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P42575

- CASP2_HUMAN

UniProt

P42575 - CASP2_HUMAN

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Protein
Caspase-2
Gene
CASP2, ICH1, NEDD2
Organism
Homo sapiens (Human)
Status
Reviewed - 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 – 2771 By similarity
Active sitei320 – 3201 By similarity

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: UniProtKB
  2. cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
  3. enzyme binding Source: UniProtKB
  4. protein binding Source: IntAct
  5. protein domain specific binding Source: BHF-UCL

GO - Biological processi

  1. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: UniProtKB
  2. aging Source: Ensembl
  3. apoptotic process Source: UniProtKB
  4. apoptotic signaling pathway Source: UniProtKB
  5. brain development Source: Ensembl
  6. cellular response to mechanical stimulus Source: UniProtKB
  7. ectopic germ cell programmed cell death Source: Ensembl
  8. execution phase of apoptosis Source: UniProtKB
  9. extrinsic apoptotic signaling pathway in absence of ligand Source: RefGenome
  10. intrinsic apoptotic signaling pathway in response to DNA damage Source: UniProtKB
  11. luteolysis Source: Ensembl
  12. neural retina development Source: Ensembl
  13. neurotrophin TRK receptor signaling pathway Source: Reactome
  14. positive regulation of apoptotic process Source: UniProtKB
  15. positive regulation of apoptotic signaling pathway Source: Ensembl
  16. positive regulation of neuron apoptotic process Source: Ensembl
  17. protein processing Source: BHF-UCL
  18. regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Reactome
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: Chromosome 7

Organism-specific databases

HGNCiHGNC:1503. CASP2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: RefGenome
  2. cytosol Source: Reactome
  3. membrane Source: Ensembl
  4. mitochondrion Source: Ensembl
  5. 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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Propeptidei2 – 169168
PRO_0000004541Add
BLAST
Chaini170 – 325156Caspase-2 subunit p18
PRO_0000004542Add
BLAST
Propeptidei326 – 3338
PRO_0000004543
Chaini334 – 452119Caspase-2 subunit p13
PRO_0000004544Add
BLAST
Chaini348 – 452105Caspase-2 subunit p12
PRO_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.

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

ArrayExpressiP42575.
BgeeiP42575.
CleanExiHS_CASP2.
GenevestigatoriP42575.

Organism-specific databases

HPAiCAB012175.

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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CASP2P42575-12EBI-520342,EBI-520357
CRADDP785609EBI-520342,EBI-520375
PRKDCP785274EBI-520342,EBI-352053

Protein-protein interaction databases

BioGridi107285. 30 interactions.
IntActiP42575. 9 interactions.
MINTiMINT-150255.
STRINGi9606.ENSP00000312664.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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 173-452.

Miscellaneous databases

EvolutionaryTraceiP42575.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 12190CARD
Add
BLAST

Sequence similaritiesi

Belongs to the peptidase C14A family.
Contains 1 CARD domain.

Phylogenomic databases

eggNOGiNOG305976.
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. Align

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

MAAPSAGSWS TFQHKELMAA DRGRRILGVC GMHPHHQETL KKNRVVLAKQ    50
LLLSELLEHL LEKDIITLEM RELIQAKVGS FSQNVELLNL LPKRGPQAFD 100
AFCEALRETK QGHLEDMLLT TLSGLQHVLP PLSCDYDLSL PFPVCESCPL 150
YKKLRLSTDT VEHSLDNKDG PVCLQVKPCT PEFYQTHFQL AYRLQSRPRG 200
LALVLSNVHF TGEKELEFRS GGDVDHSTLV TLFKLLGYDV HVLCDQTAQE 250
MQEKLQNFAQ LPAHRVTDSC IVALLSHGVE GAIYGVDGKL LQLQEVFQLF 300
DNANCPSLQN KPKMFFIQAC RGDETDRGVD QQDGKNHAGS PGCEESDAGK 350
EKLPKMRLPT RSDMICGYAC LKGTAAMRNT KRGSWYIEAL AQVFSERACD 400
MHVADMLVKV NALIKDREGY APGTEFHRCK EMSEYCSTLC RHLYLFPGHP 450
PT 452

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.
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.

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.
VSP_000801Add
BLAST
Alternative sequencei1 – 1717Missing in isoform 3.
VSP_046280Add
BLAST
Alternative sequencei107 – 1082RE → HS in isoform 3.
VSP_046281
Alternative sequencei109 – 452344Missing in isoform 3.
VSP_046282Add
BLAST
Alternative sequencei323 – 452130DETDR…GHPPT → GGAIGSLGHLLLFTAATASL AL in isoform 2.
VSP_000802Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti309 – 32214QNKPK…QACRG → EEVTSLSILSAFVT in BAD92877. 1 Publication
Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]

Polymorphism databases

DMDMi83300977.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
CCDSi CCDS5879.1. [P42575-1 ]
PIRi A54821.
RefSeqi NP_001215.1. NM_001224.4.
NP_116764.2. NM_032982.3. [P42575-1 ]
NP_116765.2. NM_032983.3.
UniGenei Hs.368982.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P42575.
SMRi P42575. Positions 173-452.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107285. 30 interactions.
IntActi P42575. 9 interactions.
MINTi MINT-150255.
STRINGi 9606.ENSP00000312664.

Chemistry

BindingDBi P42575.
ChEMBLi CHEMBL4884.
GuidetoPHARMACOLOGYi 1618.

Protein family/group databases

MEROPSi C14.006.

PTM databases

PhosphoSitei P42575.

Polymorphism databases

DMDMi 83300977.

Proteomic databases

MaxQBi P42575.
PaxDbi P42575.
PeptideAtlasi P42575.
PRIDEi P42575.

Protocols and materials databases

DNASUi 835.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000310447 ; ENSP00000312664 ; ENSG00000106144 . [P42575-1 ]
GeneIDi 835.
KEGGi hsa:835.
UCSCi uc003wco.3. human. [P42575-1 ]

Organism-specific databases

CTDi 835.
GeneCardsi GC07P142985.
HGNCi HGNC:1503. CASP2.
HPAi CAB012175.
MIMi 600639. gene.
neXtProti NX_P42575.
PharmGKBi PA26086.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG305976.
HOVERGENi HBG103962.
InParanoidi P42575.
KOi K02186.
OMAi PCLQVKP.
OrthoDBi EOG7TTQ7K.
PhylomeDBi P42575.
TreeFami TF102023.

Enzyme and pathway databases

BRENDAi 3.4.22.55. 2681.
Reactomei REACT_13526. NADE modulates death signalling.
REACT_75776. NOD1/2 Signaling Pathway.

Miscellaneous databases

EvolutionaryTracei P42575.
GeneWikii Caspase_2.
GenomeRNAii 835.
NextBioi 3472.
PMAP-CutDB P42575.
PROi P42575.
SOURCEi Search...

Gene expression databases

ArrayExpressi P42575.
Bgeei P42575.
CleanExi HS_CASP2.
Genevestigatori P42575.

Family and domain databases

Gene3Di 1.10.533.10. 1 hit.
3.40.50.1460. 1 hit.
InterProi IPR001315. 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 ]
Pfami PF00619. CARD. 1 hit.
PF00656. Peptidase_C14. 1 hit.
[Graphical view ]
PIRSFi PIRSF038001. Caspase_ICE. 1 hit.
PRINTSi PR00376. IL1BCENZYME.
SMARTi SM00114. CARD. 1 hit.
SM00115. CASc. 1 hit.
[Graphical view ]
SUPFAMi SSF47986. SSF47986. 1 hit.
PROSITEi 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 ]
ProtoNeti Search...

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. "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. 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.

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: September 3, 2014
This is version 152 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

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