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P29466

- CASP1_HUMAN

UniProt

P29466 - CASP1_HUMAN

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Protein

Caspase-1

Gene

CASP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

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

Enzyme regulationi

Specifically inhibited by the cowpox virus Crma protein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei237 – 23711 Publication
Active sitei285 – 28511 Publication

GO - Molecular functioni

  1. cysteine-type endopeptidase activator activity involved in apoptotic process Source: ProtInc
  2. cysteine-type endopeptidase activity Source: RefGenome
  3. endopeptidase activity Source: ParkinsonsUK-UCL

GO - Biological processi

  1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: GOC
  2. apoptotic process Source: ProtInc
  3. cellular response to mechanical stimulus Source: UniProtKB
  4. cellular response to organic substance Source: MGI
  5. execution phase of apoptosis Source: RefGenome
  6. innate immune response Source: Reactome
  7. interleukin-1 beta production Source: Ensembl
  8. membrane hyperpolarization Source: Ensembl
  9. mitochondrial depolarization Source: Ensembl
  10. nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway Source: Reactome
  11. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  12. positive regulation of interleukin-1 alpha secretion Source: Ensembl
  13. positive regulation of interleukin-1 beta secretion Source: Ensembl
  14. programmed necrotic cell death Source: Ensembl
  15. proteolysis Source: UniProtKB
  16. pyroptosis Source: Ensembl
  17. regulation of inflammatory response Source: RefGenome
  18. response to ATP Source: Ensembl
  19. response to hypoxia Source: Ensembl
  20. response to lipopolysaccharide Source: Ensembl
  21. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

BRENDAi3.4.22.36. 2681.
ReactomeiREACT_23950. Interleukin-1 processing.
REACT_75776. NOD1/2 Signaling Pathway.
REACT_75777. The AIM2 inflammasome.
REACT_75808. The NLRP3 inflammasome.
REACT_75892. The IPAF inflammasome.
SABIO-RKP29466.
SignaLinkiP29466.

Protein family/group databases

MEROPSiC14.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Caspase-1 (EC:3.4.22.36)
Short name:
CASP-1
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:
Gene namesi
Name:CASP1
Synonyms:IL1BC, IL1BCE
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:1499. CASP1.

Subcellular locationi

GO - Cellular componenti

  1. AIM2 inflammasome complex Source: UniProtKB
  2. cytoplasm Source: RefGenome
  3. cytosol Source: Reactome
  4. extracellular region Source: Ensembl
  5. IPAF inflammasome complex Source: UniProtKB
  6. NLRP1 inflammasome complex Source: UniProtKB
  7. NLRP3 inflammasome complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi285 – 2851C → A or S: Loss of activity. 1 Publication

Organism-specific databases

PharmGKBiPA26083.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 119119PRO_0000004521Add
BLAST
Chaini120 – 297178Caspase-1 subunit p20PRO_0000004522Add
BLAST
Propeptidei298 – 31619PRO_0000004523Add
BLAST
Chaini317 – 40488Caspase-1 subunit p10PRO_0000004524Add
BLAST

Post-translational modificationi

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

Keywords - PTMi

Zymogen

Proteomic databases

MaxQBiP29466.
PaxDbiP29466.
PRIDEiP29466.

PTM databases

PhosphoSiteiP29466.

Miscellaneous databases

PMAP-CutDBP29466.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiP29466.
CleanExiHS_CASP1.
ExpressionAtlasiP29466. baseline and differential.
GenevestigatoriP29466.

Organism-specific databases

HPAiCAB002685.
HPA003056.

Interactioni

Subunit structurei

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. Both the p10 and p20 subunits interact with MEFV. Interacts with CARD17/INCA and CARD18.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FGF2P090382EBI-516667,EBI-977447
IL1AP015833EBI-516667,EBI-1749782
NLRC4Q9NPP44EBI-516667,EBI-1222527

Protein-protein interaction databases

BioGridi107284. 30 interactions.
DIPiDIP-175N.
IntActiP29466. 6 interactions.
MINTiMINT-201196.
STRINGi9606.ENSP00000410076.

Structurei

Secondary structure

1
404
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni129 – 1324
Helixi138 – 14710
Beta strandi148 – 1503
Turni158 – 1603
Beta strandi164 – 1696
Beta strandi174 – 1763
Helixi182 – 19514
Beta strandi199 – 2057
Helixi208 – 21912
Helixi222 – 2265
Beta strandi230 – 2367
Beta strandi242 – 2443
Beta strandi250 – 2523
Beta strandi255 – 2573
Helixi258 – 2658
Turni267 – 2693
Helixi271 – 2733
Beta strandi278 – 2836
Beta strandi287 – 2893
Beta strandi291 – 2988
Helixi316 – 3194
Beta strandi326 – 3338
Beta strandi340 – 3423
Turni343 – 3453
Helixi348 – 36013
Turni361 – 3633
Helixi366 – 37611
Beta strandi381 – 3833
Beta strandi388 – 3914
Beta strandi395 – 3973

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP29466.
SMRiP29466. Positions 2-89, 125-404.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29466.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9191CARDPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C14A family.Curated
Contains 1 CARD domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG274219.
GeneTreeiENSGT00760000118912.
HOVERGENiHBG076981.
InParanoidiP29466.
KOiK01370.
OMAiKSAEIYP.
PhylomeDBiP29466.
TreeFamiTF102023.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
3.40.50.1460. 1 hit.
InterProiIPR001315. CARD.
IPR029030. Caspase-like_dom.
IPR017350. Caspase_ICE-type.
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]
PfamiPF00619. CARD. 1 hit.
PF00656. Peptidase_C14. 1 hit.
[Graphical view]
PIRSFiPIRSF038001. Caspase_ICE. 1 hit.
PRINTSiPR00376. IL1BCENZYME.
SMARTiSM00114. CARD. 1 hit.
SM00115. CASc. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
PROSITEiPS50209. 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]

Sequences (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform Alpha (identifier: P29466) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MADKVLKEKR KLFIRSMGEG TINGLLDELL QTRVLNKEEM EKVKRENATV
60 70 80 90 100
MDKTRALIDS VIPKGAQACQ ICITYICEED SYLAGTLGLS ADQTSGNYLN
110 120 130 140 150
MQDSQGVLSS FPAPQAVQDN PAMPTSSGSE GNVKLCSLEE AQRIWKQKSA
160 170 180 190 200
EIYPIMDKSS RTRLALIICN EEFDSIPRRT GAEVDITGMT MLLQNLGYSV
210 220 230 240 250
DVKKNLTASD MTTELEAFAH RPEHKTSDST FLVFMSHGIR EGICGKKHSE
260 270 280 290 300
QVPDILQLNA IFNMLNTKNC PSLKDKPKVI IIQACRGDSP GVVWFKDSVG
310 320 330 340 350
VSGNLSLPTT EEFEDDAIKK AHIEKDFIAF CSSTPDNVSW RHPTMGSVFI
360 370 380 390 400
GRLIEHMQEY ACSCDVEEIF RKVRFSFEQP DGRAQMPTTE RVTLTRCFYL

FPGH
Length:404
Mass (Da):45,159
Last modified:April 1, 1993 - v1
Checksum:iABF33CF33CC71584
GO
Isoform Beta (identifier: P29466-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     92-112: Missing.

Show »
Length:383
Mass (Da):42,888
Checksum:iC8D92A9B235B2E6F
GO
Isoform Gamma (identifier: P29466-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     20-112: Missing.

Show »
Length:311
Mass (Da):35,019
Checksum:i902A4384E49282C8
GO
Isoform Delta (identifier: P29466-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     20-112: Missing.
     288-335: Missing.

Note: Apoptosis inactive.

Show »
Length:263
Mass (Da):29,821
Checksum:i5ED98AC7864EB0BA
GO
Isoform Epsilon (identifier: P29466-5) [UniParc]FASTAAdd to Basket

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

Note: Apoptosis inactive.

Show »
Length:88
Mass (Da):10,417
Checksum:iF3D811149FCDF159
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti319 – 3191K → R in BAD97223. 1 PublicationCurated
Sequence conflicti402 – 4021P → L in BAD97223. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti15 – 151R → H.
Corresponds to variant rs1042743 [ dbSNP | Ensembl ].
VAR_048615

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei20 – 335316Missing in isoform Epsilon. 1 PublicationVSP_000797Add
BLAST
Alternative sequencei20 – 11293Missing in isoform Gamma and isoform Delta. 2 PublicationsVSP_000799Add
BLAST
Alternative sequencei92 – 11221Missing in isoform Beta. 2 PublicationsVSP_000798Add
BLAST
Alternative sequencei288 – 33548Missing in isoform Delta. 1 PublicationVSP_000800Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS53704.1. [P29466-3]
CCDS8329.1. [P29466-2]
CCDS8330.1. [P29466-1]
CCDS8331.1. [P29466-4]
CCDS8332.1. [P29466-5]
PIRiA54263. A42677.
A56084.
B56084.
C56084.
D56084.
RefSeqiNP_001214.1. NM_001223.4. [P29466-2]
NP_001244047.1. NM_001257118.2. [P29466-1]
NP_001244048.1. NM_001257119.2. [P29466-2]
NP_150634.1. NM_033292.3. [P29466-1]
NP_150635.1. NM_033293.3. [P29466-3]
NP_150636.1. NM_033294.3. [P29466-4]
NP_150637.1. NM_033295.3. [P29466-5]
UniGeneiHs.2490.

Genome annotation databases

EnsembliENST00000353247; ENSP00000344132; 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]
GeneIDi834.
KEGGihsa:834.
UCSCiuc001pig.4. human. [P29466-3]
uc001pim.5. human. [P29466-1]
uc009yxi.4. human. [P29466-2]
uc021qpr.2. human. [P29466-4]
uc021qps.2. human. [P29466-5]

Polymorphism databases

DMDMi266321.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS53704.1. [P29466-3 ]
CCDS8329.1. [P29466-2 ]
CCDS8330.1. [P29466-1 ]
CCDS8331.1. [P29466-4 ]
CCDS8332.1. [P29466-5 ]
PIRi A54263. A42677.
A56084.
B56084.
C56084.
D56084.
RefSeqi NP_001214.1. NM_001223.4. [P29466-2 ]
NP_001244047.1. NM_001257118.2. [P29466-1 ]
NP_001244048.1. NM_001257119.2. [P29466-2 ]
NP_150634.1. NM_033292.3. [P29466-1 ]
NP_150635.1. NM_033293.3. [P29466-3 ]
NP_150636.1. NM_033294.3. [P29466-4 ]
NP_150637.1. NM_033295.3. [P29466-5 ]
UniGenei Hs.2490.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P29466.
SMRi P29466. Positions 2-89, 125-404.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107284. 30 interactions.
DIPi DIP-175N.
IntActi P29466. 6 interactions.
MINTi MINT-201196.
STRINGi 9606.ENSP00000410076.

Chemistry

BindingDBi P29466.
ChEMBLi CHEMBL4801.
DrugBanki DB01017. Minocycline.
GuidetoPHARMACOLOGYi 1617.

Protein family/group databases

MEROPSi C14.001.

PTM databases

PhosphoSitei P29466.

Polymorphism databases

DMDMi 266321.

Proteomic databases

MaxQBi P29466.
PaxDbi P29466.
PRIDEi P29466.

Protocols and materials databases

DNASUi 834.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000353247 ; ENSP00000344132 ; 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 ]
GeneIDi 834.
KEGGi hsa:834.
UCSCi uc001pig.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

CTDi 834.
GeneCardsi GC11M104898.
HGNCi HGNC:1499. CASP1.
HPAi CAB002685.
HPA003056.
MIMi 147678. gene.
neXtProti NX_P29466.
PharmGKBi PA26083.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG274219.
GeneTreei ENSGT00760000118912.
HOVERGENi HBG076981.
InParanoidi P29466.
KOi K01370.
OMAi KSAEIYP.
PhylomeDBi P29466.
TreeFami TF102023.

Enzyme and pathway databases

BRENDAi 3.4.22.36. 2681.
Reactomei REACT_23950. Interleukin-1 processing.
REACT_75776. NOD1/2 Signaling Pathway.
REACT_75777. The AIM2 inflammasome.
REACT_75808. The NLRP3 inflammasome.
REACT_75892. The IPAF inflammasome.
SABIO-RK P29466.
SignaLinki P29466.

Miscellaneous databases

ChiTaRSi CASP1. human.
EvolutionaryTracei P29466.
GeneWikii Caspase_1.
GenomeRNAii 834.
NextBioi 3460.
PMAP-CutDB P29466.
PROi P29466.
SOURCEi Search...

Gene expression databases

Bgeei P29466.
CleanExi HS_CASP1.
ExpressionAtlasi P29466. baseline and differential.
Genevestigatori P29466.

Family and domain databases

Gene3Di 1.10.533.10. 1 hit.
3.40.50.1460. 1 hit.
InterProi IPR001315. CARD.
IPR029030. Caspase-like_dom.
IPR017350. Caspase_ICE-type.
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 ]
Pfami PF00619. CARD. 1 hit.
PF00656. Peptidase_C14. 1 hit.
[Graphical view ]
PIRSFi PIRSF038001. Caspase_ICE. 1 hit.
PRINTSi PR00376. IL1BCENZYME.
SMARTi SM00114. CARD. 1 hit.
SM00115. CASc. 1 hit.
[Graphical view ]
SUPFAMi SSF47986. SSF47986. 1 hit.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), PARTIAL PROTEIN SEQUENCE, ACTIVE SITE.
  2. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. 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.

Entry informationi

Entry nameiCASP1_HUMAN
AccessioniPrimary (citable) accession number: P29466
Secondary accession number(s): B5MDZ1
, Q53EY6, Q6DMQ1, Q6GSS3, Q6PI75, Q9UCN3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: October 29, 2014
This is version 169 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3