Caspase-4 precursor - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P49662 (CASP4_HUMAN)

Last modified November 25, 2008. Version 84. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Caspase-4
      Short name=CASP-4
    EC=3.4.22.57
Alternative name(s):
    ICH-2 protease
    TX protease
    ICE(rel)-II
Cleaved into the following 2 chains:
    1- Recommended name:
            Caspase-4 subunit 1
    2- Recommended name:
            Caspase-4 subunit 2

Gene names

Name:	CASP4
Synonyms:	ICH2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	377 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Involved in the activation cascade of caspases responsible for apoptosis execution. Cleaves caspase-1.
Catalytic activity	Strict requirement for Asp at the P1 position. It has a preferred cleavage sequence of Tyr-Val-Ala-Asp-\|- but also cleaves at Asp-Glu-Val-Asp-\|-.
Subunit structure	Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a small and a large subunit By similarity.
Tissue specificity	Widely expressed, with highest levels in spleen and lung. Moderate expression in heart and liver, low expression in skeletal muscle, kidney and testis. Not found in the brain.
Post-translational modification	The two subunits are derived from the precursor sequence by an autocatalytic mechanism or by cleavage by Caspase-8.
Sequence similarities	Belongs to the peptidase C14 family. Contains 1 CARD domain.

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Ontologies

Keywords
Biological process	Apoptosis
Molecular function	Hydrolase Protease Thiol protease
PTM	Phosphoprotein Zymogen
Gene Ontology (GO)
Biological process	induction of apoptosis Ref.1 Traceable author statement. Source: ProtInc proteolysis Ref.3 Traceable author statement. Source: ProtInc
Cellular component	intracellular Inferred from electronic annotation. Source: InterPro
Molecular function	cysteine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
CDK2	P24941	1	EBI-1057327,EBI-375096
CTNNBIP1	Q9NSA3	1	EBI-1057327,EBI-747082
EIF2S3	P41091	1	EBI-1057327,EBI-1054228
GSN	P06396	1	EBI-1057327,EBI-351506
HEATR2	Q86Y56	1	EBI-1057327,EBI-719966
HIGD1A	Q9Y241	1	EBI-1057327,EBI-1051940
KIAA0776	O94874	1	EBI-1057327,EBI-1048088
MSH6	P52701	1	EBI-1057327,EBI-395529
MTHFD1L	Q6UB35	1	EBI-1057327,EBI-1046835
NUP93	Q8N1F7	1	EBI-1057327,EBI-1042703
PSMB1	P20618	1	EBI-1057327,EBI-372273
SLC25A22	Q9H936	1	EBI-1057327,EBI-1050588
SMC1A	Q14683	1	EBI-1057327,EBI-80690
SMC3	Q9UQE7	1	EBI-1057327,EBI-80718
SRPRB	Q9Y5M8	1	EBI-1057327,EBI-355393
VDAC3	Q9Y277	1	EBI-1057327,EBI-354196

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – ?80

Potential

PRO_0000004596

Chain

?81 – 270

190

Caspase-4 subunit 1

PRO_0000004597

Propeptide

271 – 289

Potential

PRO_0000004598

Chain

290 – 377

Caspase-4 subunit 2

PRO_0000004599

Regions

Domain

1 – 91

CARD

Sites

Active site

210

By similarity

Active site

258

Amino acid modifications

Modified residue

Phosphoserine

Experimental info

Mutagenesis

258

C → S: Loss of activity

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Sequences

Sequence

Length

Mass (Da)

Tools

P49662-1 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: DC7CCEC6E9D483EB
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FASTA

377

43,262

        10         20         30         40         50         60 
MAEGNHRKKP LKVLESLGKD FLTGVLDNLV EQNVLNWKEE EKKKYYDAKT EDKVRVMADS 

        70         80         90        100        110        120 
MQEKQRMAGQ MLLQTFFNID QISPNKKAHP NMEAGPPESG ESTDALKLCP HEEFLRLCKE 

       130        140        150        160        170        180 
RAEEIYPIKE RNNRTRLALI ICNTEFDHLP PRNGADFDIT GMKELLEGLD YSVDVEENLT 

       190        200        210        220        230        240 
ARDMESALRA FATRPEHKSS DSTFLVLMSH GILEGICGTV HDEKKPDVLL YDTIFQIFNN 

       250        260        270        280        290        300 
RNCLSLKDKP KVIIVQACRG ANRGELWVRD SPASLEVASS QSSENLEEDA VYKTHVEKDF 

       310        320        330        340        350        360 
IAFCSSTPHN VSWRDSTMGS IFITQLITCF QKYSWCCHLE EVFRKVQQSF ETPRAKAQMP 

       370 
TIERLSMTRY FYLFPGN

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel human protease similar to the interleukin-1 beta converting enzyme induces apoptosis in transfected cells." Faucheu C., Diu A., Chan A.W.E., Blanchet A.-M., Miossec C., Herve F., Collard-Dutilleul V., Gu Y., Aldape R.A., Lippke J.A., Rocher C., Su M.S.-S., Livingston D.J., Hercend T., Lalanne J.-L. EMBO J. 14:1914-1922(1995) [PubMed: 7743998] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF CYS-258, 3D-STRUCTURE MODELING. Tissue: Placenta.
[2]	"Molecular cloning and pro-apoptotic activity of ICErelII and ICErelIII, members of the ICE/CED-3 family of cysteine proteases." Munday N.A., Vaillancourt J.P., Ali A., Casano F.J., Miller D.K., Molineaux S.M., Yamin T.-T., Yu V.L., Nicholson D.W. J. Biol. Chem. 270:15870-15876(1995) [PubMed: 7797592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Identification and characterization of ICH-2, a novel member of the interleukin-1 beta-converting enzyme family of cysteine proteases." Kamens J., Paskind M., Hugunin M., Talanian R.V., Allen H., Banach D., Bump N.J., Hackett M.C., Johnston C.G., Li P., Mankovich J.A., Terranova M., Ghayur T. J. Biol. Chem. 270:15250-15256(1995) [PubMed: 7797510] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION. Tissue: Thymus.
[4]	"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]. Tissue: Testis.
[5]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	Z48810 mRNA. Translation: CAA88750.1. U28014 mRNA. Translation: AAA75171.1. U25804 mRNA. Translation: AAA86890.1. BC017839 mRNA. Translation: AAH17839.1.
PIR	A57511.
RefSeq	NP_001216.1.
UniGene	Hs.138378
3D structure databases
HSSP	HSSP built from PDB template 1ICE based on UniProtKB P29466.
ModBase	Search...
Protein-protein interaction databases
IntAct	P49662.
Protein family/group databases
MEROPS	C14.007.
PTM databases
PhosphoSite	P49662.
Genome annotation databases
Ensembl	ENSG00000196954. Homo sapiens. [Contig view]
GeneID	837.
KEGG	hsa:837.
Organism-specific databases
H-InvDB	HIX0010073.
HGNC	HGNC:1505. CASP4.
MIM	602664. gene.
PharmGKB	PA26088.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOGENOM	P49662.
HOVERGEN	P49662.
Gene expression databases
ArrayExpress	P49662.
CleanEx	HS_CASP4.
GermOnline	ENSG00000196954. 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
LinkHub	P49662.
NextBio	3484.
SOURCE	Search...

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Entry information

Entry name

CASP4_HUMAN

Accession

Primary (citable) accession number: P49662

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	November 25, 2008
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 11

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

MIM cross-references

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

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents