P51878 (CASP5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	434 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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.
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.

Ontologies

Keywords
Biological process	Apoptosis
Coding sequence diversity	Alternative initiation Alternative splicing Polymorphism
Molecular function	Hydrolase Protease Thiol protease
PTM	Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Traceable author statement Ref.4. Source: ProtInc cellular response to mechanical stimulus Inferred from expression pattern PubMed 19593445. Source: UniProtKB proteolysis Traceable author statement Ref.4. Source: ProtInc regulation of apoptotic process Inferred from electronic annotation. Source: InterPro
Cellular_component	NLRP1 inflammasome complex Inferred from direct assay PubMed 12191486. Source: UniProtKB
Molecular_function	cysteine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro cysteine-type peptidase activity Traceable author statement Ref.4. Source: ProtInc
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Propeptide	1 – 136	136	Potential		PRO_0000004604
	Chain	137 – 327	191	Caspase-5 subunit p20		PRO_0000004605
	Propeptide	328 – 346	19	Potential		PRO_0000004606
	Chain	347 – 434	88	Caspase-5 subunit p10		PRO_0000004607
Regions
	Domain	56 – 148	93	CARD
Sites
	Active site	267	1	By similarity
	Active site	315	1
Natural variations
	Alternative sequence	1 – 145	145	MAEDS…TSVKP → MAA in isoform 3.		VSP_038990
	Alternative sequence	1 – 70	70	Missing in isoform 6.		VSP_038991
	Alternative sequence	1 – 2	2	MA → MAAVPRVEGVFIFLI in isoform 5.		VSP_038992
	Alternative sequence	5 – 62	58	Missing in isoform 2 and isoform 4.		VSP_038993
	Alternative sequence	145 – 166	22	PLLQI…ILKLC → HLSNKKERGPQTPGSHHMQY KV in isoform 4.		VSP_038994
	Alternative sequence	167 – 434	268	Missing in isoform 4.		VSP_038995
	Natural variant	19	1	K → N. Ref.7 Corresponds to variant rs45483102 [ dbSNP | Ensembl ].		VAR_047216
	Natural variant	26	1	L → W. Corresponds to variant rs1792778 [ dbSNP | Ensembl ].		VAR_047217
	Natural variant	29	1	F → L. Ref.5 Ref.7 Corresponds to variant rs3181320 [ dbSNP | Ensembl ].		VAR_024403
	Natural variant	75	1	L → R. Ref.7		VAR_054480
	Natural variant	106	1	T → A. Ref.1 Ref.2 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Corresponds to variant rs507879 [ dbSNP | Ensembl ].		VAR_047218
	Natural variant	168	1	R → H. Ref.5 Ref.7 Corresponds to variant rs3181179 [ dbSNP | Ensembl ].		VAR_024404
	Natural variant	217	1	V → L. Ref.5 Ref.7 Corresponds to variant rs3181326 [ dbSNP | Ensembl ].		VAR_024405
	Natural variant	298	1	R → H. Ref.7		VAR_054481
	Natural variant	334	1	L → V. Ref.1 Ref.4 Ref.5 Ref.7 Corresponds to variant rs523104 [ dbSNP | Ensembl ].		VAR_047219
	Natural variant	353	1	E → K. Ref.7 Corresponds to variant rs45619739 [ dbSNP | Ensembl ].		VAR_047220
	Natural variant	382	1	E → Q. Ref.7 Corresponds to variant rs45458695 [ dbSNP | Ensembl ].		VAR_054482

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (caspase-5/a) [UniParc]. Last modified April 20, 2010. Version 3. Checksum: C5257C2BF15EB6D5	FASTA	434	49,736
	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
	Isoform 2 (Caspase-5/b) [UniParc]. Checksum: 7D3035A84418FE31	FASTA	376	43,261
	10 20 30 40 50 60 MAEDNHKKKT VKMLEYLGKD VLHGVFNYLA KHDVLTLKEE EKKKYYDTKI EDKALILVDS 70 80 90 100 110 120 LRKNRVAHQM FTQTLLNMDQ KITSVKPLLQ IEAGPPESAE STNILKLCPR EEFLRLCKKN 130 140 150 160 170 180 HDEIYPIKKR EDRRRLALII CNTKFDHLPA RNGAHYDIVG MKRLLQGLGY TVVDEKNLTA 190 200 210 220 230 240 RDMESVLRAF AARPEHKSSD STFLVLMSHG ILEGICGTAH KKKKPDVLLY DTIFQIFNNR 250 260 270 280 290 300 NCLSLKDKPK VIIVQACRGE KHGELWVRDS PASLALISSQ SSENLEADSV CKIHEEKDFI 310 320 330 340 350 360 AFCSSTPHNV SWRDRTRGSI FITELITCFQ KYSCCCHLME IFRKVQKSFE VPQAKAQMPT 370 IERATLTRDF YLFPGN
	Isoform 3 (Caspase-5/c) [UniParc]. Checksum: FD1D1199CB76E857	FASTA	292	33,304
	10 20 30 40 50 60 MAALLQIEAG PPESAESTNI LKLCPREEFL RLCKKNHDEI YPIKKREDRR RLALIICNTK 70 80 90 100 110 120 FDHLPARNGA HYDIVGMKRL LQGLGYTVVD EKNLTARDME SVLRAFAARP EHKSSDSTFL 130 140 150 160 170 180 VLMSHGILEG ICGTAHKKKK PDVLLYDTIF QIFNNRNCLS LKDKPKVIIV QACRGEKHGE 190 200 210 220 230 240 LWVRDSPASL ALISSQSSEN LEADSVCKIH EEKDFIAFCS STPHNVSWRD RTRGSIFITE 250 260 270 280 290 LITCFQKYSC CCHLMEIFRK VQKSFEVPQA KAQMPTIERA TLTRDFYLFP GN
	Isoform 4 (Caspase-5/e) [UniParc]. Checksum: 2A441B191C453A3C	FASTA	108	12,694
	10 20 30 40 50 60 MAEDNHKKKT VKMLEYLGKD VLHGVFNYLA KHDVLTLKEE EKKKYYDTKI EDKALILVDS 70 80 90 100 LRKNRVAHQM FTQTLLNMDQ KITSVKHLSN KKERGPQTPG SHHMQYKV
	Isoform 5 (Caspase-5/f) [UniParc]. Checksum: 39D5955FA0419B68	FASTA	447	51,177
	10 20 30 40 50 60 MAAVPRVEGV FIFLIEDSGK KKRRKNFEAM FKGILQSGLD NFVINHMLKN NVAGQTSIQT 70 80 90 100 110 120 LVPNTDQKST SVKKDNHKKK TVKMLEYLGK DVLHGVFNYL AKHDVLTLKE EEKKKYYDTK 130 140 150 160 170 180 IEDKALILVD SLRKNRVAHQ MFTQTLLNMD QKITSVKPLL QIEAGPPESA ESTNILKLCP 190 200 210 220 230 240 REEFLRLCKK NHDEIYPIKK REDRRRLALI ICNTKFDHLP ARNGAHYDIV GMKRLLQGLG 250 260 270 280 290 300 YTVVDEKNLT ARDMESVLRA FAARPEHKSS DSTFLVLMSH GILEGICGTA HKKKKPDVLL 310 320 330 340 350 360 YDTIFQIFNN RNCLSLKDKP KVIIVQACRG EKHGELWVRD SPASLALISS QSSENLEADS 370 380 390 400 410 420 VCKIHEEKDF IAFCSSTPHN VSWRDRTRGS IFITELITCF QKYSCCCHLM EIFRKVQKSF 430 440 EVPQAKAQMP TIERATLTRD FYLFPGN
	Isoform 6 (Caspase-5-S) [UniParc]. Checksum: 64533BAB7E528B37	FASTA	364	41,851
	10 20 30 40 50 60 MLEYLGKDVL HGVFNYLAKH DVLTLKEEEK KKYYDTKIED KALILVDSLR KNRVAHQMFT 70 80 90 100 110 120 QTLLNMDQKI TSVKPLLQIE AGPPESAEST NILKLCPREE FLRLCKKNHD EIYPIKKRED 130 140 150 160 170 180 RRRLALIICN TKFDHLPARN GAHYDIVGMK RLLQGLGYTV VDEKNLTARD MESVLRAFAA 190 200 210 220 230 240 RPEHKSSDST FLVLMSHGIL EGICGTAHKK KKPDVLLYDT IFQIFNNRNC LSLKDKPKVI 250 260 270 280 290 300 IVQACRGEKH GELWVRDSPA SLALISSQSS ENLEADSVCK IHEEKDFIAF CSSTPHNVSW 310 320 330 340 350 360 RDRTRGSIFI TELITCFQKY SCCCHLMEIF RKVQKSFEVP QAKAQMPTIE RATLTRDFYL FPGN

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

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.
IPI	IPI00020978. IPI00784640. IPI00914544. IPI00914557. IPI00942522. IPI00979949.
PIR	B57511.
RefSeq	NP_001129581.1. NM_001136109.1. NP_001129582.1. NM_001136110.1. NP_001129584.1. NM_001136112.1. NP_004338.3. NM_004347.3.
UniGene	Hs.213327.
3D structure databases
ProteinModelPortal	P51878.
SMR	P51878. Positions 163-434.
ModBase	Search...
Protein-protein interaction databases
IntAct	P51878. 1 interaction.
STRING	9606.ENSP00000376849.
Protein family/group databases
MEROPS	C14.008.
PTM databases
PhosphoSite	P51878.
Polymorphism databases
DMDM	294862523.
Proteomic databases
PaxDb	P51878.
PRIDE	P51878.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000260315; ENSP00000260315; ENSG00000137757. ENST00000393141; ENSP00000376849; ENSG00000137757. ENST00000418434; ENSP00000398130; ENSG00000137757. ENST00000444749; ENSP00000388365; ENSG00000137757. ENST00000456200; ENSP00000408455; ENSG00000137757. ENST00000526056; ENSP00000436877; ENSG00000137757. ENST00000531367; ENSP00000434471; ENSG00000137757.
GeneID	838.
KEGG	hsa:838.
UCSC	uc010ruz.1. human. uc010rva.1. human. uc010rvb.1. human. uc010rvc.1. human.
Organism-specific databases
CTD	838.
GeneCards	GC11M104864.
HGNC	HGNC:1506. CASP5.
HPA	HPA040937.
MIM	602665. gene.
neXtProt	NX_P51878.
PharmGKB	PA26089.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG326166.
HOVERGEN	HBG076981.
InParanoid	P51878.
KO	K04395.
OMA	CHLMEIF.
Enzyme and pathway databases
BRENDA	3.4.22.58. 2681.
SABIO-RK	P51878.
Gene expression databases
ArrayExpress	P51878.
Bgee	P51878.
CleanEx	HS_CASP5.
Genevestigator	P51878.
GermOnline	ENSG00000137757. Homo sapiens.
Family and domain databases
Gene3D	1.10.533.10. 1 hit.
InterPro	IPR001315. CARD. IPR017350. Caspase_IL-1_beta. IPR011029. DEATH-like_dom. 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]
PANTHER	PTHR10454. PTHR10454. 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]
SUPFAM	SSF47986. DEATH_like. 1 hit.
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
BindingDB	P51878.
ChEMBL	CHEMBL3131.
GenomeRNAi	838.
NextBio	3490.
SOURCE	Search...

Entry information

Entry name

CASP5_HUMAN

Accession

Primary (citable) accession number: P51878
Secondary accession number(s): B4DKP5 , 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:	May 1, 2013
This is version 123 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.