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P29466 (CASP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 163. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | 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-1

Short name=CASP-1
EC=3.4.22.36
Alternative name(s):
Interleukin-1 beta convertase
Short name=IL-1BC
Interleukin-1 beta-converting enzyme
Short name=ICE
Short name=IL-1 beta-converting enzyme
p45

Cleaved into the following 2 chains:

  1. Caspase-1 subunit p20
  2. Caspase-1 subunit p10
Gene names
Name:CASP1
Synonyms:IL1BC, IL1BCE
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length404 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Thiol protease that cleaves IL-1 beta between an Asp and an Ala, releasing the mature cytokine which is involved in a variety of inflammatory processes. Important for defense against pathogens. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Can also promote apoptosis. Ref.3 Ref.7

Catalytic activity

Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Tyr-Val-Ala-Asp-|-.

Enzyme regulation

Specifically inhibited by the cowpox virus Crma protein.

Subunit structure

Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 20 kDa (p20) and a 10 kDa (p10) subunit. The p20 subunit can also form a heterodimer with the epsilon isoform whichthen has an inhibitory effect. May be a component of the inflammasome, a protein complex which also includes PYCARD, CARD8 and NALP2 and whose function would be the activation of proinflammatory caspases. Both the p10 and p20 subunits interact with MEFV. Interacts with CARD17/INCA and CARD18. Ref.9 Ref.11 Ref.12 Ref.14

Subcellular location

Cytoplasm.

Tissue specificity

Expressed in larger amounts in spleen and lung. Detected in liver, heart, small intestine, colon, thymus, prostate, skeletal muscle, peripheral blood leukocytes, kidney and testis. No expression in the brain. Ref.7

Post-translational modification

The two subunits are derived from the precursor sequence by an autocatalytic mechanism.

Sequence similarities

Belongs to the peptidase C14A family.

Contains 1 CARD domain.

Sequence caution

The sequence AAT72297.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAT72297.1 differs from that shown. Reason: Probable cloning artifact.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionHydrolase
Protease
Thiol protease
   PTMZymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of cysteine-type endopeptidase activity involved in apoptotic process

Traceable author statement PubMed 10799503. Source: GOC

apoptotic process

Traceable author statement Ref.3. Source: ProtInc

cellular response to mechanical stimulus

Inferred from expression pattern PubMed 19593445. Source: UniProtKB

cellular response to organic substance

Inferred from direct assay PubMed 19158679. Source: MGI

innate immune response

Traceable author statement. Source: Reactome

interleukin-1 beta production

Inferred from electronic annotation. Source: Ensembl

membrane hyperpolarization

Inferred from electronic annotation. Source: Ensembl

mitochondrial depolarization

Inferred from electronic annotation. Source: Ensembl

nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway

Traceable author statement. Source: Reactome

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

Inferred from expression pattern PubMed 12761501. Source: UniProtKB

positive regulation of interleukin-1 alpha secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-1 beta secretion

Inferred from electronic annotation. Source: Ensembl

proteolysis

Inferred from direct assay PubMed 12888622. Source: UniProtKB

pyroptosis

Inferred from electronic annotation. Source: Ensembl

regulation of inflammatory response

Inferred from electronic annotation. Source: Ensembl

response to ATP

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement Ref.2. Source: ProtInc

   Cellular_componentAIM2 inflammasome complex

Inferred from direct assay PubMed 19158676. Source: UniProtKB

IPAF inflammasome complex

Inferred from sequence or structural similarity. Source: UniProtKB

NLRP1 inflammasome complex

Inferred from direct assay PubMed 12191486. Source: UniProtKB

NLRP3 inflammasome complex

Inferred from direct assay Ref.10. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

extracellular region

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncysteine-type endopeptidase activator activity involved in apoptotic process

Traceable author statement PubMed 10799503. Source: ProtInc

cysteine-type endopeptidase activity

Traceable author statement. Source: Reactome

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform Alpha (identifier: P29466-1)

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 Beta (identifier: P29466-2)

The sequence of this isoform differs from the canonical sequence as follows:
     92-112: Missing.
Isoform Gamma (identifier: P29466-3)

The sequence of this isoform differs from the canonical sequence as follows:
     20-112: Missing.
Isoform Delta (identifier: P29466-4)

The sequence of this isoform differs from the canonical sequence as follows:
     20-112: Missing.
     288-335: Missing.
Note: Apoptosis inactive.
Isoform Epsilon (identifier: P29466-5)

The sequence of this isoform differs from the canonical sequence as follows:
     20-335: Missing.
Note: Apoptosis inactive.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 119119
PRO_0000004521
Chain120 – 297178Caspase-1 subunit p20
PRO_0000004522
Propeptide298 – 31619
PRO_0000004523
Chain317 – 40488Caspase-1 subunit p10
PRO_0000004524

Regions

Domain1 – 9191CARD

Sites

Active site2371 Ref.1
Active site2851 Ref.1

Natural variations

Alternative sequence20 – 335316Missing in isoform Epsilon.
VSP_000797
Alternative sequence20 – 11293Missing in isoform Gamma and isoform Delta.
VSP_000799
Alternative sequence92 – 11221Missing in isoform Beta.
VSP_000798
Alternative sequence288 – 33548Missing in isoform Delta.
VSP_000800
Natural variant151R → H.
Corresponds to variant rs1042743 [ dbSNP | Ensembl ].
VAR_048615

Experimental info

Mutagenesis2851C → A or S: Loss of activity. Ref.7
Sequence conflict3191K → R in BAD97223. Ref.4
Sequence conflict4021P → L in BAD97223. Ref.4

Secondary structure

......................................................... 404
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Alpha [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: ABF33CF33CC71584

FASTA40445,159
        10         20         30         40         50         60 
MADKVLKEKR KLFIRSMGEG TINGLLDELL QTRVLNKEEM EKVKRENATV MDKTRALIDS 

        70         80         90        100        110        120 
VIPKGAQACQ ICITYICEED SYLAGTLGLS ADQTSGNYLN MQDSQGVLSS FPAPQAVQDN 

       130        140        150        160        170        180 
PAMPTSSGSE GNVKLCSLEE AQRIWKQKSA EIYPIMDKSS RTRLALIICN EEFDSIPRRT 

       190        200        210        220        230        240 
GAEVDITGMT MLLQNLGYSV DVKKNLTASD MTTELEAFAH RPEHKTSDST FLVFMSHGIR 

       250        260        270        280        290        300 
EGICGKKHSE QVPDILQLNA IFNMLNTKNC PSLKDKPKVI IIQACRGDSP GVVWFKDSVG 

       310        320        330        340        350        360 
VSGNLSLPTT EEFEDDAIKK AHIEKDFIAF CSSTPDNVSW RHPTMGSVFI GRLIEHMQEY 

       370        380        390        400 
ACSCDVEEIF RKVRFSFEQP DGRAQMPTTE RVTLTRCFYL FPGH 

« Hide

Isoform Beta [UniParc].

Checksum: C8D92A9B235B2E6F
Show »

FASTA38342,888
Isoform Gamma [UniParc].

Checksum: 902A4384E49282C8
Show »

FASTA31135,019
Isoform Delta [UniParc].

Checksum: 5ED98AC7864EB0BA
Show »

FASTA26329,821
Isoform Epsilon [UniParc].

Checksum: F3D811149FCDF159
Show »

FASTA8810,417

References

« Hide 'large scale' references
[1]"A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes."
Thornberry N.A., Bull H.G., Calaycay J.R., Chapman K.T., Howard A.D., Kostura M.J., Miller D.K., Molineaux S.M., Weidner J.R., Aunins J., Elliston K.O., Ayala J.M., Casano F.J., Chin J., Ding G.J.-F., Egger L.A., Gaffney E.P., Limjuco G. expand/collapse author list , Palyha O.C., Raju M., Rolando A.M., Salley J.P., Yamin T.-T., Lee T.D., Shively J.E., McCross M., Mumford R.A., Schmidt J.A., Tocci M.J.
Nature 356:768-774(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), PARTIAL PROTEIN SEQUENCE, ACTIVE SITE.
[2]"Molecular cloning of the interleukin-1 beta converting enzyme."
Cerretti D.P., Kozlosky C.J., Mosley B., Nelson N., van Ness K., Greenstreet T.A., March C.J., Kronheim S.R., Druck T., Cannizzaro L.A., Huebner K., Black R.A.
Science 256:97-100(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), PROTEIN SEQUENCE OF 120-142.
[3]"Cloning and expression of four novel isoforms of human interleukin-1 beta converting enzyme with different apoptotic activities."
Alnemri E.S., Fernandes-Alnemri T., Litwack G.
J. Biol. Chem. 270:4312-4317(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA; DELTA; EPSILON AND GAMMA), ALTERNATIVE SPLICING, FUNCTION.
[4]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
[5]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
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. expand/collapse author list , 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.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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 GAMMA), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-404 (ISOFORM BETA).
Tissue: Testis.
[7]"Caspase-1 zeta, a new splice variant of caspase-1 gene."
Feng Q., Li P., Leung P.C.K., Auersperg N.
Genomics 84:587-591(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 32-404 (ISOFORM ALPHA), FUNCTION, MUTAGENESIS OF CYS-285, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[8]"Purification of interleukin-1 beta converting enzyme, the protease that cleaves the interleukin-1 beta precursor."
Kronheim S.R., Mumma A., Greenstreet T., Glackin P.J., Van Ness K., March C.J., Black R.A.
Arch. Biochem. Biophys. 296:698-703(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 120-142.
[9]"ICEBERG: a novel inhibitor of interleukin-1beta generation."
Humke E.W., Shriver S.K., Starovasnik M.A., Fairbrother W.J., Dixit V.M.
Cell 103:99-111(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CARD18.
[10]"NALP3 forms an IL-1beta-processing inflammasome with increased activity in Muckle-Wells autoinflammatory disorder."
Agostini L., Martinon F., Burns K., McDermott M.F., Hawkins P.N., Tschopp J.
Immunity 20:319-325(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: COMPONENT OF THE INFLAMMASOME.
[11]"INCA, a novel human caspase recruitment domain protein that inhibits interleukin-1beta generation."
Lamkanfi M., Denecker G., Kalai M., D'hondt K., Meeus A., Declercq W., Saelens X., Vandenabeele P.
J. Biol. Chem. 279:51729-51738(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CARD17.
[12]"The B30.2 domain of pyrin, the familial Mediterranean fever protein, interacts directly with caspase-1 to modulate IL-1beta production."
Chae J.J., Wood G., Masters S.L., Richard K., Park G., Smith B.J., Kastner D.L.
Proc. Natl. Acad. Sci. U.S.A. 103:9982-9987(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MEFV.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Crystal structure of the cysteine protease interleukin-1 beta-converting enzyme: a (p20/p10)2 homodimer."
Walker N.P.C., Talanian R.V., Brady K.D., Dang L.C., Bump N.J., Ferenz C.R., Franklin S., Ghayur T., Hackett M.C., Hammill L.D., Herzog L., Hugunin M., Houy W., Mankovich J.A., McGuiness L., Orlewicz E., Paskind M., Pratt C.A. expand/collapse author list , Reis P., Summani A., Terranova M., Welch J.P., Xiong L., Moeller A., Tracey D.E., Kamen R., Wong W.W.
Cell 78:343-352(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), SUBUNIT.
[15]"A combinatorial approach for determining protease specificities: application to interleukin-1beta converting enzyme (ICE)."
Rano T.A., Timkey T., Peterson E.P., Rotonda J., Nicholson D.W., Becker J.W., Chapman K.T., Thornberry N.A.
Chem. Biol. 4:149-155(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.73 ANGSTROMS).
[16]"Peptide based interleukin-1 beta converting enzyme (ICE) inhibitors: synthesis, structure activity relationships and crystallographic study of the ICE-inhibitor complex."
Okamoto Y., Anan H., Nakai E., Morihira K., Yonetoku Y., Kurihara H., Sakashita H., Terai Y., Takeuchi M., Shibanuma T., Isomura Y.
Chem. Pharm. Bull. 47:11-21(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
[17]"Crystal structures of a ligand-free and malonate-bound human caspase-1: implications for the mechanism of substrate binding."
Romanowski M.J., Scheer J.M., O'Brien T., McDowell R.S.
Structure 12:1361-1371(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 120-404 OF MUTANT ALA-285.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X65019 mRNA. Translation: CAA46153.1.
M87507 mRNA. Translation: AAA66942.1.
U13697 mRNA. Translation: AAC50107.1.
U13698 mRNA. Translation: AAC50108.1.
U13699 mRNA. Translation: AAC50109.1.
U13700 mRNA. Translation: AAC50110.1.
AK223503 mRNA. Translation: BAD97223.1.
AP001153 Genomic DNA. No translation available.
BC041689 mRNA. Translation: AAH41689.1.
BC062327 mRNA. Translation: AAH62327.1.
AY660536 mRNA. Translation: AAT72297.1. Sequence problems.
PIRA42677. A54263.
A56084.
B56084.
C56084.
D56084.
RefSeqNP_001214.1. NM_001223.4.
NP_001244047.1. NM_001257118.2.
NP_001244048.1. NM_001257119.2.
NP_150634.1. NM_033292.3.
NP_150635.1. NM_033293.3.
NP_150636.1. NM_033294.3.
NP_150637.1. NM_033295.3.
UniGeneHs.2490.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BMQX-ray2.50A131-297[»]
B317-404[»]
1IBCX-ray2.73A104-297[»]
B317-404[»]
1ICEX-ray2.60A131-297[»]
B317-404[»]
1RWKX-ray2.30A120-297[»]
B317-404[»]
1RWMX-ray2.70A120-297[»]
B317-404[»]
1RWNX-ray2.00A120-297[»]
B317-404[»]
1RWOX-ray2.10A120-297[»]
B317-404[»]
1RWPX-ray2.20A120-297[»]
B317-404[»]
1RWVX-ray2.10A120-297[»]
B317-404[»]
1RWWX-ray2.80A120-297[»]
B317-404[»]
1RWXX-ray1.85A120-297[»]
B317-404[»]
1SC1X-ray2.60A120-297[»]
B317-404[»]
1SC3X-ray1.80A120-297[»]
B317-404[»]
1SC4X-ray2.10A120-297[»]
B317-404[»]
2FQQX-ray3.30A120-297[»]
B317-404[»]
2H48X-ray2.20A120-297[»]
B317-404[»]
2H4WX-ray2.00A120-297[»]
B317-404[»]
2H4YX-ray1.90A120-297[»]
B317-404[»]
2H51X-ray2.10A120-297[»]
B317-404[»]
2H54X-ray1.80A120-297[»]
B317-404[»]
2HBQX-ray1.80A120-297[»]
B317-404[»]
2HBRX-ray2.20A120-297[»]
B317-404[»]
2HBYX-ray2.10A120-297[»]
B317-404[»]
2HBZX-ray1.90A120-297[»]
B317-404[»]
3D6FX-ray1.90A120-297[»]
B317-404[»]
3D6HX-ray2.00A120-297[»]
B317-404[»]
3D6MX-ray1.80A120-297[»]
B317-404[»]
3E4CX-ray2.05A/B104-404[»]
3NS7X-ray2.60A136-297[»]
B317-404[»]
ProteinModelPortalP29466.
SMRP29466. Positions 2-89, 125-404.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107284. 24 interactions.
DIPDIP-175N.
IntActP29466. 6 interactions.
MINTMINT-201196.
STRING9606.ENSP00000410076.

Chemistry

BindingDBP29466.
ChEMBLCHEMBL4801.
DrugBankDB01017. Minocycline.
DB00859. Penicillamine.
GuidetoPHARMACOLOGY1617.

Protein family/group databases

MEROPSC14.001.

PTM databases

PhosphoSiteP29466.

Polymorphism databases

DMDM266321.

Proteomic databases

PaxDbP29466.
PRIDEP29466.

Protocols and materials databases

DNASU834.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000353247; ENSP00000344132; ENSG00000137752. [P29466-5]
ENST00000393136; ENSP00000376844; ENSG00000137752. [P29466-2]
ENST00000415981; ENSP00000408446; ENSG00000137752. [P29466-5]
ENST00000436863; ENSP00000410076; ENSG00000137752. [P29466-1]
ENST00000446369; ENSP00000403260; ENSG00000137752. [P29466-4]
ENST00000525825; ENSP00000434779; ENSG00000137752. [P29466-2]
ENST00000526568; ENSP00000434250; ENSG00000137752. [P29466-3]
ENST00000531166; ENSP00000434303; ENSG00000137752. [P29466-5]
ENST00000533400; ENSP00000433138; ENSG00000137752. [P29466-1]
ENST00000534497; ENSP00000436875; ENSG00000137752. [P29466-4]
ENST00000593315; ENSP00000469724; ENSG00000137752. [P29466-2]
ENST00000594519; ENSP00000472457; ENSG00000137752. [P29466-4]
ENST00000598974; ENSP00000470811; ENSG00000137752. [P29466-1]
GeneID834.
KEGGhsa:834.
UCSCuc001pig.4. human. [P29466-3]
uc001pim.5. human. [P29466-1]
uc009yxi.4. human. [P29466-2]
uc021qpr.2. human. [P29466-4]
uc021qps.2. human. [P29466-5]

Organism-specific databases

CTD834.
GeneCardsGC11M104898.
HGNCHGNC:1499. CASP1.
HPACAB002685.
HPA003056.
MIM147678. gene.
neXtProtNX_P29466.
PharmGKBPA26083.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG274219.
HOVERGENHBG076981.
InParanoidP29466.
KOK01370.
OMAKSAEIYP.
PhylomeDBP29466.
TreeFamTF102023.

Enzyme and pathway databases

BRENDA3.4.22.36. 2681.
ReactomeREACT_6900. Immune System.
SABIO-RKP29466.
SignaLinkP29466.

Gene expression databases

ArrayExpressP29466.
BgeeP29466.
CleanExHS_CASP1.
GenevestigatorP29466.

Family and domain databases

Gene3D1.10.533.10. 1 hit.
InterProIPR001315. CARD.
IPR017350. Caspase_IL-1_beta.
IPR011029. DEATH-like_dom.
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]
PfamPF00619. CARD. 1 hit.
PF00656. Peptidase_C14. 1 hit.
[Graphical view]
PIRSFPIRSF038001. Caspase_ICE. 1 hit.
PRINTSPR00376. IL1BCENZYME.
SMARTSM00114. CARD. 1 hit.
SM00115. CASc. 1 hit.
[Graphical view]
SUPFAMSSF47986. SSF47986. 1 hit.
PROSITEPS50209. CARD. 1 hit.
PS01122. CASPASE_CYS. 1 hit.
PS01121. CASPASE_HIS. 1 hit.
PS50207. CASPASE_P10. 1 hit.
PS50208. CASPASE_P20. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCASP1. human.
EvolutionaryTraceP29466.
GeneWikiCaspase_1.
GenomeRNAi834.
NextBio3460.
PMAP-CutDBP29466.
PROP29466.
SOURCESearch...

Entry information

Entry nameCASP1_HUMAN
AccessionPrimary (citable) accession number: P29466
Secondary accession number(s): B5MDZ1 expand/collapse secondary AC list , Q53EY6, Q6DMQ1, Q6GSS3, Q6PI75, Q9UCN3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: April 16, 2014
This is version 163 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 11

Human chromosome 11: entries, gene names and cross-references to MIM