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P55210

- CASP7_HUMAN

UniProt

P55210 - CASP7_HUMAN

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Protein

Caspase-7

Gene
CASP7, MCH3
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. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Overexpression promotes programmed cell death.

Catalytic activityi

Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Asp-Glu-Val-Asp-|-.

Enzyme regulationi

Inhibited by isatin sulfonamides.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei144 – 1441 By similarity
Active sitei186 – 1861

GO - Molecular functioni

  1. aspartic-type endopeptidase activity Source: Ensembl
  2. cysteine-type endopeptidase activity Source: RefGenome
  3. cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
  4. cysteine-type peptidase activity Source: ProtInc
  5. protein binding Source: UniProtKB

GO - Biological processi

  1. activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c Source: Reactome
  2. aging Source: Ensembl
  3. apoptotic process Source: Reactome
  4. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
  5. execution phase of apoptosis Source: RefGenome
  6. heart development Source: Ensembl
  7. intrinsic apoptotic signaling pathway Source: Reactome
  8. positive regulation of neuron apoptotic process Source: Ensembl
  9. proteolysis Source: UniProtKB
  10. release of cytochrome c from mitochondria Source: Ensembl
  11. response to UV Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

BRENDAi3.4.22.60. 2681.
ReactomeiREACT_107. Apoptotic cleavage of cellular proteins.
REACT_13541. Caspase-mediated cleavage of cytoskeletal proteins.
REACT_607. Activation of caspases through apoptosome-mediated cleavage.

Protein family/group databases

MEROPSiC14.004.

Names & Taxonomyi

Protein namesi
Recommended name:
Caspase-7 (EC:3.4.22.60)
Short name:
CASP-7
Alternative name(s):
Apoptotic protease Mch-3
CMH-1
ICE-like apoptotic protease 3
Short name:
ICE-LAP3
Cleaved into the following 2 chains:
Gene namesi
Name:CASP7
Synonyms:MCH3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:1508. CASP7.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. cytosol Source: UniProtKB
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi186 – 1861C → A: No apoptotic activity.

Organism-specific databases

PharmGKBiPA26091.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Propeptidei2 – 2322PRO_0000004616Add
BLAST
Chaini24 – 198175Caspase-7 subunit p20PRO_0000004617Add
BLAST
Propeptidei199 – 2068PRO_0000004618
Chaini207 – 30397Caspase-7 subunit p11PRO_0000004619Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications

Post-translational modificationi

Cleavages by granzyme B or caspase-10 generate the two active subunits. Propeptide domains can also be cleaved efficiently by caspase-3. Active heterodimers between the small subunit of caspase-7 and the large subunit of caspase-3, and vice versa, also occur.1 Publication

Keywords - PTMi

Acetylation, Zymogen

Proteomic databases

MaxQBiP55210.
PaxDbiP55210.
PRIDEiP55210.

PTM databases

PhosphoSiteiP55210.

Miscellaneous databases

PMAP-CutDBP55210.

Expressioni

Tissue specificityi

Highly expressed in lung, skeletal muscle, liver, kidney, spleen and heart, and moderately in testis. No expression in the brain.

Gene expression databases

ArrayExpressiP55210.
BgeeiP55210.
CleanExiHS_CASP7.
GenevestigatoriP55210.

Organism-specific databases

HPAiCAB025563.

Interactioni

Subunit structurei

Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 20 kDa (p20) and a 11 kDa (p11) subunit. Interacts with BIRC6/bruce.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BIRC2Q134902EBI-523958,EBI-514538
PAK2Q131776EBI-523958,EBI-1045887
SMPD1P174056EBI-523958,EBI-7095800
XIAPP981702EBI-523958,EBI-517127

Protein-protein interaction databases

BioGridi107290. 46 interactions.
DIPiDIP-29973N.
IntActiP55210. 8 interactions.
MINTiMINT-147084.
STRINGi9606.ENSP00000298700.

Structurei

Secondary structure

1
303
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi56 – 583
Beta strandi64 – 663
Beta strandi68 – 747
Helixi80 – 823
Helixi90 – 10415
Beta strandi106 – 1138
Helixi116 – 12712
Helixi131 – 1333
Beta strandi137 – 1437
Beta strandi149 – 1524
Beta strandi155 – 1584
Helixi159 – 1635
Helixi164 – 1663
Turni168 – 1703
Helixi172 – 1743
Beta strandi179 – 1857
Beta strandi188 – 1903
Turni209 – 2113
Turni215 – 2184
Beta strandi219 – 2257
Beta strandi227 – 2293
Beta strandi232 – 2343
Turni235 – 2373
Helixi240 – 25213
Turni253 – 2553
Helixi258 – 27215
Helixi280 – 2823
Beta strandi290 – 2934
Beta strandi296 – 2983

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F1JX-ray2.35A/B2-303[»]
1GQFX-ray2.90A/B47-303[»]
1I4OX-ray2.40A/B24-303[»]
1I51X-ray2.45A/C51-198[»]
B/D199-303[»]
1K86X-ray2.60A/B51-303[»]
1K88X-ray2.70A/B51-303[»]
1KMCX-ray2.90A/B1-303[»]
1MIAmodel-A57-193[»]
B211-303[»]
1SHJX-ray2.80A/B50-303[»]
1SHLX-ray3.00A/B57-303[»]
2QL5X-ray2.34A/C24-196[»]
B/D207-303[»]
2QL7X-ray2.40A/C24-196[»]
B/D207-303[»]
2QL9X-ray2.14A/C24-196[»]
B/D207-303[»]
2QLBX-ray2.25A/C24-196[»]
B/D207-303[»]
2QLFX-ray2.80A/C24-196[»]
B/D207-303[»]
2QLJX-ray2.60A/C24-196[»]
B/D207-303[»]
3EDRX-ray2.45A/C24-196[»]
B/D207-303[»]
3H1PX-ray2.61A/B50-303[»]
3IBCX-ray2.75A/C24-196[»]
B/D207-303[»]
3IBFX-ray2.50A/C24-196[»]
B/D207-303[»]
3R5KX-ray2.86A/B1-303[»]
4FDLX-ray2.80A/B2-303[»]
4FEAX-ray3.79A/B57-303[»]
4HQ0X-ray3.00A/B47-303[»]
4HQRX-ray3.00A/B47-303[»]
4JB8X-ray1.70A24-198[»]
B207-303[»]
4JJ8X-ray2.94A/B57-303[»]
4JR1X-ray2.15A/B57-303[»]
4JR2X-ray1.65A/B57-303[»]
ProteinModelPortaliP55210.
SMRiP55210. Positions 47-303.

Miscellaneous databases

EvolutionaryTraceiP55210.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C14A family.

Phylogenomic databases

eggNOGiNOG279444.
HOVERGENiHBG050802.
InParanoidiP55210.
KOiK04397.
OMAiDANPRHK.
PhylomeDBiP55210.
TreeFamiTF102023.

Family and domain databases

Gene3Di3.40.50.1460. 1 hit.
InterProiIPR029030. Caspase-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]
PfamiPF00656. Peptidase_C14. 1 hit.
[Graphical view]
PRINTSiPR00376. IL1BCENZYME.
SMARTiSM00115. CASc. 1 hit.
[Graphical view]
PROSITEiPS01122. CASPASE_CYS. 1 hit.
PS01121. CASPASE_HIS. 1 hit.
PS50207. CASPASE_P10. 1 hit.
PS50208. CASPASE_P20. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform Alpha (identifier: P55210-1) [UniParc]FASTAAdd to Basket

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

MADDQGCIEE QGVEDSANED SVDAKPDRSS FVPSLFSKKK KNVTMRSIKT    50
TRDRVPTYQY NMNFEKLGKC IIINNKNFDK VTGMGVRNGT DKDAEALFKC 100
FRSLGFDVIV YNDCSCAKMQ DLLKKASEED HTNAACFACI LLSHGEENVI 150
YGKDGVTPIK DLTAHFRGDR CKTLLEKPKL FFIQACRGTE LDDGIQADSG 200
PINDTDANPR YKIPVEADFL FAYSTVPGYY SWRSPGRGSW FVQALCSILE 250
EHGKDLEIMQ ILTRVNDRVA RHFESQSDDP HFHEKKQIPC VVSMLTKELY 300
FSQ 303
Length:303
Mass (Da):34,277
Last modified:October 1, 1996 - v1
Checksum:iCD373EE54A232CA4
GO
Isoform Beta (identifier: P55210-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     149-303: VIYGKDGVTP...MLTKELYFSQ → MESCSVTQAG...TWKSCRSSPG

Note: Lacks enzymatic activity.

Show »
Length:253
Mass (Da):28,030
Checksum:i514964EF3F6229E1
GO
Isoform Alpha' (identifier: P55210-3) [UniParc]FASTAAdd to Basket

Also known as: Beta

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MDCVGWPPGRKWHLEKNTSCGGSSGICASYVTQM

Note: What we call isoform Alpha' is also known as Beta (PubMed:9070923).

Show »
Length:336
Mass (Da):37,815
Checksum:i34EEFF8AF5C318A2
GO
Isoform 4 (identifier: P55210-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MADDQGCIEEQGVEDSANEDSVDAKPDRSSFVPSLF → MQRGLFSDGDT

Show »
Length:278
Mass (Da):31,614
Checksum:iFAF2707D22D9CDE3
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti4 – 41D → E.2 Publications
Corresponds to variant rs11593766 [ dbSNP | Ensembl ].
VAR_048617
Natural varianti255 – 2551D → E.
Corresponds to variant rs2227310 [ dbSNP | Ensembl ].
VAR_048618

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3636MADDQ…VPSLF → MQRGLFSDGDT in isoform 4. VSP_045325Add
BLAST
Alternative sequencei1 – 11M → MDCVGWPPGRKWHLEKNTSC GGSSGICASYVTQM in isoform Alpha'. VSP_000806
Alternative sequencei149 – 303155VIYGK…LYFSQ → MESCSVTQAGVQRRDLGRLQ PPPPRLAEGPSLMMASRPTR GPSMTQMLILDTRSQWKLTS SSPIPRFQAITRGGAQEEAP GLCKPSAPSWRSTEKTWKSC RSSPG in isoform Beta. VSP_000807Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti194 – 1941G → A in AAC50346. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U37448 mRNA. Translation: AAC50303.1.
U37449 mRNA. Translation: AAC50304.1.
U39613 mRNA. Translation: AAC50346.1.
U40281 mRNA. Translation: AAC50352.1.
U67319 mRNA. Translation: AAC51152.1.
U67320 mRNA. Translation: AAC51153.1.
U67206 mRNA. Translation: AAF21460.1.
BT006683 mRNA. Translation: AAP35329.1.
AB451281 mRNA. Translation: BAG70095.1.
AB451413 mRNA. Translation: BAG70227.1.
AK298964 mRNA. Translation: BAG61059.1.
AL592546, AL627395 Genomic DNA. Translation: CAI12638.1.
AL592546, AL627395 Genomic DNA. Translation: CAI12639.1.
AL627395, AL592546 Genomic DNA. Translation: CAI16004.1.
AL627395, AL592546 Genomic DNA. Translation: CAI16005.1.
CH471066 Genomic DNA. Translation: EAW49494.1.
CH471066 Genomic DNA. Translation: EAW49495.1.
CH471066 Genomic DNA. Translation: EAW49498.1.
CH471066 Genomic DNA. Translation: EAW49496.1.
CH471066 Genomic DNA. Translation: EAW49497.1.
BC015799 mRNA. Translation: AAH15799.1.
CCDSiCCDS58096.1. [P55210-4]
CCDS7580.1. [P55210-3]
CCDS7581.1. [P55210-1]
CCDS7582.1. [P55210-2]
RefSeqiNP_001218.1. NM_001227.4. [P55210-1]
NP_001253985.1. NM_001267056.1. [P55210-1]
NP_001253986.1. NM_001267057.1.
NP_001253987.1. NM_001267058.1. [P55210-4]
NP_203124.1. NM_033338.5. [P55210-3]
NP_203125.1. NM_033339.4. [P55210-1]
NP_203126.1. NM_033340.3. [P55210-2]
UniGeneiHs.9216.

Genome annotation databases

EnsembliENST00000345633; ENSP00000298701; ENSG00000165806. [P55210-1]
ENST00000369315; ENSP00000358321; ENSG00000165806. [P55210-1]
ENST00000369318; ENSP00000358324; ENSG00000165806. [P55210-1]
ENST00000369321; ENSP00000358327; ENSG00000165806. [P55210-3]
ENST00000369331; ENSP00000358337; ENSG00000165806. [P55210-2]
ENST00000452490; ENSP00000398107; ENSG00000165806. [P55210-4]
GeneIDi840.
KEGGihsa:840.
UCSCiuc001lam.4. human. [P55210-2]
uc001lan.4. human. [P55210-1]
uc001lao.4. human. [P55210-3]

Polymorphism databases

DMDMi1730092.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U37448 mRNA. Translation: AAC50303.1 .
U37449 mRNA. Translation: AAC50304.1 .
U39613 mRNA. Translation: AAC50346.1 .
U40281 mRNA. Translation: AAC50352.1 .
U67319 mRNA. Translation: AAC51152.1 .
U67320 mRNA. Translation: AAC51153.1 .
U67206 mRNA. Translation: AAF21460.1 .
BT006683 mRNA. Translation: AAP35329.1 .
AB451281 mRNA. Translation: BAG70095.1 .
AB451413 mRNA. Translation: BAG70227.1 .
AK298964 mRNA. Translation: BAG61059.1 .
AL592546 , AL627395 Genomic DNA. Translation: CAI12638.1 .
AL592546 , AL627395 Genomic DNA. Translation: CAI12639.1 .
AL627395 , AL592546 Genomic DNA. Translation: CAI16004.1 .
AL627395 , AL592546 Genomic DNA. Translation: CAI16005.1 .
CH471066 Genomic DNA. Translation: EAW49494.1 .
CH471066 Genomic DNA. Translation: EAW49495.1 .
CH471066 Genomic DNA. Translation: EAW49498.1 .
CH471066 Genomic DNA. Translation: EAW49496.1 .
CH471066 Genomic DNA. Translation: EAW49497.1 .
BC015799 mRNA. Translation: AAH15799.1 .
CCDSi CCDS58096.1. [P55210-4 ]
CCDS7580.1. [P55210-3 ]
CCDS7581.1. [P55210-1 ]
CCDS7582.1. [P55210-2 ]
RefSeqi NP_001218.1. NM_001227.4. [P55210-1 ]
NP_001253985.1. NM_001267056.1. [P55210-1 ]
NP_001253986.1. NM_001267057.1.
NP_001253987.1. NM_001267058.1. [P55210-4 ]
NP_203124.1. NM_033338.5. [P55210-3 ]
NP_203125.1. NM_033339.4. [P55210-1 ]
NP_203126.1. NM_033340.3. [P55210-2 ]
UniGenei Hs.9216.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1F1J X-ray 2.35 A/B 2-303 [» ]
1GQF X-ray 2.90 A/B 47-303 [» ]
1I4O X-ray 2.40 A/B 24-303 [» ]
1I51 X-ray 2.45 A/C 51-198 [» ]
B/D 199-303 [» ]
1K86 X-ray 2.60 A/B 51-303 [» ]
1K88 X-ray 2.70 A/B 51-303 [» ]
1KMC X-ray 2.90 A/B 1-303 [» ]
1MIA model - A 57-193 [» ]
B 211-303 [» ]
1SHJ X-ray 2.80 A/B 50-303 [» ]
1SHL X-ray 3.00 A/B 57-303 [» ]
2QL5 X-ray 2.34 A/C 24-196 [» ]
B/D 207-303 [» ]
2QL7 X-ray 2.40 A/C 24-196 [» ]
B/D 207-303 [» ]
2QL9 X-ray 2.14 A/C 24-196 [» ]
B/D 207-303 [» ]
2QLB X-ray 2.25 A/C 24-196 [» ]
B/D 207-303 [» ]
2QLF X-ray 2.80 A/C 24-196 [» ]
B/D 207-303 [» ]
2QLJ X-ray 2.60 A/C 24-196 [» ]
B/D 207-303 [» ]
3EDR X-ray 2.45 A/C 24-196 [» ]
B/D 207-303 [» ]
3H1P X-ray 2.61 A/B 50-303 [» ]
3IBC X-ray 2.75 A/C 24-196 [» ]
B/D 207-303 [» ]
3IBF X-ray 2.50 A/C 24-196 [» ]
B/D 207-303 [» ]
3R5K X-ray 2.86 A/B 1-303 [» ]
4FDL X-ray 2.80 A/B 2-303 [» ]
4FEA X-ray 3.79 A/B 57-303 [» ]
4HQ0 X-ray 3.00 A/B 47-303 [» ]
4HQR X-ray 3.00 A/B 47-303 [» ]
4JB8 X-ray 1.70 A 24-198 [» ]
B 207-303 [» ]
4JJ8 X-ray 2.94 A/B 57-303 [» ]
4JR1 X-ray 2.15 A/B 57-303 [» ]
4JR2 X-ray 1.65 A/B 57-303 [» ]
ProteinModelPortali P55210.
SMRi P55210. Positions 47-303.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107290. 46 interactions.
DIPi DIP-29973N.
IntActi P55210. 8 interactions.
MINTi MINT-147084.
STRINGi 9606.ENSP00000298700.

Chemistry

BindingDBi P55210.
ChEMBLi CHEMBL3468.
GuidetoPHARMACOLOGYi 1623.

Protein family/group databases

MEROPSi C14.004.

PTM databases

PhosphoSitei P55210.

Polymorphism databases

DMDMi 1730092.

Proteomic databases

MaxQBi P55210.
PaxDbi P55210.
PRIDEi P55210.

Protocols and materials databases

DNASUi 840.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000345633 ; ENSP00000298701 ; ENSG00000165806 . [P55210-1 ]
ENST00000369315 ; ENSP00000358321 ; ENSG00000165806 . [P55210-1 ]
ENST00000369318 ; ENSP00000358324 ; ENSG00000165806 . [P55210-1 ]
ENST00000369321 ; ENSP00000358327 ; ENSG00000165806 . [P55210-3 ]
ENST00000369331 ; ENSP00000358337 ; ENSG00000165806 . [P55210-2 ]
ENST00000452490 ; ENSP00000398107 ; ENSG00000165806 . [P55210-4 ]
GeneIDi 840.
KEGGi hsa:840.
UCSCi uc001lam.4. human. [P55210-2 ]
uc001lan.4. human. [P55210-1 ]
uc001lao.4. human. [P55210-3 ]

Organism-specific databases

CTDi 840.
GeneCardsi GC10P115428.
HGNCi HGNC:1508. CASP7.
HPAi CAB025563.
MIMi 601761. gene.
neXtProti NX_P55210.
PharmGKBi PA26091.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG279444.
HOVERGENi HBG050802.
InParanoidi P55210.
KOi K04397.
OMAi DANPRHK.
PhylomeDBi P55210.
TreeFami TF102023.

Enzyme and pathway databases

BRENDAi 3.4.22.60. 2681.
Reactomei REACT_107. Apoptotic cleavage of cellular proteins.
REACT_13541. Caspase-mediated cleavage of cytoskeletal proteins.
REACT_607. Activation of caspases through apoptosome-mediated cleavage.

Miscellaneous databases

EvolutionaryTracei P55210.
GeneWikii Caspase_7.
GenomeRNAii 840.
NextBioi 3500.
PMAP-CutDB P55210.
PROi P55210.
SOURCEi Search...

Gene expression databases

ArrayExpressi P55210.
Bgeei P55210.
CleanExi HS_CASP7.
Genevestigatori P55210.

Family and domain databases

Gene3Di 3.40.50.1460. 1 hit.
InterProi IPR029030. Caspase-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 PF00656. Peptidase_C14. 1 hit.
[Graphical view ]
PRINTSi PR00376. IL1BCENZYME.
SMARTi SM00115. CASc. 1 hit.
[Graphical view ]
PROSITEi 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. "Mch3, a novel human apoptotic cysteine protease highly related to CPP32."
    Fernandes-Alnemri T., Takahashi A., Armstrong R.C., Krebs J., Fritz L.C., Tomaselli K.J., Wang L., Yu Z., Croce C.M., Salveson G., Earnshaw W.C., Litwack G., Alnemri E.S.
    Cancer Res. 55:6045-6052(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
    Tissue: T-cell.
  2. "ICE-LAP3, a novel mammalian homologue of the Caenorhabditis elegans cell death protein Ced-3 is activated during Fas- and tumor necrosis factor-induced apoptosis."
    Duan H., Chinnaiyan A.M., Hudson P.L., Wing J.P., He W.-W., Dixit V.M.
    J. Biol. Chem. 271:1621-1625(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
  3. "Identification and characterization of CPP32/Mch2 homolog 1, a novel cysteine protease similar to CPP32."
    Lippke J.A., Gu Y., Sarnecki C., Caron P.R., Su M.S.-S.
    J. Biol. Chem. 271:1825-1828(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
    Tissue: Spleen.
  4. "Identification and mapping of Casp7, a cysteine protease resembling CPP32 beta, interleukin-1 beta converting enzyme, and CED-3."
    Juan T.S.-C., McNiece I.K., Argento J.M., Jenkins N.A., Gilbert D.J., Copeland N.G., Fletcher F.A.
    Genomics 40:86-93(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND ALPHA').
    Tissue: Fetal lung and Fetal spleen.
  5. "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] (ISOFORM ALPHA), VARIANT GLU-4.
  6. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
    Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
    , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
    Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA').
  7. "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 4).
  8. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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 ALPHA), VARIANT GLU-4.
    Tissue: Skin.
  11. "In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains."
    Fernandes-Alnemri T., Armstrong R.C., Krebs J.F., Srinivasula S.M., Wang L., Bullrich F., Fritz L.C., Trapani J.A., Tomaselli K.J., Litwack G., Alnemri E.S.
    Proc. Natl. Acad. Sci. U.S.A. 93:7464-7469(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING.
  12. "Dual role of BRUCE as an antiapoptotic IAP and a chimeric E2/E3 ubiquitin ligase."
    Bartke T., Pohl C., Pyrowolakis G., Jentsch S.
    Mol. Cell 14:801-811(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BIRC6/BRUCE.
  13. "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].
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Crystal structure of a procaspase-7 zymogen: mechanisms of activation and substrate binding."
    Chai J., Wu Q., Shiozaki E., Srinivasula S.M., Alnemri E.S., Shi Y.
    Cell 107:399-407(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 51-303, SUBUNIT.

Entry informationi

Entry nameiCASP7_HUMAN
AccessioniPrimary (citable) accession number: P55210
Secondary accession number(s): B4DQU7
, B5BU45, D3DRB8, Q13364, Q53YD5, Q5SVL0, Q5SVL3, Q96BA0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 3, 2014
This is version 156 of the entry and version 1 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 10
    Human chromosome 10: 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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