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P31944

- CASPE_HUMAN

UniProt

P31944 - CASPE_HUMAN

Protein

Caspase-14

Gene

CASP14

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 2 (11 Jan 2001)
      Previous versions | rss
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    Functioni

    Believed to be a non-apoptotic caspase which is involved in epidermal differentiation. Seems to play a role in keratinocyte differentiation and cornification. Probably regulates maturation of the epidermis by proteolytically processing filaggrin By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei89 – 891By similarity
    Active sitei132 – 1321By similarity

    GO - Molecular functioni

    1. cysteine-type endopeptidase activity Source: RefGenome

    GO - Biological processi

    1. cornification Source: UniProtKB
    2. epidermis development Source: ProtInc
    3. extrinsic apoptotic signaling pathway in absence of ligand Source: RefGenome
    4. intrinsic apoptotic signaling pathway in response to DNA damage Source: RefGenome
    5. keratinization Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Differentiation

    Protein family/group databases

    MEROPSiC14.018.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Caspase-14 (EC:3.4.22.-)
    Short name:
    CASP-14
    Cleaved into the following 2 chains:
    Gene namesi
    Name:CASP14
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:1502. CASP14.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: RefGenome
    2. extracellular vesicular exosome Source: UniProt
    3. keratin filament Source: Ensembl
    4. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26085.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 152Caspase-14 subunit p19PRO_0000004653
    Propeptidei1 – ?Sequence AnalysisPRO_0000004652
    Chaini153 – 24290Caspase-14 subunit p10PRO_0000004654Add
    BLAST

    Keywords - PTMi

    Zymogen

    Proteomic databases

    MaxQBiP31944.
    PaxDbiP31944.
    PeptideAtlasiP31944.
    PRIDEiP31944.

    Miscellaneous databases

    PMAP-CutDBP31944.

    Expressioni

    Tissue specificityi

    Expressed in keratinocytes of adult skin suprabasal layers (from spinous layers to the stratum granulosum and stratum corneum) (at protein level). Expressed in keratinocytes of hair shaft and sebaceous glands (at protein level). In psoriatic skin only expressed at very low levels.1 Publication

    Inductioni

    In undifferentiated keratinocytes under postconfluency growth conditions (in vitro).1 Publication

    Gene expression databases

    ArrayExpressiP31944.
    BgeeiP31944.
    CleanExiHS_CASP14.
    GenevestigatoriP31944.

    Organism-specific databases

    HPAiCAB010059.
    HPA027062.

    Interactioni

    Subunit structurei

    Complex of unprocessed caspase-14 and processed 19 kDa (p19) and 10 kDa (p10) subunits.1 Publication

    Protein-protein interaction databases

    BioGridi117116. 15 interactions.
    IntActiP31944. 4 interactions.
    STRINGi9606.ENSP00000221740.

    Structurei

    3D structure databases

    ProteinModelPortaliP31944.
    SMRiP31944. Positions 28-241.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase C14A family.Curated

    Phylogenomic databases

    eggNOGiNOG327631.
    HOGENOMiHOG000231878.
    HOVERGENiHBG050804.
    InParanoidiP31944.
    KOiK04401.
    OMAiCVTKARE.
    OrthoDBiEOG7VQJDT.
    PhylomeDBiP31944.
    TreeFamiTF102023.

    Family and domain databases

    Gene3Di3.40.50.1460. 1 hit.
    InterProiIPR029030. 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]
    PfamiPF00656. Peptidase_C14. 1 hit.
    [Graphical view]
    PRINTSiPR00376. IL1BCENZYME.
    SMARTiSM00115. CASc. 1 hit.
    [Graphical view]
    PROSITEiPS01122. CASPASE_CYS. 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.

    P31944-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSNPRSLEEE KYDMSGARLA LILCVTKARE GSEEDLDALE HMFRQLRFES    50
    TMKRDPTAEQ FQEELEKFQQ AIDSREDPVS CAFVVLMAHG REGFLKGEDG 100
    EMVKLENLFE ALNNKNCQAL RAKPKVYIIQ ACRGEQRDPG ETVGGDEIVM 150
    VIKDSPQTIP TYTDALHVYS TVEGYIAYRH DQKGSCFIQT LVDVFTKRKG 200
    HILELLTEVT RRMAEAELVQ EGKARKTNPE IQSTLRKRLY LQ 242
    Length:242
    Mass (Da):27,680
    Last modified:January 11, 2001 - v2
    Checksum:iE539FB7E8DD808A2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF097874 mRNA. Translation: AAD16173.1.
    BC069541 mRNA. Translation: AAH69541.1.
    BC103868 mRNA. Translation: AAI03869.1.
    BC103869 mRNA. Translation: AAI03870.1.
    CCDSiCCDS12323.1.
    PIRiJC7517.
    RefSeqiNP_036246.1. NM_012114.2.
    UniGeneiHs.466057.

    Genome annotation databases

    EnsembliENST00000427043; ENSP00000393417; ENSG00000105141.
    GeneIDi23581.
    KEGGihsa:23581.
    UCSCiuc010dzv.2. human.

    Polymorphism databases

    DMDMi12231007.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF097874 mRNA. Translation: AAD16173.1 .
    BC069541 mRNA. Translation: AAH69541.1 .
    BC103868 mRNA. Translation: AAI03869.1 .
    BC103869 mRNA. Translation: AAI03870.1 .
    CCDSi CCDS12323.1.
    PIRi JC7517.
    RefSeqi NP_036246.1. NM_012114.2.
    UniGenei Hs.466057.

    3D structure databases

    ProteinModelPortali P31944.
    SMRi P31944. Positions 28-241.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117116. 15 interactions.
    IntActi P31944. 4 interactions.
    STRINGi 9606.ENSP00000221740.

    Chemistry

    BindingDBi P31944.
    ChEMBLi CHEMBL5991.

    Protein family/group databases

    MEROPSi C14.018.

    Polymorphism databases

    DMDMi 12231007.

    Proteomic databases

    MaxQBi P31944.
    PaxDbi P31944.
    PeptideAtlasi P31944.
    PRIDEi P31944.

    Protocols and materials databases

    DNASUi 23581.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000427043 ; ENSP00000393417 ; ENSG00000105141 .
    GeneIDi 23581.
    KEGGi hsa:23581.
    UCSCi uc010dzv.2. human.

    Organism-specific databases

    CTDi 23581.
    GeneCardsi GC19P015160.
    HGNCi HGNC:1502. CASP14.
    HPAi CAB010059.
    HPA027062.
    MIMi 605848. gene.
    neXtProti NX_P31944.
    PharmGKBi PA26085.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG327631.
    HOGENOMi HOG000231878.
    HOVERGENi HBG050804.
    InParanoidi P31944.
    KOi K04401.
    OMAi CVTKARE.
    OrthoDBi EOG7VQJDT.
    PhylomeDBi P31944.
    TreeFami TF102023.

    Miscellaneous databases

    GeneWikii Caspase_14.
    GenomeRNAii 23581.
    NextBioi 46186.
    PMAP-CutDB P31944.
    PROi P31944.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P31944.
    Bgeei P31944.
    CleanExi HS_CASP14.
    Genevestigatori P31944.

    Family and domain databases

    Gene3Di 3.40.50.1460. 1 hit.
    InterProi IPR029030. 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 ]
    Pfami PF00656. Peptidase_C14. 1 hit.
    [Graphical view ]
    PRINTSi PR00376. IL1BCENZYME.
    SMARTi SM00115. CASc. 1 hit.
    [Graphical view ]
    PROSITEi PS01122. CASPASE_CYS. 1 hit.
    PS50207. CASPASE_P10. 1 hit.
    PS50208. CASPASE_P20. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Caspase-14: analysis of gene structure and mRNA expression during keratinocyte differentiation."
      Eckhart L., Ban J., Fischer H., Tschachler E.
      Biochem. Biophys. Res. Commun. 277:655-659(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Expression and transcriptional regulation of caspase-14 in simple and complex epithelia."
      Pistritto G., Jost M., Srinivasula S.M., Baffa R., Poyet J.-L., Kari C., Lazebnik Y., Rodeck U., Alnemri E.S.
      Cell Death Differ. 9:995-1006(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    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].
    4. "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
      Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
      Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 68-74; 137-147 AND 154-162.
      Tissue: Keratinocyte.
    5. "Epidermal differentiation does not involve the pro-apoptotic executioner caspases, but is associated with caspase-14 induction and processing."
      Lippens S., Kockx M., Knaapen M., Mortier L., Polakowska R., Verheyen A., Garmyn M., Zwijsen A., Formstecher P., Huylebroeck D., Vandenabeele P., Declercq W.
      Cell Death Differ. 7:1218-1224(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
    6. "Processing of native caspase-14 occurs at an atypical cleavage site in normal epidermal differentiation."
      Chien A.J., Presland R.B., Kuechle M.K.
      Biochem. Biophys. Res. Commun. 296:911-917(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 153-163, PROTEOLYTIC PROCESSING, SUBUNIT, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiCASPE_HUMAN
    AccessioniPrimary (citable) accession number: P31944
    Secondary accession number(s): O95823, Q3SYC9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: January 11, 2001
    Last modified: October 1, 2014
    This is version 132 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. Peptidase families
      Classification of peptidase families and list of entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3