Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Caspase-2

Gene

Casp2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. May be important in multistep carcinogenesis.

Catalytic activityi

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-|-.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei277 – 2771By similarity
Active sitei320 – 3201By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

BRENDAi3.4.22.55. 3474.
ReactomeiR-MMU-205025. NADE modulates death signalling.
R-MMU-6803207. TP53 Regulates Transcription of Caspase Activators and Caspases.

Protein family/group databases

MEROPSiC14.006.

Names & Taxonomyi

Protein namesi
Recommended name:
Caspase-2 (EC:3.4.22.55)
Short name:
CASP-2
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:
Gene namesi
Name:Casp2
Synonyms:Ich1, Nedd-2, Nedd2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:97295. Casp2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • membrane Source: Ensembl
  • mitochondrion Source: Ensembl
  • nucleus Source: MGI
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi320 – 3201C → G: Loss of function.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Propeptidei2 – 169168By similarityPRO_0000004546Add
BLAST
Chaini170 – 333164Caspase-2 subunit p18By similarityPRO_0000004547Add
BLAST
Chaini334 – 452119Caspase-2 subunit p13By similarityPRO_0000004548Add
BLAST
Chaini348 – 452105Caspase-2 subunit p12By similarityPRO_0000004549Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei340 – 3401PhosphoserineBy similarity

Post-translational modificationi

The mature protease can process its own propeptide, but not that of other caspases.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Zymogen

Proteomic databases

EPDiP29594.
MaxQBiP29594.
PaxDbiP29594.
PRIDEiP29594.

PTM databases

iPTMnetiP29594.
PhosphoSiteiP29594.

Expressioni

Tissue specificityi

High level expression seen in the embryonic CNS, liver, lung, kidney, small intestine, and hair follicles of vibrissae. Moderate expression seen in the skin, oral mucosa, skeletal muscle, submandibular gland and thymus. In the adult, it is highly expressed in spleen, lung and kidney. Moderately in the brain, heart, testis, liver. Low levels in the thymus, skeletal muscle, ovary and gut.

Developmental stagei

During embryonic development is highly expressed in several types of mouse tissue undergoing high rates of programmed cell death such as central nervous system and kidney.

Gene expression databases

BgeeiP29594.
CleanExiMM_CASP2.
ExpressionAtlasiP29594. baseline and differential.
GenevisibleiP29594. MM.

Interactioni

Subunit structurei

Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a p18 subunit and a p12 subunit. Interacts with LRDD. Interacts with NOL3 (via CARD domain); inhibits CASP2 activity in a phosphorylation-dependent manner (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198496. 1 interaction.
STRINGi10090.ENSMUSP00000031895.

Structurei

3D structure databases

ProteinModelPortaliP29594.
SMRiP29594. Positions 176-452.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 12190CARDPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C14A family.Curated
Contains 1 CARD domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3573. Eukaryota.
ENOG410ZQIE. LUCA.
GeneTreeiENSGT00760000118912.
HOGENOMiHOG000290714.
HOVERGENiHBG103962.
InParanoidiP29594.
KOiK02186.
OMAiPNLQNKP.
OrthoDBiEOG7TTQ7K.
PhylomeDBiP29594.
TreeFamiTF102023.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
3.40.50.1460. 1 hit.
InterProiIPR001315. CARD.
IPR029030. Caspase-like_dom.
IPR033139. Caspase_cys_AS.
IPR016129. Caspase_his_AS.
IPR011029. DEATH-like_dom.
IPR002138. Pept_C14_p10.
IPR001309. Pept_C14_p20.
IPR015917. Pept_C14A.
IPR017350. Pept_C14A_CASP1-typ.
[Graphical view]
PfamiPF00619. CARD. 1 hit.
[Graphical view]
PIRSFiPIRSF038001. Caspase_ICE. 1 hit.
PRINTSiPR00376. IL1BCENZYME.
SMARTiSM00114. CARD. 1 hit.
SM00115. CASc. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
SSF52129. SSF52129. 1 hit.
PROSITEiPS50209. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P29594-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAPSGRSQS SLHRKGLMAA DRRSRILAVC GMHPDHQETL KKNRVVLAKQ
60 70 80 90 100
LLLSELLEHL LEKDIITLEM RELIQAKGGS FSQNVELLNL LPKRGPQAFD
110 120 130 140 150
AFCEALRETR QGHLEDLLLT TLSDIQHVLP PLSCDYDTSL PFSVCESCPP
160 170 180 190 200
HKQLRLSTDA TEHSLDNGDG PPCLLVKPCT PEFYQAHYQL AYRLQSQPRG
210 220 230 240 250
LALVLSNVHF TGEKDLEFRS GGDVDHTTLV TLFKLLGYNV HVLHDQTAQE
260 270 280 290 300
MQEKLQNFAQ LPAHRVTDSC VVALLSHGVE GGIYGVDGKL LQLQEVFRLF
310 320 330 340 350
DNANCPSLQN KPKMFFIQAC RGDETDRGVD QQDGKNHTQS PGCEESDAGK
360 370 380 390 400
EELMKMRLPT RSDMICGYAC LKGNAAMRNT KRGSWYIEAL TQVFSERACD
410 420 430 440 450
MHVADMLVKV NALIKEREGY APGTEFHRCK EMSEYCSTLC QQLYLFPGYP

PT
Length:452
Mass (Da):50,661
Last modified:December 6, 2005 - v5
Checksum:iA4DE25A712FAB855
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti85 – 10218VELLN…AFDAF → EGCGGWRGPAFVCFVGGA in BAE41936 (PubMed:16141072).CuratedAdd
BLAST
Sequence conflicti88 – 881Missing no nucleotide entry (PubMed:9038361).Curated
Sequence conflicti234 – 2341K → R in BAC31153 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D28492 mRNA. Translation: BAA25876.1.
Y13085 mRNA. Translation: CAA73527.1.
AK042072 mRNA. Translation: BAC31153.1.
AK170649 mRNA. Translation: BAE41936.1.
BC034262 mRNA. Translation: AAH34262.1.
CCDSiCCDS20064.1.
RefSeqiNP_031636.1. NM_007610.2.
UniGeneiMm.3921.
Mm.488970.

Genome annotation databases

EnsembliENSMUST00000031895; ENSMUSP00000031895; ENSMUSG00000029863.
GeneIDi12366.
KEGGimmu:12366.
UCSCiuc009bqq.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D28492 mRNA. Translation: BAA25876.1.
Y13085 mRNA. Translation: CAA73527.1.
AK042072 mRNA. Translation: BAC31153.1.
AK170649 mRNA. Translation: BAE41936.1.
BC034262 mRNA. Translation: AAH34262.1.
CCDSiCCDS20064.1.
RefSeqiNP_031636.1. NM_007610.2.
UniGeneiMm.3921.
Mm.488970.

3D structure databases

ProteinModelPortaliP29594.
SMRiP29594. Positions 176-452.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198496. 1 interaction.
STRINGi10090.ENSMUSP00000031895.

Protein family/group databases

MEROPSiC14.006.

PTM databases

iPTMnetiP29594.
PhosphoSiteiP29594.

Proteomic databases

EPDiP29594.
MaxQBiP29594.
PaxDbiP29594.
PRIDEiP29594.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031895; ENSMUSP00000031895; ENSMUSG00000029863.
GeneIDi12366.
KEGGimmu:12366.
UCSCiuc009bqq.2. mouse.

Organism-specific databases

CTDi835.
MGIiMGI:97295. Casp2.

Phylogenomic databases

eggNOGiKOG3573. Eukaryota.
ENOG410ZQIE. LUCA.
GeneTreeiENSGT00760000118912.
HOGENOMiHOG000290714.
HOVERGENiHBG103962.
InParanoidiP29594.
KOiK02186.
OMAiPNLQNKP.
OrthoDBiEOG7TTQ7K.
PhylomeDBiP29594.
TreeFamiTF102023.

Enzyme and pathway databases

BRENDAi3.4.22.55. 3474.
ReactomeiR-MMU-205025. NADE modulates death signalling.
R-MMU-6803207. TP53 Regulates Transcription of Caspase Activators and Caspases.

Miscellaneous databases

PROiP29594.
SOURCEiSearch...

Gene expression databases

BgeeiP29594.
CleanExiMM_CASP2.
ExpressionAtlasiP29594. baseline and differential.
GenevisibleiP29594. MM.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
3.40.50.1460. 1 hit.
InterProiIPR001315. CARD.
IPR029030. Caspase-like_dom.
IPR033139. Caspase_cys_AS.
IPR016129. Caspase_his_AS.
IPR011029. DEATH-like_dom.
IPR002138. Pept_C14_p10.
IPR001309. Pept_C14_p20.
IPR015917. Pept_C14A.
IPR017350. Pept_C14A_CASP1-typ.
[Graphical view]
PfamiPF00619. CARD. 1 hit.
[Graphical view]
PIRSFiPIRSF038001. Caspase_ICE. 1 hit.
PRINTSiPR00376. IL1BCENZYME.
SMARTiSM00114. CARD. 1 hit.
SM00115. CASc. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
SSF52129. SSF52129. 1 hit.
PROSITEiPS50209. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Induction of apoptosis by the mouse Nedd2 gene, which encodes a protein similar to the product of the Caenorhabditis elegans cell death gene ced-3 and the mammalian IL-1 beta-converting enzyme."
    Kumar S., Kinoshita M., Noda M., Copeland N.G., Jenkins N.A.
    Genes Dev. 8:1613-1626(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C3H/An.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
  4. "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].
    Strain: FVB/N.
    Tissue: Mammary gland.
  5. "Identification of a set of genes with developmentally down-regulated expression in the mouse brain."
    Kumar S., Tomooka Y., Noda M.
    Biochem. Biophys. Res. Commun. 185:1155-1161(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY PARTIAL NUCLEOTIDE SEQUENCE.
    Tissue: Brain.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen.

Entry informationi

Entry nameiCASP2_MOUSE
AccessioniPrimary (citable) accession number: P29594
Secondary accession number(s): O08737
, Q3TCM0, Q8C9H7, Q8K241
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: December 6, 2005
Last modified: June 8, 2016
This is version 160 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.