P29466 (CASP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	404 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 which then 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. Interacts with CARD17/INCA and CARD18. Ref.9 Ref.11 Ref.13
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 process	Apoptosis
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Hydrolase Protease Thiol protease
PTM	Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	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 induction of apoptosis Inferred from electronic annotation. Source: Compara innate immune response Traceable author statement. Source: Reactome interleukin-1 beta production Inferred from electronic annotation. Source: Compara nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway Traceable author statement. Source: Reactome positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from expression pattern PubMed 12761501. Source: UniProtKB positive regulation of interleukin-1 alpha secretion Inferred from electronic annotation. Source: Compara positive regulation of interleukin-1 beta secretion Inferred from electronic annotation. Source: Compara protein processing Inferred from electronic annotation. Source: Compara proteolysis Inferred from direct assay PubMed 12888622. Source: UniProtKB response to ATP Inferred from electronic annotation. Source: Compara response to hypoxia Inferred from electronic annotation. Source: Compara
Cellular_component	AIM2 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: Compara
Molecular_function	cysteine-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

With	Entry	#Exp.	IntAct	Notes
FGF2	P09038	2	EBI-516667,EBI-977447
IL1A	P01583	3	EBI-516667,EBI-1749782
NLRC4	Q9NPP4	4	EBI-516667,EBI-1222527

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 119

119

PRO_0000004521

Chain

120 – 297

178

Caspase-1 subunit p20

PRO_0000004522

Propeptide

298 – 316

19

PRO_0000004523

Chain

317 – 404

88

Caspase-1 subunit p10

PRO_0000004524

Regions

Domain

1 – 91

91

CARD

Sites

Active site

237

1

Ref.1

Active site

285

1

Ref.1

Natural variations

Alternative sequence

20 – 335

316

Missing in isoform Epsilon.

VSP_000797

Alternative sequence

20 – 112

93

Missing in isoform Gamma and isoform Delta.

VSP_000799

Alternative sequence

92 – 112

21

Missing in isoform Beta.

VSP_000798

Alternative sequence

288 – 335

48

Missing in isoform Delta.

VSP_000800

Natural variant

15

1

R → H.
Corresponds to variant rs1042743 [ dbSNP | Ensembl ].

VAR_048615

Experimental info

Mutagenesis

285

1

C → A or S: Loss of activity. Ref.7

Sequence conflict

319

1

K → R in BAD97223. Ref.4

Sequence conflict

402

1

P → L in BAD97223. Ref.4

Secondary structure

1

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404

Helix Strand Turn

Details...

Turn

129 – 132

4

Helix

138 – 148

11

Helix

149 – 151

3

Turn

158 – 160

3

Beta strand

164 – 169

6

Beta strand

174 – 176

3

Helix

182 – 195

14

Beta strand

199 – 205

7

Helix

208 – 219

12

Helix

222 – 226

5

Beta strand

230 – 239

10

Beta strand

242 – 244

3

Beta strand

250 – 252

3

Helix

258 – 264

7

Turn

267 – 269

3

Helix

271 – 273

3

Beta strand

278 – 285

8

Beta strand

287 – 289

3

Beta strand

291 – 298

8

Helix

316 – 319

4

Beta strand

326 – 332

7

Beta strand

340 – 342

3

Helix

348 – 360

13

Turn

361 – 363

3

Helix

366 – 376

11

Beta strand

388 – 390

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform Alpha [UniParc]. Last modified April 1, 1993. Version 1. Checksum: ABF33CF33CC71584	FASTA	404	45,159
	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
	Isoform Beta [UniParc]. Checksum: C8D92A9B235B2E6F	FASTA	383	42,888
	10 20 30 40 50 60 MADKVLKEKR KLFIRSMGEG TINGLLDELL QTRVLNKEEM EKVKRENATV MDKTRALIDS 70 80 90 100 110 120 VIPKGAQACQ ICITYICEED SYLAGTLGLS AAPQAVQDNP AMPTSSGSEG NVKLCSLEEA 130 140 150 160 170 180 QRIWKQKSAE IYPIMDKSSR TRLALIICNE EFDSIPRRTG AEVDITGMTM LLQNLGYSVD 190 200 210 220 230 240 VKKNLTASDM TTELEAFAHR PEHKTSDSTF LVFMSHGIRE GICGKKHSEQ VPDILQLNAI 250 260 270 280 290 300 FNMLNTKNCP SLKDKPKVII IQACRGDSPG VVWFKDSVGV SGNLSLPTTE EFEDDAIKKA 310 320 330 340 350 360 HIEKDFIAFC SSTPDNVSWR HPTMGSVFIG RLIEHMQEYA CSCDVEEIFR KVRFSFEQPD 370 380 GRAQMPTTER VTLTRCFYLF PGH
	Isoform Gamma [UniParc]. Checksum: 902A4384E49282C8	FASTA	311	35,019
	10 20 30 40 50 60 MADKVLKEKR KLFIRSMGEA PQAVQDNPAM PTSSGSEGNV KLCSLEEAQR IWKQKSAEIY 70 80 90 100 110 120 PIMDKSSRTR LALIICNEEF DSIPRRTGAE VDITGMTMLL QNLGYSVDVK KNLTASDMTT 130 140 150 160 170 180 ELEAFAHRPE HKTSDSTFLV FMSHGIREGI CGKKHSEQVP DILQLNAIFN MLNTKNCPSL 190 200 210 220 230 240 KDKPKVIIIQ ACRGDSPGVV WFKDSVGVSG NLSLPTTEEF EDDAIKKAHI EKDFIAFCSS 250 260 270 280 290 300 TPDNVSWRHP TMGSVFIGRL IEHMQEYACS CDVEEIFRKV RFSFEQPDGR AQMPTTERVT 310 LTRCFYLFPG H
	Isoform Delta [UniParc]. Checksum: 5ED98AC7864EB0BA	FASTA	263	29,821
	10 20 30 40 50 60 MADKVLKEKR KLFIRSMGEA PQAVQDNPAM PTSSGSEGNV KLCSLEEAQR IWKQKSAEIY 70 80 90 100 110 120 PIMDKSSRTR LALIICNEEF DSIPRRTGAE VDITGMTMLL QNLGYSVDVK KNLTASDMTT 130 140 150 160 170 180 ELEAFAHRPE HKTSDSTFLV FMSHGIREGI CGKKHSEQVP DILQLNAIFN MLNTKNCPSL 190 200 210 220 230 240 KDKPKVIIIQ ACRGDNVSWR HPTMGSVFIG RLIEHMQEYA CSCDVEEIFR KVRFSFEQPD 250 260 GRAQMPTTER VTLTRCFYLF PGH
	Isoform Epsilon [UniParc]. Checksum: F3D811149FCDF159	FASTA	88	10,417
	10 20 30 40 50 60 MADKVLKEKR KLFIRSMGED NVSWRHPTMG SVFIGRLIEH MQEYACSCDV EEIFRKVRFS 70 80 FEQPDGRAQM PTTERVTLTR CFYLFPGH

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"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].
[13]	"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. , 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.
[14]	"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).
[15]	"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.
[16]	"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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.

IPI

IPI00021800.
IPI00219307.
IPI00219308.
IPI00219309.
IPI00219310.

PIR

A42677. A54263.
A56084.
B56084.
C56084.
D56084.

RefSeq

NP_001214.1. NM_001223.4.
NP_001244047.1. NM_001257118.1.
NP_001244048.1. NM_001257119.1.
NP_150634.1. NM_033292.3.
NP_150635.1. NM_033293.3.
NP_150636.1. NM_033294.3.
NP_150637.1. NM_033295.3.

UniGene

Hs.2490.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BMQ	X-ray	2.50	A	131-297	[»]
			B	317-404	[»]
1IBC	X-ray	2.73	A	104-297	[»]
			B	317-404	[»]
1ICE	X-ray	2.60	A	131-297	[»]
			B	317-404	[»]
1RWK	X-ray	2.30	A	120-297	[»]
			B	317-404	[»]
1RWM	X-ray	2.70	A	120-297	[»]
			B	317-404	[»]
1RWN	X-ray	2.00	A	120-297	[»]
			B	317-404	[»]
1RWO	X-ray	2.10	A	120-297	[»]
			B	317-404	[»]
1RWP	X-ray	2.20	A	120-297	[»]
			B	317-404	[»]
1RWV	X-ray	2.10	A	120-297	[»]
			B	317-404	[»]
1RWW	X-ray	2.80	A	120-297	[»]
			B	317-404	[»]
1RWX	X-ray	1.85	A	120-297	[»]
			B	317-404	[»]
1SC1	X-ray	2.60	A	120-297	[»]
			B	317-404	[»]
1SC3	X-ray	1.80	A	120-297	[»]
			B	317-404	[»]
1SC4	X-ray	2.10	A	120-297	[»]
			B	317-404	[»]
2FQQ	X-ray	3.30	A	120-297	[»]
			B	317-404	[»]
2H48	X-ray	2.20	A	120-297	[»]
			B	317-404	[»]
2H4W	X-ray	2.00	A	120-297	[»]
			B	317-404	[»]
2H4Y	X-ray	1.90	A	120-297	[»]
			B	317-404	[»]
2H51	X-ray	2.10	A	120-297	[»]
			B	317-404	[»]
2H54	X-ray	1.80	A	120-297	[»]
			B	317-404	[»]
2HBQ	X-ray	1.80	A	120-297	[»]
			B	317-404	[»]
2HBR	X-ray	2.20	A	120-297	[»]
			B	317-404	[»]
2HBY	X-ray	2.10	A	120-297	[»]
			B	317-404	[»]
2HBZ	X-ray	1.90	A	120-297	[»]
			B	317-404	[»]
3D6F	X-ray	1.90	A	120-297	[»]
			B	317-404	[»]
3D6H	X-ray	2.00	A	120-297	[»]
			B	317-404	[»]
3D6M	X-ray	1.80	A	120-297	[»]
			B	317-404	[»]
3E4C	X-ray	2.05	A/B	104-404	[»]
3NS7	X-ray	2.60	A	136-297	[»]
			B	317-404	[»]

ProteinModelPortal

P29466.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-175N.

IntAct

P29466. 6 interactions.

MINT

MINT-201196.

STRING

9606.ENSP00000410076.

Protein family/group databases

MEROPS

C14.001.

PTM databases

PhosphoSite

P29466.

Polymorphism databases

DMDM

266321.

Proteomic databases

PaxDb

P29466.

PRIDE

P29466.

Protocols and materials databases

DNASU

834.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000353247; ENSP00000344132; ENSG00000137752.
ENST00000393136; ENSP00000376844; ENSG00000137752.
ENST00000415981; ENSP00000408446; ENSG00000137752.
ENST00000436863; ENSP00000410076; ENSG00000137752.
ENST00000446369; ENSP00000403260; ENSG00000137752.
ENST00000525825; ENSP00000434779; ENSG00000137752.
ENST00000526568; ENSP00000434250; ENSG00000137752.
ENST00000531166; ENSP00000434303; ENSG00000137752.
ENST00000533400; ENSP00000433138; ENSG00000137752.
ENST00000534497; ENSP00000436875; ENSG00000137752.
ENST00000593315; ENSP00000469724; ENSG00000137752.
ENST00000594519; ENSP00000472457; ENSG00000137752.
ENST00000598974; ENSP00000470811; ENSG00000137752.

GeneID

834.

KEGG

hsa:834.

UCSC

uc001pig.3. human.
uc001pim.4. human.
uc009yxi.3. human.
uc010rvh.2. human.
uc010rvi.2. human.

Organism-specific databases

CTD

834.

GeneCards

GC11M104898.

HGNC

HGNC:1499. CASP1.

HPA

CAB002685.
HPA003056.

MIM

147678. gene.

neXtProt

NX_P29466.

PharmGKB

PA26083.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG274219.

HOVERGEN

HBG076981.

InParanoid

P29466.

KO

K01370.

OMA

KSAEIYP.

OrthoDB

EOG49W2FS.

PhylomeDB

P29466.

Enzyme and pathway databases

BRENDA

3.4.22.36. 2681.

Pathway_Interaction_DB

caspase_pathway. Caspase cascade in apoptosis.
anthraxpathway. Cellular roles of Anthrax toxin.
ifngpathway. IFN-gamma pathway.
il1pathway. IL1-mediated signaling events.

Reactome

REACT_6900. Immune System.

SABIO-RK

P29466.

SignaLink

P29466.

Gene expression databases

ArrayExpress

P29466.

Bgee

P29466.

CleanEx

HS_CASP1.

Genevestigator

P29466.

GermOnline

ENSG00000137752. Homo sapiens.

Family and domain databases

Gene3D

1.10.533.10. 1 hit.

InterPro

IPR001315. CARD.
IPR017350. Caspase_IL-1_beta.
IPR011029. DEATH-like_dom.
IPR011600. Pept_C14_cat.
IPR001309. Pept_C14_ICE_p20.
IPR016129. Pept_C14_ICE_p20_AS.
IPR002138. Pept_C14_p10.
IPR002398. Pept_C14_p45.
IPR015917. Pept_C14_p45_core.
[Graphical view]

PANTHER

PTHR10454. PTHR10454. 1 hit.

Pfam

PF00619. CARD. 1 hit.
PF00656. Peptidase_C14. 1 hit.
[Graphical view]

PIRSF

PIRSF038001. Caspase_ICE. 1 hit.

PRINTS

PR00376. IL1BCENZYME.

SMART

SM00114. CARD. 1 hit.
SM00115. CASc. 1 hit.
[Graphical view]

SUPFAM

SSF47986. DEATH_like. 1 hit.

PROSITE

PS50209. 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]

ProtoNet

Search...

Other

BindingDB

P29466.

ChEMBL

CHEMBL4801.

ChiTaRS

CASP1. human.

DrugBank

DB01017. Minocycline.
DB00859. Penicillamine.

EvolutionaryTrace

P29466.

GenomeRNAi

834.

NextBio

3460.

PMAP-CutDB

P29466.

SOURCE

Search...

Entry information

Entry name

CASP1_HUMAN

Accession

Primary (citable) accession number: P29466
Secondary accession number(s): B5MDZ1 , Q53EY6, Q6DMQ1, Q6GSS3, Q6PI75, Q9UCN3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	May 29, 2013
This is version 154 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.