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Protein

Dipeptidyl peptidase 1

Gene

CTSC

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

Functioni

Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII.1 Publication

Catalytic activityi

Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, except when Xaa is Arg or Lys, or Yaa or Zaa is Pro.

Cofactori

chlorideNote: Binds 1 Cl- ion per heavy chain.

Enzyme regulationi

Strongly inhibited by the cysteine peptidase inhibitors mersalyl acid, iodoacetic acid and cystatin. Inhibited by N-ethylmaleimide, Gly-Phe-diazomethane, TLCK, TPCK and, at low pH, by dithiodipyridine. Not inhibited by the serine peptidase inhibitor PMSF, the aminopeptidase inhibitor bestatin, or metal ion chelators.1 Publication

pH dependencei

High activity at pH 4.5-6.8.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei2581
Binding sitei302Chloride1
Binding sitei304Chloride; via amide nitrogen1
Binding sitei347Chloride1
Active sitei4051
Active sitei4271

GO - Molecular functioni

  • chaperone binding Source: BHF-UCL
  • chloride ion binding Source: Ensembl
  • cysteine-type endopeptidase activity Source: GO_Central
  • cysteine-type peptidase activity Source: UniProtKB
  • peptidase activator activity involved in apoptotic process Source: Ensembl
  • phosphatase binding Source: BHF-UCL
  • serine-type endopeptidase activity Source: Ensembl

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Ligandi

Chloride

Enzyme and pathway databases

BioCyciMetaCyc:HS03265-MONOMER.
ZFISH:HS03265-MONOMER.
BRENDAi3.4.14.1. 2681.
ReactomeiR-HSA-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-HSA-2132295. MHC class II antigen presentation.
R-HSA-5694530. Cargo concentration in the ER.
R-HSA-6798695. Neutrophil degranulation.
SABIO-RKP53634.

Protein family/group databases

MEROPSiC01.070.

Names & Taxonomyi

Protein namesi
Recommended name:
Dipeptidyl peptidase 1 (EC:3.4.14.1)
Alternative name(s):
Cathepsin C
Cathepsin J
Dipeptidyl peptidase I
Short name:
DPP-I
Short name:
DPPI
Dipeptidyl transferase
Cleaved into the following 3 chains:
Alternative name(s):
Dipeptidyl peptidase I exclusion domain chain
Alternative name(s):
Dipeptidyl peptidase I heavy chain
Alternative name(s):
Dipeptidyl peptidase I light chain
Gene namesi
Name:CTSC
Synonyms:CPPI
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:2528. CTSC.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum-Golgi intermediate compartment membrane Source: Reactome
  • endoplasmic reticulum lumen Source: Reactome
  • ER to Golgi transport vesicle Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • Golgi membrane Source: GOC
  • lysosome Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Involvement in diseasei

Papillon-Lefevre syndrome (PLS)13 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive disorder characterized by palmoplantar keratosis and severe periodontitis affecting deciduous and permanent dentitions and resulting in premature tooth loss. The palmoplantar keratotic phenotype vary from mild psoriasiform scaly skin to overt hyperkeratosis. Keratosis also affects other sites such as elbows and knees.
See also OMIM:245000
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01693339W → S in PLS. 1 PublicationCorresponds to variant rs104894210dbSNPEnsembl.1
Natural variantiVAR_01903567 – 74Missing in PLS. 1 Publication8
Natural variantiVAR_016934127H → P in PLS. 1 PublicationCorresponds to variant rs104894216dbSNPEnsembl.1
Natural variantiVAR_019036129V → E in PLS. 1 PublicationCorresponds to variant rs760130711dbSNPEnsembl.1
Natural variantiVAR_019037139G → R in PLS. 2 PublicationsCorresponds to variant rs749103588dbSNPEnsembl.1
Natural variantiVAR_019038236D → Y in PLS. 2 PublicationsCorresponds to variant rs764724707dbSNPEnsembl.1
Natural variantiVAR_009541249V → F in PLS. 2 Publications1
Natural variantiVAR_009542252Q → L in PLS. 2 PublicationsCorresponds to variant rs104894207dbSNPEnsembl.1
Natural variantiVAR_019039272R → H in PLS. 1 PublicationCorresponds to variant rs587777534dbSNPEnsembl.1
Natural variantiVAR_009543272R → P in PLS. 5 PublicationsCorresponds to variant rs587777534dbSNPEnsembl.1
Natural variantiVAR_016935286Q → R in HMS and PLS. 2 PublicationsCorresponds to variant rs104894208dbSNPEnsembl.1
Natural variantiVAR_019040291C → Y in PLS. 1 PublicationCorresponds to variant rs748729285dbSNPEnsembl.1
Natural variantiVAR_039686294Y → H in PLS. 1 Publication1
Natural variantiVAR_019041300G → D in PLS. 2 Publications1
Natural variantiVAR_019042300G → S in PLS. 1 Publication1
Natural variantiVAR_009544301G → S in PLS. 4 PublicationsCorresponds to variant rs104894214dbSNPEnsembl.1
Natural variantiVAR_019043301G → V in PLS. 1 Publication1
Natural variantiVAR_019044304Y → N in PLS. 1 Publication1
Natural variantiVAR_019045312Q → R in PLS. 1 Publication1
Natural variantiVAR_019046319E → G in PLS. 1 Publication1
Natural variantiVAR_009545339R → C in PLS. 5 Publications1
Natural variantiVAR_016944340Y → C in PLS. 2 Publications1
Natural variantiVAR_009546347Y → C in PLS and AP1. 3 PublicationsCorresponds to variant rs104894211dbSNPEnsembl.1
Natural variantiVAR_027249405H → N in PLS. 1 Publication1
Natural variantiVAR_027250405H → R in PLS. 1 PublicationCorresponds to variant rs151269219dbSNPEnsembl.1
Natural variantiVAR_016936429W → C in PLS. 1 PublicationCorresponds to variant rs104894215dbSNPEnsembl.1
Natural variantiVAR_019048447E → G in PLS. 2 Publications1
Haim-Munk syndrome (HMS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive disorder characterized by palmoplantar keratosis, onychogryphosis and periodontitis. Additional features are pes planus, arachnodactyly, and acroosteolysis.
See also OMIM:245010
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_016935286Q → R in HMS and PLS. 2 PublicationsCorresponds to variant rs104894208dbSNPEnsembl.1
Periodontititis, aggressive, 1 (AP1)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease characterized by severe and protracted gingival infections, generalized or localized, leading to tooth loss. Amounts of microbial deposits are generally inconsistent with the severity of periodontal tissue destruction and the progression of attachment and bone loss may be self arresting.
See also OMIM:170650
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_009546347Y → C in PLS and AP1. 3 PublicationsCorresponds to variant rs104894211dbSNPEnsembl.1
Natural variantiVAR_019047412Y → C in AP1. 1 PublicationCorresponds to variant rs28937571dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation, Palmoplantar keratoderma

Organism-specific databases

DisGeNETi1075.
MalaCardsiCTSC.
MIMi170650. phenotype.
245000. phenotype.
245010. phenotype.
OpenTargetsiENSG00000109861.
Orphaneti2342. Haim-Munk syndrome.
678. Papillon-Lefevre syndrome.
PharmGKBiPA27028.

Chemistry databases

ChEMBLiCHEMBL2252.
GuidetoPHARMACOLOGYi2344.

Polymorphism and mutation databases

BioMutaiCTSC.
DMDMi317373330.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 243 PublicationsAdd BLAST24
ChainiPRO_000002633825 – 134Dipeptidyl peptidase 1 exclusion domain chainAdd BLAST110
PropeptideiPRO_0000026339135 – 2303 PublicationsAdd BLAST96
ChainiPRO_0000026340231 – 394Dipeptidyl peptidase 1 heavy chainAdd BLAST164
ChainiPRO_0000026341395 – 463Dipeptidyl peptidase 1 light chainAdd BLAST69

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi29N-linked (GlcNAc...)2 Publications1
Disulfide bondi30 ↔ 118
Glycosylationi53N-linked (GlcNAc...)2 Publications1
Disulfide bondi54 ↔ 136
Glycosylationi119N-linked (GlcNAc...)1 Publication1
Disulfide bondi255 ↔ 298
Glycosylationi276N-linked (GlcNAc...)1 Publication1
Disulfide bondi291 ↔ 331
Disulfide bondi321 ↔ 337

Post-translational modificationi

N-glycosylated. While glycosylation at Asn-53, Asn-119 and Asn-276 is mediated by STT3A-containing complexes, glycosylation at Asn-29 is mediated STT3B-containing complexes.5 Publications
In approximately 50% of the complexes the exclusion domain is cleaved at position 58 or 61. The two parts of the exclusion domain are held together by a disulfide bond.

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

EPDiP53634.
MaxQBiP53634.
PaxDbiP53634.
PeptideAtlasiP53634.
PRIDEiP53634.
TopDownProteomicsiP53634-1. [P53634-1]

PTM databases

iPTMnetiP53634.
PhosphoSitePlusiP53634.
SwissPalmiP53634.

Miscellaneous databases

PMAP-CutDBP53634.

Expressioni

Tissue specificityi

Ubiquitous. Highly expressed in lung, kidney and placenta. Detected at intermediate levels in colon, small intestine, spleen and pancreas.1 Publication

Inductioni

Up-regulated in lymphocytes by IL2/interleukin-2.1 Publication

Gene expression databases

BgeeiENSG00000109861.
ExpressionAtlasiP53634. baseline and differential.
GenevisibleiP53634. HS.

Organism-specific databases

HPAiCAB025364.

Interactioni

Subunit structurei

Tetramer of heterotrimers consisting of exclusion domain, heavy- and light chains.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CST7O760962EBI-1047323,EBI-2807448

GO - Molecular functioni

  • chaperone binding Source: BHF-UCL
  • phosphatase binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi107502. 24 interactors.
IntActiP53634. 22 interactors.
MINTiMINT-4655964.
STRINGi9606.ENSP00000227266.

Chemistry databases

BindingDBiP53634.

Structurei

Secondary structure

1463
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi32 – 35Combined sources4
Beta strandi37 – 48Combined sources12
Turni49 – 51Combined sources3
Helixi54 – 56Combined sources3
Beta strandi60 – 69Combined sources10
Turni70 – 72Combined sources3
Beta strandi73 – 75Combined sources3
Beta strandi81 – 87Combined sources7
Turni88 – 90Combined sources3
Beta strandi91 – 96Combined sources6
Beta strandi99 – 110Combined sources12
Beta strandi113 – 121Combined sources9
Beta strandi123 – 128Combined sources6
Beta strandi133 – 141Combined sources9
Beta strandi254 – 256Combined sources3
Helixi258 – 274Combined sources17
Turni275 – 277Combined sources3
Helixi285 – 291Combined sources7
Helixi297 – 299Combined sources3
Helixi303 – 306Combined sources4
Helixi309 – 313Combined sources5
Helixi319 – 321Combined sources3
Beta strandi342 – 347Combined sources6
Helixi357 – 367Combined sources11
Beta strandi370 – 374Combined sources5
Helixi378 – 382Combined sources5
Beta strandi385 – 388Combined sources4
Beta strandi405 – 414Combined sources10
Turni416 – 418Combined sources3
Beta strandi421 – 426Combined sources6
Beta strandi431 – 433Combined sources3
Beta strandi438 – 442Combined sources5
Turni443 – 446Combined sources4
Helixi447 – 449Combined sources3
Beta strandi455 – 459Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K3BX-ray2.15A25-143[»]
B231-394[»]
C395-463[»]
2DJFX-ray2.00A25-143[»]
B231-394[»]
C395-463[»]
2DJGX-ray2.05A25-143[»]
B231-394[»]
C395-463[»]
3PDFX-ray1.85A25-463[»]
4CDCX-ray2.40A/D/G/J25-143[»]
B/E/H/K230-394[»]
C/F/I/L395-463[»]
4CDDX-ray2.35A/D25-144[»]
B/E230-394[»]
C/F395-463[»]
4CDEX-ray2.40A/D25-143[»]
B/E230-394[»]
C/F395-463[»]
4CDFX-ray2.20A/D25-144[»]
B/E229-394[»]
C/F395-463[»]
4OELX-ray1.40A25-394[»]
B395-463[»]
4OEMX-ray1.52A25-394[»]
B395-463[»]
ProteinModelPortaliP53634.
SMRiP53634.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53634.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1543. Eukaryota.
COG4870. LUCA.
GeneTreeiENSGT00760000118871.
HOGENOMiHOG000127503.
HOVERGENiHBG005248.
InParanoidiP53634.
KOiK01275.
OMAiYDDFLHY.
OrthoDBiEOG091G06TT.
PhylomeDBiP53634.
TreeFamiTF313225.

Family and domain databases

Gene3Di2.40.128.80. 1 hit.
InterProiIPR014882. CathepsinC_exc.
IPR033161. DPP_I.
IPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PTHR12411:SF354. PTHR12411:SF354. 1 hit.
PfamiPF08773. CathepsinC_exc. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00645. Pept_C1. 1 hit.
[Graphical view]
SUPFAMiSSF75001. SSF75001. 1 hit.
PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P53634-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MGAGPSLLLA ALLLLLSGDG AVRCDTPANC TYLDLLGTWV FQVGSSGSQR
60 70 80 90 100
DVNCSVMGPQ EKKVVVYLQK LDTAYDDLGN SGHFTIIYNQ GFEIVLNDYK
110 120 130 140 150
WFAFFKYKEE GSKVTTYCNE TMTGWVHDVL GRNWACFTGK KVGTASENVY
160 170 180 190 200
VNIAHLKNSQ EKYSNRLYKY DHNFVKAINA IQKSWTATTY MEYETLTLGD
210 220 230 240 250
MIRRSGGHSR KIPRPKPAPL TAEIQQKILH LPTSWDWRNV HGINFVSPVR
260 270 280 290 300
NQASCGSCYS FASMGMLEAR IRILTNNSQT PILSPQEVVS CSQYAQGCEG
310 320 330 340 350
GFPYLIAGKY AQDFGLVEEA CFPYTGTDSP CKMKEDCFRY YSSEYHYVGG
360 370 380 390 400
FYGGCNEALM KLELVHHGPM AVAFEVYDDF LHYKKGIYHH TGLRDPFNPF
410 420 430 440 450
ELTNHAVLLV GYGTDSASGM DYWIVKNSWG TGWGENGYFR IRRGTDECAI
460
ESIAVAATPI PKL
Length:463
Mass (Da):51,854
Last modified:January 11, 2011 - v2
Checksum:i4C9C7C24D900CEE6
GO
Isoform 2 (identifier: P53634-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     107-137: YKEEGSKVTTYCNETMTGWVHDVLGRNWACF → DVTDFISHLFMQLGTVGIYDLPHLRNKLVIK
     138-463: Missing.

Show »
Length:137
Mass (Da):15,169
Checksum:iC68FC076FCB30601
GO
Isoform 3 (identifier: P53634-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     107-141: YKEEGSKVTTYCNETMTGWVHDVLGRNWACFTGKK → DVTDFISHLFMQLGTVGIYDLPHLRNKLAMNRRWG
     142-463: Missing.

Note: No experimental confirmation available.
Show »
Length:141
Mass (Da):15,700
Checksum:iFAD4B1B511F91F66
GO

Sequence cautioni

The sequence CAD97897 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti63K → I in BAD96758 (Ref. 6) Curated1
Sequence conflicti237W → V AA sequence (PubMed:1586157).Curated1
Sequence conflicti321C → S AA sequence (PubMed:1586157).Curated1
Sequence conflicti355C → M AA sequence (PubMed:1586157).Curated1
Sequence conflicti366H → R AA sequence (PubMed:1586157).Curated1
Sequence conflicti376 – 378VYD → YVY AA sequence (PubMed:1586157).Curated3

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01693339W → S in PLS. 1 PublicationCorresponds to variant rs104894210dbSNPEnsembl.1
Natural variantiVAR_01903567 – 74Missing in PLS. 1 Publication8
Natural variantiVAR_016934127H → P in PLS. 1 PublicationCorresponds to variant rs104894216dbSNPEnsembl.1
Natural variantiVAR_019036129V → E in PLS. 1 PublicationCorresponds to variant rs760130711dbSNPEnsembl.1
Natural variantiVAR_019037139G → R in PLS. 2 PublicationsCorresponds to variant rs749103588dbSNPEnsembl.1
Natural variantiVAR_016943153I → T.12 PublicationsCorresponds to variant rs217086dbSNPEnsembl.1
Natural variantiVAR_019038236D → Y in PLS. 2 PublicationsCorresponds to variant rs764724707dbSNPEnsembl.1
Natural variantiVAR_009541249V → F in PLS. 2 Publications1
Natural variantiVAR_009542252Q → L in PLS. 2 PublicationsCorresponds to variant rs104894207dbSNPEnsembl.1
Natural variantiVAR_019039272R → H in PLS. 1 PublicationCorresponds to variant rs587777534dbSNPEnsembl.1
Natural variantiVAR_009543272R → P in PLS. 5 PublicationsCorresponds to variant rs587777534dbSNPEnsembl.1
Natural variantiVAR_016935286Q → R in HMS and PLS. 2 PublicationsCorresponds to variant rs104894208dbSNPEnsembl.1
Natural variantiVAR_019040291C → Y in PLS. 1 PublicationCorresponds to variant rs748729285dbSNPEnsembl.1
Natural variantiVAR_039686294Y → H in PLS. 1 Publication1
Natural variantiVAR_019041300G → D in PLS. 2 Publications1
Natural variantiVAR_019042300G → S in PLS. 1 Publication1
Natural variantiVAR_009544301G → S in PLS. 4 PublicationsCorresponds to variant rs104894214dbSNPEnsembl.1
Natural variantiVAR_019043301G → V in PLS. 1 Publication1
Natural variantiVAR_019044304Y → N in PLS. 1 Publication1
Natural variantiVAR_019045312Q → R in PLS. 1 Publication1
Natural variantiVAR_019046319E → G in PLS. 1 Publication1
Natural variantiVAR_009545339R → C in PLS. 5 Publications1
Natural variantiVAR_016944340Y → C in PLS. 2 Publications1
Natural variantiVAR_009546347Y → C in PLS and AP1. 3 PublicationsCorresponds to variant rs104894211dbSNPEnsembl.1
Natural variantiVAR_016945401E → K.1 PublicationCorresponds to variant rs200627023dbSNPEnsembl.1
Natural variantiVAR_027249405H → N in PLS. 1 Publication1
Natural variantiVAR_027250405H → R in PLS. 1 PublicationCorresponds to variant rs151269219dbSNPEnsembl.1
Natural variantiVAR_019047412Y → C in AP1. 1 PublicationCorresponds to variant rs28937571dbSNPEnsembl.1
Natural variantiVAR_016936429W → C in PLS. 1 PublicationCorresponds to variant rs104894215dbSNPEnsembl.1
Natural variantiVAR_019048447E → G in PLS. 2 Publications1
Natural variantiVAR_016946453I → V Rare polymorphism. 1 PublicationCorresponds to variant rs3888798dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_043232107 – 141YKEEG…FTGKK → DVTDFISHLFMQLGTVGIYD LPHLRNKLAMNRRWG in isoform 3. 1 PublicationAdd BLAST35
Alternative sequenceiVSP_039123107 – 137YKEEG…NWACF → DVTDFISHLFMQLGTVGIYD LPHLRNKLVIK in isoform 2. 3 PublicationsAdd BLAST31
Alternative sequenceiVSP_039124138 – 463Missing in isoform 2. 3 PublicationsAdd BLAST326
Alternative sequenceiVSP_043233142 – 463Missing in isoform 3. 1 PublicationAdd BLAST322

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X87212 mRNA. Translation: CAA60671.1.
U79415 Genomic DNA. Translation: AAC51341.1.
AF234263 mRNA. Translation: AAL48191.1.
AF234264 mRNA. Translation: AAL48192.1.
AF254757 mRNA. Translation: AAL48195.1.
AF525032 mRNA. Translation: AAQ08887.1.
AF525033 mRNA. Translation: AAQ08888.1.
AK292117 mRNA. Translation: BAF84806.1.
AK311923 mRNA. Translation: BAG34864.1.
AK223038 mRNA. Translation: BAD96758.1.
BX537913 mRNA. Translation: CAD97897.1. Different initiation.
AC011088 Genomic DNA. No translation available.
CH471185 Genomic DNA. Translation: EAW59364.1.
BC054028 mRNA. Translation: AAH54028.1.
BC100891 mRNA. Translation: AAI00892.1.
BC100892 mRNA. Translation: AAI00893.1.
BC100893 mRNA. Translation: AAI00894.1.
BC100894 mRNA. Translation: AAI00895.1.
BC109386 mRNA. Translation: AAI09387.1.
BC110071 mRNA. Translation: AAI10072.1.
BC113850 mRNA. Translation: AAI13851.1.
BC113897 mRNA. Translation: AAI13898.1.
CCDSiCCDS31654.1. [P53634-2]
CCDS44693.1. [P53634-3]
CCDS8282.1. [P53634-1]
PIRiS23941.
S66504.
RefSeqiNP_001107645.1. NM_001114173.2. [P53634-3]
NP_001805.3. NM_001814.5.
NP_680475.1. NM_148170.4. [P53634-2]
UniGeneiHs.128065.

Genome annotation databases

EnsembliENST00000227266; ENSP00000227266; ENSG00000109861. [P53634-1]
ENST00000524463; ENSP00000432541; ENSG00000109861. [P53634-2]
ENST00000529974; ENSP00000433539; ENSG00000109861. [P53634-3]
GeneIDi1075.
KEGGihsa:1075.
UCSCiuc001pck.5. human. [P53634-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

CTSCbase

CTSC mutation db

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X87212 mRNA. Translation: CAA60671.1.
U79415 Genomic DNA. Translation: AAC51341.1.
AF234263 mRNA. Translation: AAL48191.1.
AF234264 mRNA. Translation: AAL48192.1.
AF254757 mRNA. Translation: AAL48195.1.
AF525032 mRNA. Translation: AAQ08887.1.
AF525033 mRNA. Translation: AAQ08888.1.
AK292117 mRNA. Translation: BAF84806.1.
AK311923 mRNA. Translation: BAG34864.1.
AK223038 mRNA. Translation: BAD96758.1.
BX537913 mRNA. Translation: CAD97897.1. Different initiation.
AC011088 Genomic DNA. No translation available.
CH471185 Genomic DNA. Translation: EAW59364.1.
BC054028 mRNA. Translation: AAH54028.1.
BC100891 mRNA. Translation: AAI00892.1.
BC100892 mRNA. Translation: AAI00893.1.
BC100893 mRNA. Translation: AAI00894.1.
BC100894 mRNA. Translation: AAI00895.1.
BC109386 mRNA. Translation: AAI09387.1.
BC110071 mRNA. Translation: AAI10072.1.
BC113850 mRNA. Translation: AAI13851.1.
BC113897 mRNA. Translation: AAI13898.1.
CCDSiCCDS31654.1. [P53634-2]
CCDS44693.1. [P53634-3]
CCDS8282.1. [P53634-1]
PIRiS23941.
S66504.
RefSeqiNP_001107645.1. NM_001114173.2. [P53634-3]
NP_001805.3. NM_001814.5.
NP_680475.1. NM_148170.4. [P53634-2]
UniGeneiHs.128065.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K3BX-ray2.15A25-143[»]
B231-394[»]
C395-463[»]
2DJFX-ray2.00A25-143[»]
B231-394[»]
C395-463[»]
2DJGX-ray2.05A25-143[»]
B231-394[»]
C395-463[»]
3PDFX-ray1.85A25-463[»]
4CDCX-ray2.40A/D/G/J25-143[»]
B/E/H/K230-394[»]
C/F/I/L395-463[»]
4CDDX-ray2.35A/D25-144[»]
B/E230-394[»]
C/F395-463[»]
4CDEX-ray2.40A/D25-143[»]
B/E230-394[»]
C/F395-463[»]
4CDFX-ray2.20A/D25-144[»]
B/E229-394[»]
C/F395-463[»]
4OELX-ray1.40A25-394[»]
B395-463[»]
4OEMX-ray1.52A25-394[»]
B395-463[»]
ProteinModelPortaliP53634.
SMRiP53634.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107502. 24 interactors.
IntActiP53634. 22 interactors.
MINTiMINT-4655964.
STRINGi9606.ENSP00000227266.

Chemistry databases

BindingDBiP53634.
ChEMBLiCHEMBL2252.
GuidetoPHARMACOLOGYi2344.

Protein family/group databases

MEROPSiC01.070.

PTM databases

iPTMnetiP53634.
PhosphoSitePlusiP53634.
SwissPalmiP53634.

Polymorphism and mutation databases

BioMutaiCTSC.
DMDMi317373330.

Proteomic databases

EPDiP53634.
MaxQBiP53634.
PaxDbiP53634.
PeptideAtlasiP53634.
PRIDEiP53634.
TopDownProteomicsiP53634-1. [P53634-1]

Protocols and materials databases

DNASUi1075.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000227266; ENSP00000227266; ENSG00000109861. [P53634-1]
ENST00000524463; ENSP00000432541; ENSG00000109861. [P53634-2]
ENST00000529974; ENSP00000433539; ENSG00000109861. [P53634-3]
GeneIDi1075.
KEGGihsa:1075.
UCSCiuc001pck.5. human. [P53634-1]

Organism-specific databases

CTDi1075.
DisGeNETi1075.
GeneCardsiCTSC.
HGNCiHGNC:2528. CTSC.
HPAiCAB025364.
MalaCardsiCTSC.
MIMi170650. phenotype.
245000. phenotype.
245010. phenotype.
602365. gene.
neXtProtiNX_P53634.
OpenTargetsiENSG00000109861.
Orphaneti2342. Haim-Munk syndrome.
678. Papillon-Lefevre syndrome.
PharmGKBiPA27028.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1543. Eukaryota.
COG4870. LUCA.
GeneTreeiENSGT00760000118871.
HOGENOMiHOG000127503.
HOVERGENiHBG005248.
InParanoidiP53634.
KOiK01275.
OMAiYDDFLHY.
OrthoDBiEOG091G06TT.
PhylomeDBiP53634.
TreeFamiTF313225.

Enzyme and pathway databases

BioCyciMetaCyc:HS03265-MONOMER.
ZFISH:HS03265-MONOMER.
BRENDAi3.4.14.1. 2681.
ReactomeiR-HSA-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-HSA-2132295. MHC class II antigen presentation.
R-HSA-5694530. Cargo concentration in the ER.
R-HSA-6798695. Neutrophil degranulation.
SABIO-RKP53634.

Miscellaneous databases

ChiTaRSiCTSC. human.
EvolutionaryTraceiP53634.
GeneWikiiCathepsin_C.
GenomeRNAii1075.
PMAP-CutDBP53634.
PROiP53634.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000109861.
ExpressionAtlasiP53634. baseline and differential.
GenevisibleiP53634. HS.

Family and domain databases

Gene3Di2.40.128.80. 1 hit.
InterProiIPR014882. CathepsinC_exc.
IPR033161. DPP_I.
IPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PTHR12411:SF354. PTHR12411:SF354. 1 hit.
PfamiPF08773. CathepsinC_exc. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00645. Pept_C1. 1 hit.
[Graphical view]
SUPFAMiSSF75001. SSF75001. 1 hit.
PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCATC_HUMAN
AccessioniPrimary (citable) accession number: P53634
Secondary accession number(s): A8K7V2
, B5MDD5, Q2HIY8, Q53G93, Q71E75, Q71E76, Q7M4N9, Q7Z3G7, Q7Z5U7, Q8WY99, Q8WYA7, Q8WYA8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 11, 2011
Last modified: November 30, 2016
This is version 179 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 11
    Human chromosome 11: 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

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 one 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.