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O08736

- CASPC_MOUSE

UniProt

O08736 - CASPC_MOUSE

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Protein

Caspase-12

Gene

Casp12

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei250 – 2501By similarity
Active sitei298 – 2981By similarity

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: RefGenome

GO - Biological processi

  1. apoptotic process Source: MGI
  2. endoplasmic reticulum unfolded protein response Source: MGI
  3. intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: UniProtKB
  4. regulation of apoptotic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Apoptosis

Protein family/group databases

MEROPSiC14.013.

Names & Taxonomyi

Protein namesi
Recommended name:
Caspase-12 (EC:3.4.22.-)
Short name:
CASP-12
Gene namesi
Name:Casp12
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:1312922. Casp12.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: RefGenome
  2. endoplasmic reticulum Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 419Caspase-12PRO_0000004648
Propeptidei1 – ?Sequence AnalysisPRO_0000004647

Keywords - PTMi

Zymogen

Proteomic databases

MaxQBiO08736.
PRIDEiO08736.

Expressioni

Tissue specificityi

Mainly expressed in skeletal muscle and lung.

Gene expression databases

BgeeiO08736.
CleanExiMM_CASP12.
ExpressionAtlasiO08736. baseline and differential.
GenevestigatoriO08736.

Interactioni

Subunit structurei

Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by two subunits Potential. Interacts with TRAF2 under resting conditions; this interaction is reduced in ER stress conditions.1 PublicationCurated

Binary interactionsi

WithEntry#Exp.IntActNotes
TRAF2Q129336EBI-6140033,EBI-355744From a different organism.

Protein-protein interaction databases

BioGridi198494. 3 interactions.
IntActiO08736. 1 interaction.
MINTiMINT-204464.

Structurei

3D structure databases

ProteinModelPortaliO08736.
SMRiO08736. Positions 139-419.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9292CARDPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C14A family.Curated
Contains 1 CARD domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG257064.
GeneTreeiENSGT00760000118912.
HOGENOMiHOG000234399.
HOVERGENiHBG076981.
InParanoidiO08736.
KOiK04741.
OMAiYFKEYSW.
OrthoDBiEOG7FXZZ6.
PhylomeDBiO08736.
TreeFamiTF102023.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
3.40.50.1460. 1 hit.
InterProiIPR001315. CARD.
IPR029030. Caspase-like_dom.
IPR017350. Caspase_ICE-type.
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]
PfamiPF00619. CARD. 1 hit.
PF00656. Peptidase_C14. 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.
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.

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

O08736-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAARRTHERD PIYKIKGLAK DMLDGVFDDL VEKNVLNGDE LLKIGESASF
60 70 80 90 100
ILNKAENLVE NFLEKTDMAG KIFAGHIANS QEQLSLQFSN DEDDGPQKIC
110 120 130 140 150
TPSSPSESKR KVEDDEMEVN AGLAHESHLM LTAPHGLQSS EVQDTLKLCP
160 170 180 190 200
RDQFCKIKTE RAKEIYPVME KEGRTRLALI ICNKKFDYLF DRDNADTDIL
210 220 230 240 250
NMQELLENLG YSVVLKENLT AQEMETELMQ FAGRPEHQSS DSTFLVFMSH
260 270 280 290 300
GILEGICGVK HRNKKPDVLH DDTIFKIFNN SNCRSLRNKP KILIMQACRG
310 320 330 340 350
RYNGTIWVST NKGIATADTD EERVLSCKWN NSITKAHVET DFIAFKSSTP
360 370 380 390 400
HNISWKVGKT GSLFISKLID CFKKYCWCYH LEEIFRKVQH SFEVPGELTQ
410
MPTIERVSMT RYFYLFPGN
Length:419
Mass (Da):47,854
Last modified:July 1, 1997 - v1
Checksum:iB94B0FED16B1CB40
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y13090 mRNA. Translation: CAA73532.1.
AK077256 mRNA. Translation: BAC36712.1.
AK161525 mRNA. Translation: BAE36443.1.
BC028979 mRNA. Translation: AAH28979.1.
CCDSiCCDS22800.1.
RefSeqiNP_033938.3. NM_009808.4.
UniGeneiMm.42163.

Genome annotation databases

EnsembliENSMUST00000027009; ENSMUSP00000027009; ENSMUSG00000025887.
GeneIDi12364.
KEGGimmu:12364.
UCSCiuc009obx.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y13090 mRNA. Translation: CAA73532.1 .
AK077256 mRNA. Translation: BAC36712.1 .
AK161525 mRNA. Translation: BAE36443.1 .
BC028979 mRNA. Translation: AAH28979.1 .
CCDSi CCDS22800.1.
RefSeqi NP_033938.3. NM_009808.4.
UniGenei Mm.42163.

3D structure databases

ProteinModelPortali O08736.
SMRi O08736. Positions 139-419.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198494. 3 interactions.
IntActi O08736. 1 interaction.
MINTi MINT-204464.

Protein family/group databases

MEROPSi C14.013.

Proteomic databases

MaxQBi O08736.
PRIDEi O08736.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000027009 ; ENSMUSP00000027009 ; ENSMUSG00000025887 .
GeneIDi 12364.
KEGGi mmu:12364.
UCSCi uc009obx.2. mouse.

Organism-specific databases

CTDi 100506742.
MGIi MGI:1312922. Casp12.

Phylogenomic databases

eggNOGi NOG257064.
GeneTreei ENSGT00760000118912.
HOGENOMi HOG000234399.
HOVERGENi HBG076981.
InParanoidi O08736.
KOi K04741.
OMAi YFKEYSW.
OrthoDBi EOG7FXZZ6.
PhylomeDBi O08736.
TreeFami TF102023.

Miscellaneous databases

NextBioi 281040.
PROi O08736.
SOURCEi Search...

Gene expression databases

Bgeei O08736.
CleanExi MM_CASP12.
ExpressionAtlasi O08736. baseline and differential.
Genevestigatori O08736.

Family and domain databases

Gene3Di 1.10.533.10. 1 hit.
3.40.50.1460. 1 hit.
InterProi IPR001315. CARD.
IPR029030. Caspase-like_dom.
IPR017350. Caspase_ICE-type.
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 ]
Pfami PF00619. CARD. 1 hit.
PF00656. Peptidase_C14. 1 hit.
[Graphical view ]
PIRSFi PIRSF038001. Caspase_ICE. 1 hit.
PRINTSi PR00376. IL1BCENZYME.
SMARTi SM00114. CARD. 1 hit.
SM00115. CASc. 1 hit.
[Graphical view ]
SUPFAMi SSF47986. SSF47986. 1 hit.
PROSITEi PS50209. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C3H/An.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Ovary and Uterus.
  3. "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].
    Strain: FVB/N-3.
    Tissue: Mammary gland.
  4. "Activation of caspase-12, an endoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress."
    Yoneda T., Imaizumi K., Oono K., Yui D., Gomi F., Katayama T., Tohyama M.
    J. Biol. Chem. 276:13935-13940(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRAF2.

Entry informationi

Entry nameiCASPC_MOUSE
AccessioniPrimary (citable) accession number: O08736
Secondary accession number(s): Q3TT82
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 1, 1997
Last modified: October 29, 2014
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3