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P51878 (CASP5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Caspase-5

Short name=CASP-5
EC=3.4.22.58
Alternative name(s):
ICE(rel)-III
Protease ICH-3
Protease TY

Cleaved into the following 2 chains:

  1. Caspase-5 subunit p20
  2. Caspase-5 subunit p10
Gene names
Name:CASP5
Synonyms:ICH3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length434 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. Interacts with MEFV.

Tissue specificity

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

Induction

Up-regulated by bacterial lipopolysaccharides (LPS). Ref.1

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 AAA75172.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAH74994.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAI13407.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence ABF47103.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAG59257.1 differs from that shown. Reason: Frameshift at position 10.

The sequence CAA64450.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative products

This entry describes 6 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]
Isoform 1 (identifier: P51878-1)

Also known as: caspase-5/a;

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.
Note: Most abundant isoform.
Isoform 2 (identifier: P51878-2)

Also known as: Caspase-5/b;

The sequence of this isoform differs from the canonical sequence as follows:
     5-62: Missing.
Note: Most abundant isoform.
Isoform 3 (identifier: P51878-3)

Also known as: Caspase-5/c;

The sequence of this isoform differs from the canonical sequence as follows:
     1-145: MAEDSGKKKR...MDQKITSVKP → MAA
Isoform 4 (identifier: P51878-4)

Also known as: Caspase-5/e;

The sequence of this isoform differs from the canonical sequence as follows:
     5-62: Missing.
     145-166: PLLQIEAGPPESAESTNILKLC → HLSNKKERGPQTPGSHHMQYKV
     167-434: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 5 (identifier: P51878-5)

Also known as: Caspase-5/f;

The sequence of this isoform differs from the canonical sequence as follows:
     1-2: MA → MAAVPRVEGVFIFLI
Isoform 6 (identifier: P51878-6)

Also known as: Caspase-5-S;

The sequence of this isoform differs from the canonical sequence as follows:
     1-70: Missing.
Note: Produced by alternative initiation at Met-71 of isoform 1.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 136136 Potential
PRO_0000004604
Chain137 – 327191Caspase-5 subunit p20
PRO_0000004605
Propeptide328 – 34619 Potential
PRO_0000004606
Chain347 – 43488Caspase-5 subunit p10
PRO_0000004607

Regions

Domain56 – 14893CARD

Sites

Active site2671 By similarity
Active site3151

Natural variations

Alternative sequence1 – 145145MAEDS…TSVKP → MAA in isoform 3.
VSP_038990
Alternative sequence1 – 7070Missing in isoform 6.
VSP_038991
Alternative sequence1 – 22MA → MAAVPRVEGVFIFLI in isoform 5.
VSP_038992
Alternative sequence5 – 6258Missing in isoform 2 and isoform 4.
VSP_038993
Alternative sequence145 – 16622PLLQI…ILKLC → HLSNKKERGPQTPGSHHMQY KV in isoform 4.
VSP_038994
Alternative sequence167 – 434268Missing in isoform 4.
VSP_038995
Natural variant191K → N. Ref.7
Corresponds to variant rs45483102 [ dbSNP | Ensembl ].
VAR_047216
Natural variant261L → W.
Corresponds to variant rs1792778 [ dbSNP | Ensembl ].
VAR_047217
Natural variant291F → L. Ref.5 Ref.7
Corresponds to variant rs3181320 [ dbSNP | Ensembl ].
VAR_024403
Natural variant751L → R. Ref.7
Corresponds to variant rs45585331 [ dbSNP | Ensembl ].
VAR_054480
Natural variant1061T → A. Ref.1 Ref.2 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8
Corresponds to variant rs507879 [ dbSNP | Ensembl ].
VAR_047218
Natural variant1681R → H. Ref.5 Ref.7
Corresponds to variant rs3181179 [ dbSNP | Ensembl ].
VAR_024404
Natural variant2171V → L. Ref.5 Ref.7
Corresponds to variant rs3181326 [ dbSNP | Ensembl ].
VAR_024405
Natural variant2981R → H. Ref.7
Corresponds to variant rs45464699 [ dbSNP | Ensembl ].
VAR_054481
Natural variant3341L → V. Ref.1 Ref.4 Ref.5 Ref.7
Corresponds to variant rs523104 [ dbSNP | Ensembl ].
VAR_047219
Natural variant3531E → K. Ref.7
Corresponds to variant rs45619739 [ dbSNP | Ensembl ].
VAR_047220
Natural variant3821E → Q. Ref.7
Corresponds to variant rs45458695 [ dbSNP | Ensembl ].
VAR_054482

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (caspase-5/a) [UniParc].

Last modified April 20, 2010. Version 3.
Checksum: C5257C2BF15EB6D5

FASTA43449,736
        10         20         30         40         50         60 
MAEDSGKKKR RKNFEAMFKG ILQSGLDNFV INHMLKNNVA GQTSIQTLVP NTDQKSTSVK 

        70         80         90        100        110        120 
KDNHKKKTVK MLEYLGKDVL HGVFNYLAKH DVLTLKEEEK KKYYDTKIED KALILVDSLR 

       130        140        150        160        170        180 
KNRVAHQMFT QTLLNMDQKI TSVKPLLQIE AGPPESAEST NILKLCPREE FLRLCKKNHD 

       190        200        210        220        230        240 
EIYPIKKRED RRRLALIICN TKFDHLPARN GAHYDIVGMK RLLQGLGYTV VDEKNLTARD 

       250        260        270        280        290        300 
MESVLRAFAA RPEHKSSDST FLVLMSHGIL EGICGTAHKK KKPDVLLYDT IFQIFNNRNC 

       310        320        330        340        350        360 
LSLKDKPKVI IVQACRGEKH GELWVRDSPA SLALISSQSS ENLEADSVCK IHEEKDFIAF 

       370        380        390        400        410        420 
CSSTPHNVSW RDRTRGSIFI TELITCFQKY SCCCHLMEIF RKVQKSFEVP QAKAQMPTIE 

       430 
RATLTRDFYL FPGN 

« Hide

Isoform 2 (Caspase-5/b) [UniParc].

Checksum: 7D3035A84418FE31
Show »

FASTA37643,261
Isoform 3 (Caspase-5/c) [UniParc].

Checksum: FD1D1199CB76E857
Show »

FASTA29233,304
Isoform 4 (Caspase-5/e) [UniParc].

Checksum: 2A441B191C453A3C
Show »

FASTA10812,694
Isoform 5 (Caspase-5/f) [UniParc].

Checksum: 39D5955FA0419B68
Show »

FASTA44751,177
Isoform 6 (Caspase-5-S) [UniParc].

Checksum: 64533BAB7E528B37
Show »

FASTA36441,851

References

« Hide 'large scale' references
[1]"Identification of a novel exon encoding the amino-terminus of the predominant caspase-5 variants."
Eckhart L., Kittel C., Gawlas S., Gruber F., Mildner M., Jilma B., Tschachler E.
Biochem. Biophys. Res. Commun. 348:682-688(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5), ALTERNATIVE SPLICING (ISOFORM 6), VARIANTS ALA-106 AND VAL-334, INDUCTION BY LPS.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT ALA-106.
Tissue: Colon.
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-434 (ISOFORM 1), VARIANTS ALA-106 AND VAL-334.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-434 (ISOFORM 1), VARIANTS LEU-29; ALA-106; HIS-168; LEU-217 AND VAL-334.
Tissue: Colon.
[6]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 37-434, VARIANT ALA-106.
Tissue: Placenta and Spleen.
[7]NIEHS SNPs program
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASN-19; LEU-29; ARG-75; ALA-106; HIS-168; LEU-217; HIS-298; VAL-334; LYS-353 AND GLN-382.
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ALA-106.
[9]"The SPRY domain of Pyrin, mutated in familial Mediterranean fever patients, interacts with inflammasome components and inhibits proIL-1beta processing."
Papin S., Cuenin S., Agostini L., Martinon F., Werner S., Beer H.D., Grutter C., Grutter M., Tschopp J.
Cell Death Differ. 14:1457-1466(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MEFV.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ228672 mRNA. Translation: ABB58698.1.
DQ228673 mRNA. Translation: ABB58699.1.
DQ228674 mRNA. Translation: ABB58700.1.
DQ228676 mRNA. Translation: ABB58702.1.
DQ228677 mRNA. Translation: ABB58703.1.
AK296660 mRNA. Translation: BAG59257.1. Frameshift.
AP001153 Genomic DNA. No translation available.
U28015 mRNA. Translation: AAA75172.1. Different initiation.
BC074994 mRNA. Translation: AAH74994.1. Different initiation.
BC113406 mRNA. Translation: AAI13407.1. Different initiation.
X94993 mRNA. Translation: CAA64450.1. Different initiation.
DQ508420 Genomic DNA. Translation: ABF47103.1. Different initiation.
CH471065 Genomic DNA. Translation: EAW67054.1.
PIRB57511.
RefSeqNP_001129581.1. NM_001136109.1.
NP_001129582.1. NM_001136110.1.
NP_001129584.1. NM_001136112.1.
NP_004338.3. NM_004347.3.
UniGeneHs.213327.

3D structure databases

ProteinModelPortalP51878.
SMRP51878. Positions 74-144, 163-434.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107288. 1 interaction.
DIPDIP-40038N.
IntActP51878. 1 interaction.
MINTMINT-245149.
STRING9606.ENSP00000376849.

Chemistry

BindingDBP51878.
ChEMBLCHEMBL3131.
GuidetoPHARMACOLOGY1621.

Protein family/group databases

MEROPSC14.008.

PTM databases

PhosphoSiteP51878.

Polymorphism databases

DMDM294862523.

Proteomic databases

PaxDbP51878.
PRIDEP51878.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000260315; ENSP00000260315; ENSG00000137757. [P51878-1]
ENST00000393141; ENSP00000376849; ENSG00000137757. [P51878-5]
ENST00000418434; ENSP00000398130; ENSG00000137757. [P51878-3]
ENST00000444749; ENSP00000388365; ENSG00000137757. [P51878-2]
ENST00000456200; ENSP00000408455; ENSG00000137757. [P51878-4]
ENST00000526056; ENSP00000436877; ENSG00000137757. [P51878-5]
ENST00000531367; ENSP00000434471; ENSG00000137757. [P51878-3]
GeneID838.
KEGGhsa:838.
UCSCuc009yxh.2. human. [P51878-3]
uc010ruz.1. human. [P51878-5]
uc010rva.1. human. [P51878-1]
uc010rvb.1. human. [P51878-2]

Organism-specific databases

CTD838.
GeneCardsGC11M104864.
HGNCHGNC:1506. CASP5.
HPAHPA040937.
MIM602665. gene.
neXtProtNX_P51878.
PharmGKBPA26089.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG326166.
HOVERGENHBG076981.
InParanoidP51878.
KOK04395.
OMAHDEIYPI.
TreeFamTF102023.

Enzyme and pathway databases

BRENDA3.4.22.58. 2681.
SABIO-RKP51878.

Gene expression databases

ArrayExpressP51878.
BgeeP51878.
CleanExHS_CASP5.
GenevestigatorP51878.

Family and domain databases

Gene3D1.10.533.10. 1 hit.
InterProIPR001315. CARD.
IPR017350. Caspase_IL-1_beta.
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]
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]
SUPFAMSSF47986. SSF47986. 1 hit.
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

GenomeRNAi838.
NextBio3490.
PROP51878.
SOURCESearch...

Entry information

Entry nameCASP5_HUMAN
AccessionPrimary (citable) accession number: P51878
Secondary accession number(s): B4DKP5 expand/collapse secondary AC list , Q0QVY7, Q0QVY8, Q0QVZ0, Q0QVZ1, Q0QVZ2, Q14DD6, Q1HBJ3, Q6DJV7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: April 20, 2010
Last modified: March 19, 2014
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

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