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Caspase-5 (CASP-5) (EC 3.4.22.58) (ICE(rel)-III) (Protease ICH-3) (Protease TY) [Cleaved into: Caspase-5 subunit p20; Caspase-5 subunit p10]

 CASP5_HUMAN             Reviewed;         434 AA.
P51878; B4DKP5; Q0QVY7; Q0QVY8; Q0QVZ0; Q0QVZ1; Q0QVZ2; Q14DD6;
Q1HBJ3; Q6DJV7;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
20-APR-2010, sequence version 3.
13-FEB-2019, entry version 175.
RecName: Full=Caspase-5;
Short=CASP-5;
EC=3.4.22.58;
AltName: Full=ICE(rel)-III;
AltName: Full=Protease ICH-3;
AltName: Full=Protease TY;
Contains:
RecName: Full=Caspase-5 subunit p20;
Contains:
RecName: Full=Caspase-5 subunit p10;
Flags: Precursor;
Name=CASP5; Synonyms=ICH3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5), ALTERNATIVE
SPLICING (ISOFORM 6), VARIANTS ALA-106 AND VAL-334, AND INDUCTION BY
LPS.
PubMed=16893518; DOI=10.1016/j.bbrc.2006.07.104;
Eckhart L., Kittel C., Gawlas S., Gruber F., Mildner M., Jilma B.,
Tschachler E.;
"Identification of a novel exon encoding the amino-terminus of the
predominant caspase-5 variants.";
Biochem. Biophys. Res. Commun. 348:682-688(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
ALA-106.
TISSUE=Colon;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 6-434 (ISOFORM 1), AND VARIANTS ALA-106
AND VAL-334.
PubMed=7797592; DOI=10.1074/jbc.270.26.15870;
Munday N.A., Vaillancourt J.P., Ali A., Casano F.J., Miller D.K.,
Molineaux S.M., Yamin T.-T., Yu V.L., Nicholson D.W.;
"Molecular cloning and pro-apoptotic activity of ICErelII and
ICErelIII, members of the ICE/CED-3 family of cysteine proteases.";
J. Biol. Chem. 270:15870-15876(1995).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-434 (ISOFORM 1), AND
VARIANTS LEU-29; ALA-106; HIS-168; LEU-217 AND VAL-334.
TISSUE=Colon;
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 37-434, AND VARIANT ALA-106.
TISSUE=Placenta, and Spleen;
PubMed=8617266; DOI=10.1111/j.1432-1033.1996.t01-1-00207.x;
Faucheu C., Blanchet A.-M., Collard-Dutilleul V., Lalanne J.-L.,
Diu-Hercend A.;
"Identification of a cysteine protease closely related to interleukin-
1 beta-converting enzyme.";
Eur. J. Biochem. 236:207-213(1996).
[7]
PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASN-19;
LEU-29; ARG-75; ALA-106; HIS-168; LEU-217; HIS-298; VAL-334; LYS-353
AND GLN-382.
NIEHS SNPs program;
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
[8]
PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT
ALA-106.
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., 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.
[9]
INTERACTION WITH MEFV.
PubMed=17431422; DOI=10.1038/sj.cdd.4402142;
Papin S., Cuenin S., Agostini L., Martinon F., Werner S., Beer H.D.,
Grutter C., Grutter M., Tschopp J.;
"The SPRY domain of Pyrin, mutated in familial Mediterranean fever
patients, interacts with inflammasome components and inhibits proIL-
1beta processing.";
Cell Death Differ. 14:1457-1466(2007).
[10]
FUNCTION, AND MUTAGENESIS OF CYS-315.
PubMed=28314590; DOI=10.1016/j.immuni.2017.02.011;
Wang Y., Ning X., Gao P., Wu S., Sha M., Lv M., Zhou X., Gao J.,
Fang R., Meng G., Su X., Jiang Z.;
"Inflammasome activation triggers caspase-1-mediated cleavage of cGAS
to regulate responses to DNA virus infection.";
Immunity 46:393-404(2017).
-!- FUNCTION: Mediator of programmed cell death (apoptosis). During
non-canonical inflammasome activation, cuts CGAS and may play a
role in the regulation of antiviral innate immune activation
(PubMed:28314590). {ECO:0000269|PubMed:28314590}.
-!- CATALYTIC ACTIVITY:
Reaction=Strict requirement for Asp at the P1 position. It has a
preferred cleavage sequence of Tyr-Val-Ala-Asp-|- but also
cleaves at Asp-Glu-Val-Asp-|-.; EC=3.4.22.58;
-!- SUBUNIT: Heterotetramer that consists of two anti-parallel
arranged heterodimers, each one formed by a 20 kDa (p20) and a 10
kDa (p10) subunits. Interacts with MEFV.
{ECO:0000269|PubMed:17431422}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=6;
Name=1; Synonyms=caspase-5/a;
IsoId=P51878-1; Sequence=Displayed;
Note=Most abundant isoform.;
Name=2; Synonyms=Caspase-5/b;
IsoId=P51878-2; Sequence=VSP_038993;
Note=Most abundant isoform.;
Name=3; Synonyms=Caspase-5/c;
IsoId=P51878-3; Sequence=VSP_038990;
Name=4; Synonyms=Caspase-5/e;
IsoId=P51878-4; Sequence=VSP_038993, VSP_038994, VSP_038995;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=5; Synonyms=Caspase-5/f;
IsoId=P51878-5; Sequence=VSP_038992;
Name=6; Synonyms=Caspase-5-S;
IsoId=P51878-6; Sequence=VSP_038991;
Note=Produced by alternative initiation at Met-71 of isoform 1.;
-!- TISSUE SPECIFICITY: Expressed in barely detectable amounts in most
tissues except brain, highest levels being found in lung, liver
and skeletal muscle.
-!- INDUCTION: Up-regulated by bacterial lipopolysaccharides (LPS).
{ECO:0000269|PubMed:16893518}.
-!- PTM: The two subunits are derived from the precursor sequence by
an autocatalytic mechanism.
-!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA75172.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAH74994.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAI13407.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=ABF47103.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAG59257.1; Type=Frameshift; Positions=10; Evidence={ECO:0000305};
Sequence=CAA64450.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/casp5/";
-----------------------------------------------------------------------
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EMBL; DQ228672; ABB58698.1; -; mRNA.
EMBL; DQ228673; ABB58699.1; -; mRNA.
EMBL; DQ228674; ABB58700.1; -; mRNA.
EMBL; DQ228676; ABB58702.1; -; mRNA.
EMBL; DQ228677; ABB58703.1; -; mRNA.
EMBL; AK296660; BAG59257.1; ALT_FRAME; mRNA.
EMBL; AP001153; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; U28015; AAA75172.1; ALT_INIT; mRNA.
EMBL; BC074994; AAH74994.1; ALT_INIT; mRNA.
EMBL; BC113406; AAI13407.1; ALT_INIT; mRNA.
EMBL; X94993; CAA64450.1; ALT_INIT; mRNA.
EMBL; DQ508420; ABF47103.1; ALT_INIT; Genomic_DNA.
EMBL; CH471065; EAW67054.1; -; Genomic_DNA.
CCDS; CCDS44718.1; -. [P51878-3]
CCDS; CCDS44719.1; -. [P51878-2]
CCDS; CCDS44720.1; -. [P51878-5]
CCDS; CCDS8328.2; -. [P51878-1]
PIR; B57511; B57511.
RefSeq; NP_001129581.1; NM_001136109.1. [P51878-2]
RefSeq; NP_001129582.1; NM_001136110.1. [P51878-3]
RefSeq; NP_001129584.1; NM_001136112.1. [P51878-5]
RefSeq; NP_004338.3; NM_004347.3. [P51878-1]
UniGene; Hs.213327; -.
ProteinModelPortal; P51878; -.
SMR; P51878; -.
BioGrid; 107288; 4.
CORUM; P51878; -.
DIP; DIP-40038N; -.
IntAct; P51878; 2.
STRING; 9606.ENSP00000376849; -.
BindingDB; P51878; -.
ChEMBL; CHEMBL3131; -.
GuidetoPHARMACOLOGY; 1621; -.
MEROPS; C14.008; -.
iPTMnet; P51878; -.
PhosphoSitePlus; P51878; -.
BioMuta; CASP5; -.
DMDM; 294862523; -.
EPD; P51878; -.
jPOST; P51878; -.
MaxQB; P51878; -.
PaxDb; P51878; -.
PeptideAtlas; P51878; -.
PRIDE; P51878; -.
ProteomicsDB; 56442; -.
ProteomicsDB; 56443; -. [P51878-2]
ProteomicsDB; 56444; -. [P51878-3]
ProteomicsDB; 56445; -. [P51878-4]
ProteomicsDB; 56446; -. [P51878-5]
ProteomicsDB; 56447; -. [P51878-6]
Ensembl; ENST00000260315; ENSP00000260315; ENSG00000137757. [P51878-1]
Ensembl; ENST00000393141; ENSP00000376849; ENSG00000137757. [P51878-5]
Ensembl; ENST00000418434; ENSP00000398130; ENSG00000137757. [P51878-3]
Ensembl; ENST00000444749; ENSP00000388365; ENSG00000137757. [P51878-2]
Ensembl; ENST00000456200; ENSP00000408455; ENSG00000137757. [P51878-4]
Ensembl; ENST00000526056; ENSP00000436877; ENSG00000137757. [P51878-5]
Ensembl; ENST00000531367; ENSP00000434471; ENSG00000137757. [P51878-3]
GeneID; 838; -.
KEGG; hsa:838; -.
UCSC; uc010ruz.1; human. [P51878-1]
CTD; 838; -.
DisGeNET; 838; -.
EuPathDB; HostDB:ENSG00000137757.10; -.
GeneCards; CASP5; -.
HGNC; HGNC:1506; CASP5.
HPA; HPA040937; -.
MIM; 602665; gene.
neXtProt; NX_P51878; -.
OpenTargets; ENSG00000137757; -.
PharmGKB; PA26089; -.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00940000161497; -.
HOVERGEN; HBG076981; -.
InParanoid; P51878; -.
KO; K04395; -.
OMA; CKENHDE; -.
OrthoDB; 1472750at2759; -.
PhylomeDB; P51878; -.
TreeFam; TF102023; -.
BRENDA; 3.4.22.58; 2681.
SABIO-RK; P51878; -.
ChiTaRS; CASP5; human.
GenomeRNAi; 838; -.
PRO; PR:P51878; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000137757; Expressed in 92 organ(s), highest expression level in blood.
ExpressionAtlas; P51878; baseline and differential.
Genevisible; P51878; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0072558; C:NLRP1 inflammasome complex; IDA:UniProtKB.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0097199; F:cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IBA:GO_Central.
GO; GO:0008234; F:cysteine-type peptidase activity; TAS:ProtInc.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
GO; GO:0006915; P:apoptotic process; IBA:GO_Central.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
GO; GO:0006508; P:proteolysis; TAS:ProtInc.
GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB.
CDD; cd00032; CASc; 1.
InterPro; IPR001315; CARD.
InterPro; IPR029030; Caspase-like_dom_sf.
InterPro; IPR033139; Caspase_cys_AS.
InterPro; IPR016129; Caspase_his_AS.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR002398; Pept_C14.
InterPro; IPR002138; Pept_C14_p10.
InterPro; IPR001309; Pept_C14_p20.
InterPro; IPR015917; Pept_C14A.
PANTHER; PTHR10454; PTHR10454; 1.
Pfam; PF00619; CARD; 1.
PRINTS; PR00376; IL1BCENZYME.
SMART; SM00114; CARD; 1.
SMART; SM00115; CASc; 1.
SUPFAM; SSF47986; SSF47986; 1.
SUPFAM; SSF52129; SSF52129; 1.
PROSITE; PS50209; CARD; 1.
PROSITE; PS01122; CASPASE_CYS; 1.
PROSITE; PS01121; CASPASE_HIS; 1.
PROSITE; PS50207; CASPASE_P10; 1.
PROSITE; PS50208; CASPASE_P20; 1.
1: Evidence at protein level;
Alternative initiation; Alternative splicing; Apoptosis;
Complete proteome; Hydrolase; Polymorphism; Protease;
Reference proteome; Thiol protease; Zymogen.
PROPEP 1 136 {ECO:0000255}.
/FTId=PRO_0000004604.
CHAIN 137 327 Caspase-5 subunit p20.
/FTId=PRO_0000004605.
PROPEP 328 346 {ECO:0000255}.
/FTId=PRO_0000004606.
CHAIN 347 434 Caspase-5 subunit p10.
/FTId=PRO_0000004607.
DOMAIN 56 148 CARD. {ECO:0000255|PROSITE-
ProRule:PRU00046}.
ACT_SITE 267 267 {ECO:0000250}.
ACT_SITE 315 315
VAR_SEQ 1 145 MAEDSGKKKRRKNFEAMFKGILQSGLDNFVINHMLKNNVAG
QTSIQTLVPNTDQKSTSVKKDNHKKKTVKMLEYLGKDVLHG
VFNYLAKHDVLTLKEEEKKKYYDTKIEDKALILVDSLRKNR
VAHQMFTQTLLNMDQKITSVKP -> MAA (in isoform
3). {ECO:0000303|PubMed:16893518}.
/FTId=VSP_038990.
VAR_SEQ 1 70 Missing (in isoform 6). {ECO:0000305}.
/FTId=VSP_038991.
VAR_SEQ 1 2 MA -> MAAVPRVEGVFIFLI (in isoform 5).
{ECO:0000303|PubMed:16893518}.
/FTId=VSP_038992.
VAR_SEQ 5 62 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:16893518}.
/FTId=VSP_038993.
VAR_SEQ 145 166 PLLQIEAGPPESAESTNILKLC -> HLSNKKERGPQTPGS
HHMQYKV (in isoform 4).
{ECO:0000303|PubMed:16893518}.
/FTId=VSP_038994.
VAR_SEQ 167 434 Missing (in isoform 4).
{ECO:0000303|PubMed:16893518}.
/FTId=VSP_038995.
VARIANT 19 19 K -> N (in dbSNP:rs45483102).
{ECO:0000269|Ref.7}.
/FTId=VAR_047216.
VARIANT 26 26 L -> W (in dbSNP:rs1792778).
/FTId=VAR_047217.
VARIANT 29 29 F -> L (in dbSNP:rs3181320).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.7}.
/FTId=VAR_024403.
VARIANT 75 75 L -> R (in dbSNP:rs45585331).
{ECO:0000269|Ref.7}.
/FTId=VAR_054480.
VARIANT 106 106 T -> A (in dbSNP:rs507879).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16893518,
ECO:0000269|PubMed:7797592,
ECO:0000269|PubMed:8617266,
ECO:0000269|Ref.7, ECO:0000269|Ref.8}.
/FTId=VAR_047218.
VARIANT 168 168 R -> H (in dbSNP:rs3181179).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.7}.
/FTId=VAR_024404.
VARIANT 217 217 V -> L (in dbSNP:rs3181326).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.7}.
/FTId=VAR_024405.
VARIANT 298 298 R -> H (in dbSNP:rs45464699).
{ECO:0000269|Ref.7}.
/FTId=VAR_054481.
VARIANT 334 334 L -> V (in dbSNP:rs523104).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16893518,
ECO:0000269|PubMed:7797592,
ECO:0000269|Ref.7}.
/FTId=VAR_047219.
VARIANT 353 353 E -> K (in dbSNP:rs45619739).
{ECO:0000269|Ref.7}.
/FTId=VAR_047220.
VARIANT 382 382 E -> Q (in dbSNP:rs45458695).
{ECO:0000269|Ref.7}.
/FTId=VAR_054482.
MUTAGEN 315 315 C->A: Abolishes protease activity.
{ECO:0000269|PubMed:28314590}.
SEQUENCE 434 AA; 49736 MW; C5257C2BF15EB6D5 CRC64;
MAEDSGKKKR RKNFEAMFKG ILQSGLDNFV INHMLKNNVA GQTSIQTLVP NTDQKSTSVK
KDNHKKKTVK MLEYLGKDVL HGVFNYLAKH DVLTLKEEEK KKYYDTKIED KALILVDSLR
KNRVAHQMFT QTLLNMDQKI TSVKPLLQIE AGPPESAEST NILKLCPREE FLRLCKKNHD
EIYPIKKRED RRRLALIICN TKFDHLPARN GAHYDIVGMK RLLQGLGYTV VDEKNLTARD
MESVLRAFAA RPEHKSSDST FLVLMSHGIL EGICGTAHKK KKPDVLLYDT IFQIFNNRNC
LSLKDKPKVI IVQACRGEKH GELWVRDSPA SLALISSQSS ENLEADSVCK IHEEKDFIAF
CSSTPHNVSW RDRTRGSIFI TELITCFQKY SCCCHLMEIF RKVQKSFEVP QAKAQMPTIE
RATLTRDFYL FPGN


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18-272-195092 Caspase 10 - Rabbit polyclonal to Caspase 10; EC 3.4.22.63; CASP-10; ICE-like apoptotic protease 4; Apoptotic protease Mch-4; FAS-associated death domain protein interleukin-1B-converting enzyme 2; FL 0.1 ml
18-272-197016 Caspase 10 - Rabbit polyclonal to Caspase 10; EC 3.4.22.63; CASP-10; ICE-like apoptotic protease 4; Apoptotic protease Mch-4; FAS-associated death domain protein interleukin-1B-converting enzyme 2; FL 0.1 mg
18-272-195090 Caspase 8 - Rabbit polyclonal to Caspase 8; EC 3.4.22.61; CASP-8; ICE-like apoptotic protease 5; MORT1-associated CED-3 homolog; MACH; FADD-homologous ICE_CED-3-like protease; FADD-like ICE; FLICE; Ap 0.1 ml
18-272-195091 Caspase 8 - Rabbit polyclonal to Caspase 8; EC 3.4.22.61; CASP-8; ICE-like apoptotic protease 5; MORT1-associated CED-3 homolog; MACH; FADD-homologous ICE_CED-3-like protease; FADD-like ICE; FLICE; Ap 0.1 ml
18-272-196464 Caspase 8 prediluted - Rabbit polyclonal to Caspase 8 prediluted; EC 3.4.22.61; CASP-8; ICE-like apoptotic protease 5; MORT1-associated CED-3 homolog; MACH; FADD-homologous ICE_CED-3-like protease; FA 7 ml
20-272-192408 Caspase 8 - Mouse monoclonal [C502S] to Caspase 8; EC 3.4.22.61; CASP-8; ICE-like apoptotic protease 5; MORT1-associated CED-3 homolog; MACH; FADD-homologous ICE_CED-3-like protease; FADD-like ICE; FL 0.05 mg
18-272-197069 active Caspase 9 - Rabbit polyclonal to active Caspase 9; EC 3.4.22.62; CASP-9; ICE-like apoptotic protease 6; ICE-LAP6; Apoptotic protease Mch-6; Apoptotic protease-activating factor 3; APAF-3 Polycl 0.05 mg
18-272-197070 active Caspase 9 - Rabbit polyclonal to active Caspase 9; EC 3.4.22.62; CASP-9; ICE-like apoptotic protease 6; ICE-LAP6; Apoptotic protease Mch-6; Apoptotic protease-activating factor 3; APAF-3 Polycl 0.05 mg
18-272-196465 Caspase 9 prediluted - Rabbit polyclonal to Caspase 9 prediluted; EC 3.4.22.62; CASP-9; ICE-like apoptotic protease 6; ICE-LAP6; Apoptotic protease Mch-6; Apoptotic protease-activating factor 3; APAF- 7 ml
20-272-191348 Caspase 9 - Mouse monoclonal [1-2] to Caspase 9; EC 3.4.22.62; CASP-9; ICE-like apoptotic protease 6; ICE-LAP6; Apoptotic protease Mch-6; Apoptotic protease-activating factor 3; APAF-3 Monoclonal 0.05 mg
18-272-197018 Caspase 9 - Rabbit polyclonal to Caspase 9; EC 3.4.22.62; CASP-9; ICE-like apoptotic protease 6; ICE-LAP6; Apoptotic protease Mch-6; Apoptotic protease-activating factor 3; APAF-3 Polyclonal 0.1 mg
18-272-197017 Caspase 9 - Rabbit polyclonal to Caspase 9; EC 3.4.22.62; CASP-9; ICE-like apoptotic protease 6; ICE-LAP6; Apoptotic protease Mch-6; Apoptotic protease-activating factor 3; APAF-3 Polyclonal 0.1 mg
20-002-35037 Caspase-2 (anti-human Caspase-2. clone 1C10) - EC 3.4.22.-; CASP-2; ICH-1 protease; ICH-1L_1S Monoclonal 0.05 ml
20-002-35037 Caspase-2 (anti-human Caspase-2. clone 1C10) - EC 3.4.22.-; CASP-2; ICH-1 protease; ICH-1L_1S Monoclonal 0.1 ml
20-272-190220 Caspase 4 - Mouse monoclonal [CAS4] to Caspase 4; EC 3.4.22.57; CASP-4; ICH-2 protease; TX protease; ICE(rel)-II Monoclonal 0.05 ml
20-272-190221 Caspase 5 - Mouse monoclonal [CAS5] to Caspase 5; EC 3.4.22.58; CASP-5; ICH-3 protease; TY protease; ICE(rel)-III Monoclonal 0.05 ml
18-272-196627 Caspase 5 - Rabbit polyclonal to Caspase 5; EC 3.4.22.58; CASP-5; ICH-3 protease; TY protease; ICE(rel)-III Polyclonal 0.25 ml
18-272-195088 Caspase 4 - Rabbit polyclonal to Caspase 4; EC 3.4.22.57; CASP-4; ICH-2 protease; TX protease; ICE(rel)-II Polyclonal 0.1 ml
20-272-191808 Caspase 7 - Mouse monoclonal [4G2] to Caspase 7; EC 3.4.22.60; CASP-7; ICE-like apoptotic protease 3; ICE-LAP3; Apoptotic protease Mch-3; CMH-1 Monoclonal 0.05 mg
20-272-192362 Caspase 7 - Mouse monoclonal [B4 - G2] to Caspase 7; EC 3.4.22.60; CASP-7; ICE-like apoptotic protease 3; ICE-LAP3; Apoptotic protease Mch-3; CMH-1 Monoclonal 0.05 mg
18-272-195089 Caspase 7 - Rabbit polyclonal to Caspase 7; EC 3.4.22.60; CASP-7; ICE-like apoptotic protease 3; ICE-LAP3; Apoptotic protease Mch-3; CMH-1 Polyclonal 0.1 ml

Kits Elisa; taq POLYMERASE

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Pathways :
WP1965: VEGF-receptor Signal Transduction
WP2359: Parkin-Ubiquitin Proteasomal System pathway
WP88: Toll Like Receptor signaling
WP1566: Citrate cycle (TCA cycle)
WP1614: 1- and 2-Methylnaphthalene degradation
WP1626: Benzoate degradation via CoA ligation
WP1634: Butanoate metabolism
WP1644: DNA replication
WP1655: Geraniol degradation
WP1663: Homologous recombination
WP1671: Methane metabolism
WP1672: Mismatch repair
WP1680: Oxidative phosphorylation
WP1693: Purine metabolism
WP1694: Pyrimidine metabolism
WP1711: Trinitrotoluene degradation
WP1718: Vitamin B6 metabolism
WP2199: Seed Development
WP2272: Pathogenic Escherichia coli infection
WP2292: Chemokine signaling pathway
WP470: Proteasome Degradation

Related Genes :
[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]
[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]
[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]
[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]
[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]
[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]
[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]
[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]
[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]
[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]
[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]
[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]
[Casp6] 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]
[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]
[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)]
[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)]
[Drice ICE CG7788] Caspase (EC 3.4.22.-) (drICE) [Cleaved into: Caspase subunit p21; Caspase subunit p12]
[AMC4 AMC7 MCP2D At1g79340 YUP8H12R.4] Metacaspase-4 (AtMC4) (EC 3.4.22.-) (Metacaspase 2d) (AtMCP2d) (Metacaspase-7) [Cleaved into: Metacaspase-4 subunit p20; Metacaspase-4 subunit p10]
[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]
[] Genome polyprotein [Cleaved into: N-terminal protease (N-pro) (EC 3.4.22.-) (Autoprotease p20); Capsid protein C; E(rns) glycoprotein (gp44/48); Envelope glycoprotein E1 (gp33); Envelope glycoprotein E2 (gp55); p7; Non-structural protein 2-3; Cysteine protease NS2 (EC 3.4.22.-) (Non-structural protein 2); Serine protease NS3 (EC 3.4.21.113) (EC 3.6.1.15) (EC 3.6.4.13) (Non-structural protein 3); Non-structural protein 4A (NS4A); Non-structural protein 4B (NS4B); Non-structural protein 5A (NS5A); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B)]
[CASP7 MCH3] Caspase-7 (CASP-7) (EC 3.4.22.60) (Apoptotic protease Mch-3) (ICE-like apoptotic protease 3) (ICE-LAP3) (SREBP cleavage activity 2) (SCA-2) [Cleaved into: Caspase-7 subunit p20; Caspase-7 subunit p11]
[csp-1 Y48E1B.13] Caspase A (EC 3.4.22.36) [Cleaved into: Caspase A subunit p16; Caspase A subunit p14]
[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]
[gag-pol] Gag-Pol polyprotein [Cleaved into: Matrix protein p10 (MA); p20; Capsid protein p25 (CA); Nucleocapsid protein p14 (NC-pol); Protease p15 (PR) (EC 3.4.23.-); Reverse transcriptase/ribonuclease H p90 (RT) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase p46 (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]

Bibliography :