P55210 (CASP7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Caspase-7
Short name=CASP-7
EC=3.4.22.60

Alternative name(s):
Apoptotic protease Mch-3
CMH-1
ICE-like apoptotic protease 3
Short name=ICE-LAP3

Cleaved into the following 2 chains:

1. Caspase-7 subunit p20
2. Caspase-7 subunit p11

Gene names

Name:	CASP7
Synonyms:	MCH3

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	303 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the activation cascade of caspases responsible for apoptosis execution. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Overexpression promotes programmed cell death.
Catalytic activity	Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Asp-Glu-Val-Asp-|-.
Enzyme regulation	Inhibited by isatin sulfonamides.
Subunit structure	Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 20 kDa (p20) and a 11 kDa (p11) subunit. Ref.13
Subcellular location	Cytoplasm.
Tissue specificity	Highly expressed in lung, skeletal muscle, liver, kidney, spleen and heart, and moderately in testis. No expression in the brain.
Post-translational modification	Cleavages by granzyme B or caspase-10 generate the two active subunits. Propeptide domains can also be cleaved efficiently by caspase-3. Active heterodimers between the small subunit of caspase-7 and the large subunit of caspase-3, and vice versa, also occur. Ref.10
Sequence similarities	Belongs to the peptidase C14A family.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Hydrolase Protease Thiol protease
PTM	Acetylation Phosphoprotein Zymogen
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c Traceable author statement. Source: Reactome cellular component disassembly involved in apoptosis Traceable author statement. Source: Reactome induction of apoptosis by intracellular signals Traceable author statement. Source: Reactome proteolysis Inferred from direct assay. Source: UniProtKB
Cellular component	cytosol Traceable author statement. Source: Reactome endoplasmic reticulum membrane Traceable author statement. Source: UniProtKB mitochondrial membrane Traceable author statement. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome
Molecular function	cysteine-type endopeptidase activity Traceable author statement. Source: Reactome protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BIRC2	Q13490	2	EBI-523958,EBI-514538
XIAP	P98170	2	EBI-523958,EBI-517127

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform Alpha (identifier: P55210-1)

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.

Isoform Beta (identifier: P55210-2)

The sequence of this isoform differs from the canonical sequence as follows:
     149-303: VIYGKDGVTP...MLTKELYFSQ → MESCSVTQAG...TWKSCRSSPG

Note: Lacks enzymatic activity.

Isoform Alpha' (identifier: P55210-3)

Also known as: Beta;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MDCVGWPPGRKWHLEKNTSCGGSSGICASYVTQM

Note: What we call isoform Alpha' is also known as Beta (PubMed:9070923).

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Propeptide

2 – 23

22

PRO_0000004616

Chain

24 – 198

175

Caspase-7 subunit p20

PRO_0000004617

Propeptide

199 – 206

8

PRO_0000004618

Chain

207 – 303

97

Caspase-7 subunit p11

PRO_0000004619

Sites

Active site

144

1

By similarity

Active site

186

1

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.11

Modified residue

16

1

Phosphoserine Ref.11

Natural variations

Alternative sequence

1

1

M → MDCVGWPPGRKWHLEKNTSC GGSSGICASYVTQM in isoform Alpha'.

VSP_000806

Alternative sequence

149 – 303

155

VIYGK…LYFSQ → MESCSVTQAGVQRRDLGRLQ PPPPRLAEGPSLMMASRPTR GPSMTQMLILDTRSQWKLTS SSPIPRFQAITRGGAQEEAP GLCKPSAPSWRSTEKTWKSC RSSPG in isoform Beta.

VSP_000807

Natural variant

4

1

D → E. Ref.5 Ref.9
Corresponds to variant rs11593766 [ dbSNP | Ensembl ].

VAR_048617

Natural variant

255

1

D → E.
Corresponds to variant rs2227310 [ dbSNP | Ensembl ].

VAR_048618

Experimental info

Mutagenesis

186

1

C → A: No apoptotic activity.

Sequence conflict

194

1

G → A in AAC50346. Ref.2

Secondary structure

1

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303

Helix Strand Turn

Details...

Beta strand

64 – 74

11

Turn

80 – 82

3

Helix

90 – 104

15

Beta strand

106 – 113

8

Helix

116 – 128

13

Helix

131 – 133

3

Beta strand

134 – 143

10

Beta strand

149 – 151

3

Beta strand

153 – 158

6

Helix

159 – 164

6

Turn

168 – 170

3

Helix

172 – 174

3

Beta strand

179 – 185

7

Beta strand

188 – 190

3

Turn

215 – 218

4

Beta strand

219 – 225

7

Beta strand

232 – 234

3

Turn

235 – 237

3

Helix

240 – 252

13

Turn

253 – 255

3

Helix

258 – 272

15

Helix

280 – 282

3

Beta strand

290 – 293

4

Beta strand

296 – 298

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform Alpha [UniParc]. Last modified October 1, 1996. Version 1. Checksum: CD373EE54A232CA4	FASTA	303	34,277
	10 20 30 40 50 60 MADDQGCIEE QGVEDSANED SVDAKPDRSS FVPSLFSKKK KNVTMRSIKT TRDRVPTYQY 70 80 90 100 110 120 NMNFEKLGKC IIINNKNFDK VTGMGVRNGT DKDAEALFKC FRSLGFDVIV YNDCSCAKMQ 130 140 150 160 170 180 DLLKKASEED HTNAACFACI LLSHGEENVI YGKDGVTPIK DLTAHFRGDR CKTLLEKPKL 190 200 210 220 230 240 FFIQACRGTE LDDGIQADSG PINDTDANPR YKIPVEADFL FAYSTVPGYY SWRSPGRGSW 250 260 270 280 290 300 FVQALCSILE EHGKDLEIMQ ILTRVNDRVA RHFESQSDDP HFHEKKQIPC VVSMLTKELY FSQ
	Isoform Beta [UniParc]. Checksum: 514964EF3F6229E1	FASTA	253	28,030
	10 20 30 40 50 60 MADDQGCIEE QGVEDSANED SVDAKPDRSS FVPSLFSKKK KNVTMRSIKT TRDRVPTYQY 70 80 90 100 110 120 NMNFEKLGKC IIINNKNFDK VTGMGVRNGT DKDAEALFKC FRSLGFDVIV YNDCSCAKMQ 130 140 150 160 170 180 DLLKKASEED HTNAACFACI LLSHGEENME SCSVTQAGVQ RRDLGRLQPP PPRLAEGPSL 190 200 210 220 230 240 MMASRPTRGP SMTQMLILDT RSQWKLTSSS PIPRFQAITR GGAQEEAPGL CKPSAPSWRS 250 TEKTWKSCRS SPG
	Isoform Alpha' (Beta) [UniParc]. Checksum: 34EEFF8AF5C318A2	FASTA	336	37,815
	10 20 30 40 50 60 MDCVGWPPGR KWHLEKNTSC GGSSGICASY VTQMADDQGC IEEQGVEDSA NEDSVDAKPD 70 80 90 100 110 120 RSSFVPSLFS KKKKNVTMRS IKTTRDRVPT YQYNMNFEKL GKCIIINNKN FDKVTGMGVR 130 140 150 160 170 180 NGTDKDAEAL FKCFRSLGFD VIVYNDCSCA KMQDLLKKAS EEDHTNAACF ACILLSHGEE 190 200 210 220 230 240 NVIYGKDGVT PIKDLTAHFR GDRCKTLLEK PKLFFIQACR GTELDDGIQA DSGPINDTDA 250 260 270 280 290 300 NPRYKIPVEA DFLFAYSTVP GYYSWRSPGR GSWFVQALCS ILEEHGKDLE IMQILTRVND 310 320 330 RVARHFESQS DDPHFHEKKQ IPCVVSMLTK ELYFSQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mch3, a novel human apoptotic cysteine protease highly related to CPP32." Fernandes-Alnemri T., Takahashi A., Armstrong R.C., Krebs J., Fritz L.C., Tomaselli K.J., Wang L., Yu Z., Croce C.M., Salveson G., Earnshaw W.C., Litwack G., Alnemri E.S. Cancer Res. 55:6045-6052(1995) [PubMed: 8521391] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA). Tissue: T-cell.
[2]	"ICE-LAP3, a novel mammalian homologue of the Caenorhabditis elegans cell death protein Ced-3 is activated during Fas- and tumor necrosis factor-induced apoptosis." Duan H., Chinnaiyan A.M., Hudson P.L., Wing J.P., He W.-W., Dixit V.M. J. Biol. Chem. 271:1621-1625(1996) [PubMed: 8576161] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
[3]	"Identification and characterization of CPP32/Mch2 homolog 1, a novel cysteine protease similar to CPP32." Lippke J.A., Gu Y., Sarnecki C., Caron P.R., Su M.S.-S. J. Biol. Chem. 271:1825-1828(1996) [PubMed: 8567622] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA). Tissue: Spleen.
[4]	"Identification and mapping of Casp7, a cysteine protease resembling CPP32 beta, interleukin-1 beta converting enzyme, and CED-3." Juan T.S.-C., McNiece I.K., Argento J.M., Jenkins N.A., Gilbert D.J., Copeland N.G., Fletcher F.A. Genomics 40:86-93(1997) [PubMed: 9070923] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND ALPHA'). Tissue: Fetal lung and Fetal spleen.
[5]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA), VARIANT GLU-4.
[6]	"Human protein factory for converting the transcriptome into an in vitro-expressed proteome." Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N. Nat. Methods 5:1011-1017(2008) [PubMed: 19054851] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA').
[7]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed: 15164054] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"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] (ISOFORM ALPHA), VARIANT GLU-4. Tissue: Skin.
[10]	"In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains." Fernandes-Alnemri T., Armstrong R.C., Krebs J.F., Srinivasula S.M., Wang L., Bullrich F., Fritz L.C., Trapani J.A., Tomaselli K.J., Litwack G., Alnemri E.S. Proc. Natl. Acad. Sci. U.S.A. 93:7464-7469(1996) [PubMed: 8755496] [Abstract] Cited for: PROTEOLYTIC PROCESSING.
[11]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[12]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"Crystal structure of a procaspase-7 zymogen: mechanisms of activation and substrate binding." Chai J., Wu Q., Shiozaki E., Srinivasula S.M., Alnemri E.S., Shi Y. Cell 107:399-407(2001) [PubMed: 11701129] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 51-303, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U37448 mRNA. Translation: AAC50303.1.
U37449 mRNA. Translation: AAC50304.1.
U39613 mRNA. Translation: AAC50346.1.
U40281 mRNA. Translation: AAC50352.1.
U67319 mRNA. Translation: AAC51152.1.
U67320 mRNA. Translation: AAC51153.1.
U67206 mRNA. Translation: AAF21460.1.
BT006683 mRNA. Translation: AAP35329.1.
AB451281 mRNA. Translation: BAG70095.1.
AB451413 mRNA. Translation: BAG70227.1.
AL592546, AL627395 Genomic DNA. Translation: CAI12638.1.
AL592546, AL627395 Genomic DNA. Translation: CAI12639.1.
AL627395, AL592546 Genomic DNA. Translation: CAI16004.1.
AL627395, AL592546 Genomic DNA. Translation: CAI16005.1.
CH471066 Genomic DNA. Translation: EAW49494.1.
CH471066 Genomic DNA. Translation: EAW49495.1.
CH471066 Genomic DNA. Translation: EAW49498.1.
CH471066 Genomic DNA. Translation: EAW49496.1.
CH471066 Genomic DNA. Translation: EAW49497.1.
BC015799 mRNA. Translation: AAH15799.1.

IPI

IPI00216674.
IPI00216675.
IPI00221307.

RefSeq

NP_001218.1. NM_001227.3.
NP_203124.1. NM_033338.4.
NP_203125.1. NM_033339.3.
NP_203126.1. NM_033340.2.

UniGene

Hs.9216.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F1J	X-ray	2.35	A/B	2-303	[»]
1GQF	X-ray	2.90	A/B	47-303	[»]
1I4O	X-ray	2.40	A/B	24-303	[»]
1I51	X-ray	2.45	A/C	51-198	[»]
			B/D	199-303	[»]
1K86	X-ray	2.60	A/B	51-303	[»]
1K88	X-ray	2.70	A/B	51-303	[»]
1KMC	X-ray	2.90	A/B	1-303	[»]
1MIA	model	-	A	57-193	[»]
			B	211-303	[»]
1SHJ	X-ray	2.80	A/B	50-303	[»]
1SHL	X-ray	3.00	A/B	57-303	[»]
2QL5	X-ray	2.34	A/C	24-196	[»]
			B/D	207-303	[»]
2QL7	X-ray	2.40	A/C	24-196	[»]
			B/D	207-303	[»]
2QL9	X-ray	2.14	A/C	24-196	[»]
			B/D	207-303	[»]
2QLB	X-ray	2.25	A/C	24-196	[»]
			B/D	207-303	[»]
2QLF	X-ray	2.80	A/C	24-196	[»]
			B/D	207-303	[»]
2QLJ	X-ray	2.60	A/C	24-196	[»]
			B/D	207-303	[»]
3EDR	X-ray	2.45	A/C	24-196	[»]
			B/D	207-303	[»]
3H1P	X-ray	2.61	A/B	50-303	[»]
3IBC	X-ray	2.75	A/C	24-196	[»]
			B/D	207-303	[»]
3IBF	X-ray	2.50	A/C	24-196	[»]
			B/D	207-303	[»]
3R5K	X-ray	2.86	A/B	1-303	[»]

ProteinModelPortal

P55210.

SMR

P55210. Positions 47-303.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29973N.

IntAct

P55210. 4 interactions.

MINT

MINT-147084.

STRING

P55210.

Protein family/group databases

MEROPS

C14.004.

PTM databases

PhosphoSite

P55210.

Polymorphism databases

DMDM

1730092.

Proteomic databases

PRIDE

P55210.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000298700; ENSP00000298700; ENSG00000165806.
ENST00000345633; ENSP00000298701; ENSG00000165806.
ENST00000369315; ENSP00000358321; ENSG00000165806.
ENST00000369318; ENSP00000358324; ENSG00000165806.
ENST00000369321; ENSP00000358327; ENSG00000165806.
ENST00000452490; ENSP00000398107; ENSG00000165806.

GeneID

840.

KEGG

hsa:840.

UCSC

uc001lan.1. human.

Organism-specific databases

CTD

840.

GeneCards

GC10P115428.

HGNC

HGNC:1508. CASP7.

HPA

CAB025563.

MIM

601761. gene.

neXtProt

NX_P55210.

PharmGKB

PA26091.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG16325.

HOVERGEN

HBG050802.

InParanoid

P55210.

OMA

DCSCAKM.

Enzyme and pathway databases

BRENDA

3.4.22.60. 2681.

Pathway_Interaction_DB

a6b1_a6b4_integrin_pathway. a6b1 and a6b4 Integrin signaling.
caspase_pathway. Caspase cascade in apoptosis.
faspathway. FAS signaling pathway (CD95).
hivnefpathway. HIV-1 Nef: Negative effector of Fas and TNF-alpha.

Reactome

REACT_578. Apoptosis.

Gene expression databases

ArrayExpress

P55210.

Bgee

P55210.

CleanEx

HS_CASP7.

Genevestigator

P55210.

GermOnline

ENSG00000165806. Homo sapiens.

Family and domain databases

InterPro

IPR015471. Casp7.
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]

KO

K04397.

PANTHER

PTHR10454:SF31. Casp7. 1 hit.
PTHR10454. Pept_C14_p45. 1 hit.

Pfam

PF00656. Peptidase_C14. 1 hit.
[Graphical view]

PRINTS

PR00376. IL1BCENZYME.

SMART

SM00115. CASc. 1 hit.
[Graphical view]

PROSITE

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

P55210.

NextBio

3500.

PMAP-CutDB

P55210.

SOURCE

Search...

Entry information

Entry name

CASP7_HUMAN

Accession

Primary (citable) accession number: P55210
Secondary accession number(s): B5BU45 , D3DRB8, Q13364, Q53YD5, Q5SVL0, Q5SVL3, Q96BA0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	January 25, 2012
This is version 127 of the entry and version 1 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.