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Q99895

- CTRC_HUMAN

UniProt

Q99895 - CTRC_HUMAN

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Protein
Chymotrypsin-C
Gene
CTRC, CLCR
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei74 – 741Charge relay system By similarity
Active sitei121 – 1211Charge relay system By similarity
Active sitei216 – 2161Charge relay system By similarity

GO - Molecular functioni

  1. peptidase activity Source: ProtInc
  2. serine-type endopeptidase activity Source: InterPro

GO - Biological processi

  1. proteolysis Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Enzyme and pathway databases

BRENDAi3.4.21.2. 2681.

Protein family/group databases

MEROPSiS01.157.

Names & Taxonomyi

Protein namesi
Recommended name:
Chymotrypsin-C (EC:3.4.21.2)
Alternative name(s):
Caldecrin
Gene namesi
Name:CTRC
Synonyms:CLCR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:2523. CTRC.

Pathology & Biotechi

Involvement in diseasei

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 (1 Publication). They cause loss of function by one or more of three mechanisms: reduced secretion, catalytic defect and increased degradation by trypsin (1 Publication).4 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti32 – 321G → V in PCTT; associated with disease susceptibility; highly reduced catalytic efficiency. 1 Publication
VAR_070522
Natural varianti73 – 731A → T in PCTT; associated with susceptibility to disease; results in markedly reduced protein secretion. 4 Publications
VAR_043520
Natural varianti155 – 1551C → Y in PCTT; associated with susceptibility to disease; the mutant is not secreted. 2 Publications
VAR_070526
Natural varianti178 – 1781Q → R in PCTT; associated with disease susceptibility; impaired catalytic activity. 1 Publication
Corresponds to variant rs200678111 [ dbSNP | Ensembl ].
VAR_070528
Natural varianti217 – 2171G → R in PCTT; associated with susceptibility to disease; results in markedly reduced protein secretion and loss of activity. 3 Publications
VAR_043522
Natural varianti217 – 2171G → S in PCTT; associated with susceptibility to disease; reduced protein secretion; impaired catalytic activity. 3 Publications
Corresponds to variant rs202058123 [ dbSNP | Ensembl ].
VAR_043523
Natural varianti235 – 2351V → I in PCTT; associated with susceptibility to disease; slightly reduced activity. 4 Publications
Corresponds to variant rs140993290 [ dbSNP | Ensembl ].
VAR_043527
Natural varianti247 – 2548Missing in PCTT; associated with disease susceptibility; results in reduced protein secretion and loss of activity.
VAR_070536
Natural varianti249 – 2491P → L in PCTT; associated with disease susceptibility; results in reduced protein secretion and loss of activity. 2 Publications
Corresponds to variant rs142560329 [ dbSNP | Ensembl ].
VAR_043528
Natural varianti250 – 2501V → E in PCTT; associated with disease susceptibility; results in altered enzyme specificity and loss of activity. 1 Publication
VAR_070538
Natural varianti254 – 2541R → W in PCTT; associated with susceptibility to disease; results in reduced secretion; normal activity; the mutant undergoes proteolytic degradation during trypsin-mediated activation. 5 Publications
Corresponds to variant rs121909293 [ dbSNP | Ensembl ].
VAR_043529

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi167800. phenotype.
Orphaneti676. Hereditary chronic pancreatitis.
103918. Tropical pancreatitis.
PharmGKBiPA27024.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616 Reviewed prediction
Add
BLAST
Propeptidei17 – 2913Activation peptide
PRO_0000027713Add
BLAST
Chaini30 – 268239Chymotrypsin-C
PRO_0000027714Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi17 ↔ 1411 Publication
Glycosylationi25 – 251N-linked (GlcNAc...) Reviewed prediction
Glycosylationi52 – 521N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi59 ↔ 751 Publication
Disulfide bondi155 ↔ 2221 Publication
Disulfide bondi186 ↔ 2021 Publication
Disulfide bondi212 ↔ 2431 Publication
Glycosylationi226 – 2261N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiQ99895.
PRIDEiQ99895.

Expressioni

Tissue specificityi

Pancreas.

Gene expression databases

ArrayExpressiQ99895.
BgeeiQ99895.
CleanExiHS_CTRC.
GenevestigatoriQ99895.

Organism-specific databases

HPAiHPA046920.

Interactioni

Protein-protein interaction databases

BioGridi116458. 2 interactions.
STRINGi9606.ENSP00000365116.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi44 – 518
Beta strandi54 – 6512
Beta strandi68 – 714
Helixi73 – 753
Beta strandi82 – 876
Beta strandi100 – 1023
Beta strandi104 – 1096
Turni115 – 1173
Beta strandi123 – 1297
Beta strandi155 – 1606
Beta strandi162 – 1643
Beta strandi174 – 1774
Helixi183 – 1864
Turni189 – 1924
Helixi193 – 1953
Beta strandi200 – 2034
Beta strandi206 – 2105
Beta strandi219 – 2235
Beta strandi229 – 23911
Beta strandi242 – 2454
Beta strandi250 – 2545
Helixi255 – 2573
Helixi259 – 2657

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4H4FX-ray1.90A30-268[»]
Q17-26[»]
ProteinModelPortaliQ99895.
SMRiQ99895. Positions 30-268.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 267238Peptidase S1
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5640.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiQ99895.
KOiK01311.
OMAiGKNNLEV.
OrthoDBiEOG75B84T.
PhylomeDBiQ99895.
TreeFamiTF330455.

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q99895-1 [UniParc]FASTAAdd to Basket

« Hide

MLGITVLAAL LACASSCGVP SFPPNLSARV VGGEDARPHS WPWQISLQYL    50
KNDTWRHTCG GTLIASNFVL TAAHCISNTR TYRVAVGKNN LEVEDEEGSL 100
FVGVDTIHVH KRWNALLLRN DIALIKLAEH VELSDTIQVA CLPEKDSLLP 150
KDYPCYVTGW GRLWTNGPIA DKLQQGLQPV VDHATCSRID WWGFRVKKTM 200
VCAGGDGVIS ACNGDSGGPL NCQLENGSWE VFGIVSFGSR RGCNTRKKPV 250
VYTRVSAYID WINEKMQL 268
Length:268
Mass (Da):29,484
Last modified:June 1, 2001 - v2
Checksum:i460BF33B4A96516F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti18 – 181G → 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. 1 Publication
Corresponds to variant rs200576965 [ dbSNP | Ensembl ].
VAR_070520
Natural varianti29 – 291R → Q Found in patients with chronic pancreatitis; unknown pathological significance. 1 Publication
VAR_070521
Natural varianti32 – 321G → V in PCTT; associated with disease susceptibility; highly reduced catalytic efficiency. 1 Publication
VAR_070522
Natural varianti35 – 351D → H.1 Publication
VAR_043516
Natural varianti35 – 351D → N.1 Publication
Corresponds to variant rs184977421 [ dbSNP | Ensembl ].
VAR_043517
Natural varianti35 – 351D → Y Found in a patient with chronic pancreatitis; unknown pathological significance; catalytic activity comparable to that of wild type. 1 Publication
VAR_070523
Natural varianti37 – 371R → Q Rare variant resulting in normal secretion and activity. 1 Publication
Corresponds to variant rs145868278 [ dbSNP | Ensembl ].
VAR_043518
Natural varianti48 – 481Q → R Rare variant that may be associated with susceptibility to pancreatitis; results in markedly reduced protein secretion. 3 Publications
VAR_043519
Natural varianti61 – 611G → R Found in a patient with chronic pancreatitis; unknown pathological significance; the mutant is not secreted. 1 Publication
VAR_070524
Natural varianti73 – 731A → T in PCTT; associated with susceptibility to disease; results in markedly reduced protein secretion. 4 Publications
VAR_043520
Natural varianti80 – 801R → W.1 Publication
VAR_010928
Natural varianti151 – 1511K → N Found in a patient with chronic pancreatitis; unknown pathological significance.
VAR_070525
Natural varianti155 – 1551C → Y in PCTT; associated with susceptibility to disease; the mutant is not secreted. 2 Publications
VAR_070526
Natural varianti162 – 1621R → H Rare variant; found in a patient with chronic pancreatitis; unknown pathological significance. 1 Publication
VAR_070527
Natural varianti172 – 1721K → E.3 Publications
Corresponds to variant rs34949635 [ dbSNP | Ensembl ].
VAR_043521
Natural varianti178 – 1781Q → R in PCTT; associated with disease susceptibility; impaired catalytic activity. 1 Publication
Corresponds to variant rs200678111 [ dbSNP | Ensembl ].
VAR_070528
Natural varianti200 – 2001M → V Rare variant; found in a patient with chronic pancreatitis; unknown pathological significance. 1 Publication
Corresponds to variant rs146235499 [ dbSNP | Ensembl ].
VAR_070529
Natural varianti209 – 2091I → M.1 Publication
VAR_070530
Natural varianti217 – 2171G → R in PCTT; associated with susceptibility to disease; results in markedly reduced protein secretion and loss of activity. 3 Publications
VAR_043522
Natural varianti217 – 2171G → S in PCTT; associated with susceptibility to disease; reduced protein secretion; impaired catalytic activity. 3 Publications
Corresponds to variant rs202058123 [ dbSNP | Ensembl ].
VAR_043523
Natural varianti218 – 2181G → S.1 Publication
VAR_043524
Natural varianti220 – 2201L → R Rare variant that results in impaired protein secretion. 2 Publications
VAR_043525
Natural varianti225 – 2251E → A.1 Publication
VAR_043526
Natural varianti225 – 2251E → K Found in a patient with chronic pancreatitis; unknown pathological significance. 1 Publication
VAR_070531
Natural varianti227 – 2271G → S.1 Publication
VAR_070532
Natural varianti235 – 2351V → I in PCTT; associated with susceptibility to disease; slightly reduced activity. 4 Publications
Corresponds to variant rs140993290 [ dbSNP | Ensembl ].
VAR_043527
Natural varianti239 – 2391S → A Found in patients with chronic pancreatitis; unknown pathological significance. 1 Publication
VAR_070533
Natural varianti239 – 2391S → C Found in patients with chronic pancreatitis; unknown pathological significance. 1 Publication
VAR_070534
Natural varianti246 – 2461R → C.1 Publication
Corresponds to variant rs200412314 [ dbSNP | Ensembl ].
VAR_070535
Natural varianti247 – 2548Missing in PCTT; associated with disease susceptibility; results in reduced protein secretion and loss of activity.
VAR_070536
Natural varianti247 – 2471K → E Found in patients with chronic pancreatitis; unknown pathological significance. 1 Publication
VAR_070537
Natural varianti249 – 2491P → L in PCTT; associated with disease susceptibility; results in reduced protein secretion and loss of activity. 2 Publications
Corresponds to variant rs142560329 [ dbSNP | Ensembl ].
VAR_043528
Natural varianti250 – 2501V → E in PCTT; associated with disease susceptibility; results in altered enzyme specificity and loss of activity. 1 Publication
VAR_070538
Natural varianti254 – 2541R → 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. 2 Publications
VAR_070539
Natural varianti254 – 2541R → W in PCTT; associated with susceptibility to disease; results in reduced secretion; normal activity; the mutant undergoes proteolytic degradation during trypsin-mediated activation. 5 Publications
Corresponds to variant rs121909293 [ dbSNP | Ensembl ].
VAR_043529
Natural varianti257 – 2571A → T Found in patients with chronic pancreatitis; unknown pathological significance. 1 Publication
Corresponds to variant rs200406696 [ dbSNP | Ensembl ].
VAR_070540
Natural varianti260 – 2601D → N.1 Publication
VAR_043530
Natural varianti263 – 2631N → S Found in a patient with chronic pancreatitis; unknown pathological significance. 1 Publication
VAR_070541

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161S → T in AAB47104. 1 Publication
Sequence conflicti52 – 521N → D in CAA74031. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS156.1.
PIRiS68825.
S68826.
RefSeqiNP_009203.2. NM_007272.2.
UniGeneiHs.631869.

Genome annotation databases

EnsembliENST00000375949; ENSP00000365116; ENSG00000162438.
GeneIDi11330.
KEGGihsa:11330.
UCSCiuc001awi.1. human.

Polymorphism databases

DMDMi14194504.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS156.1.
PIRi S68825.
S68826.
RefSeqi NP_009203.2. NM_007272.2.
UniGenei Hs.631869.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4H4F X-ray 1.90 A 30-268 [» ]
Q 17-26 [» ]
ProteinModelPortali Q99895.
SMRi Q99895. Positions 30-268.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116458. 2 interactions.
STRINGi 9606.ENSP00000365116.

Chemistry

BindingDBi Q99895.
ChEMBLi CHEMBL2386.

Protein family/group databases

MEROPSi S01.157.

Polymorphism databases

DMDMi 14194504.

Proteomic databases

PaxDbi Q99895.
PRIDEi Q99895.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000375949 ; ENSP00000365116 ; ENSG00000162438 .
GeneIDi 11330.
KEGGi hsa:11330.
UCSCi uc001awi.1. human.

Organism-specific databases

CTDi 11330.
GeneCardsi GC01P015764.
HGNCi HGNC:2523. CTRC.
HPAi HPA046920.
MIMi 167800. phenotype.
601405. gene.
neXtProti NX_Q99895.
Orphaneti 676. Hereditary chronic pancreatitis.
103918. Tropical pancreatitis.
PharmGKBi PA27024.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5640.
HOGENOMi HOG000251820.
HOVERGENi HBG013304.
InParanoidi Q99895.
KOi K01311.
OMAi GKNNLEV.
OrthoDBi EOG75B84T.
PhylomeDBi Q99895.
TreeFami TF330455.

Enzyme and pathway databases

BRENDAi 3.4.21.2. 2681.

Miscellaneous databases

GeneWikii Chymotrypsin-C.
GenomeRNAii 11330.
NextBioi 43039.
PROi Q99895.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q99895.
Bgeei Q99895.
CleanExi HS_CTRC.
Genevestigatori Q99895.

Family and domain databases

InterProi IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF00089. Trypsin. 1 hit.
[Graphical view ]
PRINTSi PR00722. CHYMOTRYPSIN.
SMARTi SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 1 hit.
PROSITEi PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.
    , 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.
    , 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. 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. 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.

Entry informationi

Entry nameiCTRC_HUMAN
AccessioniPrimary (citable) accession number: Q99895
Secondary accession number(s): A8K082, O00765, Q9NUH5
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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