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Q99895 (CTRC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chymotrypsin-C

EC=3.4.21.2
Alternative name(s):
Caldecrin
Gene names
Name:CTRC
Synonyms:CLCR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length268 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulates activation and degradation of trypsinogens and procarboxypeptidases by targeting specific cleavage sites within their zymogen precursors. Has chymotrypsin-type protease activity and hypocalcemic activity. Ref.8

Catalytic activity

Preferential cleavage: Leu-|-Xaa, Tyr-|-Xaa, Phe-|-Xaa, Met-|-Xaa, Trp-|-Xaa, Gln-|-Xaa, Asn-|-Xaa.

Tissue specificity

Pancreas.

Involvement in disease

Pancreatitis, hereditary (PCTT) [MIM:167800]: A disease characterized by pancreas inflammation, permanent destruction of the pancreatic parenchyma, maldigestion, and severe abdominal pain attacks.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Loss-of-function CTRC variants predispose to pancreatitis by diminishing its protective trypsin-degrading activity (Ref.10). They cause loss of function by one or more of three mechanisms: reduced secretion, catalytic defect and increased degradation by trypsin (Ref.14). Ref.9 Ref.10 Ref.13 Ref.14

Sequence similarities

Belongs to the peptidase S1 family. Elastase subfamily.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processproteolysis

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functionpeptidase activity

Traceable author statement Ref.1. Source: ProtInc

serine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Propeptide17 – 2913Activation peptide
PRO_0000027713
Chain30 – 268239Chymotrypsin-C
PRO_0000027714

Regions

Domain30 – 267238Peptidase S1

Sites

Active site741Charge relay system By similarity
Active site1211Charge relay system By similarity
Active site2161Charge relay system By similarity

Amino acid modifications

Glycosylation251N-linked (GlcNAc...) Potential
Glycosylation521N-linked (GlcNAc...) Potential
Glycosylation2261N-linked (GlcNAc...) Potential
Disulfide bond17 ↔ 141 Ref.8
Disulfide bond59 ↔ 75 Ref.8
Disulfide bond155 ↔ 222 Ref.8
Disulfide bond186 ↔ 202 Ref.8
Disulfide bond212 ↔ 243 Ref.8

Natural variations

Natural variant181G → R Found in a patient with chronic pancreatitis; unknown pathological significance; catalytic activity comparable to that of wild type; the mutant undergoes proteolytic degradation during trypsin-mediated activation. Ref.14
Corresponds to variant rs200576965 [ dbSNP | Ensembl ].
VAR_070520
Natural variant291R → Q Found in patients with chronic pancreatitis; unknown pathological significance. Ref.12
VAR_070521
Natural variant321G → V in PCTT; associated with disease susceptibility; highly reduced catalytic efficiency. Ref.14
VAR_070522
Natural variant351D → H. Ref.10
VAR_043516
Natural variant351D → N. Ref.10
Corresponds to variant rs184977421 [ dbSNP | Ensembl ].
VAR_043517
Natural variant351D → Y Found in a patient with chronic pancreatitis; unknown pathological significance; catalytic activity comparable to that of wild type. Ref.14
VAR_070523
Natural variant371R → Q Rare variant resulting in normal secretion and activity. Ref.10
Corresponds to variant rs145868278 [ dbSNP | Ensembl ].
VAR_043518
Natural variant481Q → R Rare variant that may be associated with susceptibility to pancreatitis; results in markedly reduced protein secretion. Ref.10 Ref.13 Ref.14
VAR_043519
Natural variant611G → R Found in a patient with chronic pancreatitis; unknown pathological significance; the mutant is not secreted. Ref.14
VAR_070524
Natural variant731A → T in PCTT; associated with susceptibility to disease; results in markedly reduced protein secretion. Ref.9 Ref.10 Ref.13 Ref.14
VAR_043520
Natural variant801R → W. Ref.1
VAR_010928
Natural variant1511K → N Found in a patient with chronic pancreatitis; unknown pathological significance.
VAR_070525
Natural variant1551C → Y in PCTT; associated with susceptibility to disease; the mutant is not secreted. Ref.9 Ref.14
VAR_070526
Natural variant1621R → H Rare variant; found in a patient with chronic pancreatitis; unknown pathological significance. Ref.9
VAR_070527
Natural variant1721K → E. Ref.9 Ref.10 Ref.13
Corresponds to variant rs34949635 [ dbSNP | Ensembl ].
VAR_043521
Natural variant1781Q → R in PCTT; associated with disease susceptibility; impaired catalytic activity. Ref.14
Corresponds to variant rs200678111 [ dbSNP | Ensembl ].
VAR_070528
Natural variant2001M → V Rare variant; found in a patient with chronic pancreatitis; unknown pathological significance. Ref.9
Corresponds to variant rs146235499 [ dbSNP | Ensembl ].
VAR_070529
Natural variant2091I → M. Ref.12
VAR_070530
Natural variant2171G → R in PCTT; associated with susceptibility to disease; results in markedly reduced protein secretion and loss of activity. Ref.9 Ref.10 Ref.14
VAR_043522
Natural variant2171G → S in PCTT; associated with susceptibility to disease; reduced protein secretion; impaired catalytic activity. Ref.9 Ref.10 Ref.14
Corresponds to variant rs202058123 [ dbSNP | Ensembl ].
VAR_043523
Natural variant2181G → S. Ref.10
VAR_043524
Natural variant2201L → R Rare variant that results in impaired protein secretion. Ref.10 Ref.14
VAR_043525
Natural variant2251E → A. Ref.10
VAR_043526
Natural variant2251E → K Found in a patient with chronic pancreatitis; unknown pathological significance. Ref.11
VAR_070531
Natural variant2271G → S. Ref.14
VAR_070532
Natural variant2351V → I in PCTT; associated with susceptibility to disease; slightly reduced activity. Ref.9 Ref.10 Ref.13 Ref.14
Corresponds to variant rs140993290 [ dbSNP | Ensembl ].
VAR_043527
Natural variant2391S → A Found in patients with chronic pancreatitis; unknown pathological significance. Ref.12
VAR_070533
Natural variant2391S → C Found in patients with chronic pancreatitis; unknown pathological significance. Ref.12
VAR_070534
Natural variant2461R → C. Ref.13
Corresponds to variant rs200412314 [ dbSNP | Ensembl ].
VAR_070535
Natural variant247 – 2548Missing in PCTT; associated with disease susceptibility; results in reduced protein secretion and loss of activity.
VAR_070536
Natural variant2471K → E Found in patients with chronic pancreatitis; unknown pathological significance. Ref.12
VAR_070537
Natural variant2491P → L in PCTT; associated with disease susceptibility; results in reduced protein secretion and loss of activity. Ref.10 Ref.14
Corresponds to variant rs142560329 [ dbSNP | Ensembl ].
VAR_043528
Natural variant2501V → E in PCTT; associated with disease susceptibility; results in altered enzyme specificity and loss of activity. Ref.14
VAR_070538
Natural variant2541R → Q Found in a patient with chronic pancreatitis; unknown pathological significance; mutant protein secretion, activity and trypsin-mediated degradation are comparable to those of wild-type. Ref.11 Ref.14
VAR_070539
Natural variant2541R → W in PCTT; associated with susceptibility to disease; results in reduced secretion; normal activity; the mutant undergoes proteolytic degradation during trypsin-mediated activation. Ref.9 Ref.10 Ref.12 Ref.13 Ref.14
Corresponds to variant rs121909293 [ dbSNP | Ensembl ].
VAR_043529
Natural variant2571A → T Found in patients with chronic pancreatitis; unknown pathological significance. Ref.13
Corresponds to variant rs200406696 [ dbSNP | Ensembl ].
VAR_070540
Natural variant2601D → N. Ref.10
VAR_043530
Natural variant2631N → S Found in a patient with chronic pancreatitis; unknown pathological significance. Ref.11
VAR_070541

Experimental info

Sequence conflict161S → T in AAB47104. Ref.1
Sequence conflict521N → D in CAA74031. Ref.6

Secondary structure

............................................. 268
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q99895 [UniParc].

Last modified June 1, 2001. Version 2.
Checksum: 460BF33B4A96516F

FASTA26829,484
        10         20         30         40         50         60 
MLGITVLAAL LACASSCGVP SFPPNLSARV VGGEDARPHS WPWQISLQYL KNDTWRHTCG 

        70         80         90        100        110        120 
GTLIASNFVL TAAHCISNTR TYRVAVGKNN LEVEDEEGSL FVGVDTIHVH KRWNALLLRN 

       130        140        150        160        170        180 
DIALIKLAEH VELSDTIQVA CLPEKDSLLP KDYPCYVTGW GRLWTNGPIA DKLQQGLQPV 

       190        200        210        220        230        240 
VDHATCSRID WWGFRVKKTM VCAGGDGVIS ACNGDSGGPL NCQLENGSWE VFGIVSFGSR 

       250        260 
RGCNTRKKPV VYTRVSAYID WINEKMQL 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and expression of human caldecrin."
Tomomura A., Akiyama M., Itoh H., Yoshino I., Tomomura M., Nishii Y., Noikura T., Saheki T.
FEBS Lett. 386:26-28(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT TRP-80.
Tissue: Pancreas.
[2]"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. expand/collapse author list , 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: Urinary bladder.
[3]"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. expand/collapse author list , 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].
[4]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. expand/collapse author list , 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].
[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].
Tissue: Pancreas.
[6]"A human pancreatic chymotrypsin: biochemical and molecular characterization."
Sziegoleit A.
Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 17-268.
Tissue: Pancreas.
[7]"Caldecrin is a novel-type serine protease expressed in pancreas, but its homologue, elastase IV, is an artifact during cloning derived from caldecrin gene."
Yoshino-Yasuda I., Kobayashi K., Akiyama M., Itoh H., Tomomura A., Saheki T.
J. Biochem. 123:546-554(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[8]"Long-range electrostatic complementarity governs substrate recognition by human chymotrypsin C, a key regulator of digestive enzyme activation."
Batra J., Szabo A., Caulfield T.R., Soares A.S., Sahin-Toth M., Radisky E.S.
J. Biol. Chem. 288:9848-9859(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 17-268 IN COMPLEX WITH INHIBITOR, FUNCTION, DISULFIDE BONDS.
[9]"Association of rare chymotrypsinogen C (CTRC) gene variations in patients with idiopathic chronic pancreatitis."
Masson E., Chen J.M., Scotet V., Le Marechal C., Ferec C.
Hum. Genet. 123:83-91(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PCTT THR-73; TYR-155; SER-217; ARG-217; ILE-235; 247-LYS--ARG-254 DEL AND TRP-254, VARIANTS HIS-162; GLU-172 AND VAL-200.
[10]"Chymotrypsin C (CTRC) variants that diminish activity or secretion are associated with chronic pancreatitis."
Rosendahl J., Witt H., Szmola R., Bhatia E., Ozsvari B., Landt O., Schulz H.-U., Gress T.M., Pfuetzer R., Loehr M., Kovacs P., Blueher M., Stumvoll M., Choudhuri G., Hegyi P., te Morsche R.H.M., Drenth J.P.H., Truninger K. expand/collapse author list , Macek M. Jr., Puhl G., Witt U., Schmidt H., Buening C., Ockenga J., Kage A., Groneberg D.A., Nickel R., Berg T., Wiedenmann B., Boedeker H., Keim V., Moessner J., Teich N., Sahin-Toth M.
Nat. Genet. 40:78-82(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PCTT THR-73; SER-217; ARG-217; ILE-235 AND TRP-254, VARIANTS HIS-35; ASN-35; GLN-37; ARG-48; GLU-172; SER-218; ARG-220; ALA-225; LEU-249 AND ASN-260, CHARACTERIZATION OF VARIANTS PCTT THR-73; SER-217; ILE-235 AND TRP-254, CHARACTERIZATION OF VARIANTS GLN-37 AND ARG-48.
[11]"Association of novel chymotrypsin C gene variations and haplotypes in patients with chronic pancreatitis in Chinese in Taiwan."
Chang M.C., Chang Y.T., Wei S.C., Liang P.C., Jan I.S., Su Y.N., Kuo C.H., Wong J.M.
Pancreatology 9:287-292(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LYS-225; GLN-254 AND SER-263.
[12]"Identification of novel missense CTRC variants in Japanese patients with chronic pancreatitis."
Masamune A., Nakano E., Kume K., Kakuta Y., Ariga H., Shimosegawa T.
Gut 62:653-654(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLN-29; MET-209; ALA-239; CYS-239; GLU-247 AND TRP-254.
[13]"Comprehensive screening of chymotrypsin C (CTRC) gene in tropical calcific pancreatitis identifies novel variants."
Paliwal S., Bhaskar S., Mani K.R., Reddy D.N., Rao G.V., Singh S.P., Thomas V., Chandak G.R.
Gut 62:1602-1606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ARG-48; GLU-172; CYS-246 AND THR-257, VARIANTS PCTT THR-73; ILE-235 AND TRP-254.
[14]"Comprehensive functional analysis of chymotrypsin C (CTRC) variants reveals distinct loss-of-function mechanisms associated with pancreatitis risk."
Beer S., Zhou J., Szabo A., Keiles S., Chandak G.R., Witt H., Sahin-Toth M.
Gut 62:1616-1624(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ARG-18; TYR-35 AND SER-227, VARIANTS PCTT ARG-178 AND GLU-250, CHARACTERIZATION OF VARIANTS ARG-18; TYR-35; ARG-48; ARG-61; ARG-220 AND GLN-254, CHARACTERIZATION OF VARIANTS PCTT VAL-32; THR-73; TYR-155; ARG-178; ARG-217; SER-217; ILE-235; 247-LYS--ARG-254 DEL; LEU-249; GLU-250 AND TRP-254.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S82198 mRNA. Translation: AAB47104.2. Sequence problems.
AK289447 mRNA. Translation: BAF82136.1.
AL031283 Genomic DNA. Translation: CAB77355.1.
CH471167 Genomic DNA. Translation: EAW51726.1.
BC015118 mRNA. Translation: AAH15118.1.
Y13697 mRNA. Translation: CAA74031.1.
CCDSCCDS156.1.
PIRS68825.
S68826.
RefSeqNP_009203.2. NM_007272.2.
UniGeneHs.631869.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4H4FX-ray1.90A30-268[»]
Q17-26[»]
ProteinModelPortalQ99895.
SMRQ99895. Positions 30-268.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116458. 2 interactions.
STRING9606.ENSP00000365116.

Chemistry

BindingDBQ99895.
ChEMBLCHEMBL2386.

Protein family/group databases

MEROPSS01.157.

Polymorphism databases

DMDM14194504.

Proteomic databases

PaxDbQ99895.
PRIDEQ99895.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375949; ENSP00000365116; ENSG00000162438.
GeneID11330.
KEGGhsa:11330.
UCSCuc001awi.1. human.

Organism-specific databases

CTD11330.
GeneCardsGC01P015764.
HGNCHGNC:2523. CTRC.
HPAHPA046920.
MIM167800. phenotype.
601405. gene.
neXtProtNX_Q99895.
Orphanet676. Hereditary chronic pancreatitis.
103918. Tropical pancreatitis.
PharmGKBPA27024.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000251820.
HOVERGENHBG013304.
InParanoidQ99895.
KOK01311.
OMAGKNNLEV.
OrthoDBEOG75B84T.
PhylomeDBQ99895.
TreeFamTF330455.

Enzyme and pathway databases

BRENDA3.4.21.2. 2681.

Gene expression databases

ArrayExpressQ99895.
BgeeQ99895.
CleanExHS_CTRC.
GenevestigatorQ99895.

Family and domain databases

InterProIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiChymotrypsin-C.
GenomeRNAi11330.
NextBio43039.
PROQ99895.
SOURCESearch...

Entry information

Entry nameCTRC_HUMAN
AccessionPrimary (citable) accession number: Q99895
Secondary accession number(s): A8K082, O00765, Q9NUH5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM