GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

Caspase-14 (CASP-14) (EC 3.4.22.-) [Cleaved into: Caspase-14 subunit p17, mature form; Caspase-14 subunit p10, mature form; Caspase-14 subunit p20, intermediate form; Caspase-14 subunit p8, intermediate form]

 CASPE_HUMAN             Reviewed;         242 AA.
P31944; O95823; Q3SYC9;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
11-JAN-2001, sequence version 2.
03-JUL-2019, entry version 176.
RecName: Full=Caspase-14;
Short=CASP-14;
EC=3.4.22.-;
Contains:
RecName: Full=Caspase-14 subunit p17, mature form;
Contains:
RecName: Full=Caspase-14 subunit p10, mature form;
Contains:
RecName: Full=Caspase-14 subunit p20, intermediate form;
Contains:
RecName: Full=Caspase-14 subunit p8, intermediate form;
Flags: Precursor;
Name=CASP14;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11062009; DOI=10.1006/bbrc.2000.3698;
Eckhart L., Ban J., Fischer H., Tschachler E.;
"Caspase-14: analysis of gene structure and mRNA expression during
keratinocyte differentiation.";
Biochem. Biophys. Res. Commun. 277:655-659(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=12181750; DOI=10.1038/sj.cdd.4401061;
Pistritto G., Jost M., Srinivasula S.M., Baffa R., Poyet J.-L.,
Kari C., Lazebnik Y., Rodeck U., Alnemri E.S.;
"Expression and transcriptional regulation of caspase-14 in simple and
complex epithelia.";
Cell Death Differ. 9:995-1006(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 68-74; 137-147 AND 154-162.
TISSUE=Keratinocyte;
PubMed=1286667; DOI=10.1002/elps.11501301199;
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
Vandekerckhove J.;
"Microsequences of 145 proteins recorded in the two-dimensional gel
protein database of normal human epidermal keratinocytes.";
Electrophoresis 13:960-969(1992).
[5]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=11175259; DOI=10.1038/sj.cdd.4400785;
Lippens S., Kockx M., Knaapen M., Mortier L., Polakowska R.,
Verheyen A., Garmyn M., Zwijsen A., Formstecher P., Huylebroeck D.,
Vandenabeele P., Declercq W.;
"Epidermal differentiation does not involve the pro-apoptotic
executioner caspases, but is associated with caspase-14 induction and
processing.";
Cell Death Differ. 7:1218-1224(2000).
[6]
PROTEIN SEQUENCE OF 153-163, PROTEOLYTIC PROCESSING, SUBUNIT, AND
SUBCELLULAR LOCATION.
PubMed=12200134; DOI=10.1016/S0006-291X(02)02015-6;
Chien A.J., Presland R.B., Kuechle M.K.;
"Processing of native caspase-14 occurs at an atypical cleavage site
in normal epidermal differentiation.";
Biochem. Biophys. Res. Commun. 296:911-917(2002).
[7]
FUNCTION.
PubMed=15301553; DOI=10.1021/bi0498048;
Mikolajczyk J., Scott F.L., Krajewski S., Sutherlin D.P.,
Salvesen G.S.;
"Activation and substrate specificity of caspase-14.";
Biochemistry 43:10560-10569(2004).
[8]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=15556625; DOI=10.1016/j.febslet.2004.10.046;
Fischer H., Stichenwirth M., Dockal M., Ghannadan M., Buchberger M.,
Bach J., Kapetanopoulos A., Declercq W., Tschachler E., Eckhart L.;
"Stratum corneum-derived caspase-14 is catalytically active.";
FEBS Lett. 577:446-450(2004).
[9]
FUNCTION.
PubMed=16854378; DOI=10.1016/j.bbrc.2006.06.156;
Park K., Kuechle M.K., Choe Y., Craik C.S., Lawrence O.T.,
Presland R.B.;
"Expression and characterization of constitutively active human
caspase-14.";
Biochem. Biophys. Res. Commun. 347:941-948(2006).
[10]
PROTEOLYTIC PROCESSING, SUBUNIT, ACTIVITY REGULATION, AND FUNCTION.
PubMed=19960512; DOI=10.1002/jcb.22425;
Hibino T., Fujita E., Tsuji Y., Nakanishi J., Iwaki H., Katagiri C.,
Momoi T.;
"Purification and characterization of active caspase-14 from human
epidermis and development of the cleavage site-directed antibody.";
J. Cell. Biochem. 109:487-497(2010).
[11]
PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
SUBUNIT, AND FUNCTION.
PubMed=22825846; DOI=10.1074/jbc.M112.357467;
Yamamoto M., Miyai M., Matsumoto Y., Tsuboi R., Hibino T.;
"Kallikrein-related peptidase-7 regulates caspase-14 maturation during
keratinocyte terminal differentiation by generating an intermediate
form.";
J. Biol. Chem. 287:32825-32834(2012).
[12]
INDUCTION, AND FUNCTION.
PubMed=25121097; DOI=10.1155/2014/417986;
Beasley S., El-Sherbiny M., Megyerdi S., El-Shafey S., Choksi K.,
Kaddour-Djebbar I., Sheibani N., Hsu S., Al-Shabrawey M.;
"Caspase-14 expression impairs retinal pigment epithelium barrier
function: potential role in diabetic macular edema.";
Biomed. Res. Int. 2014:417986-417986(2014).
[13]
FUNCTION.
PubMed=24743736; DOI=10.1038/cddis.2014.145;
Yamamoto-Tanaka M., Makino T., Motoyama A., Miyai M., Tsuboi R.,
Hibino T.;
"Multiple pathways are involved in DNA degradation during keratinocyte
terminal differentiation.";
Cell Death Dis. 5:E1181-E1181(2014).
[14]
INVOLVEMENT IN ARCI12.
PubMed=27494380; DOI=10.2340/00015555-2510;
Kirchmeier P., Zimmer A., Bouadjar B., Roesler B., Fischer J.;
"Whole-Exome-Sequencing reveals small deletions in CASP14 in patients
with autosomal recessive inherited ichthyosis.";
Acta Derm. Venereol. 96:102-104(2017).
-!- FUNCTION: Non-apoptotic caspase involved in epidermal
differentiation. Is the predominant caspase in epidermal stratum
corneum (PubMed:15556625). Seems to play a role in keratinocyte
differentiation and is required for cornification. Regulates
maturation of the epidermis by proteolytically processing
filaggrin (By similarity). In vitro has a preference for the
substrate [WY]-X-X-D motif and is active on the synthetic caspase
substrate WEHD-ACF (PubMed:16854378, PubMed:19960512). Involved in
processing of prosaposin in the epidermis (By similarity). May be
involved in retinal pigment epithelium cell barrier function
(PubMed:25121097). Involved in DNA degradation in differentiated
keratinocytes probably by cleaving DFFA/ICAD leading to liberation
of DFFB/CAD (PubMed:24743736). {ECO:0000250|UniProtKB:O89094,
ECO:0000269|PubMed:15301553, ECO:0000269|PubMed:15556625,
ECO:0000269|PubMed:16854378, ECO:0000269|PubMed:19960512,
ECO:0000269|PubMed:22825846, ECO:0000269|PubMed:24743736,
ECO:0000305|PubMed:25121097}.
-!- ACTIVITY REGULATION: Inhibited by caspase-1 inhibitor YVAD-FMK and
the pan-caspase inhibitor VAD-FMK. {ECO:0000269|PubMed:19960512}.
-!- SUBUNIT: Heterodimer of a large and a small subunit, both
processed from the precursor; the mature active form is a p17/p10
dimer and the intermediate form a p20/p8 dimer.
{ECO:0000269|PubMed:12200134, ECO:0000269|PubMed:19960512,
ECO:0000269|PubMed:22825846}.
-!- INTERACTION:
P50222:MEOX2; NbExp=3; IntAct=EBI-2510738, EBI-748397;
P07602:PSAP; NbExp=3; IntAct=EBI-2510738, EBI-716699;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11175259,
ECO:0000269|PubMed:12200134, ECO:0000269|PubMed:22825846}. Nucleus
{ECO:0000269|PubMed:11175259}.
-!- TISSUE SPECIFICITY: Expressed in keratinocytes of adult skin
suprabasal layers (from spinous layers to the stratum granulosum
and stratum corneum) (at protein level). Expressed in
keratinocytes of hair shaft and sebaceous glands (at protein
level). In psoriatic skin only expressed at very low levels
(PubMed:11175259). The p17/10 mature form is expressed in
epidermis stratum corneum, the p20/p8 intermediate form in
epidermis upper granular cells of the stratum granulosum
(PubMed:22825846). {ECO:0000269|PubMed:11175259,
ECO:0000269|PubMed:15556625, ECO:0000269|PubMed:22825846}.
-!- INDUCTION: In undifferentiated keratinocytes under postconfluency
growth conditions (in vitro) (PubMed:11175259). By high glucose in
retinal pigment epithelia cells (PubMed:25121097).
{ECO:0000269|PubMed:11175259, ECO:0000269|PubMed:25121097}.
-!- PTM: Maturation by proteolytic processing appears to be a two-step
process. The precursor is processed by KLK7 to yield the p20/p8
intermediate form which acts on the precursor to yield the p17/p10
mature form (PubMed:22825846). Initially, cleavage between Ile-152
and Lys-153 has been proposed to yield the large and small
subunits of the active enzyme (PubMed:12200134).
{ECO:0000269|PubMed:19960512, ECO:0000269|PubMed:22825846,
ECO:0000305|PubMed:12200134}.
-!- DISEASE: Ichthyosis, congenital, autosomal recessive 12 (ARCI12)
[MIM:617320]: A form of autosomal recessive congenital ichthyosis,
a disorder of keratinization with abnormal differentiation and
desquamation of the epidermis, resulting in abnormal skin scaling
over the whole body. The main skin phenotypes are lamellar
ichthyosis (LI) and non-bullous congenital ichthyosiform
erythroderma (NCIE), although phenotypic overlap within the same
patient or among patients from the same family can occur. Lamellar
ichthyosis is a condition often associated with an embedment in a
collodion-like membrane at birth; skin scales later develop,
covering the entire body surface. Non-bullous congenital
ichthyosiform erythroderma characterized by fine whitish scaling
on an erythrodermal background; larger brownish scales are present
on the buttocks, neck and legs. {ECO:0000269|PubMed:27494380}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- MISCELLANEOUS: Expressed in bacteria requires high concentrations
of kosmotropic salts to be activated (PubMed:15301553). The mature
and the intermediate form differ in activity towards synthetic
caspase substrates: the p17/p10 mature form but not the p20/p8
intermediate form is active on WEHD-MCA; p20/p8 is active on a
number of other caspase substrates without any marked preference
(VEID-AFC, DEVD-AFC, LEVD-AFC and LEHD-AFC) (PubMed:22825846).
{ECO:0000269|PubMed:15301553, ECO:0000269|PubMed:22825846}.
-!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF097874; AAD16173.1; -; mRNA.
EMBL; BC069541; AAH69541.1; -; mRNA.
EMBL; BC103868; AAI03869.1; -; mRNA.
EMBL; BC103869; AAI03870.1; -; mRNA.
CCDS; CCDS12323.1; -.
PIR; JC7517; JC7517.
RefSeq; NP_036246.1; NM_012114.2.
BioGrid; 117116; 35.
IntAct; P31944; 15.
STRING; 9606.ENSP00000393417; -.
BindingDB; P31944; -.
ChEMBL; CHEMBL5991; -.
GuidetoPHARMACOLOGY; 1627; -.
MEROPS; C14.018; -.
iPTMnet; P31944; -.
PhosphoSitePlus; P31944; -.
BioMuta; CASP14; -.
DMDM; 12231007; -.
EPD; P31944; -.
jPOST; P31944; -.
MaxQB; P31944; -.
PaxDb; P31944; -.
PeptideAtlas; P31944; -.
PRIDE; P31944; -.
ProteomicsDB; 54815; -.
TopDownProteomics; P31944; -.
DNASU; 23581; -.
Ensembl; ENST00000427043; ENSP00000393417; ENSG00000105141.
GeneID; 23581; -.
KEGG; hsa:23581; -.
UCSC; uc010dzv.3; human.
CTD; 23581; -.
DisGeNET; 23581; -.
GeneCards; CASP14; -.
GeneReviews; CASP14; -.
HGNC; HGNC:1502; CASP14.
HPA; CAB010059; -.
HPA; HPA027062; -.
MalaCards; CASP14; -.
MIM; 605848; gene.
MIM; 617320; phenotype.
neXtProt; NX_P31944; -.
OpenTargets; ENSG00000105141; -.
PharmGKB; PA26085; -.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00940000162117; -.
HOGENOM; HOG000231878; -.
InParanoid; P31944; -.
KO; K04401; -.
OMA; STMKRDP; -.
OrthoDB; 885776at2759; -.
PhylomeDB; P31944; -.
TreeFam; TF102023; -.
Reactome; R-HSA-6809371; Formation of the cornified envelope.
ChiTaRS; CASP14; human.
GeneWiki; Caspase_14; -.
GenomeRNAi; 23581; -.
PMAP-CutDB; P31944; -.
PRO; PR:P31944; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000105141; Expressed in 62 organ(s), highest expression level in skin of leg.
ExpressionAtlas; P31944; baseline and differential.
Genevisible; P31944; HS.
GO; GO:0005737; C:cytoplasm; IDA:CACAO.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0045095; C:keratin filament; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:CACAO.
GO; GO:0004197; F:cysteine-type endopeptidase activity; TAS:ProtInc.
GO; GO:0097153; F:cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
GO; GO:0006915; P:apoptotic process; IBA:GO_Central.
GO; GO:0070268; P:cornification; TAS:UniProtKB.
GO; GO:0008544; P:epidermis development; TAS:ProtInc.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IBA:GO_Central.
GO; GO:0031424; P:keratinization; TAS:UniProtKB.
CDD; cd00032; CASc; 1.
InterPro; IPR033174; Caspase-14.
InterPro; IPR029030; Caspase-like_dom_sf.
InterPro; IPR033139; Caspase_cys_AS.
InterPro; IPR002398; Pept_C14.
InterPro; IPR002138; Pept_C14_p10.
InterPro; IPR001309; Pept_C14_p20.
InterPro; IPR015917; Pept_C14A.
PANTHER; PTHR10454; PTHR10454; 1.
PANTHER; PTHR10454:SF131; PTHR10454:SF131; 1.
PRINTS; PR00376; IL1BCENZYME.
SMART; SM00115; CASc; 1.
SUPFAM; SSF52129; SSF52129; 1.
PROSITE; PS01122; CASPASE_CYS; 1.
PROSITE; PS50207; CASPASE_P10; 1.
PROSITE; PS50208; CASPASE_P20; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Differentiation;
Direct protein sequencing; Hydrolase; Ichthyosis; Nucleus; Protease;
Reference proteome; Thiol protease; Zymogen.
CHAIN 1 178 Caspase-14 subunit p20, intermediate
form.
/FTId=PRO_0000432793.
PROPEP 1 5 {ECO:0000269|PubMed:19960512}.
/FTId=PRO_0000004652.
CHAIN 6 146 Caspase-14 subunit p17, mature form.
/FTId=PRO_0000432794.
PROPEP 147 152 {ECO:0000269|PubMed:19960512}.
/FTId=PRO_0000432795.
CHAIN 153 242 Caspase-14 subunit p10, mature form.
/FTId=PRO_0000004654.
CHAIN 179 242 Caspase-14 subunit p8, intermediate form.
/FTId=PRO_0000432796.
ACT_SITE 89 89 {ECO:0000250|UniProtKB:P29466}.
ACT_SITE 132 132 {ECO:0000250|UniProtKB:P29466}.
SEQUENCE 242 AA; 27680 MW; E539FB7E8DD808A2 CRC64;
MSNPRSLEEE KYDMSGARLA LILCVTKARE GSEEDLDALE HMFRQLRFES TMKRDPTAEQ
FQEELEKFQQ AIDSREDPVS CAFVVLMAHG REGFLKGEDG EMVKLENLFE ALNNKNCQAL
RAKPKVYIIQ ACRGEQRDPG ETVGGDEIVM VIKDSPQTIP TYTDALHVYS TVEGYIAYRH
DQKGSCFIQT LVDVFTKRKG HILELLTEVT RRMAEAELVQ EGKARKTNPE IQSTLRKRLY
LQ


Related products :

Catalog number Product name Quantity
U1058h CLIA CAD,CAD,Caspase-activated deoxyribonuclease,Caspase-activated DNase,Caspase-activated nuclease,CPAN,DFF2,DFF40,DFF-40,DFFB,DNA fragmentation factor 40 kDa subunit,DNA fragmentation factor subunit 96T
18-661-15034 DNA fragmentation factor subunit beta - EC 3.-.-.-; DNA fragmentation factor 40 kDa subunit; DFF-40; Caspase-activated deoxyribonuclease; Caspase-activated DNase; CAD; Caspase-activated nuclease; CPAN 0.1 mg
18-661-15054 DNA fragmentation factor subunit beta - EC 3.-.-.-; DNA fragmentation factor 40 kDa subunit; DFF-40; Caspase-activated deoxyribonuclease; Caspase-activated DNase; CAD; Caspase-activated nuclease; CPAN 0.1 mg
18-661-15032 DNA fragmentation factor subunit beta - EC 3.-.-.-; DNA fragmentation factor 40 kDa subunit; DFF-40; Caspase-activated deoxyribonuclease; Caspase-activated DNase; CAD; Caspase-activated nuclease; CPAN 0.1 mg
18-661-15033 DNA fragmentation factor subunit beta - EC 3.-.-.-; DNA fragmentation factor 40 kDa subunit; DFF-40; Caspase-activated deoxyribonuclease; Caspase-activated DNase; CAD; Caspase-activated nuclease; CPAN 0.1 mg
18-661-15069 DNA fragmentation factor subunit beta - EC 3.-.-.-; DNA fragmentation factor 40 kDa subunit; DFF-40; Caspase-activated deoxyribonuclease; Caspase-activated DNase; CAD; Caspase-activated nuclease; CPAN 0.1 mg
18-661-15031 DNA fragmentation factor subunit beta - EC 3.-.-.-; DNA fragmentation factor 40 kDa subunit; DFF-40; Caspase-activated deoxyribonuclease; Caspase-activated DNase; CAD; Caspase-activated nuclease; CPAN 0.1 mg
bs-0087P Peptides: active Caspase 3(caspase-3 p12 subunit) Protein Length:12-25 amino acids. 200ug lyophilized
24016 Primary antibody Caspase-10 Antibody, Source Rabbit, Species Reactivity Antibody only recognizes FLICE2 form of caspase-10. 100ug
E1058r ELISA kit CAD,Cad,Caspase-activated deoxyribonuclease,Caspase-activated DNase,DFF-40,Dffb,DNA fragmentation factor 40 kDa subunit,DNA fragmentation factor subunit beta,Rat,Rattus norvegicus 96T
U1058r CLIA CAD,Cad,Caspase-activated deoxyribonuclease,Caspase-activated DNase,DFF-40,Dffb,DNA fragmentation factor 40 kDa subunit,DNA fragmentation factor subunit beta,Rat,Rattus norvegicus 96T
E1058m ELISA CAD,Cad,Caspase-activated deoxyribonuclease,Caspase-activated DNase,DFF-40,Dffb,DNA fragmentation factor 40 kDa subunit,DNA fragmentation factor subunit beta,Mouse,Mus musculus 96T
E1058r ELISA CAD,Cad,Caspase-activated deoxyribonuclease,Caspase-activated DNase,DFF-40,Dffb,DNA fragmentation factor 40 kDa subunit,DNA fragmentation factor subunit beta,Rat,Rattus norvegicus 96T
E1058m ELISA kit CAD,Cad,Caspase-activated deoxyribonuclease,Caspase-activated DNase,DFF-40,Dffb,DNA fragmentation factor 40 kDa subunit,DNA fragmentation factor subunit beta,Mouse,Mus musculus 96T
U1058m CLIA CAD,Cad,Caspase-activated deoxyribonuclease,Caspase-activated DNase,DFF-40,Dffb,DNA fragmentation factor 40 kDa subunit,DNA fragmentation factor subunit beta,Mouse,Mus musculus 96T
E1058h ELISA CAD,CAD,Caspase-activated deoxyribonuclease,Caspase-activated DNase,Caspase-activated nuclease,CPAN,DFF2,DFF40,DFF-40,DFFB,DNA fragmentation factor 40 kDa subunit,DNA fragmentation factor subuni 96T
E1058h ELISA kit CAD,CAD,Caspase-activated deoxyribonuclease,Caspase-activated DNase,Caspase-activated nuclease,CPAN,DFF2,DFF40,DFF-40,DFFB,DNA fragmentation factor 40 kDa subunit,DNA fragmentation factor s 96T
18-783-76408 RABBIT ANTI MOUSE CAD (aa314-329) - EC 3.-.-.-; DNA fragmentation factor 40 kDa subunit; DFF-40; Caspase-activated deoxyribonuclease; Caspase-activated DNase; CAD Polyclonal 0.1 mg
18-783-76333 RABBIT ANTI MOUSE CAD (aa205-222) - EC 3.-.-.-; DNA fragmentation factor 40 kDa subunit; DFF-40; Caspase-activated deoxyribonuclease; Caspase-activated DNase; CAD Polyclonal 0.1 mg
AS03 037 rabbit polyclonal RbcL | Rubisco large subunit, form I and form II 50;
AS03 037-HRP rabbit polyclonal RbcL | Rubisco large subunit, form I and form II 40
AS03 037-200 Antibody: RbcL | Rubisco large subunit, form I and form II (200 200 ul
AS03 037-10 Antibody: RbcL | Rubisco large subunit, form I and form II (10 10
AS03 037 Antibody: RbcL | Rubisco large subunit, form I and form II (100 100
AS03037-200 RbcL | Rubisco large subunit, form I and form II (200ug) 200 ug
Pathways :
WP2359: Parkin-Ubiquitin Proteasomal System pathway
WP1965: VEGF-receptor Signal Transduction
WP88: Toll Like Receptor signaling
WP1711: Trinitrotoluene degradation
WP1566: Citrate cycle (TCA cycle)
WP1626: Benzoate degradation via CoA ligation
WP1655: Geraniol degradation
WP1672: Mismatch repair
WP1694: Pyrimidine metabolism
WP1614: 1- and 2-Methylnaphthalene degradation
WP2292: Chemokine signaling pathway
WP1644: DNA replication
WP1671: Methane metabolism
WP1693: Purine metabolism
WP1718: Vitamin B6 metabolism
WP2272: Pathogenic Escherichia coli infection
WP1634: Butanoate metabolism
WP1663: Homologous recombination
WP1680: Oxidative phosphorylation
WP1502: Mitochondrial biogenesis
WP1984: Integrated Breast Cancer Pathway
WP1358: Selenium metabolism Selenoproteins
WP108: Selenium metabolism/Selenoproteins
WP1328: EBV LMP1 signaling
WP1571: EBV LMP1 signaling

Related Genes :
[CASP14] Caspase-14 (CASP-14) (EC 3.4.22.-) [Cleaved into: Caspase-14 subunit p17, mature form; Caspase-14 subunit p10, mature form; Caspase-14 subunit p20, intermediate form; Caspase-14 subunit p8, intermediate form]
[Casp4 Casp11 Caspl Ich3] Caspase-4 (CASP-4) (EC 3.4.22.64) (Caspase-11) (CASP-11) (Protease ICH-3) [Cleaved into: Caspase-4 subunit p10; Caspase-4 subunit p20]
[Casp3 Cpp32] Caspase-3 (CASP-3) (EC 3.4.22.56) (Apopain) (Cysteine protease CPP32) (CPP-32) (LICE) (Protein Yama) (SREBP cleavage activity 1) (SCA-1) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[csp-2 Y73B6BL.7] Putative inactive caspase B [Cleaved into: Putative inactive caspase B subunit p31; Putative inactive caspase B subunit p17; Putative inactive caspase subunit p14]
[CASP3 CPP32] Caspase-3 (CASP-3) (EC 3.4.22.56) (Apopain) (Cysteine protease CPP32) (CPP-32) (Protein Yama) (SREBP cleavage activity 1) (SCA-1) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[Casp3 Cpp32] Caspase-3 (CASP-3) (EC 3.4.22.56) (Apopain) (Cysteine protease CPP32) (CPP-32) (IRP) (LICE) (Protein Yama) (SREBP cleavage activity 1) (SCA-1) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[CASP3] Caspase-3 (CASP-3) (EC 3.4.22.56) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[CASP3] Caspase-3 (CASP-3) (EC 3.4.22.56) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[Casp7 Lice2 Mch3] Caspase-7 (CASP-7) (EC 3.4.22.60) (Apoptotic protease Mch-3) (Cysteine protease LICE2) [Cleaved into: Caspase-7 subunit p20; Caspase-7 subunit p11]
[CASP8 MCH5] Caspase-8 (CASP-8) (EC 3.4.22.61) (Apoptotic cysteine protease) (Apoptotic protease Mch-5) (CAP4) (FADD-homologous ICE/ced-3-like protease) (FADD-like ICE) (FLICE) (ICE-like apoptotic protease 5) (MORT1-associated ced-3 homolog) (MACH) [Cleaved into: Caspase-8 subunit p18; Caspase-8 subunit p10]
[csp-1 Y48E1B.13] Caspase A (EC 3.4.22.36) [Cleaved into: Caspase A subunit p16; Caspase A subunit p14]
[CASP7 MCH3] Caspase-7 (CASP-7) (EC 3.4.22.60) (Apoptotic protease Mch-3) (CMH-1) (ICE-like apoptotic protease 3) (ICE-LAP3) [Cleaved into: Caspase-7 subunit p20; Caspase-7 subunit p11]
[Dredd DCP2 CG7486] Caspase-8 (EC 3.4.22.61) (Death-related ced-3/NEDD2-like protein) [Cleaved into: Caspase-8 subunit p15; Caspase-8 subunit p10]
[Casp2 Ich1 Nedd-2 Nedd2] Caspase-2 (CASP-2) (EC 3.4.22.55) (Neural precursor cell expressed developmentally down-regulated protein 2) (NEDD-2) (Protease ICH-1) [Cleaved into: Caspase-2 subunit p18; Caspase-2 subunit p13; Caspase-2 subunit p12]
[CASP2 ICH1 NEDD2] Caspase-2 (CASP-2) (EC 3.4.22.55) (Neural precursor cell expressed developmentally down-regulated protein 2) (NEDD-2) (Protease ICH-1) [Cleaved into: Caspase-2 subunit p18; Caspase-2 subunit p13; Caspase-2 subunit p12]
[Casp2 Ich1] Caspase-2 (CASP-2) (EC 3.4.22.55) (Protease ICH-1) [Cleaved into: Caspase-2 subunit p18; Caspase-2 subunit p13; Caspase-2 subunit p12]
[ced-3 C48D1.2] Cell death protein 3 (EC 3.4.22.60) (Caspase ced-3) [Cleaved into: Cell death protein 3 subunit p17; Cell death protein 3 subunit p15; Cell death protein 3 subunit p13]
[CASP4 ICH2] Caspase-4 (CASP-4) (EC 3.4.22.57) (ICE and Ced-3 homolog 2) (ICH-2) (ICE(rel)-II) (Mih1) (Protease TX) [Cleaved into: Caspase-4 subunit 1; Caspase-4 subunit 2]
[Casp6] Caspase-6 (CASP-6) (EC 3.4.22.59) (Apoptotic protease Mch-2) [Cleaved into: Caspase-6 subunit p18; Caspase-6 subunit p11]
[CASP10 MCH4] Caspase-10 (CASP-10) (EC 3.4.22.63) (Apoptotic protease Mch-4) (FAS-associated death domain protein interleukin-1B-converting enzyme 2) (FLICE2) (ICE-like apoptotic protease 4) [Cleaved into: Caspase-10 subunit p23/17; Caspase-10 subunit p12]
[CASP6 MCH2] Caspase-6 (CASP-6) (EC 3.4.22.59) (Apoptotic protease Mch-2) [Cleaved into: Caspase-6 subunit p18; Caspase-6 subunit p11]
[Casp6 Mch2] Caspase-6 (CASP-6) (EC 3.4.22.59) (Apoptotic protease Mch-2) [Cleaved into: Caspase-6 subunit p18; Caspase-6 subunit p11]
[CASP3] Caspase-3 (CASP-3) (EC 3.4.22.56) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[Drice ICE CG7788] Caspase (EC 3.4.22.-) (drICE) [Cleaved into: Caspase subunit p21; Caspase subunit p12]
[CFLAR CASH CASP8AP1 CLARP MRIT] CASP8 and FADD-like apoptosis regulator (Caspase homolog) (CASH) (Caspase-eight-related protein) (Casper) (Caspase-like apoptosis regulatory protein) (CLARP) (Cellular FLICE-like inhibitory protein) (c-FLIP) (FADD-like antiapoptotic molecule 1) (FLAME-1) (Inhibitor of FLICE) (I-FLICE) (MACH-related inducer of toxicity) (MRIT) (Usurpin) [Cleaved into: CASP8 and FADD-like apoptosis regulator subunit p43; CASP8 and FADD-like apoptosis regulator subunit p12]
[CASP3] Caspase-3 (CASP-3) (EC 3.4.22.56) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[AMC9 MCP2F At5g04200 F21E1.120] Metacaspase-9 (AtMC9) (EC 3.4.22.-) [Cleaved into: Metacaspase-9 subunit p20; Metacaspase-9 subunit p10 (Metacaspase 2f) (AtMCP2f)]
[Cflar Cash] CASP8 and FADD-like apoptosis regulator (Caspase homolog) (CASH) (Caspase-eight-related protein) (Casper) (Caspase-like apoptosis regulatory protein) (CLARP) (Cellular FLICE-like inhibitory protein) (c-FLIP) (FADD-like antiapoptotic molecule 1) (FLAME-1) (Inhibitor of FLICE) (I-FLICE) (MACH-related inducer of toxicity) (MRIT) (Usurpin) [Cleaved into: CASP8 and FADD-like apoptosis regulator subunit p43; CASP8 and FADD-like apoptosis regulator subunit p12]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]

Bibliography :