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Protein

Caspase-2

Gene

CASP2

Organism
Homo sapiens (Human)
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.

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

  • cysteine-type endopeptidase activity Source: UniProtKB
  • cysteine-type endopeptidase activity involved in apoptotic signaling pathway Source: GO_Central
  • enzyme binding Source: UniProtKB
  • protein domain specific binding Source: BHF-UCL

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. 2681.
ReactomeiREACT_13526. NADE modulates death signalling.
REACT_75776. NOD1/2 Signaling Pathway.

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, NEDD2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:1503. CASP2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • cytosol Source: Reactome
  • membrane Source: Ensembl
  • mitochondrion Source: Ensembl
  • nucleus Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi320 – 3201C → S: Loss of function.
Mutagenesisi369 – 3691A → T: Loss of function.

Organism-specific databases

PharmGKBiPA26086.

Polymorphism and mutation databases

BioMutaiCASP2.
DMDMi83300977.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Propeptidei2 – 169168PRO_0000004541Add
BLAST
Chaini170 – 325156Caspase-2 subunit p18PRO_0000004542Add
BLAST
Propeptidei326 – 3338PRO_0000004543
Chaini334 – 452119Caspase-2 subunit p13PRO_0000004544Add
BLAST
Chaini348 – 452105Caspase-2 subunit p12PRO_0000004545Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei340 – 3401Phosphoserine1 Publication

Post-translational modificationi

The mature protease can process its own propeptide, but not that of other caspases.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Zymogen

Proteomic databases

MaxQBiP42575.
PaxDbiP42575.
PeptideAtlasiP42575.
PRIDEiP42575.

PTM databases

PhosphoSiteiP42575.

Miscellaneous databases

PMAP-CutDBP42575.

Expressioni

Tissue specificityi

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.

Gene expression databases

BgeeiP42575.
CleanExiHS_CASP2.
ExpressionAtlasiP42575. baseline and differential.
GenevisibleiP42575. HS.

Organism-specific databases

HPAiCAB012175.
HPA050678.

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 similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CASP2P42575-12EBI-520342,EBI-520357
CRADDP7856012EBI-520342,EBI-520375
PRKDCP785274EBI-520342,EBI-352053

Protein-protein interaction databases

BioGridi107285. 32 interactions.
IntActiP42575. 9 interactions.
MINTiMINT-150255.

Structurei

Secondary structure

1
452
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi181 – 1877Combined sources
Helixi188 – 1903Combined sources
Beta strandi197 – 20610Combined sources
Beta strandi212 – 2143Combined sources
Helixi222 – 23514Combined sources
Beta strandi238 – 2458Combined sources
Helixi248 – 25912Combined sources
Helixi262 – 2654Combined sources
Beta strandi267 – 27610Combined sources
Beta strandi282 – 2843Combined sources
Beta strandi290 – 2923Combined sources
Helixi293 – 2997Combined sources
Turni302 – 3043Combined sources
Helixi306 – 3083Combined sources
Beta strandi313 – 3197Combined sources
Beta strandi321 – 3244Combined sources
Beta strandi363 – 3708Combined sources
Beta strandi377 – 3793Combined sources
Turni380 – 3823Combined sources
Helixi385 – 39713Combined sources
Turni398 – 4003Combined sources
Helixi403 – 41513Combined sources
Turni425 – 4284Combined sources
Beta strandi434 – 4374Combined sources
Beta strandi440 – 4423Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP42575.
SMRiP42575. Positions 32-122, 173-452.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42575.

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

eggNOGiNOG305976.
GeneTreeiENSGT00760000118912.
HOVERGENiHBG103962.
InParanoidiP42575.
KOiK02186.
OMAiPCLQVKP.
OrthoDBiEOG7TTQ7K.
PhylomeDBiP42575.
TreeFamiTF102023.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
3.40.50.1460. 1 hit.
InterProiIPR001315. 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]
PfamiPF00619. CARD. 1 hit.
PF00656. Peptidase_C14. 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.
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]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

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

Isoform 1 (identifier: P42575-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAAPSAGSWS TFQHKELMAA DRGRRILGVC GMHPHHQETL KKNRVVLAKQ
60 70 80 90 100
LLLSELLEHL LEKDIITLEM RELIQAKVGS FSQNVELLNL LPKRGPQAFD
110 120 130 140 150
AFCEALRETK QGHLEDMLLT TLSGLQHVLP PLSCDYDLSL PFPVCESCPL
160 170 180 190 200
YKKLRLSTDT VEHSLDNKDG PVCLQVKPCT PEFYQTHFQL AYRLQSRPRG
210 220 230 240 250
LALVLSNVHF TGEKELEFRS GGDVDHSTLV TLFKLLGYDV HVLCDQTAQE
260 270 280 290 300
MQEKLQNFAQ LPAHRVTDSC IVALLSHGVE GAIYGVDGKL LQLQEVFQLF
310 320 330 340 350
DNANCPSLQN KPKMFFIQAC RGDETDRGVD QQDGKNHAGS PGCEESDAGK
360 370 380 390 400
EKLPKMRLPT RSDMICGYAC LKGTAAMRNT KRGSWYIEAL AQVFSERACD
410 420 430 440 450
MHVADMLVKV NALIKDREGY APGTEFHRCK EMSEYCSTLC RHLYLFPGHP

PT
Note: Acts as a positive regulator of apoptosis.
Length:452
Mass (Da):50,685
Last modified:December 6, 2005 - v2
Checksum:i6EF0ED05EF808385
GO
Isoform 2 (identifier: P42575-2) [UniParc]FASTAAdd to basket

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.
Show »
Length:313
Mass (Da):34,923
Checksum:iFA1E307A41B8299E
GO
Isoform 3 (identifier: P42575-3) [UniParc]FASTAAdd to basket

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.
Show »
Length:91
Mass (Da):10,309
Checksum:iE80E3D9233686A98
GO

Sequence cautioni

The sequence AAA58959.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAO25653.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAP22346.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAP22349.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAD92877.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti309 – 32214QNKPK…QACRG → EEVTSLSILSAFVT in BAD92877 (Ref. 10) CuratedAdd
BLAST

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti105 – 1051A → G.
Corresponds to variant rs4647298 [ dbSNP | Ensembl ].
VAR_055621
Natural varianti172 – 1721V → L.3 Publications
Corresponds to variant rs4647297 [ dbSNP | Ensembl ].
VAR_016334
Natural varianti178 – 1781P → A.1 Publication
Corresponds to variant rs4647298 [ dbSNP | Ensembl ].
VAR_016335
Natural varianti441 – 4411R → G.1 Publication
Corresponds to variant rs4647338 [ dbSNP | Ensembl ].
VAR_016336

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3131Missing in isoform 2. 2 PublicationsVSP_000801Add
BLAST
Alternative sequencei1 – 1717Missing in isoform 3. 1 PublicationVSP_046280Add
BLAST
Alternative sequencei107 – 1082RE → HS in isoform 3. 1 PublicationVSP_046281
Alternative sequencei109 – 452344Missing in isoform 3. 1 PublicationVSP_046282Add
BLAST
Alternative sequencei323 – 452130DETDR…GHPPT → GGAIGSLGHLLLFTAATASL AL in isoform 2. 2 PublicationsVSP_000802Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS5879.1. [P42575-1]
PIRiA54821.
RefSeqiNP_001215.1. NM_001224.4.
NP_116764.2. NM_032982.3. [P42575-1]
NP_116765.2. NM_032983.3.
UniGeneiHs.368982.

Genome annotation databases

EnsembliENST00000310447; ENSP00000312664; ENSG00000106144. [P42575-1]
GeneIDi835.
KEGGihsa:835.
UCSCiuc003wco.3. human. [P42575-1]
uc003wcp.3. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS5879.1. [P42575-1]
PIRiA54821.
RefSeqiNP_001215.1. NM_001224.4.
NP_116764.2. NM_032982.3. [P42575-1]
NP_116765.2. NM_032983.3.
UniGeneiHs.368982.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP42575.
SMRiP42575. Positions 32-122, 173-452.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107285. 32 interactions.
IntActiP42575. 9 interactions.
MINTiMINT-150255.

Chemistry

BindingDBiP42575.
ChEMBLiCHEMBL4884.
GuidetoPHARMACOLOGYi1618.

Protein family/group databases

MEROPSiC14.006.

PTM databases

PhosphoSiteiP42575.

Polymorphism and mutation databases

BioMutaiCASP2.
DMDMi83300977.

Proteomic databases

MaxQBiP42575.
PaxDbiP42575.
PeptideAtlasiP42575.
PRIDEiP42575.

Protocols and materials databases

DNASUi835.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000310447; ENSP00000312664; ENSG00000106144. [P42575-1]
GeneIDi835.
KEGGihsa:835.
UCSCiuc003wco.3. human. [P42575-1]
uc003wcp.3. human.

Organism-specific databases

CTDi835.
GeneCardsiGC07P142985.
HGNCiHGNC:1503. CASP2.
HPAiCAB012175.
HPA050678.
MIMi600639. gene.
neXtProtiNX_P42575.
PharmGKBiPA26086.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG305976.
GeneTreeiENSGT00760000118912.
HOVERGENiHBG103962.
InParanoidiP42575.
KOiK02186.
OMAiPCLQVKP.
OrthoDBiEOG7TTQ7K.
PhylomeDBiP42575.
TreeFamiTF102023.

Enzyme and pathway databases

BRENDAi3.4.22.55. 2681.
ReactomeiREACT_13526. NADE modulates death signalling.
REACT_75776. NOD1/2 Signaling Pathway.

Miscellaneous databases

ChiTaRSiCASP2. human.
EvolutionaryTraceiP42575.
GeneWikiiCaspase_2.
GenomeRNAii835.
NextBioi3472.
PMAP-CutDBP42575.
PROiP42575.
SOURCEiSearch...

Gene expression databases

BgeeiP42575.
CleanExiHS_CASP2.
ExpressionAtlasiP42575. baseline and differential.
GenevisibleiP42575. HS.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
3.40.50.1460. 1 hit.
InterProiIPR001315. 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]
PfamiPF00619. CARD. 1 hit.
PF00656. Peptidase_C14. 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.
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. "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. 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. "ARC, an inhibitor of apoptosis expressed in skeletal muscle and heart that interacts selectively with caspases."
    Koseki T., Inohara N., Chen S., Nunez G.
    Proc. Natl. Acad. Sci. U.S.A. 95:5156-5160(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NOL3.
  13. "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.
  14. "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.
  15. "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].
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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].
  18. "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.

Entry informationi

Entry nameiCASP2_HUMAN
AccessioniPrimary (citable) accession number: P42575
Secondary accession number(s): A8K5F9
, D3DXD6, E9PDN0, P42576, Q59F21, Q7KZL6, Q86UJ3, Q9BUP7, Q9BZK9, Q9BZL0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: December 6, 2005
Last modified: June 24, 2015
This is version 161 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.