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P55210 (CASP7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 155. Feed History...

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

Names and origin

Protein namesRecommended name:
Caspase-7

Short name=CASP-7
EC=3.4.22.60
Alternative name(s):
Apoptotic protease Mch-3
CMH-1
ICE-like apoptotic protease 3
Short name=ICE-LAP3

Cleaved into the following 2 chains:

  1. Caspase-7 subunit p20
  2. Caspase-7 subunit p11
Gene names
Name:CASP7
Synonyms:MCH3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length303 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the activation cascade of caspases responsible for apoptosis execution. 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 activity

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

Enzyme regulation

Inhibited by isatin sulfonamides.

Subunit structure

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. Ref.12 Ref.16

Subcellular location

Cytoplasm.

Tissue specificity

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

Post-translational modification

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. Ref.11

Sequence similarities

Belongs to the peptidase C14A family.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionHydrolase
Protease
Thiol protease
   PTMAcetylation
Zymogen
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c

Traceable author statement. Source: Reactome

aging

Inferred from electronic annotation. Source: Ensembl

apoptotic process

Traceable author statement. Source: Reactome

cellular component disassembly involved in execution phase of apoptosis

Traceable author statement. Source: Reactome

execution phase of apoptosis

Inferred from Biological aspect of Ancestor. Source: RefGenome

heart development

Inferred from electronic annotation. Source: Ensembl

intrinsic apoptotic signaling pathway

Traceable author statement. Source: Reactome

positive regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

proteolysis

Inferred from direct assay PubMed 12888622. Source: UniProtKB

release of cytochrome c from mitochondria

Inferred from electronic annotation. Source: Ensembl

response to UV

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Traceable author statement Ref.2. Source: ProtInc

cytosol

Inferred from direct assay PubMed 17167422. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 17167422. Source: UniProtKB

   Molecular_functionaspartic-type endopeptidase activity

Inferred from electronic annotation. Source: Ensembl

cysteine-type endopeptidase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

cysteine-type endopeptidase activity involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

cysteine-type peptidase activity

Traceable author statement Ref.3. Source: ProtInc

protein binding

Inferred from physical interaction PubMed 12888622. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform Alpha (identifier: P55210-1)

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.
Isoform Beta (identifier: P55210-2)

The sequence of this isoform differs from the canonical sequence as follows:
     149-303: VIYGKDGVTP...MLTKELYFSQ → MESCSVTQAG...TWKSCRSSPG
Note: Lacks enzymatic activity.
Isoform Alpha' (identifier: P55210-3)

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).
Isoform 4 (identifier: P55210-4)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.13
Propeptide2 – 2322
PRO_0000004616
Chain24 – 198175Caspase-7 subunit p20
PRO_0000004617
Propeptide199 – 2068
PRO_0000004618
Chain207 – 30397Caspase-7 subunit p11
PRO_0000004619

Sites

Active site1441 By similarity
Active site1861

Amino acid modifications

Modified residue21N-acetylalanine Ref.13 Ref.15

Natural variations

Alternative sequence1 – 3636MADDQ…VPSLF → MQRGLFSDGDT in isoform 4.
VSP_045325
Alternative sequence11M → MDCVGWPPGRKWHLEKNTSC GGSSGICASYVTQM in isoform Alpha'.
VSP_000806
Alternative sequence149 – 303155VIYGK…LYFSQ → MESCSVTQAGVQRRDLGRLQ PPPPRLAEGPSLMMASRPTR GPSMTQMLILDTRSQWKLTS SSPIPRFQAITRGGAQEEAP GLCKPSAPSWRSTEKTWKSC RSSPG in isoform Beta.
VSP_000807
Natural variant41D → E. Ref.5 Ref.10
Corresponds to variant rs11593766 [ dbSNP | Ensembl ].
VAR_048617
Natural variant2551D → E.
Corresponds to variant rs2227310 [ dbSNP | Ensembl ].
VAR_048618

Experimental info

Mutagenesis1861C → A: No apoptotic activity.
Sequence conflict1941G → A in AAC50346. Ref.2

Secondary structure

...................................................... 303
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Alpha [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: CD373EE54A232CA4

FASTA30334,277
        10         20         30         40         50         60 
MADDQGCIEE QGVEDSANED SVDAKPDRSS FVPSLFSKKK KNVTMRSIKT TRDRVPTYQY 

        70         80         90        100        110        120 
NMNFEKLGKC IIINNKNFDK VTGMGVRNGT DKDAEALFKC FRSLGFDVIV YNDCSCAKMQ 

       130        140        150        160        170        180 
DLLKKASEED HTNAACFACI LLSHGEENVI YGKDGVTPIK DLTAHFRGDR CKTLLEKPKL 

       190        200        210        220        230        240 
FFIQACRGTE LDDGIQADSG PINDTDANPR YKIPVEADFL FAYSTVPGYY SWRSPGRGSW 

       250        260        270        280        290        300 
FVQALCSILE EHGKDLEIMQ ILTRVNDRVA RHFESQSDDP HFHEKKQIPC VVSMLTKELY 


FSQ 

« Hide

Isoform Beta [UniParc].

Checksum: 514964EF3F6229E1
Show »

FASTA25328,030
Isoform Alpha' (Beta) [UniParc].

Checksum: 34EEFF8AF5C318A2
Show »

FASTA33637,815
Isoform 4 [UniParc].

Checksum: FAF2707D22D9CDE3
Show »

FASTA27831,614

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS58096.1. [P55210-4]
CCDS7580.1. [P55210-3]
CCDS7581.1. [P55210-1]
CCDS7582.1. [P55210-2]
RefSeqNP_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]
UniGeneHs.9216.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP55210.
SMRP55210. Positions 47-303.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107290. 46 interactions.
DIPDIP-29973N.
IntActP55210. 8 interactions.
MINTMINT-147084.
STRING9606.ENSP00000298700.

Chemistry

BindingDBP55210.
ChEMBLCHEMBL3468.
GuidetoPHARMACOLOGY1623.

Protein family/group databases

MEROPSC14.004.

PTM databases

PhosphoSiteP55210.

Polymorphism databases

DMDM1730092.

Proteomic databases

MaxQBP55210.
PaxDbP55210.
PRIDEP55210.

Protocols and materials databases

DNASU840.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000345633; 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]
GeneID840.
KEGGhsa:840.
UCSCuc001lam.4. human. [P55210-2]
uc001lan.4. human. [P55210-1]
uc001lao.4. human. [P55210-3]

Organism-specific databases

CTD840.
GeneCardsGC10P115428.
HGNCHGNC:1508. CASP7.
HPACAB025563.
MIM601761. gene.
neXtProtNX_P55210.
PharmGKBPA26091.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG279444.
HOVERGENHBG050802.
InParanoidP55210.
KOK04397.
OMADANPRHK.
PhylomeDBP55210.
TreeFamTF102023.

Enzyme and pathway databases

BRENDA3.4.22.60. 2681.
ReactomeREACT_578. Apoptosis.

Gene expression databases

ArrayExpressP55210.
BgeeP55210.
CleanExHS_CASP7.
GenevestigatorP55210.

Family and domain databases

Gene3D3.40.50.1460. 1 hit.
InterProIPR029030. 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]
PfamPF00656. Peptidase_C14. 1 hit.
[Graphical view]
PRINTSPR00376. IL1BCENZYME.
SMARTSM00115. CASc. 1 hit.
[Graphical view]
PROSITEPS01122. CASPASE_CYS. 1 hit.
PS01121. CASPASE_HIS. 1 hit.
PS50207. CASPASE_P10. 1 hit.
PS50208. CASPASE_P20. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP55210.
GeneWikiCaspase_7.
GenomeRNAi840.
NextBio3500.
PMAP-CutDBP55210.
PROP55210.
SOURCESearch...

Entry information

Entry nameCASP7_HUMAN
AccessionPrimary (citable) accession number: P55210
Secondary accession number(s): B4DQU7 expand/collapse secondary AC list , B5BU45, D3DRB8, Q13364, Q53YD5, Q5SVL0, Q5SVL3, Q96BA0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 155 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM