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Reviewed, UniProtKB/Swiss-Prot P51878 (CASP5_HUMAN)

Last modified November 25, 2008. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Caspase-5
      Short name=CASP-5
    EC=3.4.22.58
Alternative name(s):
    ICH-3 protease
    TY protease
    ICE(rel)-III
Cleaved into the following 2 chains:
    1- Recommended name:
            Caspase-5 subunit p20
    2- Recommended name:
            Caspase-5 subunit p10
Gene names
Name: CASP5
Synonyms: ICH3
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length418 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Mediator of programmed cell death (apoptosis).

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 20 kDa (p20) and a 10 kDa (p10) subunits.

Tissue specificity

Expressed in barely detectable amounts in most tissues except brain, highest levels being found in lung, liver and skeletal muscle.

Post-translational modification

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

Sequence similarities

Belongs to the peptidase C14 family.

Contains 1 CARD domain.

Ontologies

Keywords

   Biological processApoptosis
   Coding sequence diversityPolymorphism
   Molecular functionHydrolase
Protease
Thiol protease
   PTMZymogen

Gene Ontology (GO)

   Biological processproteolysis Ref.1

Traceable author statement. Source: ProtInc

regulation of apoptosis

Inferred from electronic annotation. Source: InterPro

   Cellular componentintracellular

Inferred from electronic annotation. Source: InterPro

   Molecular functioncysteine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NLRP1Q9C0001EBI-1246700,EBI-1220518

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 120120 Potential
PRO_0000004604
Chain121 – 311191Caspase-5 subunit p20
PRO_0000004605
Propeptide312 – 33019 Potential
PRO_0000004606
Chain331 – 41888Caspase-5 subunit p10
PRO_0000004607

Regions

Domain40 – 13293CARD

Sites

Active site2511 By similarity
Active site2991

Natural variations

Natural variant31K → N: dbSNP rs45483102.
VAR_047216
Natural variant101L → W: dbSNP rs1792778.
VAR_047217
Natural variant131F → L: dbSNP rs3181320.
VAR_024403
Natural variant901T → A: dbSNP rs507879.
VAR_047218
Natural variant1521R → H: dbSNP rs3181179.
VAR_024404
Natural variant2011V → L: dbSNP rs3181326.
VAR_024405
Natural variant3181L → V: dbSNP rs523104.
VAR_047219
Natural variant3371E → K: dbSNP rs45619739.
VAR_047220

Sequences

Sequence LengthMass (Da)Tools
P51878-1 [UniParc].

Last modified November 4, 2008. Version 2.
Checksum: 018E53BCA9801368

FASTA41847,858
        10         20         30         40         50         60 
MFKGILQSGL DNFVINHMLK NNVAGQTSIQ TLVPNTDQKS TSVKKDNHKK KTVKMLEYLG 

        70         80         90        100        110        120 
KDVLHGVFNY LAKHDVLTLK EEEKKKYYDT KIEDKALILV DSLRKNRVAH QMFTQTLLNM 

       130        140        150        160        170        180 
DQKITSVKPL LQIEAGPPES AESTNILKLC PREEFLRLCK KNHDEIYPIK KREDRRRLAL 

       190        200        210        220        230        240 
IICNTKFDHL PARNGAHYDI VGMKRLLQGL GYTVVDEKNL TARDMESVLR AFAARPEHKS 

       250        260        270        280        290        300 
SDSTFLVLMS HGILEGICGT AHKKKKPDVL LYDTIFQIFN NRNCLSLKDK PKVIIVQACR 

       310        320        330        340        350        360 
GEKHGELWVR DSPASLALIS SQSSENLEAD SVCKIHEEKD FIAFCSSTPH NVSWRDRTRG 

       370        380        390        400        410 
SIFITELITC FQKYSCCCHL MEIFRKVQKS FEVPQAKAQM PTIERATLTR DFYLFPGN 

« Hide

References

« Hide 'large scale' references
[1]"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], VARIANTS ALA-90 AND VAL-318.
[2]"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: 16554811] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Identification of a cysteine protease closely related to interleukin-1 beta-converting enzyme."
Faucheu C., Blanchet A.-M., Collard-Dutilleul V., Lalanne J.-L., Diu-Hercend A.
Eur. J. Biochem. 236:207-213(1996) [PubMed: 8617266] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 21-418, VARIANT ALA-90.
Tissue: Placenta and Spleen.
+Additional computationally mapped references.

Cross-references

Sequence databases

U28015 mRNA. Translation: AAA75172.1.
AP001153 Genomic DNA. No translation available.
X94993 mRNA. Translation: CAA64450.1. Different initiation.
PIRB57511.
RefSeqNP_004338.2.
UniGeneHs.213327

3D structure databases

HSSPHSSP built from PDB template 1ICE based on UniProtKB P29466.
ModBaseSearch...

Protein-protein interaction databases

IntActP51878.

Protein family/group databases

MEROPSC14.008.

PTM databases

PhosphoSiteP51878.

Genome annotation databases

EnsemblENSG00000137757. Homo sapiens. [Contig view]
GeneID838.

Organism-specific databases

HGNCHGNC:1506. CASP5.
MIM602665. gene.
PharmGKBPA26089.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOVERGENP51878.

Gene expression databases

ArrayExpressP51878.
CleanExHS_CASP5.
GermOnlineENSG00000137757. Homo sapiens.

Family and domain databases

InterProIPR001315. 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]
Gene3DG3DSA:1.10.533.10. DEATH_like. 1 hit.
PANTHERPTHR10454. Pept_C14_p45. 1 hit.
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]
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 Resources

BindingDBP51878.
SOURCESearch...

Entry information

Entry nameCASP5_HUMAN
AccessionPrimary (citable) accession number: P51878
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 4, 2008
Last modified: November 25, 2008
This is version 76 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 11

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

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 · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents