GO - Molecular functioni

  1. collagen binding Source: BHF-UCL
  2. cysteine-type endopeptidase activity Source: UniProtKB
  3. cysteine-type peptidase activity Source: UniProtKB
  4. fibronectin binding Source: BHF-UCL
  5. histone binding Source: BHF-UCL
  6. proteoglycan binding Source: BHF-UCL
  7. serpin family protein binding Source: UniProtKB

GO - Biological processi

  1. adaptive immune response Source: UniProtKB
  2. antigen processing and presentation Source: UniProtKB
  3. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
  4. cellular response to thyroid hormone stimulus Source: UniProtKB
  5. collagen catabolic process Source: BHF-UCL
  6. extracellular matrix disassembly Source: Reactome
  7. extracellular matrix organization Source: Reactome
  8. innate immune response Source: Reactome
  9. macrophage apoptotic process Source: BHF-UCL
  10. proteolysis Source: UniProtKB
  11. proteolysis involved in cellular protein catabolic process Source: BHF-UCL
  12. toll-like receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

BRENDAi3.4.22.15. 2681.
ReactomeiREACT_111168. Endosomal/Vacuolar pathway.
REACT_118572. Degradation of the extracellular matrix.
REACT_118632. Trafficking and processing of endosomal TLR.
REACT_121399. MHC class II antigen presentation.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_150401. Collagen degradation.

Protein family/group databases

MEROPSiC01.032.

Names & Taxonomyi

Protein namesi
Recommended name:
Cathepsin L1 (EC:3.4.22.15)
Alternative name(s):
Cathepsin L
Major excreted protein
Short name:
MEP
Cleaved into the following 2 chains:
Gene namesi
Name:CTSL
Synonyms:CTSL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:2537. CTSL.

Subcellular locationi

GO - Cellular componenti

  1. endolysosome lumen Source: Reactome
  2. extracellular region Source: UniProtKB
  3. extracellular space Source: BHF-UCL
  4. extracellular vesicular exosome Source: UniProtKB
  5. lysosomal lumen Source: Reactome
  6. lysosome Source: UniProtKB
  7. nucleus Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162382890.

Polymorphism and mutation databases

BioMutaiCTSL.
DMDMi115741.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Propeptidei18 – 11396Activation peptidePRO_0000026244Add
BLAST
Chaini114 – 288175Cathepsin L1 heavy chainPRO_0000026245Add
BLAST
Propeptidei289 – 2913PRO_0000026246
Chaini292 – 33342Cathepsin L1 light chainPRO_0000026247Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi135 ↔ 178
Disulfide bondi169 ↔ 211
Glycosylationi221 – 2211N-linked (GlcNAc...)3 Publications
Disulfide bondi269 ↔ 322Interchain (between heavy and light chains)

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiP07711.
PaxDbiP07711.
PeptideAtlasiP07711.
PRIDEiP07711.

PTM databases

PhosphoSiteiP07711.

Miscellaneous databases

PMAP-CutDBP07711.

Expressioni

Gene expression databases

BgeeiP07711.
CleanExiHS_CTSL1.
ExpressionAtlasiP07711. baseline and differential.
GenevestigatoriP07711.

Organism-specific databases

HPAiCAB000459.

Interactioni

Subunit structurei

Dimer of a heavy and a light chain linked by disulfide bonds.

Binary interactionsi

WithEntry#Exp.IntActNotes
SGTAO437653EBI-1220160,EBI-347996
srp-6G5EFH42EBI-1220160,EBI-1549936From a different organism.

Protein-protein interaction databases

BioGridi107894. 21 interactions.
IntActiP07711. 14 interactions.
MINTiMINT-3005764.
STRINGi9606.ENSP00000345344.

Structurei

Secondary structure

1
333
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi23 – 253Combined sources
Helixi26 – 3510Combined sources
Helixi44 – 6724Combined sources
Beta strandi72 – 754Combined sources
Turni79 – 824Combined sources
Helixi85 – 928Combined sources
Beta strandi103 – 1053Combined sources
Helixi120 – 1234Combined sources
Beta strandi134 – 1363Combined sources
Helixi138 – 15518Combined sources
Helixi163 – 1697Combined sources
Turni171 – 1744Combined sources
Helixi177 – 1793Combined sources
Helixi183 – 19311Combined sources
Beta strandi196 – 1983Combined sources
Turni199 – 2013Combined sources
Helixi215 – 2173Combined sources
Beta strandi218 – 2203Combined sources
Beta strandi223 – 2275Combined sources
Helixi232 – 24110Combined sources
Beta strandi245 – 2495Combined sources
Helixi254 – 2574Combined sources
Beta strandi261 – 2644Combined sources
Beta strandi271 – 2733Combined sources
Beta strandi276 – 28510Combined sources
Beta strandi289 – 2913Combined sources
Beta strandi294 – 2996Combined sources
Beta strandi304 – 3063Combined sources
Beta strandi311 – 3155Combined sources
Beta strandi317 – 3204Combined sources
Helixi321 – 3233Combined sources
Turni324 – 3263Combined sources
Beta strandi329 – 3324Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CJLX-ray2.20A22-333[»]
1CS8X-ray1.80A19-333[»]
1ICFX-ray2.00A/C114-288[»]
B/D292-333[»]
1MHWX-ray1.90A/B114-288[»]
C/D292-333[»]
2NQDX-ray1.75B113-333[»]
2VHSX-ray1.50A/B/C/D114-285[»]
A/B/C/D294-333[»]
2XU1X-ray1.45A/B/C/D114-333[»]
2XU3X-ray0.90A114-333[»]
2XU4X-ray1.12A114-333[»]
2XU5X-ray1.60A114-333[»]
2YJ2X-ray1.15A114-333[»]
2YJ8X-ray1.30A114-333[»]
2YJ9X-ray1.35A114-333[»]
2YJBX-ray1.40A114-333[»]
2YJCX-ray1.14A114-333[»]
3BC3X-ray2.20A/B114-333[»]
3H89X-ray2.50A/B/C/D/E/F114-333[»]
3H8BX-ray1.80A/B/C/D/E/F114-333[»]
3H8CX-ray2.50A/B114-333[»]
3HHAX-ray1.27A/B/C/D114-333[»]
3HWNX-ray2.33A/B/C/D76-333[»]
3IV2X-ray2.20A/B114-333[»]
3K24X-ray2.50A/B114-333[»]
3KSEX-ray1.71A/B/C114-333[»]
3OF8X-ray2.20A113-333[»]
3OF9X-ray1.76A113-333[»]
4AXLX-ray1.92A114-333[»]
4AXMX-ray2.80A/B/F/I/L/O114-333[»]
ProteinModelPortaliP07711.
SMRiP07711. Positions 18-333.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07711.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4870.
GeneTreeiENSGT00760000118871.
HOGENOMiHOG000230774.
HOVERGENiHBG011513.
InParanoidiP07711.
KOiK01365.
OMAiNPEYSVA.
OrthoDBiEOG786H3P.
PhylomeDBiP07711.
TreeFamiTF313739.

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.

P07711-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPTLILAAF CLGIASATLT FDHSLEAQWT KWKAMHNRLY GMNEEGWRRA
60 70 80 90 100
VWEKNMKMIE LHNQEYREGK HSFTMAMNAF GDMTSEEFRQ VMNGFQNRKP
110 120 130 140 150
RKGKVFQEPL FYEAPRSVDW REKGYVTPVK NQGQCGSCWA FSATGALEGQ
160 170 180 190 200
MFRKTGRLIS LSEQNLVDCS GPQGNEGCNG GLMDYAFQYV QDNGGLDSEE
210 220 230 240 250
SYPYEATEES CKYNPKYSVA NDTGFVDIPK QEKALMKAVA TVGPISVAID
260 270 280 290 300
AGHESFLFYK EGIYFEPDCS SEDMDHGVLV VGYGFESTES DNNKYWLVKN
310 320 330
SWGEEWGMGG YVKMAKDRRN HCGIASAASY PTV
Length:333
Mass (Da):37,564
Last modified:October 1, 1989 - v2
Checksum:i8CD17D00EF859D85
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti56 – 561M → V in AAH12612 (PubMed:15489334).Curated
Sequence conflicti268 – 2681D → N AA sequence (PubMed:3342889).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12451 mRNA. Translation: CAA30981.1.
M20496 mRNA. Translation: AAA66974.1.
CR457053 mRNA. Translation: CAG33334.1.
BX537395 mRNA. Translation: CAD97637.1.
AL160279 Genomic DNA. Translation: CAI16308.1.
BC012612 mRNA. Translation: AAH12612.1.
X05256 mRNA. Translation: CAA28877.1.
CCDSiCCDS6675.1.
PIRiS01002. KHHUL.
RefSeqiNP_001244900.1. NM_001257971.1.
NP_001244901.1. NM_001257972.1.
NP_001903.1. NM_001912.4.
NP_666023.1. NM_145918.2.
XP_005251773.1. XM_005251716.2.
UniGeneiHs.731507.

Genome annotation databases

EnsembliENST00000340342; ENSP00000365061; ENSG00000135047.
ENST00000343150; ENSP00000345344; ENSG00000135047.
GeneIDi1514.
KEGGihsa:1514.
UCSCiuc004aph.3. human.

Polymorphism and mutation databases

BioMutaiCTSL.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12451 mRNA. Translation: CAA30981.1.
M20496 mRNA. Translation: AAA66974.1.
CR457053 mRNA. Translation: CAG33334.1.
BX537395 mRNA. Translation: CAD97637.1.
AL160279 Genomic DNA. Translation: CAI16308.1.
BC012612 mRNA. Translation: AAH12612.1.
X05256 mRNA. Translation: CAA28877.1.
CCDSiCCDS6675.1.
PIRiS01002. KHHUL.
RefSeqiNP_001244900.1. NM_001257971.1.
NP_001244901.1. NM_001257972.1.
NP_001903.1. NM_001912.4.
NP_666023.1. NM_145918.2.
XP_005251773.1. XM_005251716.2.
UniGeneiHs.731507.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CJLX-ray2.20A22-333[»]
1CS8X-ray1.80A19-333[»]
1ICFX-ray2.00A/C114-288[»]
B/D292-333[»]
1MHWX-ray1.90A/B114-288[»]
C/D292-333[»]
2NQDX-ray1.75B113-333[»]
2VHSX-ray1.50A/B/C/D114-285[»]
A/B/C/D294-333[»]
2XU1X-ray1.45A/B/C/D114-333[»]
2XU3X-ray0.90A114-333[»]
2XU4X-ray1.12A114-333[»]
2XU5X-ray1.60A114-333[»]
2YJ2X-ray1.15A114-333[»]
2YJ8X-ray1.30A114-333[»]
2YJ9X-ray1.35A114-333[»]
2YJBX-ray1.40A114-333[»]
2YJCX-ray1.14A114-333[»]
3BC3X-ray2.20A/B114-333[»]
3H89X-ray2.50A/B/C/D/E/F114-333[»]
3H8BX-ray1.80A/B/C/D/E/F114-333[»]
3H8CX-ray2.50A/B114-333[»]
3HHAX-ray1.27A/B/C/D114-333[»]
3HWNX-ray2.33A/B/C/D76-333[»]
3IV2X-ray2.20A/B114-333[»]
3K24X-ray2.50A/B114-333[»]
3KSEX-ray1.71A/B/C114-333[»]
3OF8X-ray2.20A113-333[»]
3OF9X-ray1.76A113-333[»]
4AXLX-ray1.92A114-333[»]
4AXMX-ray2.80A/B/F/I/L/O114-333[»]
ProteinModelPortaliP07711.
SMRiP07711. Positions 18-333.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107894. 21 interactions.
IntActiP07711. 14 interactions.
MINTiMINT-3005764.
STRINGi9606.ENSP00000345344.

Chemistry

BindingDBiP07711.
ChEMBLiCHEMBL2111380.
GuidetoPHARMACOLOGYi2351.

Protein family/group databases

MEROPSiC01.032.

PTM databases

PhosphoSiteiP07711.

Polymorphism and mutation databases

BioMutaiCTSL.
DMDMi115741.

Proteomic databases

MaxQBiP07711.
PaxDbiP07711.
PeptideAtlasiP07711.
PRIDEiP07711.

Protocols and materials databases

DNASUi1514.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000340342; ENSP00000365061; ENSG00000135047.
ENST00000343150; ENSP00000345344; ENSG00000135047.
GeneIDi1514.
KEGGihsa:1514.
UCSCiuc004aph.3. human.

Organism-specific databases

CTDi1514.
GeneCardsiGC09P090352.
H-InvDBHIX0058839.
HIX0170314.
HGNCiHGNC:2537. CTSL.
HPAiCAB000459.
MIMi116880. gene.
neXtProtiNX_P07711.
PharmGKBiPA162382890.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG4870.
GeneTreeiENSGT00760000118871.
HOGENOMiHOG000230774.
HOVERGENiHBG011513.
InParanoidiP07711.
KOiK01365.
OMAiNPEYSVA.
OrthoDBiEOG786H3P.
PhylomeDBiP07711.
TreeFamiTF313739.

Enzyme and pathway databases

BRENDAi3.4.22.15. 2681.
ReactomeiREACT_111168. Endosomal/Vacuolar pathway.
REACT_118572. Degradation of the extracellular matrix.
REACT_118632. Trafficking and processing of endosomal TLR.
REACT_121399. MHC class II antigen presentation.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_150401. Collagen degradation.

Miscellaneous databases

EvolutionaryTraceiP07711.
GeneWikiiCathepsin_L1.
GenomeRNAii1514.
NextBioi6271.
PMAP-CutDBP07711.
PROiP07711.
SOURCEiSearch...

Gene expression databases

BgeeiP07711.
CleanExiHS_CTSL1.
ExpressionAtlasiP07711. baseline and differential.
GenevestigatoriP07711.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and sequence of a cDNA for human pro-(cathepsin L)."
    Gal S., Gottesman M.M.
    Biochem. J. 253:303-306(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Complete nucleotide and deduced amino acid sequences of human and murine preprocathepsin L. An abundant transcript induced by transformation of fibroblasts."
    Joseph L.J., Chang L.C., Stamenkovich D., Sukhatme V.P.
    J. Clin. Invest. 81:1621-1629(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Colon endothelium.
  5. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Prostate.
  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 114-288 AND 292-333.
  8. "The major ras induced protein in NIH3T3 cells is cathepsin L."
    Joseph L.J., Lapid S., Sukhatme V.P.
    Nucleic Acids Res. 15:3186-3186(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 113-154.
  9. "The N-terminal amino acid sequences of the heavy and light chains of human cathepsin L. Relationship to a cDNA clone for a major cysteine proteinase from a mouse macrophage cell line."
    Mason R.W., Walker J.E., Northrop F.D.
    Biochem. J. 240:373-377(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 114-154 AND 292-333.
  10. "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
    Zhang H., Li X.-J., Martin D.B., Aebersold R.
    Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-221.
  11. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-221.
    Tissue: Plasma.
  12. "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-221.
    Tissue: Liver.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  16. "Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment."
    Coulombe R., Grochulski P., Sivaraman J., Menard R., Mort J.S., Cygler M.
    EMBO J. 15:5492-5503(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 18-333.
  17. "The crystal structure of human cathepsin L complexed with E-64."
    Fujishima A., Imai Y., Nomura T., Fujisawa Y., Yamamoto Y., Sugarawa T.
    FEBS Lett. 407:47-50(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 114-333.
  18. Cygler M., Coulombe R.
    Submitted (AUG-1999) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 18-333.

Entry informationi

Entry nameiCATL1_HUMAN
AccessioniPrimary (citable) accession number: P07711
Secondary accession number(s): Q6IAV1, Q96QJ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: October 1, 1989
Last modified: April 29, 2015
This is version 177 of the entry and version 2 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 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.