Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Caspase

Gene

Casp9

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei275 – 2751UniRule annotation
Active sitei325 – 3251UniRule annotation

GO - Molecular functioni

GO - Biological processi

  • activation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
  • aging Source: RGD
  • apoptotic process Source: RGD
  • cellular response to dexamethasone stimulus Source: Ensembl
  • cellular response to organic cyclic compound Source: RGD
  • cellular response to UV Source: Ensembl
  • glial cell apoptotic process Source: RGD
  • intrinsic apoptotic signaling pathway in response to DNA damage Source: Ensembl
  • positive regulation of apoptotic process Source: RGD
  • positive regulation of neuron apoptotic process Source: Ensembl
  • proteolysis Source: RGD
  • regulation of response to DNA damage stimulus Source: Ensembl
  • response to antibiotic Source: RGD
  • response to cobalt ion Source: RGD
  • response to estradiol Source: RGD
  • response to lipopolysaccharide Source: RGD
  • response to organic cyclic compound Source: RGD
  • signal transduction in response to DNA damage Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol proteaseUniRule annotationSAAS annotation

Enzyme and pathway databases

ReactomeiR-RNO-111458. Formation of apoptosome.
R-RNO-111459. Activation of caspases through apoptosome-mediated cleavage.
R-RNO-198323. AKT phosphorylates targets in the cytosol.
R-RNO-418889. Ligand-independent caspase activation via DCC.

Protein family/group databases

MEROPSiC14.010.

Names & Taxonomyi

Protein namesi
Recommended name:
CaspaseUniRule annotation
Gene namesi
Name:Casp9Imported
Synonyms:RNCASP9Imported
ORF Names:rCG_30964Imported
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi61867. Casp9.

Subcellular locationi

GO - Cellular componenti

  • apoptosome Source: Ensembl
  • cytoplasm Source: RGD
  • cytosol Source: RGD
  • mitochondrion Source: RGD
  • nucleus Source: RGD
Complete GO annotation...

PTM / Processingi

Keywords - PTMi

ZymogenUniRule annotation

PTM databases

iPTMnetiQ9JHK1.

Expressioni

Gene expression databases

ExpressionAtlasiQ9JHK1. baseline.

Interactioni

Protein-protein interaction databases

IntActiQ9JHK1. 2 interactions.
MINTiMINT-3369959.
STRINGi10116.ENSRNOP00000017972.

Structurei

3D structure databases

SMRiQ9JHK1. Positions 1-96, 186-454.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9292CARDInterPro annotationAdd
BLAST
Domaini197 – 329133CASPASE_P20InterPro annotationAdd
BLAST
Domaini369 – 45385CASPASE_P10InterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C14A family.UniRule annotationSAAS annotation

Phylogenomic databases

eggNOGiKOG3573. Eukaryota.
ENOG410ZQIE. LUCA.
GeneTreeiENSGT00760000118912.
HOGENOMiHOG000231878.
HOVERGENiHBG059022.
KOiK04399.
OMAiVFEQWAH.
OrthoDBiEOG7TTQ7K.
PhylomeDBiQ9JHK1.
TreeFamiTF102023.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
3.40.50.1460. 1 hit.
InterProiIPR001315. CARD.
IPR033171. Caspase-9.
IPR029030. Caspase-like_dom.
IPR033139. Caspase_cys_AS.
IPR016129. Caspase_his_AS.
IPR011029. DEATH-like_dom.
IPR002138. Pept_C14_p10.
IPR001309. Pept_C14_p20.
IPR015917. Pept_C14A.
IPR017350. Pept_C14A_CASP1-typ.
[Graphical view]
PANTHERiPTHR10454:SF157. PTHR10454:SF157. 1 hit.
PfamiPF00619. CARD. 1 hit.
[Graphical view]
PIRSFiPIRSF038001. Caspase_ICE. 1 hit.
PRINTSiPR00376. IL1BCENZYME.
SMARTiSM00114. CARD. 1 hit.
SM00115. CASc. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
SSF52129. SSF52129. 1 hit.
PROSITEiPS50209. CARD. 1 hit.
PS01122. CASPASE_CYS. 1 hit.
PS01121. CASPASE_HIS. 1 hit.
PS50207. CASPASE_P10. 1 hit.
PS50208. CASPASE_P20. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9JHK1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEEADRQLLR RCRVRLVREL QVAELWDALL SRELFTRDMI EDIQRAGSGS
60 70 80 90 100
RRDQARQLVI DLETRGRQAL PRFISCLEDT GQGSLASFLQ SSGQAAKQDP
110 120 130 140 150
EAVTPLDHLV PVVLGPMGLK SKEQKVVKLD PSQPALGNLT PVVLGPEELW
160 170 180 190 200
PTRLRPEVLT PETPRPVDIG SGRAHDVCTP GKIERHADMA YTLDSDPCGH
210 220 230 240 250
CLIINNVNFC PSSGLSTRIG SHVDCEKLQH RFCWLRFMVE VKNDLTAKKM
260 270 280 290 300
VTALMEMAHR DHRALDCFVV VILSHGCQAS HLQFPGAVYG TDGCSVSIER
310 320 330 340 350
IVNIFNGTGC PSLGGKPKLF FIQACGGEQK DHGFEVAFTS SQDKAFDSDS
360 370 380 390 400
EPDAVPYQEG PRTLDQLDAV SSLPTPSDIL VSYSTFPGFV SWRDKKSGSW
410 420 430 440 450
YIETLDGVLE QWARSEDLQS LLLRVANAVS EKGVYKQIPG CFNFLRKKLF

FKTS
Length:454
Mass (Da):50,400
Last modified:October 1, 2000 - v1
Checksum:i501623B29E6ED6FC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07050305 Genomic DNA. No translation available.
AF271996 mRNA. Translation: AAF76217.1.
AF262319 mRNA. Translation: AAF85658.1.
AF286006 mRNA. Translation: AAF99705.1.
AY027667 mRNA. Translation: AAK26235.1.
AF308469 mRNA. Translation: AAK35159.1.
CH473968 Genomic DNA. Translation: EDL81013.1.
RefSeqiNP_113820.1. NM_031632.1.
UniGeneiRn.32199.

Genome annotation databases

EnsembliENSRNOT00000017972; ENSRNOP00000017972; ENSRNOG00000012944.
ENSRNOT00000085378; ENSRNOP00000072710; ENSRNOG00000012944.
GeneIDi58918.
KEGGirno:58918.
UCSCiRGD:61867. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07050305 Genomic DNA. No translation available.
AF271996 mRNA. Translation: AAF76217.1.
AF262319 mRNA. Translation: AAF85658.1.
AF286006 mRNA. Translation: AAF99705.1.
AY027667 mRNA. Translation: AAK26235.1.
AF308469 mRNA. Translation: AAK35159.1.
CH473968 Genomic DNA. Translation: EDL81013.1.
RefSeqiNP_113820.1. NM_031632.1.
UniGeneiRn.32199.

3D structure databases

SMRiQ9JHK1. Positions 1-96, 186-454.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9JHK1. 2 interactions.
MINTiMINT-3369959.
STRINGi10116.ENSRNOP00000017972.

Protein family/group databases

MEROPSiC14.010.

PTM databases

iPTMnetiQ9JHK1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000017972; ENSRNOP00000017972; ENSRNOG00000012944.
ENSRNOT00000085378; ENSRNOP00000072710; ENSRNOG00000012944.
GeneIDi58918.
KEGGirno:58918.
UCSCiRGD:61867. rat.

Organism-specific databases

CTDi842.
RGDi61867. Casp9.

Phylogenomic databases

eggNOGiKOG3573. Eukaryota.
ENOG410ZQIE. LUCA.
GeneTreeiENSGT00760000118912.
HOGENOMiHOG000231878.
HOVERGENiHBG059022.
KOiK04399.
OMAiVFEQWAH.
OrthoDBiEOG7TTQ7K.
PhylomeDBiQ9JHK1.
TreeFamiTF102023.

Enzyme and pathway databases

ReactomeiR-RNO-111458. Formation of apoptosome.
R-RNO-111459. Activation of caspases through apoptosome-mediated cleavage.
R-RNO-198323. AKT phosphorylates targets in the cytosol.
R-RNO-418889. Ligand-independent caspase activation via DCC.

Miscellaneous databases

PROiQ9JHK1.

Gene expression databases

ExpressionAtlasiQ9JHK1. baseline.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
3.40.50.1460. 1 hit.
InterProiIPR001315. CARD.
IPR033171. Caspase-9.
IPR029030. Caspase-like_dom.
IPR033139. Caspase_cys_AS.
IPR016129. Caspase_his_AS.
IPR011029. DEATH-like_dom.
IPR002138. Pept_C14_p10.
IPR001309. Pept_C14_p20.
IPR015917. Pept_C14A.
IPR017350. Pept_C14A_CASP1-typ.
[Graphical view]
PANTHERiPTHR10454:SF157. PTHR10454:SF157. 1 hit.
PfamiPF00619. CARD. 1 hit.
[Graphical view]
PIRSFiPIRSF038001. Caspase_ICE. 1 hit.
PRINTSiPR00376. IL1BCENZYME.
SMARTiSM00114. CARD. 1 hit.
SM00115. CASc. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
SSF52129. SSF52129. 1 hit.
PROSITEiPS50209. CARD. 1 hit.
PS01122. CASPASE_CYS. 1 hit.
PS01121. CASPASE_HIS. 1 hit.
PS50207. CASPASE_P10. 1 hit.
PS50208. CASPASE_P20. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Itoh T., Itoh A., Pleasure D.
    Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: Sprague-DawleyImported.
  2. "cDNA cloning and promoter analysis of rat caspase-9."
    Nishiyama J., Yi X., Venkatachalam M.A., Dong Z.
    Biochem. J. 360:49-56(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: WKYImported.
  3. "Characterization of a novel isoform of caspase-9 that inhibits apoptosis."
    Angelastro J.M., Moon N.Y., Liu D.X., Yang A.-S., Greene L.A., Franke T.F.
    J. Biol. Chem. 276:12190-12200(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  4. "Cloning of a novel Apaf-1-interacting protein: a potent suppressor of apoptosis and ischemic neuronal cell death."
    Cao G., Xiao M., Sun F., Xiao X., Pei W., Li J., Graham S.H., Simon R.P., Chen J.
    J. Neurosci. 24:6189-6201(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: Sprague-DawleyImported.
    Tissue: CerebellumImported.
  5. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Rat Genome Sequencing Project Consortium
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown NorwayImported.
  6. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  7. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  8. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.
  9. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Ensembl
    Submitted (JUN-2015) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.

Entry informationi

Entry nameiQ9JHK1_RAT
AccessioniPrimary (citable) accession number: Q9JHK1
Secondary accession number(s): F1M776
Entry historyi
Integrated into UniProtKB/TrEMBL: October 1, 2000
Last sequence update: October 1, 2000
Last modified: June 8, 2016
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.