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UniProtKB/Swiss-Prot entry P55211


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CASP9_HUMAN
Primary accession number P55211
Secondary accession numbers O95348 Q92852 Q9BQ62 Q9UEQ3 Q9UIJ8
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on February 22, 2003 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 101)
Name and origin of the protein
Protein name Caspase-9 [Precursor]
Synonyms CASP-9
EC 3.4.22.62
ICE-like apoptotic protease 6
ICE-LAP6
Apoptotic protease Mch-6
Apoptotic protease-activating factor 3
APAF-3
Contains Caspase-9 subunit p35
Caspase-9 subunit p10
Gene name
Name: CASP9
Synonyms: MCH6
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS VAL-28 AND ARG-221.
DOI=10.1074/jbc.271.28.16720; PubMed=8663294 [NCBI, ExPASy, EBI, Israel, Japan]
Duan H., Orth K., Chinnaiyan A.M., Poirier G.G., Froelich C.J., He W.-W., Dixit V.M.;
"ICE-LAP6, a novel member of the ICE/Ced-3 gene family, is activated by the cytotoxic T cell protease granzyme B.";
J. Biol. Chem. 271:16720-16724(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEOLYTIC PROCESSING.
TISSUE=T-cell;
DOI=10.1074/jbc.271.43.27099; PubMed=8900201 [NCBI, ExPASy, EBI, Israel, Japan]
Srinivasula S.M., Fernandes-Alnemri T., Zangrilli J., Robertson N., Armstrong R.C., Wang L., Trapani J.A., Tomaselli K.J., Litwack G., Alnemri E.S.;
"The Ced-3/interleukin 1beta converting enzyme-like homolog Mch6 and the lamin-cleaving enzyme Mch2alpha are substrates for the apoptotic mediator CPP32.";
J. Biol. Chem. 271:27099-27106(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1007/s003359901086; PubMed=10384055 [NCBI, ExPASy, EBI, Israel, Japan]
Hadano S., Nasir J., Nichol K., Rasper D.M., Vaillancourt J.P., Sherer S.W., Beatty B.G., Ikeda J.E., Nicholson D.W., Hayden M.R.;
"Genomic organization of the human caspase-9 gene on chromosome 1p36.1-p36.3.";
Mamm. Genome 10:757-760(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=10070954 [NCBI, ExPASy, EBI, Israel, Japan]
Srinivasula S.M., Ahmad M., Guo Y., Zhan Y., Lazebnik Y., Fernandes-Alnemri T., Alnemri E.S.;
"Identification of an endogenous dominant-negative short isoform of caspase-9 that can regulate apoptosis.";
Cancer Res. 59:999-1002(1999).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Stomach cancer;
Izawa M., Mori T., Ito H., Sairenji T.;
"Molecular cloning and sequencing of a cDNA predicting an alternative form of pro-caspase-9 from human castric cancer cell lines.";
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Miho Y., Momoi T., Fujita E.;
"A novel splicing product of human caspase-9 lacking protease activity.";
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT VAL-28.
DOI=10.1074/jbc.274.4.2072; PubMed=9890966 [NCBI, ExPASy, EBI, Israel, Japan]
Seol D.W., Billiar T.R.;
"A caspase-9 variant missing the catalytic site is an endogenous inhibitor of apoptosis.";
J. Biol. Chem. 274:2072-2076(1999).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-28; LEU-99; ILE-102; VAL-106; ASP-114; HIS-173 AND ARG-221.
Rieder M.J., Livingston R.J., Daniels M.R., Montoya M.A., Chung M.-W., Miyamoto K.E., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D., Schackwitz W.S., Sherwood J.K., Witrak L.A., Nickerson D.A.;
"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Eye, and Lymph;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 140-416, AND SUBUNIT.
DOI=10.1073/pnas.231465798; PubMed=11734640 [NCBI, ExPASy, EBI, Israel, Japan]
Renatus M., Stennicke H.R., Scott F.L., Liddington R.C., Salvesen G.S.;
"Dimer formation drives the activation of the cell death protease caspase 9.";
Proc. Natl. Acad. Sci. U.S.A. 98:14250-14255(2001).
[12]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 140-416 IN COMPLEX WITH BIRC4/XIAP.
DOI=10.1016/S1097-2765(03)00054-6; PubMed=12620238 [NCBI, ExPASy, EBI, Israel, Japan]
Shiozaki E.N., Chai J., Rigotti D.J., Riedl S.J., Li P., Srinivasula S.M., Alnemri E.S., Fairman R., Shi Y.;
"Mechanism of XIAP-mediated inhibition of caspase-9.";
Mol. Cell 11:519-527(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U56390; AAC50640.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U60521; AAC50776.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB019205; BAA82697.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF093130; AAD12248.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB015653; BAA78780.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB020979; BAA87905.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF110376; AAD13615.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY214168; AAO21133.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL512883; CAC42423.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002452; AAH02452.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC006463; AAH06463.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR G02635; G02635.
RefSeq NP_001220.2; -.
NP_127463.1; -.
UniGene Hs.329502
3D structure databases
PDB
1JXQ; X-ray; 2.80 A; A/B/C/D=140-416.[ExPASy / RCSB / EBI]
1NW9; X-ray; 2.40 A; B=140-416.[ExPASy / RCSB / EBI]
2AR9; X-ray; 2.80 A; A/B/C/D=140-416.[ExPASy / RCSB / EBI]
3YGS; X-ray; 2.50 A; P=1-95.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1JXQ; -.
1NW9; -.
2AR9; -.
3YGS; -.
ModBase P55211.
Protein-protein interaction databases
DIP DIP:27625N; -.
IntAct P55211; -.
Protein family/group databases
MEROPS C14.010; -.
PTM databases
PhosphoSite P55211; -.
Enzyme and pathway databases
Reactome REACT_578; Apoptosis.
Polymorphism databases
NIEHS-SNPs CASP9.
Organism-specific databases
H-InvDB HIX0000153; -.
HGNC HGNC:1511; CASP9.
GenAtlas CASP9.
HPA CAB004348; -.
HPA001473; -.
MIM 602234; gene. [NCBI / EBI]
PharmGKB PA26094; -.
GeneCards P55211.
Gene expression databases
ArrayExpress P55211; -.
CleanEx HS_CASP9; -.
GermOnline ENSG00000132906; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0030693; Molecular function: caspase activity (traceable author statement from ProtInc).
GO:0008047; Molecular function: enzyme activator activity (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0008635; Biological process: caspase activation via cytochrome c (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR001315; CARD.
IPR017350; Caspase_IL-1_beta.
IPR011029; DEATH_like.
IPR011600; Pept_C14_cat.
IPR001309; Pept_C14_ICE_p20.
IPR016129; Pept_C14_ICE_p20_AS.
IPR002138; Pept_C14_p10.
IPR002398; Pept_C14_p45.
IPR015917; Pept_C14_p45_core.
Graphical view of domain structure.
Gene3D G3DSA:1.10.533.10; DEATH_like; 1.
PANTHER PTHR10454; Pept_C14_p45; 1.
Pfam PF00619; CARD; 1.
PF00656; Peptidase_C14; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF038001; Caspase_ICE; 1.
PRINTS PR00376; IL1BCENZYME.
SMART SM00114; CARD; 1.
SM00115; CASc; 1.
SMART graphical view of domain structure.
PROSITE PS50209; CARD; 1.
PS01122; CASPASE_CYS; 1.
PS01121; CASPASE_HIS; 1.
PS50207; CASPASE_P10; 1.
PS50208; CASPASE_P20; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P55211.
Genome annotation databases
Ensembl ENSG00000132906; Homo sapiens. [Contig view]
GeneID 842; -.
KEGG hsa:842; -.
Phylogenomic databases
HOVERGEN P55211; -.
Other
LinkHub P55211; -.
SOURCE CASP9; Homo sapiens.
ProtoNet P55211.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Apoptosis; Hydrolase; Polymorphism; Protease; Thiol protease; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
PROPEP   1     ?        Potential. PRO_0000004640
CHAIN   ?   315        Caspase-9 subunit p35. PRO_0000004641
PROPEP   316   330  15      PRO_0000004642
CHAIN   331   416  86     Caspase-9 subunit p10. PRO_0000004643
DOMAIN   1    92  92     CARD. 
ACT_SITE   237   237        By similarity. 
ACT_SITE   287   287        By similarity. 
VAR_SEQ   140   289        Missing (in isoform 2). VSP_000818
VARIANT   28    28  1     A -> V (in dbSNP:rs1052571 [NCBI]). VAR_015415 [3D]
VARIANT   99    99  1     S -> L (in dbSNP:rs4646008 [NCBI]). VAR_015416 
VARIANT   102   102  1     T -> I (in dbSNP:rs2308941 [NCBI]). VAR_015417 
VARIANT   106   106  1     L -> V (in dbSNP:rs2308938 [NCBI]). VAR_015418 
VARIANT   114   114  1     E -> D (in dbSNP:rs2020897 [NCBI]). VAR_015419 
VARIANT   173   173  1     R -> H (in dbSNP:rs2308950 [NCBI]). VAR_015420 [3D]
VARIANT   176   176  1     G -> R (in dbSNP:rs2308949 [NCBI]). VAR_016131 [3D]
VARIANT   185   185  1     I -> M (in dbSNP:rs9282624 [NCBI]). VAR_022053 [3D]
VARIANT   192   192  1     R -> C (in dbSNP:rs2308939 [NCBI]). VAR_016132 [3D]
VARIANT   221   221  1     Q -> R (in dbSNP:rs1052576 [NCBI]). VAR_015421 [3D]
CONFLICT   32    32        R -> S (in Ref. 2, 3 and 6). 
CONFLICT   96    96        A -> G (in Ref. 1; AAC50640). 
CONFLICT   197   197        L -> P (in Ref. 2 and 3). 
HELIX   3    11  9      
HELIX   13    19  7      
TURN   23    25  3      
HELIX   26    31  6      
HELIX   37    44  8      
HELIX   51    62  12      
HELIX   69    78  10      
TURN   79    81  3      
HELIX   83    94  12      
HELIX   143   147  5      
TURN   149   151  3      
STRAND   161   167  7      
HELIX   173   175  3      
HELIX   183   196  14      
STRAND   199   206  8      
HELIX   209   221  13      
STRAND   228   239  12      
STRAND   244   246  3      
STRAND   249   251  3      
STRAND   257   259  3      
HELIX   260   265  6      
TURN   269   271  3      
HELIX   273   275  3      
STRAND   280   287  8      
STRAND   340   346  7      
STRAND   351   353  3      
HELIX   362   374  13      
TURN   375   377  3      
HELIX   380   392  13      
STRAND   408   410  3      
Sequence information
Length: 416 AA [This is the length of the unprocessed precursor] Molecular weight: 46281 Da [This is the MW of the unprocessed precursor] CRC64: 78E0180DF2A3BDD2 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MDEADRRLLR RCRLRLVEEL QVDQLWDALL SRELFRPHMI EDIQRAGSGS RRDQARQLII 

        70         80         90        100        110        120 
DLETRGSQAL PLFISCLEDT GQDMLASFLR TNRQAAKLSK PTLENLTPVV LRPEIRKPEV 

       130        140        150        160        170        180 
LRPETPRPVD IGSGGFGDVG ALESLRGNAD LAYILSMEPC GHCLIINNVN FCRESGLRTR 

       190        200        210        220        230        240 
TGSNIDCEKL RRRFSSLHFM VEVKGDLTAK KMVLALLELA QQDHGALDCC VVVILSHGCQ 

       250        260        270        280        290        300 
ASHLQFPGAV YGTDGCPVSV EKIVNIFNGT SCPSLGGKPK LFFIQACGGE QKDHGFEVAS 

       310        320        330        340        350        360 
TSPEDESPGS NPEPDATPFQ EGLRTFDQLD AISSLPTPSD IFVSYSTFPG FVSWRDPKSG 

       370        380        390        400        410 
SWYVETLDDI FEQWAHSEDL QSLLLRVANA VSVKGIYKQM PGCFNFLRKK LFFKTS 

P55211 in FASTA format

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