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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]

 CASPA_HUMAN             Reviewed;         521 AA.
Q92851; Q68HC0; Q6KF62; Q6KF63; Q8IUP5; Q8WYQ8; Q99845; Q9Y2U6;
Q9Y2U7;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
11-JAN-2001, sequence version 3.
03-JUL-2019, entry version 206.
RecName: Full=Caspase-10;
Short=CASP-10;
EC=3.4.22.63;
AltName: Full=Apoptotic protease Mch-4;
AltName: Full=FAS-associated death domain protein interleukin-1B-converting enzyme 2;
Short=FLICE2;
AltName: Full=ICE-like apoptotic protease 4;
Contains:
RecName: Full=Caspase-10 subunit p23/17;
Contains:
RecName: Full=Caspase-10 subunit p12;
Flags: Precursor;
Name=CASP10; Synonyms=MCH4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND VARIANT ILE-479 (ISOFORM
B).
TISSUE=T-cell;
PubMed=8755496; DOI=10.1073/pnas.93.15.7464;
Fernandes-Alnemri T., Armstrong R.C., Krebs J.F., Srinivasula S.M.,
Wang L., Bullrich F., Fritz L.C., Trapani J.A., Tomaselli K.J.,
Litwack G., Alnemri E.S.;
"In vitro activation of CPP32 and Mch3 by Mch4, a novel human
apoptotic cysteine protease containing two FADD-like domains.";
Proc. Natl. Acad. Sci. U.S.A. 93:7464-7469(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
PubMed=9045686; DOI=10.1074/jbc.272.10.6578;
Vincenz C., Dixit V.M.;
"Fas-associated death domain protein interleukin-1beta-converting
enzyme 2 (FLICE2), an ICE/Ced-3 homologue, is proximally involved in
CD95- and p55-mediated death signaling.";
J. Biol. Chem. 272:6578-6583(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS C AND D), VARIANT ILE-410, AND
VARIANT ILE-522 (ISOFORM D).
TISSUE=Spleen, and Thymus;
PubMed=10187817; DOI=10.1074/jbc.274.15.10301;
Ng P.W., Porter A.G., Janicke R.U.;
"Molecular cloning and characterization of two novel pro-apoptotic
isoforms of caspase-10.";
J. Biol. Chem. 274:10301-10308(1999).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS A
AND B), AND VARIANT ILE-479 (ISOFORM B).
PubMed=11161814; DOI=10.1006/geno.2000.6392;
Hadano S., Yanagisawa Y., Skaug J., Fichter K., Nasir J.,
Martindale D., Koop B.F., Scherer S.W., Nicholson D.W., Rouleau G.A.,
Ikeda J.-E., Hayden M.R.;
"Cloning and characterization of three novel genes, ALS2CR1, ALS2CR2,
and ALS2CR3, in the juvenile amyotrophic lateral sclerosis (ALS2)
critical region at chromosome 2q33-q34: candidate genes for ALS2.";
Genomics 71:200-213(2001).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6), AND VARIANT ILE-455
(ISOFORM 6).
TISSUE=Blood;
Vonarbourg C., Fischer A., Rieux-Laucat F.;
"A novel human caspase 10 isoform participating in Fas-induced
apoptosis.";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), AND FUNCTION (ISOFORM 7).
PubMed=17822854; DOI=10.1016/j.bbagen.2007.07.010;
Wang H., Wang P., Sun X., Luo Y., Wang X., Ma D., Wu J.;
"Cloning and characterization of a novel caspase-10 isoform that
activates NF-kappa B activity.";
Biochim. Biophys. Acta 1770:1528-1537(2007).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CYS-239; ILE-410;
SER-444; CYS-446 AND ILE-522 (ISOFORM 2).
NIEHS SNPs program;
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
TISSUE=Brain;
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).
[11]
PARTIAL PROTEIN SEQUENCE, AND PROTEOLYTIC PROCESSING.
PubMed=8962078; DOI=10.1073/pnas.93.25.14486;
Srinivasula S.M., Ahmad M., Fernandes-Alnemri T., Litwack G.,
Alnemri E.S.;
"Molecular ordering of the Fas-apoptotic pathway: the Fas/APO-1
protease Mch5 is a CrmA-inhibitable protease that activates multiple
Ced-3/ICE-like cysteine proteases.";
Proc. Natl. Acad. Sci. U.S.A. 93:14486-14491(1996).
[12]
FUNCTION, SELF-ASSOCIATION, INTERACTION WITH FADD, INTERACTION WITH
CASP8, IDENTIFICATION IN A COMPLEX WITH FAS; FADD AND CASP8, AND
MUTAGENESIS OF CYS-401.
PubMed=11717445; DOI=10.1073/pnas.241358198;
Wang J., Chun H.J., Wong W., Spencer D.M., Lenardo M.J.;
"Caspase-10 is an initiator caspase in death receptor signaling.";
Proc. Natl. Acad. Sci. U.S.A. 98:13884-13888(2001).
[13]
SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
Hillman R.T., Green R.E., Brenner S.E.;
"An unappreciated role for RNA surveillance.";
Genome Biol. 5:R8.1-R8.16(2004).
[14]
INTERACTION WITH RFFL AND RNF34.
PubMed=15069192; DOI=10.1073/pnas.0307459101;
McDonald E.R. III, El-Deiry W.S.;
"Suppression of caspase-8- and -10-associated RING proteins results in
sensitization to death ligands and inhibition of tumor cell growth.";
Proc. Natl. Acad. Sci. U.S.A. 101:6170-6175(2004).
[15]
INTERACTION WITH RIOK3.
PubMed=19557502; DOI=10.1007/s11010-009-0180-8;
Shan J., Wang P., Zhou J., Wu D., Shi H., Huo K.;
"RIOK3 interacts with caspase-10 and negatively regulates the NF-
kappaB signaling pathway.";
Mol. Cell. Biochem. 332:113-120(2009).
[16]
VARIANT ALPS2A PHE-285, VARIANT ILE-410, AND ALTERNATIVE SPLICING
(ISOFORMS B AND D).
PubMed=10412980; DOI=10.1016/S0092-8674(00)80605-4;
Wang J., Zheng L., Lobito A., Chan F.K., Dale J., Sneller M., Yao X.,
Puck J.M., Straus S.E., Lenardo M.J.;
"Inherited human caspase 10 mutations underlie defective lymphocyte
and dendritic cell apoptosis in autoimmune lymphoproliferative
syndrome type II.";
Cell 98:47-58(1999).
[17]
VARIANT NHL VAL-414.
PubMed=12010812; DOI=10.1182/blood.V99.11.4094;
Shin M.S., Kim H.S., Kang C.S., Park W.S., Kim S.Y., Lee S.N.,
Lee J.H., Park J.Y., Jang J.J., Kim C.W., Kim S.H., Lee J.Y.,
Yoo N.J., Lee S.H.;
"Inactivating mutations of CASP10 gene in non-Hodgkin lymphomas.";
Blood 99:4094-4099(2002).
[18]
VARIANT GASC THR-147, AND CHARACTERIZATION OF VARIANT GASC THR-147.
PubMed=11973654; DOI=10.1038/sj.onc.1205394;
Park W.S., Lee J.H., Shin M.S., Park J.Y., Kim H.S., Lee J.H.,
Kim Y.S., Lee S.N., Xiao W., Park C.H., Lee S.H., Yoo N.J., Lee J.Y.;
"Inactivating mutations of the caspase-10 gene in gastric cancer.";
Oncogene 21:2919-2925(2002).
[19]
VARIANTS LEU-406; ILE-410 AND CYS-446, AND CHARACTERIZATION OF
VARIANTS LEU-406; ILE-410 AND CYS-446.
PubMed=16446975; DOI=10.1007/s00439-006-0138-9;
Zhu S., Hsu A.P., Vacek M.M., Zheng L., Schaeffer A.A., Dale J.K.,
Davis J., Fischer R.E., Straus S.E., Boruchov D., Saulsbury F.T.,
Lenardo M.J., Puck J.M.;
"Genetic alterations in caspase-10 may be causative or protective in
autoimmune lymphoproliferative syndrome.";
Hum. Genet. 119:284-294(2006).
[20]
VARIANT ILE-522 (ISOFORM D), AND RISK FACTOR FOR CUTANEOUS MELANOMA.
PubMed=18563783; DOI=10.1002/humu.20803;
Li C., Zhao H., Hu Z., Liu Z., Wang L.-E., Gershenwald J.E.,
Prieto V.G., Lee J.E., Duvic M., Grimm E.A., Wei Q.;
"Genetic variants and haplotypes of the caspase-8 and caspase-10 genes
contribute to susceptibility to cutaneous melanoma.";
Hum. Mutat. 29:1443-1451(2008).
[21]
VARIANTS CYS-21 AND PRO-285.
PubMed=19900088; DOI=10.1080/00313020903041143;
Kim M.S., Oh J.E., Min C.K., Lee S., Chung N.G., Yoo N.J., Lee S.H.;
"Mutational analysis of CASP10 gene in acute leukaemias and multiple
myelomas.";
Pathology 41:484-487(2009).
[22]
VARIANT THR-14.
PubMed=20025484; DOI=10.3109/00313020903434371;
Oh J.E., Kim M.S., Ahn C.H., Kim S.S., Han J.Y., Lee S.H., Yoo N.J.;
"Mutational analysis of CASP10 gene in colon, breast, lung and
hepatocellular carcinomas.";
Pathology 42:73-76(2010).
[23]
VARIANT LEU-406.
PubMed=27378136; DOI=10.1016/j.imlet.2016.07.001;
Tripodi S.I., Mazza C., Moratto D., Ramenghi U., Caorsi R.,
Gattorno M., Badolato R.;
"Atypical presentation of autoimmune lymphoproliferative syndrome due
to CASP10 mutation.";
Immunol. Lett. 177:22-24(2016).
[24]
VARIANT LEU-406.
PubMed=27535533; DOI=10.1038/nature19057;
Exome Aggregation Consortium;
Lek M., Karczewski K.J., Minikel E.V., Samocha K.E., Banks E.,
Fennell T., O'Donnell-Luria A.H., Ware J.S., Hill A.J., Cummings B.B.,
Tukiainen T., Birnbaum D.P., Kosmicki J.A., Duncan L.E., Estrada K.,
Zhao F., Zou J., Pierce-Hoffman E., Berghout J., Cooper D.N.,
Deflaux N., DePristo M., Do R., Flannick J., Fromer M., Gauthier L.,
Goldstein J., Gupta N., Howrigan D., Kiezun A., Kurki M.I.,
Moonshine A.L., Natarajan P., Orozco L., Peloso G.M., Poplin R.,
Rivas M.A., Ruano-Rubio V., Rose S.A., Ruderfer D.M., Shakir K.,
Stenson P.D., Stevens C., Thomas B.P., Tiao G., Tusie-Luna M.T.,
Weisburd B., Won H.H., Yu D., Altshuler D.M., Ardissino D.,
Boehnke M., Danesh J., Donnelly S., Elosua R., Florez J.C.,
Gabriel S.B., Getz G., Glatt S.J., Hultman C.M., Kathiresan S.,
Laakso M., McCarroll S., McCarthy M.I., McGovern D., McPherson R.,
Neale B.M., Palotie A., Purcell S.M., Saleheen D., Scharf J.M.,
Sklar P., Sullivan P.F., Tuomilehto J., Tsuang M.T., Watkins H.C.,
Wilson J.G., Daly M.J., MacArthur D.G.;
"Analysis of protein-coding genetic variation in 60,706 humans.";
Nature 536:285-291(2016).
-!- FUNCTION: Involved in the activation cascade of caspases
responsible for apoptosis execution. Recruited to both Fas- and
TNFR-1 receptors in a FADD dependent manner. May participate in
the granzyme B apoptotic pathways. Cleaves and activates caspase-
3, -4, -6, -7, -8, and -9. Hydrolyzes the small- molecule
substrates, Tyr-Val-Ala-Asp-|-AMC and Asp-Glu-Val-Asp-|-AMC.
{ECO:0000269|PubMed:11717445}.
-!- FUNCTION: Isoform 7 can enhance NF-kappaB activity but promotes
only slight apoptosis. {ECO:0000269|PubMed:17822854}.
-!- FUNCTION: Isoform C is proteolytically inactive.
{ECO:0000269|PubMed:11717445}.
-!- CATALYTIC ACTIVITY:
Reaction=Strict requirement for Asp at position P1 and has a
preferred cleavage sequence of Leu-Gln-Thr-Asp-|-Gly.;
EC=3.4.22.63;
-!- SUBUNIT: Heterotetramer that consists of two anti-parallel
arranged heterodimers, each one formed by a 23/17 kDa (p23/17)
(depending on the splicing events) and a 12 kDa (p12) subunit (By
similarity). Self-associates. Interacts with FADD and CASP8. Found
in a Fas signaling complex consisting of FAS, FADD, CASP8 and
CASP10. Interacts with RFFL and RNF34; negatively regulate CASP10
through proteasomal degradation. Interacts with RIOK3.
{ECO:0000250, ECO:0000269|PubMed:11717445,
ECO:0000269|PubMed:15069192, ECO:0000269|PubMed:19557502}.
-!- INTERACTION:
Q14790:CASP8; NbExp=3; IntAct=EBI-495095, EBI-78060;
O15519:CFLAR; NbExp=3; IntAct=EBI-495095, EBI-514941;
O14730:RIOK3; NbExp=6; IntAct=EBI-495095, EBI-1047061;
Q13546:RIPK1; NbExp=2; IntAct=EBI-495095, EBI-358507;
P98170:XIAP; NbExp=3; IntAct=EBI-6621134, EBI-517127;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=A; Synonyms=10-A;
IsoId=Q92851-1; Sequence=Displayed;
Name=B; Synonyms=10-B, 10-S;
IsoId=Q92851-2; Sequence=VSP_000819, VSP_000820;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.
Variant in position: 479:L->I (in dbSNP:rs13006529).;
Name=D; Synonyms=10-D, 10-L;
IsoId=Q92851-4; Sequence=VSP_000820;
Note=Variant in position: 522:L->I (not associated with
significantly altered cutaneous melanoma risk,
dbSNP:rs13006529).;
Name=C; Synonyms=10-C;
IsoId=Q92851-3; Sequence=VSP_000821, VSP_000822;
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;
IsoId=Q92851-5; Sequence=VSP_000819;
Name=6;
IsoId=Q92851-6; Sequence=VSP_037229, VSP_000820;
Note=Variant in position: 455:L->I (in dbSNP:rs13006529).;
Name=7; Synonyms=10-G, 10g;
IsoId=Q92851-7; Sequence=VSP_053333, VSP_053334;
-!- TISSUE SPECIFICITY: Detectable in most tissues. Lowest expression
is seen in brain, kidney, prostate, testis and colon.
-!- PTM: Cleavage by granzyme B and autocatalytic activity generate
the two active subunits.
-!- DISEASE: Autoimmune lymphoproliferative syndrome 2A (ALPS2A)
[MIM:603909]: A disorder of apoptosis that manifests in early
childhood and results in the accumulation of autoreactive
lymphocytes. It is characterized by non-malignant lymphadenopathy
with hepatosplenomegaly, and autoimmune hemolytic anemia,
thrombocytopenia and neutropenia. {ECO:0000269|PubMed:10412980}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Familial non-Hodgkin lymphoma (NHL) [MIM:605027]: Cancer
that starts in cells of the lymph system, which is part of the
body's immune system. NHLs can occur at any age and are often
marked by enlarged lymph nodes, fever and weight loss.
{ECO:0000269|PubMed:12010812}. Note=The gene represented in this
entry is involved in disease pathogenesis.
-!- DISEASE: Gastric cancer (GASC) [MIM:613659]: A malignant disease
which starts in the stomach, can spread to the esophagus or the
small intestine, and can extend through the stomach wall to nearby
lymph nodes and organs. It also can metastasize to other parts of
the body. The term gastric cancer or gastric carcinoma refers to
adenocarcinoma of the stomach that accounts for most of all
gastric malignant tumors. Two main histologic types are
recognized, diffuse type and intestinal type carcinomas. Diffuse
tumors are poorly differentiated infiltrating lesions, resulting
in thickening of the stomach. In contrast, intestinal tumors are
usually exophytic, often ulcerating, and associated with
intestinal metaplasia of the stomach, most often observed in
sporadic disease. {ECO:0000269|PubMed:11973654}. Note=The gene
represented in this entry is involved in disease pathogenesis.
-!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
-!- WEB RESOURCE: Name=CASP10base; Note=CASP10 mutation db;
URL="http://structure.bmc.lu.se/idbase/CASP10base/";
-!- WEB RESOURCE: Name=Autoimmune Lymphoproliferative Syndrome
Database (ALPSbase); Note=Caspase-10 mutations causing ALPS type
II;
URL="https://www.niaid.nih.gov/diseases-conditions/autoimmune-lymphoproliferative-syndrome-alps";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/casp10/";
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EMBL; U60519; AAC50644.1; -; mRNA.
EMBL; U86214; AAB46730.1; -; mRNA.
EMBL; AF111344; AAD28402.1; -; mRNA.
EMBL; AF111345; AAD28403.1; -; mRNA.
EMBL; AB038979; BAB32553.1; -; Genomic_DNA.
EMBL; AB038979; BAB32554.1; -; Genomic_DNA.
EMBL; AJ487678; CAD32371.1; -; mRNA.
EMBL; AJ487679; CAD32372.1; -; mRNA.
EMBL; AY690601; AAU00989.1; -; mRNA.
EMBL; EF050529; ABJ53426.1; -; Genomic_DNA.
EMBL; AC007283; AAY24291.1; -; Genomic_DNA.
EMBL; CH471063; EAW70248.1; -; Genomic_DNA.
EMBL; CH471063; EAW70249.1; -; Genomic_DNA.
EMBL; BC042844; AAH42844.1; -; mRNA.
CCDS; CCDS2338.1; -. [Q92851-1]
CCDS; CCDS2339.1; -. [Q92851-2]
CCDS; CCDS2340.1; -. [Q92851-4]
CCDS; CCDS56159.1; -. [Q92851-6]
CCDS; CCDS56160.1; -. [Q92851-5]
CCDS; CCDS77506.1; -. [Q92851-7]
RefSeq; NP_001193453.1; NM_001206524.1. [Q92851-6]
RefSeq; NP_001193471.1; NM_001206542.1. [Q92851-5]
RefSeq; NP_001221.2; NM_001230.4. [Q92851-2]
RefSeq; NP_001293012.1; NM_001306083.1. [Q92851-7]
RefSeq; NP_116756.2; NM_032974.4. [Q92851-1]
RefSeq; NP_116758.1; NM_032976.3. [Q92851-3]
RefSeq; NP_116759.2; NM_032977.3. [Q92851-4]
SMR; Q92851; -.
BioGrid; 107293; 91.
CORUM; Q92851; -.
IntAct; Q92851; 22.
MINT; Q92851; -.
STRING; 9606.ENSP00000286186; -.
BindingDB; Q92851; -.
ChEMBL; CHEMBL5037; -.
MEROPS; C14.011; -.
iPTMnet; Q92851; -.
PhosphoSitePlus; Q92851; -.
BioMuta; CASP10; -.
DMDM; 12644463; -.
jPOST; Q92851; -.
MaxQB; Q92851; -.
PaxDb; Q92851; -.
PeptideAtlas; Q92851; -.
PRIDE; Q92851; -.
ProteomicsDB; 75543; -.
ProteomicsDB; 75544; -. [Q92851-2]
ProteomicsDB; 75545; -. [Q92851-3]
ProteomicsDB; 75546; -. [Q92851-4]
ProteomicsDB; 75547; -. [Q92851-5]
ProteomicsDB; 75548; -. [Q92851-6]
Ensembl; ENST00000272879; ENSP00000272879; ENSG00000003400. [Q92851-1]
Ensembl; ENST00000286186; ENSP00000286186; ENSG00000003400. [Q92851-4]
Ensembl; ENST00000313728; ENSP00000314599; ENSG00000003400. [Q92851-6]
Ensembl; ENST00000346817; ENSP00000237865; ENSG00000003400. [Q92851-2]
Ensembl; ENST00000360132; ENSP00000353250; ENSG00000003400. [Q92851-3]
Ensembl; ENST00000374650; ENSP00000363781; ENSG00000003400. [Q92851-7]
Ensembl; ENST00000448480; ENSP00000396835; ENSG00000003400. [Q92851-5]
GeneID; 843; -.
KEGG; hsa:843; -.
UCSC; uc002uxi.2; human. [Q92851-1]
CTD; 843; -.
DisGeNET; 843; -.
GeneCards; CASP10; -.
GeneReviews; CASP10; -.
HGNC; HGNC:1500; CASP10.
HPA; CAB003780; -.
HPA; HPA017059; -.
MalaCards; CASP10; -.
MIM; 601762; gene.
MIM; 603909; phenotype.
MIM; 605027; phenotype.
MIM; 613659; phenotype.
neXtProt; NX_Q92851; -.
OpenTargets; ENSG00000003400; -.
Orphanet; 3261; Autoimmune lymphoproliferative syndrome.
PharmGKB; PA26084; -.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00940000160994; -.
HOGENOM; HOG000140947; -.
InParanoid; Q92851; -.
KO; K04400; -.
OMA; DRKHRGH; -.
OrthoDB; 939331at2759; -.
PhylomeDB; Q92851; -.
TreeFam; TF102023; -.
BRENDA; 3.4.22.63; 2681.
Reactome; R-HSA-6803207; TP53 Regulates Transcription of Caspase Activators and Caspases.
Reactome; R-HSA-75157; FasL/ CD95L signaling.
Reactome; R-HSA-75158; TRAIL signaling.
Reactome; R-HSA-933543; NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
SIGNOR; Q92851; -.
ChiTaRS; CASP10; human.
GeneWiki; Caspase_10; -.
GenomeRNAi; 843; -.
PRO; PR:Q92851; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000003400; Expressed in 152 organ(s), highest expression level in blood.
ExpressionAtlas; Q92851; baseline and differential.
Genevisible; Q92851; HS.
GO; GO:0031265; C:CD95 death-inducing signaling complex; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0097342; C:ripoptosome; IDA:UniProtKB.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0097153; F:cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
GO; GO:0097199; F:cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:0035877; F:death effector domain binding; IPI:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
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:0097190; P:apoptotic signaling pathway; TAS:Reactome.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:Reactome.
GO; GO:0097194; P:execution phase of apoptosis; IBA:GO_Central.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; TAS:Reactome.
CDD; cd00032; CASc; 1.
InterPro; IPR029030; Caspase-like_dom_sf.
InterPro; IPR035701; Caspase_10.
InterPro; IPR033139; Caspase_cys_AS.
InterPro; IPR016129; Caspase_his_AS.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR001875; DED_dom.
InterPro; IPR002398; Pept_C14.
InterPro; IPR002138; Pept_C14_p10.
InterPro; IPR001309; Pept_C14_p20.
InterPro; IPR015917; Pept_C14A.
PANTHER; PTHR10454; PTHR10454; 1.
PANTHER; PTHR10454:SF26; PTHR10454:SF26; 1.
Pfam; PF01335; DED; 2.
PRINTS; PR00376; IL1BCENZYME.
SMART; SM00115; CASc; 1.
SMART; SM00031; DED; 2.
SUPFAM; SSF47986; SSF47986; 2.
SUPFAM; SSF52129; SSF52129; 1.
PROSITE; PS01122; CASPASE_CYS; 1.
PROSITE; PS01121; CASPASE_HIS; 1.
PROSITE; PS50207; CASPASE_P10; 1.
PROSITE; PS50208; CASPASE_P20; 1.
PROSITE; PS50168; DED; 2.
1: Evidence at protein level;
Alternative splicing; Apoptosis; Complete proteome;
Direct protein sequencing; Disease mutation; Hydrolase; Polymorphism;
Protease; Reference proteome; Repeat; Thiol protease; Zymogen.
PROPEP 1 219
/FTId=PRO_0000004644.
CHAIN 220 415 Caspase-10 subunit p23/17.
/FTId=PRO_0000004645.
CHAIN 416 521 Caspase-10 subunit p12.
/FTId=PRO_0000004646.
DOMAIN 19 97 DED 1. {ECO:0000255|PROSITE-
ProRule:PRU00065}.
DOMAIN 114 187 DED 2. {ECO:0000255|PROSITE-
ProRule:PRU00065}.
ACT_SITE 358 358 {ECO:0000250}.
ACT_SITE 401 401 {ECO:0000250}.
VAR_SEQ 229 271 Missing (in isoform B and isoform 5).
{ECO:0000303|PubMed:8755496,
ECO:0000303|Ref.5}.
/FTId=VSP_000819.
VAR_SEQ 229 247 QESWQNKHAGSNGNRATNG -> EGVFVFLNEGDRGNSPDD
L (in isoform 7).
{ECO:0000303|PubMed:17822854}.
/FTId=VSP_053333.
VAR_SEQ 241 307 Missing (in isoform 6).
{ECO:0000303|Ref.5}.
/FTId=VSP_037229.
VAR_SEQ 241 273 GNRATNGAPSLVSRGMQGASANTLNSETSTKRA -> EGSC
VQDESEPQRPLCHCQQPQLYLPEGQTRNP (in isoform
C). {ECO:0000303|PubMed:10187817}.
/FTId=VSP_000821.
VAR_SEQ 248 521 Missing (in isoform 7).
{ECO:0000303|PubMed:17822854}.
/FTId=VSP_053334.
VAR_SEQ 274 521 Missing (in isoform C).
{ECO:0000303|PubMed:10187817}.
/FTId=VSP_000822.
VAR_SEQ 473 521 MLKFLEKTMEIRGRKRTVWGAKQISATSLPTAISAQTPRPP
MRRWSSVS -> HEDILSILTAVNDDVSRRVDKQGTKKQMP
QPAFTLRKKLVFPVPLDALSL (in isoform B,
isoform D and isoform 6).
{ECO:0000303|PubMed:10187817,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8755496,
ECO:0000303|Ref.5}.
/FTId=VSP_000820.
VARIANT 14 14 K -> T (found in a colon cancer sample;
somatic mutation).
{ECO:0000269|PubMed:20025484}.
/FTId=VAR_065233.
VARIANT 21 21 R -> C (found in a multiple myeloma
sample; somatic mutation;
dbSNP:rs559979934).
{ECO:0000269|PubMed:19900088}.
/FTId=VAR_065234.
VARIANT 147 147 M -> T (in GASC; somatic mutation;
impairs CASP10-mediated apoptosis;
dbSNP:rs121909776).
{ECO:0000269|PubMed:11973654}.
/FTId=VAR_037428.
VARIANT 239 239 S -> C (in dbSNP:rs41473647).
/FTId=VAR_055361.
VARIANT 285 285 L -> F (in ALPS2A; dbSNP:rs17860403).
{ECO:0000269|PubMed:10412980}.
/FTId=VAR_014071.
VARIANT 285 285 L -> P (found in a T-acute lymphoblastic
leukemia sample; somatic mutation).
{ECO:0000269|PubMed:19900088}.
/FTId=VAR_065235.
VARIANT 406 406 I -> L (functional polymorphism; the
mutant protein has defective apoptosis
and exerts a dominant-negative effect
when cotransfected with the wild-type
protein; dbSNP:rs80358239).
{ECO:0000269|PubMed:16446975,
ECO:0000269|PubMed:27378136,
ECO:0000269|PubMed:27535533}.
/FTId=VAR_037429.
VARIANT 410 410 V -> I (does not interfere with apoptosis
in a dominant negative manner;
dbSNP:rs13010627).
{ECO:0000269|PubMed:10187817,
ECO:0000269|PubMed:10412980,
ECO:0000269|PubMed:16446975}.
/FTId=VAR_014072.
VARIANT 414 414 A -> V (in NHL; somatic mutation;
dbSNP:rs28936699).
{ECO:0000269|PubMed:12010812}.
/FTId=VAR_037430.
VARIANT 444 444 P -> S (in dbSNP:rs41513147).
/FTId=VAR_055362.
VARIANT 446 446 Y -> C (associated with ALPS2A; does not
interfere with apoptosis in a dominant
negative manner; dbSNP:rs17860405).
{ECO:0000269|PubMed:16446975}.
/FTId=VAR_037431.
MUTAGEN 401 401 C->A: Abolishes proteolytic activity.
{ECO:0000269|PubMed:11717445}.
CONFLICT 68 68 E -> G (in Ref. 2; AAB46730).
{ECO:0000305}.
CONFLICT 268 268 T -> A (in Ref. 3; AAD28403).
{ECO:0000305}.
SEQUENCE 521 AA; 58951 MW; 840348AE602B8243 CRC64;
MKSQGQHWYS SSDKNCKVSF REKLLIIDSN LGVQDVENLK FLCIGLVPNK KLEKSSSASD
VFEHLLAEDL LSEEDPFFLA ELLYIIRQKK LLQHLNCTKE EVERLLPTRQ RVSLFRNLLY
ELSEGIDSEN LKDMIFLLKD SLPKTEMTSL SFLAFLEKQG KIDEDNLTCL EDLCKTVVPK
LLRNIEKYKR EKAIQIVTPP VDKEAESYQG EEELVSQTDV KTFLEALPQE SWQNKHAGSN
GNRATNGAPS LVSRGMQGAS ANTLNSETST KRAAVYRMNR NHRGLCVIVN NHSFTSLKDR
QGTHKDAEIL SHVFQWLGFT VHIHNNVTKV EMEMVLQKQK CNPAHADGDC FVFCILTHGR
FGAVYSSDEA LIPIREIMSH FTALQCPRLA EKPKLFFIQA CQGEEIQPSV SIEADALNPE
QAPTSLQDSI PAEADFLLGL ATVPGYVSFR HVEEGSWYIQ SLCNHLKKLV PRMLKFLEKT
MEIRGRKRTV WGAKQISATS LPTAISAQTP RPPMRRWSSV S


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