Reviewed, UniProtKB/Swiss-Prot P29466 (CASP1_HUMAN)

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=IL-1 beta-converting enzyme
      Short name=ICE
    p45
Cleaved into the following 2 chains:
    1- Recommended name:
            Caspase-1 subunit p20
    2- Recommended name:
            Caspase-1 subunit p10

Gene names

Name:	CASP1
Synonyms:	IL1BC, IL1BCE

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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.8 Ref.10 Ref.12
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.3
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.

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 Direct protein sequencing
Gene Ontology (GO)
Biological process	apoptosis Ref.7 Traceable author statement. Source: ProtInc positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from expression pattern. Source: UniProtKB proteolysis Ref.7 Inferred from direct assay. Source: UniProtKB regulation of apoptosis Inferred from electronic annotation. Source: InterPro signal transduction Ref.2 Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Inferred from direct assay. Source: HPA nucleus Inferred from direct assay. Source: HPA
Molecular function	caspase activator activity Traceable author statement. Source: ProtInc cysteine-type endopeptidase activity Traceable author statement. Source: ProtInc protein binding Ref.9 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FGF2	P09038	1	EBI-516667,EBI-977447
IL1A	P01583	3	EBI-516667,EBI-1749782
NLRC4	Q9NPP4	1	EBI-516667,EBI-1222527
NLRP1	Q9C000	1	EBI-516667,EBI-1220518

Alternative products

This entry describes 6 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.

Isoform Zeta (identifier: P29466-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: Missing.

Note: Can promote apoptosis.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 119

119

Ref.2 Ref.6

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

1 – 39

39

Missing in isoform Zeta.

VSP_021670

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: dbSNP rs1042743.

VAR_048615

Experimental info

Mutagenesis

285

1

C → A or S: Loss of activity. Ref.3

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 – 147

10

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 – 236

7

Beta strand

242 – 244

3

Beta strand

250 – 252

3

Helix

258 – 265

8

Turn

267 – 269

3

Helix

271 – 273

3

Beta strand

278 – 284

7

Beta strand

286 – 289

4

Beta strand

292 – 296

5

Beta strand

318 – 324

7

Beta strand

326 – 333

8

Turn

343 – 345

3

Helix

348 – 360

13

Turn

361 – 363

3

Helix

366 – 376

11

Beta strand

388 – 392

5

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. 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. 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. 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. Checksum: F3D811149FCDF159	FASTA	88	10,417
	10 20 30 40 50 60 MADKVLKEKR KLFIRSMGED NVSWRHPTMG SVFIGRLIEH MQEYACSCDV EEIFRKVRFS 70 80 FEQPDGRAQM PTTERVTLTR CFYLFPGH
	Isoform Zeta. Checksum: 13EDDE92AEB115E0	FASTA	365	40,659
	10 20 30 40 50 60 MEKVKRENAT VMDKTRALID SVIPKGAQAC QICITYICEE DSYLAGTLGL SADQTSGNYL 70 80 90 100 110 120 NMQDSQGVLS SFPAPQAVQD NPAMPTSSGS EGNVKLCSLE EAQRIWKQKS AEIYPIMDKS 130 140 150 160 170 180 SRTRLALIIC NEEFDSIPRR TGAEVDITGM TMLLQNLGYS VDVKKNLTAS DMTTELEAFA 190 200 210 220 230 240 HRPEHKTSDS TFLVFMSHGI REGICGKKHS EQVPDILQLN AIFNMLNTKN CPSLKDKPKV 250 260 270 280 290 300 IIIQACRGDS PGVVWFKDSV GVSGNLSLPT TEEFEDDAIK KAHIEKDFIA FCSSTPDNVS 310 320 330 340 350 360 WRHPTMGSVF IGRLIEHMQE YACSCDVEEI FRKVRFSFEQ PDGRAQMPTT ERVTLTRCFY LFPGH

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: 1574116] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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: 1373520] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE OF 120-142.
[3]	"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: 15498465] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ZETA), FUNCTION, MUTAGENESIS OF CYS-285, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[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]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GAMMA), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-404 (ISOFORM BETA). Tissue: Testis.
[6]	"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: 1321594] [Abstract] Cited for: PROTEIN SEQUENCE OF 120-142.
[7]	"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: 7876192] [Abstract] Cited for: ALTERNATIVE SPLICING, FUNCTION.
[8]	"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: 11051551] [Abstract] Cited for: INTERACTION WITH CARD18.
[9]	"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: 15030775] [Abstract] Cited for: COMPONENT OF THE INFLAMMASOME.
[10]	"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: 15383541] [Abstract] Cited for: INTERACTION WITH CARD17.
[11]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[12]	"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: 8044845] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), SUBUNIT.
[13]	"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: 9190289] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.73 ANGSTROMS).
[14]	"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: 9987822] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
[15]	"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: 15296730] [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

EMBLGenBankDDBJ

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.
AY660536 mRNA. Translation: AAT72297.1.
AK223503 mRNA. Translation: BAD97223.1.
BC041689 mRNA. Translation: AAH41689.1.
BC062327 mRNA. Translation: AAH62327.1.

IPI

IPI00021800.
IPI00219307.
IPI00219308.
IPI00219309.
IPI00219310.
IPI00797075.

PIR

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

RefSeq

NP_001214.1.
NP_150634.1.
NP_150635.1.
NP_150636.1.
NP_150637.1.

UniGene

Hs.2490

3D structure databases

PDBPDBe

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	[»]
3E4C	X-ray	2.05	A/B	104-404	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:175N.

IntAct

P29466. 5 interactions.

Protein family/group databases

MEROPS

C14.001.

PTM databases

PhosphoSite

P29466.

Proteomic databases

PRIDE

P29466.

Genome annotation databases

Ensembl

ENSG00000137752. Homo sapiens. [Contig view]

GeneID

834.

KEGG

hsa:834.

Organism-specific databases

GeneCards

GC11M104401.

H-InvDB

HIX0026261.
HIX0035831.

HGNC

HGNC:1499. CASP1.

HPA

CAB002685.
HPA003056.

MIM

147678. gene.

PharmGKB

PA26083.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P29466.

HOVERGEN

P29466.

OMA

P29466. RFSFEQP.

Enzyme and pathway databases

BRENDA

3.4.22.36. 247.

Pathway_Interaction_DB

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

Gene expression databases

ArrayExpress

P29466.

Bgee

P29466.

CleanEx

HS_CASP1.

GermOnline

ENSG00000137752. Homo sapiens.

Family and domain databases

InterPro

IPR001315. CARD.
IPR017350. Caspase_IL-1_beta.
IPR011029. DEATH-like.
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]

Gene3D

G3DSA:1.10.533.10. DEATH_like. 1 hit.

PANTHER

PTHR10454. Pept_C14_p45. 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]

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 Resources

BindingDB

P29466.

DrugBank

DB01017. Minocycline.
DB00859. Penicillamine.

NextBio

3460.

PMAP-CutDB

P29466.

SOURCE

Search...

Entry information

Entry name

CASP1_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	June 16, 2009
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)