CASP8 and FADD-like apoptosis regulator

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• cysteine-type endopeptidase activity involved in apoptotic process Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• cysteine-type endopeptidase activity involved in apoptotic signaling pathway Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• death receptor binding Source: Ensembl
• enzyme activator activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • Ref.1

    "Casper is a FADD- and caspase-related inducer of apoptosis."
    Shu H.-B., Halpin D.R., Goeddel D.V.
    Immunity 6:751-763(1997) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 13 AND 14), MUTAGENESIS OF TYR-360.
• peptidase activator activity Source: Ensembl
• protease binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • Ref.1

    "Casper is a FADD- and caspase-related inducer of apoptosis."
    Shu H.-B., Halpin D.R., Goeddel D.V.
    Immunity 6:751-763(1997) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 13 AND 14), MUTAGENESIS OF TYR-360.
• protein-containing complex binding Source: Ensembl
• protein heterodimerization activity Source: Ensembl

GO - Biological processⁱ

• activation of cysteine-type endopeptidase activity involved in apoptotic process Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• apoptotic process Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "cIAPs block Ripoptosome formation, a RIP1/caspase-8 containing intracellular cell death complex differentially regulated by cFLIP isoforms."
    Feoktistova M., Geserick P., Kellert B., Dimitrova D.P., Langlais C., Hupe M., Cain K., MacFarlane M., Hacker G., Leverkus M.
    Mol. Cell 43:449-463(2011) [PubMed] [Europe PMC] [Abstract]
• cellular response to dexamethasone stimulus Source: Ensembl
• cellular response to epidermal growth factor stimulus Source: Ensembl
• cellular response to estradiol stimulus Source: Ensembl
• cellular response to hypoxia Source: Ensembl
• cellular response to insulin stimulus Source: Ensembl
• cellular response to nitric oxide Source: Ensembl
• negative regulation of apoptotic process Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementⁱ
  • Ref.3

    "Inhibition of death receptor signals by cellular FLIP."
    Irmler M., Thome M., Hahne M., Schneider P., Hofmann K., Steiner V., Bodmer J.-L., Schroeter M., Burns K., Mattmann C., Rimoldi D., French L.E., Tschopp J.
    Nature 388:190-195(1997) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
• negative regulation of cardiac muscle cell apoptotic process Source: Ensembl
• negative regulation of cellular response to transforming growth factor beta stimulus Source: Ensembl
• negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
• negative regulation of extrinsic apoptotic signaling pathway Source: UniProtKBInferred from direct assayⁱ
  • Ref.1

    "Casper is a FADD- and caspase-related inducer of apoptosis."
    Shu H.-B., Halpin D.R., Goeddel D.V.
    Immunity 6:751-763(1997) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 13 AND 14), MUTAGENESIS OF TYR-360.
• negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: MGIInferred from direct assayⁱ
  • "Lifeguard Inhibits Fas Ligand-mediated Endoplasmic Reticulum-Calcium Release Mandatory for Apoptosis in Type II Apoptotic Cells."
    Urresti J., Ruiz-Meana M., Coccia E., Arevalo J.C., Castellano J., Fernandez-Sanz C., Galenkamp K.M., Planells-Ferrer L., Moubarak R.S., Llecha-Cano N., Reix S., Garcia-Dorado D., Barneda-Zahonero B., Comella J.X.
    J. Biol. Chem. 291:1221-1234(2016) [PubMed] [Europe PMC] [Abstract]
• negative regulation of hepatocyte apoptotic process Source: Ensembl
• negative regulation of myoblast fusion Source: BHF-UCL
• negative regulation of necroptotic process Source: Ensembl
• negative regulation of reactive oxygen species biosynthetic process Source: Ensembl
• positive regulation of ERK1 and ERK2 cascade Source: Ensembl
• positive regulation of extracellular matrix organization Source: Ensembl
• positive regulation of glomerular mesangial cell proliferation Source: Ensembl
• positive regulation of hepatocyte proliferation Source: Ensembl
• positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ
  • "Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways."
    Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O., Nagano Y., Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H., Sugano S.
    Oncogene 22:3307-3318(2003) [PubMed] [Europe PMC] [Abstract]
• positive regulation of neuron projection development Source: Ensembl
• positive regulation of NF-kappaB transcription factor activity Source: BHF-UCL
• regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: Reactome
• regulation of necroptotic process Source: UniProtKBInferred from direct assayⁱ
  • "cIAPs block Ripoptosome formation, a RIP1/caspase-8 containing intracellular cell death complex differentially regulated by cFLIP isoforms."
    Feoktistova M., Geserick P., Kellert B., Dimitrova D.P., Langlais C., Hupe M., Cain K., MacFarlane M., Hacker G., Leverkus M.
    Mol. Cell 43:449-463(2011) [PubMed] [Europe PMC] [Abstract]
• regulation of skeletal muscle satellite cell proliferation Source: BHF-UCL
• response to bacterium Source: Ensembl
• response to testosterone Source: Ensembl
• skeletal muscle atrophy Source: BHF-UCL
• skeletal muscle tissue development Source: BHF-UCL
• skeletal muscle tissue regeneration Source: BHF-UCL
• skeletal myofibril assembly Source: BHF-UCL
• viral process Source: UniProtKB-KW

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Mutagenesis

Organism-specific databases

Miscellaneous databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductionⁱ

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• death receptor binding Source: Ensembl
• protease binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.1

    "Casper is a FADD- and caspase-related inducer of apoptosis."
    Shu H.-B., Halpin D.R., Goeddel D.V.
    Immunity 6:751-763(1997) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 13 AND 14), MUTAGENESIS OF TYR-360.
• protein heterodimerization activity Source: Ensembl

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Domains and Repeats

Region

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domainⁱ

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (15+)ⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry has 15 described isoforms and 10 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MSAEVIHQVE EALDTDEKEM LLFLCRDVAI DVVPPNVRDL LDILRERGKL 
        60         70         80         90        100
SVGDLAELLY RVRRFDLLKR ILKMDRKAVE THLLRNPHLV SDYRVLMAEI 
       110        120        130        140        150
GEDLDKSDVS SLIFLMKDYM GRGKISKEKS FLDLVVELEK LNLVAPDQLD 
       160        170        180        190        200
LLEKCLKNIH RIDLKTKIQK YKQSVQGAGT SYRNVLQAAI QKSLKDPSNN 
       210        220        230        240        250
FRLHNGRSKE QRLKEQLGAQ QEPVKKSIQE SEAFLPQSIP EERYKMKSKP 
       260        270        280        290        300
LGICLIIDCI GNETELLRDT FTSLGYEVQK FLHLSMHGIS QILGQFACMP 
       310        320        330        340        350
EHRDYDSFVC VLVSRGGSQS VYGVDQTHSG LPLHHIRRMF MGDSCPYLAG 
       360        370        380        390        400
KPKMFFIQNY VVSEGQLEDS SLLEVDGPAM KNVEFKAQKR GLCTVHREAD 
       410        420        430        440        450
FFWSLCTADM SLLEQSHSSP SLYLQCLSQK LRQERKRPLL DLHIELNGYM 
       460        470        480
YDWNSRVSAK EKYYVWLQHT LRKKLILSYT                       

        10         20         30         40         50
MSAEVIHQVE EALDTDEKEM LLFLCRDVAI DVVPPNVRDL LDILRERGKL 
        60         70         80         90        100
SVGDLAELLY RVRRFDLLKR ILKMDRKAVE THLLRNPHLV SDYRVLMAEI 
       110        120        130        140        150
GEDLDKSDVS SLIFLMKDYM GRGKISKEKS FLDLVVELEK LNLVAPDQLD 
       160        170        180        190        200
LLEKCLKNIH RIDLKTKIQK YKQSVQGAGT SYRNVLQAAI QKSLKDPSNN 
       210        220 
FRMITPYAHC PDLKILGNCS M                                

        10         20         30         40         50
MAEIGEDLDK SDVSSLIFLM KDYMGRGKIS KEKSFLDLVV ELEKLNLVAP 
        60         70         80         90        100
DQLDLLEKCL KNIHRIDLKT KIQKYKQSVQ GAGTSYRNVL QAAIQKSLKD 
       110        120        130        140        150
PSNNFRLHNG RSKEQRLKEQ LGAQQEPVKK SIQESEAFLP QSIPEERYKM 
       160        170        180        190        200
KSKPLGICLI IDCIGNETEL LRDTFTSLGY EVQKFLHLSM HGISQILGQF 
       210        220        230        240        250
ACMPEHRDYD SFVCVLVSRG GSQSVYGVDQ THSGLPLHHI RRMFMGDSCP 
       260        270        280        290        300
YLAGKPKMFF IQNYVVSEGQ LEDSSLLEVD GPAMKNVEFK AQKRGLCTVH 
       310        320        330        340        350
READFFWSLC TADMSLLEQS HSSPSLYLQC LSQKLRQERG TIPGSGITES 
       360 
KDMHFSSLGC ILLDVL                                      

        10         20         30         40         50
MKSKPLGICL IIDCIGNETE LLRDTFTSLG YEVQKFLHLS MHGISQILGQ 
        60         70         80         90        100
FACMPEHRDY DSFVCVLVSR GGSQSVYGVD QTHSGLPLHH IRRMFMGDSC 
       110        120        130        140        150
PYLAGKPKMF FIQNYVVSEG QLEDSSLLEV DGPAMKNVEF KAQKRGLCTV 
       160        170        180        190        200
HREADFFWSL CTADMSLLEQ SHSSPSLYLQ CLSQKLRQER KRPLLDLHIE 
       210        220        230 
LNGYMYDWNS RVSAKEKYYV WLQHTLRKKL ILSYT                 

        10         20         30         40         50
MSAEVIHQVE EALDTDEKEM LLFLCRDVAI DVVPPNVRDL LDILRERGKL 
        60         70         80         90        100
SVGDLAELLY RVRRFDLLKR ILKMDRKAVE THLLRNPHLV SDYRVLMAEI 
       110        120        130        140        150
GEDLDKSDVS SLIFLMKDYM GRGKISKEKS FLDLVVELEK LNLVAPDQLD 
       160        170        180        190        200
LLEKCLKNIH RIDLKTKIQK YKQSVQGAGT SYRNVLQAAI QKSLKDPSNN 
       210        220        230        240        250
FRLHNGRSKE QRLKEQLGAQ QEPVKKSIQE SEAFLPQSIP EERYKMKSKP 
       260        270        280        290        300
LGICLIIDCI GNETELLRDT FTSLGYEVQK FLHLSMHGIS QILGQFACMP 
       310        320        330        340        350
EHRDYDSFVC VLVSRGGSQS VYGVDQTHSG LPLHHIRRMF MGDSCPYLAG 
       360        370        380        390        400
KPKMFFIQNY VVSEGQLEDS SLLEVDGPAM KNVEFKAQKR GLCTVHREAD 
       410        420        430        440 
FFWSLCTADM SLLEQSHSSP SLYLQCLSQK LRQERKRPLL DLHIELNGL  

        10         20         30         40         50
MLERPPVCSK VDVVPPNVRD LLDILRERGK LSVGDLAELL YRVRRFDLLK 
        60         70         80         90        100
RILKMDRKAV ETHLLRNPHL VSDYRVLMAE IGEDLDKSDV SSLIFLMKDY 
       110        120        130        140        150
MGRGKISKEK SFLDLVVELE KLNLVAPDQL DLLEKCLKNI HRIDLKTKIQ 
       160        170        180        190        200
KYKQSVQGAG TSYRNVLQAA IQKSLKDPSN NFRLHNGRSK EQRLKEQLGA 
       210        220        230        240        250
QQEPVKKSIQ ESEAFLPQSI PEERYKMKSK PLGICLIIDC IGNETELLRD 
       260        270        280        290        300
TFTSLGYEVQ KFLHLSMHGI SQILGQFACM PEHRDYDSFV CVLVSRGGSQ 
       310        320        330        340        350
SVYGVDQTHS GLPLHHIRRM FMGDSCPYLA GKPKMFFIQN YVVSEGQLED 
       360        370        380        390        400
SSLLEVDGPA MKNVEFKAQK RGLCTVHREA DFFWSLCTAD MSLLEQSHSS 
       410        420        430        440 
PSLYLQCLSQ KLRQERKRPL LDLHIELNGY MYDSLEHTGG RY         

        10         20         30         40         50
MAEIGEDLDK SDVSSLIFLM KDYMGRGKIS KEKSFLDLVV ELEKLNLVAP 
        60         70         80         90        100
DQLDLLEKCL KNIHRIDLKT KIQKYKQSVQ GAGTSYRNVL QAAIQKSLKD 
       110        120        130        140        150
PSNNFREEPV KKSIQESEAF LPQSIPEERY KMKSKPLGIC LIIDCIGNET 
       160        170        180        190        200
ELLRDTFTSL GYEVQKFLHL SMHGISQILG QFACMPEHRD YDSFVCVLVS 
       210        220        230        240        250
RGGSQSVYGV DQTHSGLPLH HIRRMFMGDS CPYLAGKPKM FFIQNYVVSE 
       260        270        280        290        300
GQLEDSSLLE VDGPAMKNVE FKAQKRGLCT VHREADFFWS LCTADMSLLE 
       310        320        330        340 
QSHSSPSLYL QCLSQKLRQE RGTIPGSGIT ESKDMHFSSL GCILLDVL   

        10         20         30         40         50
MSAEVIHQVE EALDTDEKEM LLFLCRDVAI DVVPPNVRDL LDILRERGKL 
        60         70         80         90        100
SVGDLAELLY RVRRFDLLKR ILKMDRKAVE THLLRNPHLV SDYRVLMAEI 
       110        120        130        140        150
GEDLDKSDVS SLIFLMKDYM GRGKISKEKS FLDLVVELEK LNLVAPDQLD 
       160        170        180        190        200
LLEKCLKNIH RIDLKTKIQK YKQSVQGAGT SYRNVLQAAI QKSLKDPSNN 
       210        220        230        240        250
FRSIPEERYK MKSKPLGICL IIDCIGNETE LLRDTFTSLG YEVQKFLHLS 
       260        270        280        290        300
MHGISQILGQ FACMPEHRDY DSFVCVLVSR GGSQSVYGVD QTHSGLPLHH 
       310        320        330        340        350
IRRMFMGDSC PYLAGKPKMF FIQNYVVSEG QLEDSSLLEV DGPAMKNVEF 
       360        370        380        390        400
KAQKRGLCTV HREADFFWSL CTADMSLLEQ SHSSPSLYLQ CLSQKLRQER 
       410        420        430        440 
KRPLLDLHIE LNGYMYDWNS RVSAKEKYYV WLQHTLRKKL ILSYT      

        10         20         30         40         50
MSAEVIHQVE EALDTDEKEM LLFLCRDVAI DVVPPNVRDL LDILRERGKL 
        60         70         80         90        100
SVGDLAELLY RVRRFDLLKR ILKMDRKAVE THLLRNPHLV SDYRVLMAEI 
       110        120        130        140        150
GEDLDKSDVS SLIFLMKDYM GRGKISKEKS FLDLVVELEK LNLVAPDQLD 
       160        170        180        190        200
LLEKCLKNIH RIDLKTKIQK YKQSVQGAGT SYRNVLQAAI QKSLKDPSNN 
       210        220        230        240        250
FRSIPEERYK MKSKPLGICL IIDCIGNETE LCGVRGPAGG QQPLGGGWAS 
       260        270
DEECGIQGSE ARAVHSSPRS                                  

        10         20         30         40         50
MSAEVIHQVE EALDTDEKEM LLFLCRDVAI DVVPPNVRDL LDILRERGKL 
        60         70         80         90        100
SVGDLAELLY RVRRFDLLKR ILKMDRKAVE THLLRNPHLV SDYRVLMAEI 
       110        120        130        140        150
GEDLDKSDVS SLIFLMKDYM GRGKISKEKS FLDLVVELEK LNLVAPDQLD 
       160        170        180        190        200
LLEKCLKNIH RIDLKTKIQK YKQSVQGAGT SYRNVLQAAI QKSLKDPSNN 
       210        220        230        240        250
FRLHNGRSKE QRLKEQLGAQ QEPVKKSIQE SEAFLPQSIP EERYKMKSKP 
       260        270        280        290        300
LGICLIIDCI GNETENAHSW IFTLNSMATC MIGTAEFLPR RNIMFGCSTL 

        10         20         30         40         50
MSAEVIHQVE EALDTDEKEM LLFLCRDVAI DVVPPNVRDL LDILRERGKL 
        60         70         80         90        100
SVGDLAELLY RVRRFDLLKR ILKMDRKAVE THLLRNPHLV SDYRVLMAEI 
       110        120        130        140        150
GEDLDKSDVS SLIFLMKDYM GRGKISKEKS FLDLVVELEK LNLVAPDQLD 
       160        170        180        190        200
LLEKCLKNIH RIDLKTKIQK YKQSVQGAGT SYRNVLQAAI QKSLKDPSNN 
       210        220        230        240        250
FRLHNGRSKE QRLKEQLGAQ QEPVKKSIQE SEAFLPQSIP EERYKMKSKP 
       260        270        280        290        300
LGICLIIDCI GNETELLRDT FTSLGYEVQK FLHLSMHGIS QILGQFACMP 
       310        320        330        340        350
EHRDYDSFVC VLVSRGGSQS VYGVDQTHSG LPLHHIRRMF MGDSCPYLAG 
       360        370        380        390        400
KPKMFFIQNY VVSEGQLEDS SLLEVDGPAM KNVEFKAQKR GLCTVHREAD 
       410        420        430        440        450
FFWSLCTADM SLLEQSHSSP SLYLQCLSQK LRQERGTIPG SGITESKDMH 
       460 
FSSLGCILLD VL                                          

        10         20         30         40         50
MSAEVIHQVE EALDTDEKEM LLFLCRDVAI DVVPPNVRDL LDILRERGKL 
        60         70         80         90        100
SVGDLAELLY RVRRFDLLKR ILKMDRKAVE THLLRNPHLV SDYRVLMAEI 
       110        120        130        140        150
GEDLDKSDVS SLIFLMKDYM GRGKISKEKS FLDLVVELEK LNLVAPDQLD 
       160        170        180        190        200
LLEKCLKNIH RIDLKTKIQK YKQSVQGAGT SYRNVLQAAI QKSLKDPSNN 
       210        220        230        240        250
FRLHNGRSKE QRLKEQLGAQ QEPVKKSIQE SEAFLPQSIP EERYKMKSKP 
       260        270        280        290 
LGICLIIDCI GNETGWSAMA QSQLTAISTS QVQAILLPQP PE         

        10         20         30         40         50
MSAEVIHQVE EALDTDEKEM LLFLCRDVAI DVVPPNVRDL LDILRERGKL 
        60         70         80         90        100
SVGDLAELLY RVRRFDLLKR ILKMDRKAVE THLLRNPHLV SDYRVLMAEI 
       110        120        130        140        150
GEDLDKSDVS SLIFLMKDYM GRGKISKEKS FLDLVVELEK LNLVAPDQLD 
       160        170        180        190        200
LLEKCLKNIH RIDLKTKIQK YKQSVQGAGT SYRNVLQAAI QKSLKDPSNN 

FR                                                     

        10         20         30         40         50
MSAEVIHQVE EALDTDEKEM LLFLCRDVAI DVVPPNVRDL LDILRERGKL 
        60         70         80         90        100
SVGDLAELLY RVRRFDLLKR ILKMDRKAVE THLLRNPHLV SDYRVLMAEI 
       110        120        130        140        150
GEDLDKSDVS SLIFLMKDYM GRGKISKEKS FLDLVVELEK LNLVAPDQLD 
       160        170        180        190        200
LLEKCLKNIH RIDLKTKIQK YKQSVQGAGT SYRNVLQAAI QKSLKDPSNN 
       210        220        230        240        250
FRLHNGRSKE QRLKEQLGAQ QEPVKKSIQE SEAFLPQSIP EERYKMKSKP 
       260        270        280        290        300
LGICLIIDCI GNETELLRDT FTSLGYEVQK FLHLSMHGIS QILGQFACMP 
       310        320        330        340        350
EHRDYDSFVC VLVSRGGSQS VYGVDQTHSG LPLHHIRRMF MGDSCPYLAG 
       360        370        380        390        400
KPKMFFIQNY VVSEGQLEDS SLLEVDGPAM KNVEFKAQKR GLCTVHREAD 
       410        420        430 
FFWSLCTADM SLLEQSHSSP SLYLQCLSQK LRQER                 

        10         20         30         40         50
MAEIGEDLDK SDVSSLIFLM KDYMGRGKIS KEKSFLDLVV ELEKLNLVAP 
        60         70         80         90        100
DQLDLLEKCL KNIHRIDLKT KIQKYKQSVQ GAGTSYRNVL QAAIQKSLKD 
       110        120        130        140        150
PSNNFRLHNG RSKEQRLKEQ LGAQQEPVKK SIQESEAFLP QSIPEERYKM 
       160        170        180        190        200
KSKPLGICLI IDCIGNETEL LRDTFTSLGY EVQKFLHLSM HGISQILGQF 
       210        220        230        240        250
ACMPEHRDYD SFVCVLVSRG GSQSVYGVDQ THSGLPLHHI RRMFMGDSCP 
       260        270        280        290        300
YLAGKPKMFF IQNYVVSEGQ LEDSSLLEVD GPAMKNVEFK AQKRGLCTVH 
       310        320        330        340        350
READFFWSLC TADMSLLEQS HSSPSLYLQC LSQKLRQERK RPLLDLHIEL 
       360        370        380 
NGYMYDWNSR VSAKEKYYVW LQHTLRKKLI LSYT                  

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityⁱ

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 100% Identity
• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

PTM databases

Polymorphism and mutation databases

Proteomic databases