Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P55211 (CASP9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 161. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Caspase-9

Short name=CASP-9
EC=3.4.22.62
Alternative name(s):
Apoptotic protease Mch-6
Apoptotic protease-activating factor 3
Short name=APAF-3
ICE-like apoptotic protease 6
Short name=ICE-LAP6

Cleaved into the following 2 chains:

  1. Caspase-9 subunit p35
  2. Caspase-9 subunit p10
Gene names
Name:CASP9
Synonyms:MCH6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length416 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. Binding of caspase-9 to Apaf-1 leads to activation of the protease which then cleaves and activates caspase-3. Promotes DNA damage-induced apoptosis in a ABL1/c-Abl-dependent manner. Proteolytically cleaves poly(ADP-ribose) polymerase (PARP). Ref.17 Ref.24

Isoform 2 lacks activity is an dominant-negative inhibitor of caspase-9. Ref.17 Ref.24

Catalytic activity

Strict requirement for an Asp residue at position P1 and with a marked preference for His at position P2. It has a preferred cleavage sequence of Leu-Gly-His-Asp-|-Xaa. Ref.24

Enzyme regulation

Inhibited by the effector protein NleF that is produced by pathogenic E.coli; this inhibits apoptosis. Ref.24

Subunit structure

Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 35 kDa (p35) and a 10 kDa (p10) subunit. Caspase-9 and APAF1 bind to each other via their respective NH2-terminal CED-3 homologous domains in the presence of cytochrome C and ATP. Interacts (inactive form) with EFHD2. Interacts with HAX1. Interacts with BIRC2/c-IAP1, XIAP/BIRC4, BIRC5/survivin, BIRC6/bruce and BIRC7/livin. Interacts with ABL1 (via SH3 domain); the interaction is direct and increases in the response of cells to genotoxic stress and ABL1/c-Abl activation. Interacts with NleF from pathogenic E.coli. Ref.16 Ref.17 Ref.18 Ref.20 Ref.22 Ref.24

Tissue specificity

Ubiquitous, with highest expression in the heart, moderate expression in liver, skeletal muscle, and pancreas. Low levels in all other tissues. Within the heart, specifically expressed in myocytes. Ref.18

Developmental stage

Expressed at low levels in fetal heart, at moderate levels in neonate heart, and at high levels in adult heart. Ref.18

Post-translational modification

Cleavages at Asp-315 by granzyme B and at Asp-330 by caspase-3 generate the two active subunits. Caspase-8 and -10 can also be involved in these processing events.

Phosphorylated at Thr-125 by MAPK1/ERK2. Phosphorylation at Thr-125 is sufficient to block caspase-9 processing and subsequent caspase-3 activation. Phosphorylation on Tyr-153 by ABL1/c-Abl; occurs in the response of cells to DNA damage. Ref.15 Ref.17

Sequence similarities

Belongs to the peptidase C14A family.

Contains 1 CARD domain.

Ontologies

Keywords
   Biological processApoptosis
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionHydrolase
Protease
Thiol protease
   PTMPhosphoprotein
Zymogen
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

activation 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 Ref.1. Source: UniProtKB

cellular response to DNA damage stimulus

Inferred from direct assay Ref.17. Source: UniProtKB

cellular response to UV

Inferred from direct assay Ref.17. Source: UniProtKB

cellular response to dexamethasone stimulus

Inferred from electronic annotation. Source: Ensembl

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

glial cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

intrinsic apoptotic signaling pathway

Traceable author statement. Source: Reactome

intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from mutant phenotype Ref.17. Source: UniProtKB

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

phosphatidylinositol-mediated signaling

Traceable author statement. Source: Reactome

platelet formation

Traceable author statement PubMed 18309324. Source: UniProtKB

positive regulation of apoptotic process

Traceable author statement. Source: Reactome

positive regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of apoptotic process

Traceable author statement. Source: Reactome

regulation of response to DNA damage stimulus

Inferred from mutant phenotype Ref.17. Source: UniProtKB

response to antibiotic

Inferred from electronic annotation. Source: Ensembl

response to cobalt ion

Inferred from electronic annotation. Source: Ensembl

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

signal transduction in response to DNA damage

Inferred from direct assay Ref.17. Source: UniProtKB

   Cellular_componentapoptosome

Inferred from direct assay PubMed 21827945. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 17167422. Source: UniProtKB

mitochondrion

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionSH3 domain binding

Inferred from direct assay Ref.17. Source: UniProtKB

cysteine-type endopeptidase activity

Traceable author statement. Source: ProtInc

enzyme activator activity

Traceable author statement PubMed 9390557. Source: ProtInc

peptidase activity

Inferred from direct assay PubMed 20663920. Source: MGI

protein kinase binding

Inferred from direct assay Ref.17. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P55211-1)

Also known as: 9L; Alpha;

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 2 (identifier: P55211-2)

Also known as: 9S; Beta;

The sequence of this isoform differs from the canonical sequence as follows:
     140-289: Missing.
Isoform 3 (identifier: P55211-3)

Also known as: Gamma;

The sequence of this isoform differs from the canonical sequence as follows:
     152-154: AYI → TVL
     155-416: Missing.
Note: May function as an endogenous apoptotic inhibitor, inhibits the BAX-mediated cleavage of procaspase-3.
Isoform 4 (identifier: P55211-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-83: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – ? PotentialPRO_0000004640
Chain? – 315Caspase-9 subunit p35PRO_0000004641
Propeptide316 – 33015
PRO_0000004642
Chain331 – 41686Caspase-9 subunit p10
PRO_0000004643

Regions

Domain1 – 9292CARD

Sites

Active site2371 By similarity
Active site2871 By similarity

Amino acid modifications

Modified residue1251Phosphothreonine; by MAPK1 Ref.15 Ref.19
Modified residue1531Phosphotyrosine; by ABL1 Ref.17
Modified residue3021Phosphoserine Ref.19
Modified residue3071Phosphoserine Ref.19 Ref.21

Natural variations

Alternative sequence1 – 8383Missing in isoform 4.
VSP_044256
Alternative sequence140 – 289150Missing in isoform 2.
VSP_000818
Alternative sequence152 – 1543AYI → TVL in isoform 3.
VSP_043910
Alternative sequence155 – 416262Missing in isoform 3.
VSP_043911
Natural variant281A → V. Ref.1 Ref.7 Ref.8 Ref.9
Corresponds to variant rs1052571 [ dbSNP | Ensembl ].
VAR_015415
Natural variant991S → L. Ref.9
Corresponds to variant rs4646008 [ dbSNP | Ensembl ].
VAR_015416
Natural variant1021T → I. Ref.9
Corresponds to variant rs2308941 [ dbSNP | Ensembl ].
VAR_015417
Natural variant1061L → V. Ref.9
Corresponds to variant rs2308938 [ dbSNP | Ensembl ].
VAR_015418
Natural variant1141E → D. Ref.9
Corresponds to variant rs2020897 [ dbSNP | Ensembl ].
VAR_015419
Natural variant1361F → L.
Corresponds to variant rs1820204 [ dbSNP | Ensembl ].
VAR_059198
Natural variant1731R → H. Ref.9
Corresponds to variant rs2308950 [ dbSNP | Ensembl ].
VAR_015420
Natural variant1761G → R.
Corresponds to variant rs2308949 [ dbSNP | Ensembl ].
VAR_016131
Natural variant1851I → M.
Corresponds to variant rs9282624 [ dbSNP | Ensembl ].
VAR_022053
Natural variant1921R → C.
Corresponds to variant rs2308939 [ dbSNP | Ensembl ].
VAR_016132
Natural variant2211Q → R. Ref.1 Ref.9
Corresponds to variant rs1052576 [ dbSNP | Ensembl ].
VAR_015421

Experimental info

Mutagenesis1531Y → F: Inhibits tyrosine phosphorylation. Reduces caspase-9 subunit p35 formation in response to genotoxic stress. Attenuates ABL1/c-Abl-mediated caspase-3 activation, DNA fragmentation and UV irradiation-induced apoptosis. Ref.17
Sequence conflict321R → S in AAC50776. Ref.2
Sequence conflict321R → S in BAA82697. Ref.3
Sequence conflict321R → S in BAA87905. Ref.6
Sequence conflict961A → G in AAC50640. Ref.1
Sequence conflict1971L → P in AAC50776. Ref.2
Sequence conflict1971L → P in BAA82697. Ref.3

Secondary structure

..................................................................... 416
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (9L) (Alpha) [UniParc].

Last modified February 22, 2003. Version 3.
Checksum: 78E0180DF2A3BDD2

FASTA41646,281
        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 

« Hide

Isoform 2 (9S) (Beta) [UniParc].

Checksum: A12848BEBDC35A64
Show »

FASTA26630,184
Isoform 3 (Gamma) [UniParc].

Checksum: B23A46C92AC6AA11
Show »

FASTA15417,397
Isoform 4 [UniParc].

Checksum: 2B62F8CFD1FF3145
Show »

FASTA33336,564

References

« Hide 'large scale' references
[1]"ICE-LAP6, a novel member of the ICE/Ced-3 gene family, is activated by the cytotoxic T cell protease granzyme B."
Duan H., Orth K., Chinnaiyan A.M., Poirier G.G., Froelich C.J., He W.-W., Dixit V.M.
J. Biol. Chem. 271:16720-16724(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS VAL-28 AND ARG-221.
[2]"The Ced-3/interleukin 1beta converting enzyme-like homolog Mch6 and the lamin-cleaving enzyme Mch2alpha are substrates for the apoptotic mediator CPP32."
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.
J. Biol. Chem. 271:27099-27106(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEOLYTIC PROCESSING.
Tissue: T-cell.
[3]"Genomic organization of the human caspase-9 gene on chromosome 1p36.1-p36.3."
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.
Mamm. Genome 10:757-760(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Identification of an endogenous dominant-negative short isoform of caspase-9 that can regulate apoptosis."
Srinivasula S.M., Ahmad M., Guo Y., Zhan Y., Lazebnik Y., Fernandes-Alnemri T., Alnemri E.S.
Cancer Res. 59:999-1002(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[5]"Molecular cloning and sequencing of a cDNA predicting an alternative form of pro-caspase-9 from human gastric cancer cell lines."
Izawa M., Mori T., Ito H., Sairenji T.
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Stomach cancer.
[6]"A novel splicing product of human caspase-9 lacking protease activity."
Miho Y., Momoi T., Fujita E.
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[7]"A caspase-9 variant missing the catalytic site is an endogenous inhibitor of apoptosis."
Seol D.W., Billiar T.R.
J. Biol. Chem. 274:2072-2076(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT VAL-28.
[8]"Cloning of a novel human caspase-9 splice variant containing only the CARD domain."
Wang P., Shi T., Ma D.
Life Sci. 79:934-940(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), VARIANT VAL-28.
[9]NIEHS SNPs program
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-28; LEU-99; ILE-102; VAL-106; ASP-114; HIS-173 AND ARG-221.
[10]"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 1).
[11]"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).
Tissue: Kidney.
[12]"The DNA sequence and biological annotation of human chromosome 1."
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. expand/collapse author list , 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.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[13]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[14]"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).
Tissue: Eye and Lymph.
[15]"Inhibition of caspase-9 through phosphorylation at Thr 125 by ERK MAPK."
Allan L.A., Morrice N., Brady S., Magee G., Pathak S., Clarke P.R.
Nat. Cell Biol. 5:647-654(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-125.
[16]"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.
[17]"c-Abl tyrosine kinase regulates caspase-9 autocleavage in the apoptotic response to DNA damage."
Raina D., Pandey P., Ahmad R., Bharti A., Ren J., Kharbanda S., Weichselbaum R., Kufe D.
J. Biol. Chem. 280:11147-11151(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN APOPTOSIS, INTERACTION WITH ABL1, PROTEOLYTIC PROCESSING, PHOSPHORYLATION AT TYR-153 BY ABL1, MUTAGENESIS OF TYR-153.
[18]"Overexpression of HAX-1 protects cardiac myocytes from apoptosis through caspase-9 inhibition."
Han Y., Chen Y.S., Liu Z., Bodyak N., Rigor D., Bisping E., Pu W.T., Kang P.M.
Circ. Res. 99:415-423(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HAX1, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[19]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-125; SER-302 AND SER-307, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"Comparative proteomics analysis of caspase-9-protein complexes in untreated and cytochrome c/dATP stimulated lysates of NSCLC cells."
Checinska A., Giaccone G., Rodriguez J.A., Kruyt F.A.E., Jimenez C.R.
J. Proteomics 72:575-585(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EFHD2.
[21]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"Dimer formation drives the activation of the cell death protease caspase 9."
Renatus M., Stennicke H.R., Scott F.L., Liddington R.C., Salvesen G.S.
Proc. Natl. Acad. Sci. U.S.A. 98:14250-14255(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 140-416, SUBUNIT.
[23]"Mechanism of XIAP-mediated inhibition of caspase-9."
Shiozaki E.N., Chai J., Rigotti D.J., Riedl S.J., Li P., Srinivasula S.M., Alnemri E.S., Fairman R., Shi Y.
Mol. Cell 11:519-527(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 140-416 IN COMPLEX WITH BIRC4/XIAP.
[24]"The E.coli effector protein NleF is a caspase inhibitor."
Blasche S., Moertl M., Steuber H., Siszler G., Nisa S., Schwarz F., Lavrik I., Gronewold T.M.A., Maskos K., Donnenberg M.S., Ullmann D., Uetz P., Koegl M.
PLoS ONE 0:0-0(2013)
Cited for: X-RAY CRYSTALLOGRAPHY (3.49 ANGSTROMS) OF 140-416 IN COMPLEX WITH E.COLI NLEF, INTERACTION WITH E.COLI NLEF, SUBUNIT, CATALYTIC ACTIVITY, FUNCTION, ENZYME REGULATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U56390 mRNA. Translation: AAC50640.1.
U60521 mRNA. Translation: AAC50776.1.
AB019205 Genomic DNA. Translation: BAA82697.1.
AF093130 mRNA. Translation: AAD12248.1.
AB015653 mRNA. Translation: BAA78780.1.
AB020979 mRNA. Translation: BAA87905.1.
AF110376 mRNA. Translation: AAD13615.1.
AY732490 mRNA. Translation: AAV33129.1.
AY214168 Genomic DNA. Translation: AAO21133.1.
BT006911 mRNA. Translation: AAP35557.1.
AK303743 mRNA. Translation: BAG64715.1.
AL512883 Genomic DNA. Translation: CAC42423.1.
AL512883 Genomic DNA. Translation: CAI12973.1.
CH471167 Genomic DNA. Translation: EAW51730.1.
CH471167 Genomic DNA. Translation: EAW51731.1.
BC002452 mRNA. Translation: AAH02452.1.
BC006463 mRNA. Translation: AAH06463.1.
PIRG02635.
RefSeqNP_001220.2. NM_001229.4.
NP_001264983.1. NM_001278054.1.
NP_127463.2. NM_032996.3.
XP_005246071.1. XM_005246014.1.
UniGeneHs.329502.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JXQX-ray2.80A/B/C/D140-416[»]
1NW9X-ray2.40B140-416[»]
2AR9X-ray2.80A/B/C/D140-416[»]
3D9TX-ray1.50C/D316-321[»]
3V3KX-ray3.49A/C/E/G/I/K/M/O141-416[»]
3YGSX-ray2.50P1-95[»]
ProteinModelPortalP55211.
SMRP55211. Positions 1-96, 141-416.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107292. 29 interactions.
DIPDIP-27625N.
IntActP55211. 9 interactions.
MINTMINT-89165.
STRING9606.ENSP00000330237.

Chemistry

BindingDBP55211.
ChEMBLCHEMBL2273.
GuidetoPHARMACOLOGY1625.

Protein family/group databases

MEROPSC14.010.

PTM databases

PhosphoSiteP55211.

Polymorphism databases

DMDM28558771.

Proteomic databases

PaxDbP55211.
PRIDEP55211.

Protocols and materials databases

DNASU842.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000333868; ENSP00000330237; ENSG00000132906. [P55211-1]
ENST00000348549; ENSP00000255256; ENSG00000132906. [P55211-2]
ENST00000375890; ENSP00000365051; ENSG00000132906. [P55211-4]
GeneID842.
KEGGhsa:842.
UCSCuc001awn.4. human. [P55211-1]
uc001awo.4. human. [P55211-2]

Organism-specific databases

CTD842.
GeneCardsGC01M015814.
HGNCHGNC:1511. CASP9.
HPACAB004348.
HPA001473.
MIM602234. gene.
neXtProtNX_P55211.
PharmGKBPA26094.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG319022.
HOVERGENHBG059022.
KOK04399.
PhylomeDBP55211.
TreeFamTF102023.

Enzyme and pathway databases

BRENDA3.4.22.62. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_578. Apoptosis.
REACT_6900. Immune System.
SABIO-RKP55211.

Gene expression databases

ArrayExpressP55211.
BgeeP55211.
CleanExHS_CASP9.
GenevestigatorP55211.

Family and domain databases

Gene3D1.10.533.10. 1 hit.
InterProIPR001315. CARD.
IPR017350. Caspase_IL-1_beta.
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]
PfamPF00619. CARD. 1 hit.
PF00656. Peptidase_C14. 1 hit.
[Graphical view]
PIRSFPIRSF038001. Caspase_ICE. 1 hit.
PRINTSPR00376. IL1BCENZYME.
SMARTSM00114. CARD. 1 hit.
SM00115. CASc. 1 hit.
[Graphical view]
SUPFAMSSF47986. SSF47986. 1 hit.
PROSITEPS50209. 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]
ProtoNetSearch...

Other

EvolutionaryTraceP55211.
GeneWikiCaspase-9.
GenomeRNAi842.
NextBio3524.
PMAP-CutDBP55211.
PROP55211.
SOURCESearch...

Entry information

Entry nameCASP9_HUMAN
AccessionPrimary (citable) accession number: P55211
Secondary accession number(s): B4E1A3 expand/collapse secondary AC list , O95348, Q53Y70, Q5JRU9, Q5UGI1, Q92852, Q9BQ62, Q9UEQ3, Q9UIJ8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: February 22, 2003
Last modified: April 16, 2014
This is version 161 of the entry and version 3 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 1

Human chromosome 1: entries, gene names and cross-references to MIM