P42575 (CASP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Caspase-2
Short name=CASP-2
EC=3.4.22.55

Alternative name(s):
Neural precursor cell expressed developmentally down-regulated protein 2
Short name=NEDD-2
Protease ICH-1

Cleaved into the following 3 chains:

1. Caspase-2 subunit p18
2. Caspase-2 subunit p13
3. Caspase-2 subunit p12

Gene names

Name:	CASP2
Synonyms:	ICH1, NEDD2

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	452 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. Might function by either activating some proteins required for cell death or inactivating proteins necessary for cell survival.
Catalytic activity	Strict requirement for an Asp residue at P1, with 316-asp being essential for proteolytic activity and has a preferred cleavage sequence of Val-Asp-Val-Ala-Asp-|-.
Subunit structure	Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a p18 subunit and a p12 subunit. Interacts with LRDD. Ref.12 Ref.13 Ref.16
Tissue specificity	Expressed at higher levels in the embryonic lung, liver and kidney than in the heart and brain. In adults, higher level expression is seen in the placenta, lung, kidney, and pancreas than in the heart, brain, liver and skeletal muscle.
Post-translational modification	The mature protease can process its own propeptide, but not that of other caspases.
Sequence similarities	Belongs to the peptidase C14A family. Contains 1 CARD domain.
Sequence caution	The sequence AAA58959.1 differs from that shown. Reason: Erroneous initiation. The sequence AAO25653.1 differs from that shown. Reason: Erroneous initiation. The sequence AAP22346.1 differs from that shown. Reason: Erroneous initiation. The sequence AAP22349.1 differs from that shown. Reason: Erroneous initiation. The sequence BAD92877.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Apoptosis
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Hydrolase Protease Thiol protease
PTM	Phosphoprotein Zymogen
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Inferred from mutant phenotype PubMed 21726810. Source: UniProtKB aging Inferred from electronic annotation. Source: Compara apoptotic signaling pathway Traceable author statement PubMed 18309324. Source: UniProtKB brain development Inferred from electronic annotation. Source: Compara cellular response to mechanical stimulus Inferred from expression pattern PubMed 19593445. Source: UniProtKB execution phase of apoptosis Traceable author statement PubMed 18309324. Source: UniProtKB induction of apoptosis Inferred from electronic annotation. Source: Compara luteolysis Inferred from electronic annotation. Source: Compara nerve growth factor receptor signaling pathway Traceable author statement. Source: Reactome neural retina development Inferred from electronic annotation. Source: Compara positive regulation of apoptotic process Inferred from direct assay PubMed 10980123. Source: UniProtKB positive regulation of neuron apoptotic process Inferred from electronic annotation. Source: Compara protein processing Inferred from direct assay PubMed 9044836. Source: BHF-UCL proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Traceable author statement. Source: Reactome membrane Inferred from electronic annotation. Source: Compara mitochondrion Inferred from electronic annotation. Source: Compara nucleus Inferred from electronic annotation. Source: Compara
Molecular_function	cysteine-type endopeptidase activity Inferred from direct assay PubMed 10980123PubMed 21726810. Source: UniProtKB enzyme binding Inferred from sequence or structural similarity PubMed 11076957. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CASP2	P42575-1	2	EBI-520342,EBI-520357
CRADD	P78560	9	EBI-520342,EBI-520375
PRKDC	P78527	4	EBI-520342,EBI-352053

Alternative products

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

Note: Isoforms differ in the N- and C-termini.

Isoform 1 (identifier: P42575-1)

Also known as: ICH-1L;

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: Acts as a positive regulator of apoptosis.

Isoform 2 (identifier: P42575-2)

Also known as: ICH-1S;

The sequence of this isoform differs from the canonical sequence as follows:
     1-31: Missing.
     323-452: DETDRGVDQQ...LYLFPGHPPT → GGAIGSLGHLLLFTAATASLAL

Note: Acts as a negative regulator of apoptosis.

Isoform 3 (identifier: P42575-3)

Also known as: Casp-2L-Pro;

The sequence of this isoform differs from the canonical sequence as follows:
     1-17: Missing.
     107-108: RE → HS
     109-452: Missing.

Note: May function as an endogenous apoptosis inhibitor that antagonizes caspase activation and cell death.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 169

169

PRO_0000004541

Chain

170 – 325

156

Caspase-2 subunit p18

PRO_0000004542

Propeptide

326 – 333

8

PRO_0000004543

Chain

334 – 452

119

Caspase-2 subunit p13

PRO_0000004544

Chain

348 – 452

105

Caspase-2 subunit p12

PRO_0000004545

Regions

Domain

32 – 121

90

CARD

Sites

Active site

277

1

By similarity

Active site

320

1

By similarity

Amino acid modifications

Modified residue

340

1

Phosphoserine Ref.15

Natural variations

Alternative sequence

1 – 31

31

Missing in isoform 2.

VSP_000801

Alternative sequence

1 – 17

17

Missing in isoform 3.

VSP_046280

Alternative sequence

107 – 108

2

RE → HS in isoform 3.

VSP_046281

Alternative sequence

109 – 452

344

Missing in isoform 3.

VSP_046282

Alternative sequence

323 – 452

130

DETDR…GHPPT → GGAIGSLGHLLLFTAATASL AL in isoform 2.

VSP_000802

Natural variant

105

1

A → G.
Corresponds to variant rs4647298 [ dbSNP | Ensembl ].

VAR_055621

Natural variant

172

1

V → L. Ref.5 Ref.8 Ref.9
Corresponds to variant rs4647297 [ dbSNP | Ensembl ].

VAR_016334

Natural variant

178

1

P → A. Ref.5
Corresponds to variant rs4647298 [ dbSNP | Ensembl ].

VAR_016335

Natural variant

441

1

R → G. Ref.5
Corresponds to variant rs4647338 [ dbSNP | Ensembl ].

VAR_016336

Experimental info

Mutagenesis

320

1

C → S: Loss of function.

Mutagenesis

369

1

A → T: Loss of function.

Sequence conflict

309 – 322

14

QNKPK…QACRG → EEVTSLSILSAFVT in BAD92877. Ref.10

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

452

Helix Strand Turn

Details...

Helix

181 – 187

7

Helix

188 – 190

3

Beta strand

197 – 206

10

Beta strand

212 – 214

3

Helix

222 – 235

14

Beta strand

238 – 245

8

Helix

248 – 259

12

Helix

262 – 265

4

Beta strand

267 – 276

10

Beta strand

282 – 284

3

Beta strand

290 – 292

3

Helix

293 – 299

7

Turn

302 – 304

3

Helix

306 – 308

3

Beta strand

313 – 319

7

Beta strand

321 – 324

4

Beta strand

363 – 370

8

Beta strand

377 – 379

3

Turn

380 – 382

3

Helix

385 – 397

13

Turn

398 – 400

3

Helix

403 – 415

13

Turn

425 – 428

4

Beta strand

434 – 437

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (ICH-1L) [UniParc]. Last modified December 6, 2005. Version 2. Checksum: 6EF0ED05EF808385	FASTA	452	50,685
	10 20 30 40 50 60 MAAPSAGSWS TFQHKELMAA DRGRRILGVC GMHPHHQETL KKNRVVLAKQ LLLSELLEHL 70 80 90 100 110 120 LEKDIITLEM RELIQAKVGS FSQNVELLNL LPKRGPQAFD AFCEALRETK QGHLEDMLLT 130 140 150 160 170 180 TLSGLQHVLP PLSCDYDLSL PFPVCESCPL YKKLRLSTDT VEHSLDNKDG PVCLQVKPCT 190 200 210 220 230 240 PEFYQTHFQL AYRLQSRPRG LALVLSNVHF TGEKELEFRS GGDVDHSTLV TLFKLLGYDV 250 260 270 280 290 300 HVLCDQTAQE MQEKLQNFAQ LPAHRVTDSC IVALLSHGVE GAIYGVDGKL LQLQEVFQLF 310 320 330 340 350 360 DNANCPSLQN KPKMFFIQAC RGDETDRGVD QQDGKNHAGS PGCEESDAGK EKLPKMRLPT 370 380 390 400 410 420 RSDMICGYAC LKGTAAMRNT KRGSWYIEAL AQVFSERACD MHVADMLVKV NALIKDREGY 430 440 450 APGTEFHRCK EMSEYCSTLC RHLYLFPGHP PT
	Isoform 2 (ICH-1S) [UniParc]. Checksum: FA1E307A41B8299E	FASTA	313	34,923
	10 20 30 40 50 60 MHPHHQETLK KNRVVLAKQL LLSELLEHLL EKDIITLEMR ELIQAKVGSF SQNVELLNLL 70 80 90 100 110 120 PKRGPQAFDA FCEALRETKQ GHLEDMLLTT LSGLQHVLPP LSCDYDLSLP FPVCESCPLY 130 140 150 160 170 180 KKLRLSTDTV EHSLDNKDGP VCLQVKPCTP EFYQTHFQLA YRLQSRPRGL ALVLSNVHFT 190 200 210 220 230 240 GEKELEFRSG GDVDHSTLVT LFKLLGYDVH VLCDQTAQEM QEKLQNFAQL PAHRVTDSCI 250 260 270 280 290 300 VALLSHGVEG AIYGVDGKLL QLQEVFQLFD NANCPSLQNK PKMFFIQACR GGGAIGSLGH 310 LLLFTAATAS LAL
	Isoform 3 (Casp-2L-Pro) [UniParc]. Checksum: E80E3D9233686A98	FASTA	91	10,309
	10 20 30 40 50 60 MAADRGRRIL GVCGMHPHHQ ETLKKNRVVL AKQLLLSELL EHLLEKDIIT LEMRELIQAK 70 80 90 VGSFSQNVEL LNLLPKRGPQ AFDAFCEALH S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Ich-1, an Ice/ced-3-related gene, encodes both positive and negative regulators of programmed cell death." Wang L., Miura M., Bergeron L., Zhu H., Yuan J. Cell 78:739-750(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 14-452 (ISOFORM 1). Tissue: Fetal brain.
[2]	"Identification of a caspase-2 isoform that behaves as an endogenous inhibitor of the caspase cascade." Droin N., Beauchemin M., Solary E., Bertrand R. Cancer Res. 60:7039-7047(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF 32-108 (ISOFORMS 1/2), ALTERNATIVE SPLICING.
[3]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[4]	"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 1).
[5]	NIEHS SNPs program Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-172; ALA-178 AND GLY-441.
[6]	"The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K. Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	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].
[8]	"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] (ISOFORM 1), VARIANT LEU-172. Tissue: Skin.
[9]	"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] OF 18-452 (ISOFORM 1), VARIANT LEU-172.
[10]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 194-452. Tissue: Spleen.
[11]	"The Caenorhabditis elegans cell-death protein CED-3 is a cysteine protease with substrate specificities similar to those of the human CPP32 protease." Xue D., Shaham S., Horvitz H.R. Genes Dev. 10:1073-1083(1996) [PubMed] [Europe PMC] [Abstract] Cited for: CLEAVAGE SITES.
[12]	"The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress." Tinel A., Tschopp J. Science 304:843-846(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LRDD.
[13]	"Functional connection between p53 and caspase-2 is essential for apoptosis induced by DNA damage." Vakifahmetoglu H., Olsson M., Orrenius S., Zhivotovsky B. Oncogene 25:5683-5692(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LRDD.
[14]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340, MASS SPECTROMETRY.
[16]	"Crystal structure of caspase-2, apical initiator of the intrinsic apoptotic pathway." Schweizer A., Briand C., Grutter M.G. J. Biol. Chem. 278:42441-42447(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 167-452 IN COMPLEX WITH INHIBITOR, SUBUNIT, DISULFIDE BOND.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U13021 mRNA. Translation: AAA58959.1. Different initiation.
U13022 mRNA. Translation: AAA58960.1.
AF314174 mRNA. Translation: AAK00299.1.
AF314175 mRNA. Translation: AAK00300.1.
CR541748 mRNA. Translation: CAG46548.1.
AK291274 mRNA. Translation: BAF83963.1.
AY219042 Genomic DNA. Translation: AAO25653.1. Different initiation.
AC073342 Genomic DNA. Translation: AAP22346.1. Different initiation.
AC073342 Genomic DNA. Translation: AAP22347.1.
AC073342 Genomic DNA. Translation: AAP22348.1.
AC073342 Genomic DNA. Translation: AAP22349.1. Different initiation.
CH471198 Genomic DNA. Translation: EAW51863.1.
CH471198 Genomic DNA. Translation: EAW51867.1.
CH471198 Genomic DNA. Translation: EAW51870.1.
BC002427 mRNA. Translation: AAH02427.2.
BT007240 mRNA. Translation: AAP35904.1.
AB209640 mRNA. Translation: BAD92877.1. Different initiation.

IPI

IPI00216410.
IPI00291570.
IPI00917270.

PIR

A54821.

RefSeq

NP_001215.1. NM_001224.4.
NP_116764.2. NM_032982.3.
NP_116765.2. NM_032983.3.

UniGene

Hs.368982.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PYO	X-ray	1.65	A/C	167-333	[»]
			B/D	348-452	[»]
2P2C	X-ray	3.24	A/C/E/G/I/K	167-333	[»]
			B/D/F/H/J/L	348-452	[»]
3R5J	X-ray	1.77	A/C	175-333	[»]
			B/D	349-452	[»]
3R6G	X-ray	2.07	A/C	175-333	[»]
			B/D	349-452	[»]
3R6L	X-ray	1.90	A/C	175-333	[»]
			B/D	349-452	[»]
3R7B	X-ray	1.80	A/C	175-333	[»]
			B/D	349-452	[»]
3R7N	X-ray	2.33	A/C	175-333	[»]
			B/D	349-452	[»]
3R7S	X-ray	2.25	A/C	175-333	[»]
			B/D	349-452	[»]
3RJM	X-ray	2.55	A/C	167-333	[»]
			B/D	348-452	[»]

ProteinModelPortal

P42575.

ModBase

Search...

Protein-protein interaction databases

IntAct

P42575. 5 interactions.

STRING

9606.ENSP00000312664.

Protein family/group databases

MEROPS

C14.006.

PTM databases

PhosphoSite

P42575.

Polymorphism databases

DMDM

83300977.

Proteomic databases

PaxDb

P42575.

PeptideAtlas

P42575.

PRIDE

P42575.

Protocols and materials databases

DNASU

835.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000310447; ENSP00000312664; ENSG00000106144.

GeneID

835.

KEGG

hsa:835.

UCSC

uc003wco.3. human.

Organism-specific databases

CTD

835.

GeneCards

GC07P142985.

HGNC

HGNC:1503. CASP2.

HPA

CAB012175.

MIM

600639. gene.

neXtProt

NX_P42575.

PharmGKB

PA26086.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG305976.

HOVERGEN

HBG103962.

InParanoid

P42575.

KO

K02186.

OMA

PCLQVKP.

OrthoDB

EOG4WDDBP.

PhylomeDB

P42575.

Enzyme and pathway databases

BRENDA

3.4.22.55. 2681.

Pathway_Interaction_DB

caspase_pathway. Caspase cascade in apoptosis.
hivnefpathway. HIV-1 Nef: Negative effector of Fas and TNF-alpha.

Reactome

REACT_111102. Signal Transduction.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P42575.

Bgee

P42575.

CleanEx

HS_CASP2.

Genevestigator

P42575.

GermOnline

ENSG00000106144. 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

P42575.

ChEMBL

CHEMBL4884.

EvolutionaryTrace

P42575.

GenomeRNAi

835.

NextBio

3472.

PMAP-CutDB

P42575.

SOURCE

Search...

Entry information

Entry name

CASP2_HUMAN

Accession

Primary (citable) accession number: P42575
Secondary accession number(s): A8K5F9 , D3DXD6, E9PDN0, P42576, Q59F21, Q7KZL6, Q86UJ3, Q9BUP7, Q9BZK9, Q9BZL0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	December 6, 2005
Last modified:	May 1, 2013
This is version 138 of the entry and version 2 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.