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P42575 (CASP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Gene names
Name:CASP2
Synonyms:ICH1, NEDD2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length452 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.17

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 processApoptosis
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionHydrolase
Protease
Thiol protease
   PTMAcetylation
Phosphoprotein
Zymogen
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA 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: Ensembl

apoptotic process

Non-traceable author statement Ref.2. Source: UniProtKB

apoptotic signaling pathway

Traceable author statement PubMed 18309324. Source: UniProtKB

brain development

Inferred from electronic annotation. Source: Ensembl

cellular response to mechanical stimulus

Inferred from expression pattern PubMed 19593445. Source: UniProtKB

ectopic germ cell programmed cell death

Inferred from electronic annotation. Source: Ensembl

execution phase of apoptosis

Traceable author statement PubMed 18309324. Source: UniProtKB

extrinsic apoptotic signaling pathway in absence of ligand

Inferred from Biological aspect of Ancestor. Source: RefGenome

intrinsic apoptotic signaling pathway in response to DNA damage

Traceable author statement PubMed 18309324. Source: UniProtKB

luteolysis

Inferred from electronic annotation. Source: Ensembl

neural retina development

Inferred from electronic annotation. Source: Ensembl

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

positive regulation of apoptotic process

Inferred from direct assay PubMed 10980123. Source: UniProtKB

positive regulation of apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

protein processing

Inferred from direct assay PubMed 9044836. Source: BHF-UCL

regulation of cysteine-type endopeptidase activity involved in apoptotic process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytosol

Traceable author statement. Source: Reactome

membrane

Inferred from electronic annotation. Source: Ensembl

mitochondrion

Inferred from electronic annotation. Source: Ensembl

nucleus

Traceable author statement PubMed 18309324. Source: UniProtKB

   Molecular_functioncysteine-type endopeptidase activity

Inferred from direct assay PubMed 10980123PubMed 21726810. Source: UniProtKB

cysteine-type endopeptidase activity involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

enzyme binding

Inferred from sequence or structural similarity PubMed 11076957. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.2. Source: IntAct

protein domain specific binding

Inferred from physical interaction PubMed 9044836. Source: BHF-UCL

Complete GO annotation...

Binary interactions

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.14
Propeptide2 – 169168
PRO_0000004541
Chain170 – 325156Caspase-2 subunit p18
PRO_0000004542
Propeptide326 – 3338
PRO_0000004543
Chain334 – 452119Caspase-2 subunit p13
PRO_0000004544
Chain348 – 452105Caspase-2 subunit p12
PRO_0000004545

Regions

Domain32 – 12190CARD

Sites

Active site2771 By similarity
Active site3201 By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.14
Modified residue3401Phosphoserine Ref.16

Natural variations

Alternative sequence1 – 3131Missing in isoform 2.
VSP_000801
Alternative sequence1 – 1717Missing in isoform 3.
VSP_046280
Alternative sequence107 – 1082RE → HS in isoform 3.
VSP_046281
Alternative sequence109 – 452344Missing in isoform 3.
VSP_046282
Alternative sequence323 – 452130DETDR…GHPPT → GGAIGSLGHLLLFTAATASL AL in isoform 2.
VSP_000802
Natural variant1051A → G.
Corresponds to variant rs4647298 [ dbSNP | Ensembl ].
VAR_055621
Natural variant1721V → L. Ref.5 Ref.8 Ref.9
Corresponds to variant rs4647297 [ dbSNP | Ensembl ].
VAR_016334
Natural variant1781P → A. Ref.5
Corresponds to variant rs4647298 [ dbSNP | Ensembl ].
VAR_016335
Natural variant4411R → G. Ref.5
Corresponds to variant rs4647338 [ dbSNP | Ensembl ].
VAR_016336

Experimental info

Mutagenesis3201C → S: Loss of function.
Mutagenesis3691A → T: Loss of function.
Sequence conflict309 – 32214QNKPK…QACRG → EEVTSLSILSAFVT in BAD92877. Ref.10

Secondary structure

............................................... 452
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (ICH-1L) [UniParc].

Last modified December 6, 2005. Version 2.
Checksum: 6EF0ED05EF808385

FASTA45250,685
        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 

« Hide

Isoform 2 (ICH-1S) [UniParc].

Checksum: FA1E307A41B8299E
Show »

FASTA31334,923
Isoform 3 (Casp-2L-Pro) [UniParc].

Checksum: E80E3D9233686A98
Show »

FASTA9110,309

References

« Hide '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. 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 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. expand/collapse author list , 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. 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 (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]"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] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[15]"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].
[16]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"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

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.
CCDSCCDS5879.1. [P42575-1]
PIRA54821.
RefSeqNP_001215.1. NM_001224.4.
NP_116764.2. NM_032982.3. [P42575-1]
NP_116765.2. NM_032983.3.
UniGeneHs.368982.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PYOX-ray1.65A/C167-333[»]
B/D348-452[»]
2P2CX-ray3.24A/C/E/G/I/K167-333[»]
B/D/F/H/J/L348-452[»]
3R5JX-ray1.77A/C175-333[»]
B/D349-452[»]
3R6GX-ray2.07A/C175-333[»]
B/D349-452[»]
3R6LX-ray1.90A/C175-333[»]
B/D349-452[»]
3R7BX-ray1.80A/C175-333[»]
B/D349-452[»]
3R7NX-ray2.33A/C175-333[»]
B/D349-452[»]
3R7SX-ray2.25A/C175-333[»]
B/D349-452[»]
3RJMX-ray2.55A/C167-333[»]
B/D348-452[»]
ProteinModelPortalP42575.
SMRP42575. Positions 173-452.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107285. 30 interactions.
IntActP42575. 9 interactions.
MINTMINT-150255.
STRING9606.ENSP00000312664.

Chemistry

BindingDBP42575.
ChEMBLCHEMBL4884.
GuidetoPHARMACOLOGY1618.

Protein family/group databases

MEROPSC14.006.

PTM databases

PhosphoSiteP42575.

Polymorphism databases

DMDM83300977.

Proteomic databases

MaxQBP42575.
PaxDbP42575.
PeptideAtlasP42575.
PRIDEP42575.

Protocols and materials databases

DNASU835.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000310447; ENSP00000312664; ENSG00000106144. [P42575-1]
GeneID835.
KEGGhsa:835.
UCSCuc003wco.3. human. [P42575-1]

Organism-specific databases

CTD835.
GeneCardsGC07P142985.
HGNCHGNC:1503. CASP2.
HPACAB012175.
MIM600639. gene.
neXtProtNX_P42575.
PharmGKBPA26086.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG305976.
HOVERGENHBG103962.
InParanoidP42575.
KOK02186.
OMAPCLQVKP.
OrthoDBEOG7TTQ7K.
PhylomeDBP42575.
TreeFamTF102023.

Enzyme and pathway databases

BRENDA3.4.22.55. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP42575.
BgeeP42575.
CleanExHS_CASP2.
GenevestigatorP42575.

Family and domain databases

Gene3D1.10.533.10. 1 hit.
3.40.50.1460. 1 hit.
InterProIPR001315. CARD.
IPR029030. Caspase-like_dom.
IPR017350. Caspase_ICE-type.
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

EvolutionaryTraceP42575.
GeneWikiCaspase_2.
GenomeRNAi835.
NextBio3472.
PMAP-CutDBP42575.
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Entry information

Entry nameCASP2_HUMAN
AccessionPrimary (citable) accession number: P42575
Secondary accession number(s): A8K5F9 expand/collapse secondary AC list , 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: July 9, 2014
This is version 151 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 7

Human chromosome 7: entries, gene names and cross-references to MIM