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Q92851 (CASPA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 155. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Caspase-10

Short name=CASP-10
EC=3.4.22.63
Alternative name(s):
Apoptotic protease Mch-4
FAS-associated death domain protein interleukin-1B-converting enzyme 2
Short name=FLICE2
ICE-like apoptotic protease 4

Cleaved into the following 2 chains:

  1. Caspase-10 subunit p23/17
  2. Caspase-10 subunit p12
Gene names
Name:CASP10
Synonyms:MCH4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length521 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.12

Isoform C is proteolytically inactive. Ref.12

Catalytic activity

Strict requirement for Asp at position P1 and has a preferred cleavage sequence of Leu-Gln-Thr-Asp-|-Gly.

Enzyme regulation

Negatively regulated by RFFL through proteasomal degradation. Ref.14

Subunit structure

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. Ref.12 Ref.14

Tissue specificity

Detectable in most tissues. Lowest expression is seen in brain, kidney, prostate, testis and colon.

Post-translational modification

Cleavage by granzyme B and autocatalytic activity generate the two active subunits.

Involvement in 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15 Ref.18

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.
Note: The gene represented in this entry is involved in disease pathogenesis. Ref.16

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.
Note: The gene represented in this entry is involved in disease pathogenesis. Ref.17

Sequence similarities

Belongs to the peptidase C14A family.

Contains 2 DED (death effector) domains.

Ontologies

Keywords
   Biological processApoptosis
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainRepeat
   Molecular functionHydrolase
Protease
Thiol protease
   PTMZymogen
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Traceable author statement. Source: Reactome

apoptotic signaling pathway

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype PubMed 12884866. Source: UniProtKB

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of apoptotic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentCD95 death-inducing signaling complex

Inferred from direct assay Ref.12. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

plasma membrane

Traceable author statement. Source: Reactome

ripoptosome

Inferred from direct assay PubMed 21737330. Source: UniProtKB

   Molecular_functioncysteine-type endopeptidase activity

Traceable author statement Ref.15Ref.1. Source: ProtInc

cysteine-type endopeptidase activity involved in apoptotic signaling pathway

Inferred from mutant phenotype Ref.12. Source: UniProtKB

death effector domain binding

Inferred from physical interaction Ref.12. Source: UniProtKB

ubiquitin protein ligase binding

Inferred from physical interaction Ref.14. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: Q92851-1)

Also known as: 10-A;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform B (identifier: Q92851-2)

Also known as: 10-B; 10-S;

The sequence of this isoform differs from the canonical sequence as follows:
     229-271: Missing.
     473-521: MLKFLEKTME...PPMRRWSSVS → HEDILSILTA...FPVPLDALSL
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform D (identifier: Q92851-4)

Also known as: 10-D; 10-L;

The sequence of this isoform differs from the canonical sequence as follows:
     473-521: MLKFLEKTME...PPMRRWSSVS → HEDILSILTA...FPVPLDALSL
Isoform C (identifier: Q92851-3)

Also known as: 10-C;

The sequence of this isoform differs from the canonical sequence as follows:
     241-273: GNRATNGAPSLVSRGMQGASANTLNSETSTKRA → EGSCVQDESEPQRPLCHCQQPQLYLPEGQTRNP
     274-521: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 5 (identifier: Q92851-5)

The sequence of this isoform differs from the canonical sequence as follows:
     229-271: Missing.
Isoform 6 (identifier: Q92851-6)

The sequence of this isoform differs from the canonical sequence as follows:
     241-307: Missing.
     473-521: MLKFLEKTME...PPMRRWSSVS → HEDILSILTA...FPVPLDALSL
Isoform 7 (identifier: Q92851-7)

The sequence of this isoform differs from the canonical sequence as follows:
     229-247: QESWQNKHAGSNGNRATNG → EGVFVFLNEGDRGNSPDDL
     248-521: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 219219
PRO_0000004644
Chain220 – 415196Caspase-10 subunit p23/17
PRO_0000004645
Chain416 – 521106Caspase-10 subunit p12
PRO_0000004646

Regions

Domain19 – 9779DED 1
Domain114 – 18774DED 2

Sites

Active site3581 By similarity
Active site4011 By similarity

Natural variations

Alternative sequence229 – 27143Missing in isoform B and isoform 5.
VSP_000819
Alternative sequence229 – 24719QESWQ…RATNG → EGVFVFLNEGDRGNSPDDL in isoform 7.
VSP_053333
Alternative sequence241 – 30767Missing in isoform 6.
VSP_037229
Alternative sequence241 – 27333GNRAT…STKRA → EGSCVQDESEPQRPLCHCQQ PQLYLPEGQTRNP in isoform C.
VSP_000821
Alternative sequence248 – 521274Missing in isoform 7.
VSP_053334
Alternative sequence274 – 521248Missing in isoform C.
VSP_000822
Alternative sequence473 – 52149MLKFL…WSSVS → HEDILSILTAVNDDVSRRVD KQGTKKQMPQPAFTLRKKLV FPVPLDALSL in isoform B, isoform D and isoform 6.
VSP_000820
Natural variant141K → T Found in a colon cancer sample; somatic mutation. Ref.21
VAR_065233
Natural variant211R → C Found in a multiple myeloma sample; somatic mutation. Ref.20
VAR_065234
Natural variant1471M → T in GASC; somatic mutation; impairs CASP10-mediated apoptosis. Ref.17
Corresponds to variant rs121909776 [ dbSNP | Ensembl ].
VAR_037428
Natural variant2391S → C. Ref.7
Corresponds to variant rs41473647 [ dbSNP | Ensembl ].
VAR_055361
Natural variant2851L → F in ALPS2A. Ref.15
Corresponds to variant rs17860403 [ dbSNP | Ensembl ].
VAR_014071
Natural variant2851L → P Found in a T-acute lymphoblastic leukemia sample; somatic mutation. Ref.20
VAR_065235
Natural variant4061I → L in ALPS2A; the mutant protein has defective apoptosis and exerts a dominant-negative effect when cotransfected with the wild-type protein. Ref.18
Corresponds to variant rs80358239 [ dbSNP | Ensembl ].
VAR_037429
Natural variant4101V → I Does not interfere with apoptosis in a dominant negative manner. Ref.3 Ref.7 Ref.15 Ref.18
Corresponds to variant rs13010627 [ dbSNP | Ensembl ].
VAR_014072
Natural variant4141A → V in NHL; somatic mutation. Ref.16
Corresponds to variant rs28936699 [ dbSNP | Ensembl ].
VAR_037430
Natural variant4441P → S. Ref.7
Corresponds to variant rs41513147 [ dbSNP | Ensembl ].
VAR_055362
Natural variant4461Y → C Associated with ALPS2A; does not interfere with apoptosis in a dominant negative manner. Ref.7 Ref.18
Corresponds to variant rs17860405 [ dbSNP | Ensembl ].
VAR_037431
Isoform B:
Natural variant4791L → I.
Corresponds to variant rs13006529 [ dbSNP | Ensembl ].
Isoform D:
Natural variant5221L → I Not associated with significantly altered cutaneous melanoma risk.
Corresponds to variant rs13006529 [ dbSNP | Ensembl ].
Isoform 6:
Natural variant4551L → I.
Corresponds to variant rs13006529 [ dbSNP | Ensembl ].

Experimental info

Mutagenesis4011C → A: Abolishes proteolytic activity. Ref.12
Sequence conflict681E → G in AAB46730. Ref.2
Sequence conflict2681T → A in AAD28403. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform A (10-A) [UniParc].

Last modified January 11, 2001. Version 3.
Checksum: 840348AE602B8243

FASTA52158,951
        10         20         30         40         50         60 
MKSQGQHWYS SSDKNCKVSF REKLLIIDSN LGVQDVENLK FLCIGLVPNK KLEKSSSASD 

        70         80         90        100        110        120 
VFEHLLAEDL LSEEDPFFLA ELLYIIRQKK LLQHLNCTKE EVERLLPTRQ RVSLFRNLLY 

       130        140        150        160        170        180 
ELSEGIDSEN LKDMIFLLKD SLPKTEMTSL SFLAFLEKQG KIDEDNLTCL EDLCKTVVPK 

       190        200        210        220        230        240 
LLRNIEKYKR EKAIQIVTPP VDKEAESYQG EEELVSQTDV KTFLEALPQE SWQNKHAGSN 

       250        260        270        280        290        300 
GNRATNGAPS LVSRGMQGAS ANTLNSETST KRAAVYRMNR NHRGLCVIVN NHSFTSLKDR 

       310        320        330        340        350        360 
QGTHKDAEIL SHVFQWLGFT VHIHNNVTKV EMEMVLQKQK CNPAHADGDC FVFCILTHGR 

       370        380        390        400        410        420 
FGAVYSSDEA LIPIREIMSH FTALQCPRLA EKPKLFFIQA CQGEEIQPSV SIEADALNPE 

       430        440        450        460        470        480 
QAPTSLQDSI PAEADFLLGL ATVPGYVSFR HVEEGSWYIQ SLCNHLKKLV PRMLKFLEKT 

       490        500        510        520 
MEIRGRKRTV WGAKQISATS LPTAISAQTP RPPMRRWSSV S 

« Hide

Isoform B (10-B) (10-S) [UniParc].

Checksum: 1467FD7A4EE003FF
Show »

FASTA47954,566
Isoform D (10-D) (10-L) [UniParc].

Checksum: 34847E07B3DFA688
Show »

FASTA52258,994
Isoform C (10-C) [UniParc].

Checksum: 1146630514EE38DC
Show »

FASTA27331,419
Isoform 5 [UniParc].

Checksum: E78035535F8EF57B
Show »

FASTA47854,523
Isoform 6 [UniParc].

Checksum: 89037FC3EC173616
Show »

FASTA45551,785
Isoform 7 [UniParc].

Checksum: 52370B5AD12C4DCF
Show »

FASTA24728,364

References

« Hide 'large scale' references
[1]"In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains."
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.
Proc. Natl. Acad. Sci. U.S.A. 93:7464-7469(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), VARIANT ILE-479 (ISOFORM B).
Tissue: T-cell.
[2]"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."
Vincenz C., Dixit V.M.
J. Biol. Chem. 272:6578-6583(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
[3]"Molecular cloning and characterization of two novel pro-apoptotic isoforms of caspase-10."
Ng P.W., Porter A.G., Janicke R.U.
J. Biol. Chem. 274:10301-10308(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS C AND D), VARIANT ILE-410, VARIANT ILE-522 (ISOFORM D).
Tissue: Spleen and Thymus.
[4]"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."
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.
Genomics 71:200-213(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS A AND B), VARIANT ILE-479 (ISOFORM B).
[5]"A novel human caspase 10 isoform participating in Fas-induced apoptosis."
Vonarbourg C., Fischer A., Rieux-Laucat F.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6), VARIANT ILE-455 (ISOFORM 6).
Tissue: Blood.
[6]"Three novel isoforms of caspase family that are deficient of conservative CASP domain."
Wang P.Z.
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7).
[7]NIEHS SNPs program
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CYS-239; ILE-410; SER-444; CYS-446 AND ILE-522 (ISOFORM 2).
[8]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
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. expand/collapse author list , 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.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"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] (ISOFORM D).
Tissue: Brain.
[11]"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."
Srinivasula S.M., Ahmad M., Fernandes-Alnemri T., Litwack G., Alnemri E.S.
Proc. Natl. Acad. Sci. U.S.A. 93:14486-14491(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, PROTEOLYTIC PROCESSING.
[12]"Caspase-10 is an initiator caspase in death receptor signaling."
Wang J., Chun H.J., Wong W., Spencer D.M., Lenardo M.J.
Proc. Natl. Acad. Sci. U.S.A. 98:13884-13888(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SELF-ASSOCIATION, INTERACTION WITH FADD, INTERACTION WITH CASP8, IDENTIFICATION IN A COMPLEX WITH FAS; FADD AND CASP8, MUTAGENESIS OF CYS-401.
[13]"An unappreciated role for RNA surveillance."
Hillman R.T., Green R.E., Brenner S.E.
Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
[14]"Suppression of caspase-8- and -10-associated RING proteins results in sensitization to death ligands and inhibition of tumor cell growth."
McDonald E.R. III, El-Deiry W.S.
Proc. Natl. Acad. Sci. U.S.A. 101:6170-6175(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RFFL, ENZYME REGULATION.
[15]"Inherited human caspase 10 mutations underlie defective lymphocyte and dendritic cell apoptosis in autoimmune lymphoproliferative syndrome type II."
Wang J., Zheng L., Lobito A., Chan F.K., Dale J., Sneller M., Yao X., Puck J.M., Straus S.E., Lenardo M.J.
Cell 98:47-58(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ALPS2A PHE-285, VARIANT ILE-410, ALTERNATIVE SPLICING (ISOFORMS B AND D).
[16]"Inactivating mutations of CASP10 gene in non-Hodgkin lymphomas."
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.
Blood 99:4094-4099(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT NHL VAL-414.
[17]"Inactivating mutations of the caspase-10 gene in gastric cancer."
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.
Oncogene 21:2919-2925(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GASC THR-147, CHARACTERIZATION OF VARIANT GASC THR-147.
[18]"Genetic alterations in caspase-10 may be causative or protective in autoimmune lymphoproliferative syndrome."
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.
Hum. Genet. 119:284-294(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ALPS2A LEU-406, VARIANTS ILE-410 AND CYS-446, CHARACTERIZATION OF VARIANTS ALPS2A LEU-406, CHARACTERIZATION OF VARIANTS ILE-410 AND CYS-446.
[19]"Genetic variants and haplotypes of the caspase-8 and caspase-10 genes contribute to susceptibility to cutaneous melanoma."
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.
Hum. Mutat. 29:1443-1451(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ILE-522 (ISOFORM D), RISK FACTOR FOR CUTANEOUS MELANOMA.
[20]"Mutational analysis of CASP10 gene in acute leukaemias and multiple myelomas."
Kim M.S., Oh J.E., Min C.K., Lee S., Chung N.G., Yoo N.J., Lee S.H.
Pathology 41:484-487(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CYS-21 AND PRO-285.
[21]"Mutational analysis of CASP10 gene in colon, breast, lung and hepatocellular carcinomas."
Oh J.E., Kim M.S., Ahn C.H., Kim S.S., Han J.Y., Lee S.H., Yoo N.J.
Pathology 42:73-76(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT THR-14.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U60519 mRNA. Translation: AAC50644.1.
U86214 mRNA. Translation: AAB46730.1.
AF111344 mRNA. Translation: AAD28402.1.
AF111345 mRNA. Translation: AAD28403.1.
AB038979 Genomic DNA. Translation: BAB32553.1.
AB038979 Genomic DNA. Translation: BAB32554.1.
AJ487678 mRNA. Translation: CAD32371.1.
AJ487679 mRNA. Translation: CAD32372.1.
AY690601 mRNA. Translation: AAU00989.1.
EF050529 Genomic DNA. Translation: ABJ53426.1.
AC007283 Genomic DNA. Translation: AAY24291.1.
CH471063 Genomic DNA. Translation: EAW70248.1.
CH471063 Genomic DNA. Translation: EAW70249.1.
BC042844 mRNA. Translation: AAH42844.1.
RefSeqNP_001193453.1. NM_001206524.1.
NP_001193471.1. NM_001206542.1.
NP_001221.2. NM_001230.4.
NP_116756.2. NM_032974.4.
NP_116758.1. NM_032976.3.
NP_116759.2. NM_032977.3.
XP_005246967.1. XM_005246910.1.
XP_005246968.1. XM_005246911.1.
UniGeneHs.5353.

3D structure databases

ProteinModelPortalQ92851.
SMRQ92851. Positions 19-95, 113-191, 274-511.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107293. 88 interactions.
IntActQ92851. 21 interactions.
MINTMINT-201954.
STRING9606.ENSP00000286186.

Chemistry

BindingDBQ92851.
ChEMBLCHEMBL5037.

Protein family/group databases

MEROPSC14.011.

PTM databases

PhosphoSiteQ92851.

Polymorphism databases

DMDM12644463.

Proteomic databases

PaxDbQ92851.
PRIDEQ92851.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000272879; ENSP00000272879; ENSG00000003400. [Q92851-1]
ENST00000286186; ENSP00000286186; ENSG00000003400. [Q92851-4]
ENST00000313728; ENSP00000314599; ENSG00000003400. [Q92851-6]
ENST00000346817; ENSP00000237865; ENSG00000003400. [Q92851-2]
ENST00000360132; ENSP00000353250; ENSG00000003400. [Q92851-3]
ENST00000374650; ENSP00000363781; ENSG00000003400. [Q92851-7]
ENST00000448480; ENSP00000396835; ENSG00000003400. [Q92851-5]
GeneID843.
KEGGhsa:843.
UCSCuc002uxj.1. human. [Q92851-4]
uc002uxk.1. human. [Q92851-2]
uc002uxl.2. human. [Q92851-1]
uc002uxm.2. human. [Q92851-5]
uc010fta.1. human. [Q92851-6]
uc010ftb.2. human. [Q92851-3]

Organism-specific databases

CTD843.
GeneCardsGC02P202047.
HGNCHGNC:1500. CASP10.
HPACAB003780.
HPA017059.
MIM601762. gene.
603909. phenotype.
605027. phenotype.
613659. phenotype.
neXtProtNX_Q92851.
Orphanet3261. Autoimmune lymphoproliferative syndrome.
PharmGKBPA26084.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG303276.
HOVERGENHBG050803.
KOK04400.
OMAFTAKQCP.
OrthoDBEOG7CRTQM.
PhylomeDBQ92851.
TreeFamTF102023.

Enzyme and pathway databases

BRENDA3.4.22.63. 2681.
ReactomeREACT_578. Apoptosis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressQ92851.
BgeeQ92851.
CleanExHS_CASP10.
GenevestigatorQ92851.

Family and domain databases

Gene3D1.10.533.10. 2 hits.
InterProIPR011029. DEATH-like_dom.
IPR001875. DED.
IPR011600. Pept_C14_caspase.
IPR001309. Pept_C14_ICE_p20.
IPR016129. Pept_C14_ICE_p20_AS.
IPR002138. Pept_C14_p10.
IPR015917. Pept_C14A_p45_core.
[Graphical view]
PfamPF01335. DED. 2 hits.
PF00656. Peptidase_C14. 1 hit.
[Graphical view]
PRINTSPR00376. IL1BCENZYME.
SMARTSM00115. CASc. 1 hit.
SM00031. DED. 2 hits.
[Graphical view]
SUPFAMSSF47986. SSF47986. 2 hits.
PROSITEPS01122. CASPASE_CYS. 1 hit.
PS01121. CASPASE_HIS. 1 hit.
PS50207. CASPASE_P10. 1 hit.
PS50208. CASPASE_P20. 1 hit.
PS50168. DED. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCASP10. human.
GeneWikiCaspase_10.
GenomeRNAi843.
NextBio3530.
PMAP-CutDBQ8IUP5.
PROQ92851.
SOURCESearch...

Entry information

Entry nameCASPA_HUMAN
AccessionPrimary (citable) accession number: Q92851
Secondary accession number(s): Q68HC0 expand/collapse secondary AC list , Q6KF62, Q6KF63, Q8IUP5, Q8WYQ8, Q99845, Q9Y2U6, Q9Y2U7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 11, 2001
Last modified: April 16, 2014
This is version 155 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM