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Q9UKL3

- C8AP2_HUMAN

UniProt

Q9UKL3 - C8AP2_HUMAN

Protein

CASP8-associated protein 2

Gene

CASP8AP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Participates in TNF-alpha-induced blockade of glucocorticoid receptor (GR) transactivation at the nuclear receptor coactivator level, upstream and independently of NF-kappa-B. Suppresses both NCOA2- and NCOA3-induced enhancement of GR transactivation. Involved in TNF-alpha-induced activation of NF-kappa-B via a TRAF2-dependent pathway. Acts as a downstream mediator for CASP8-induced activation of NF-kappa-B. Required for the activation of CASP8 in FAS-mediated apoptosis. Required for histone gene transcription and progression through S phase.4 Publications

    GO - Molecular functioni

    1. cysteine-type endopeptidase activator activity involved in apoptotic process Source: UniProtKB
    2. death receptor binding Source: ProtInc
    3. DNA binding Source: InterPro
    4. peptidase activator activity involved in apoptotic process Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. SUMO polymer binding Source: UniProtKB
    7. transcription corepressor activity Source: UniProtKB

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    2. apoptotic signaling pathway Source: ProtInc
    3. cell cycle Source: UniProtKB-KW
    4. cellular response to mechanical stimulus Source: UniProtKB
    5. extrinsic apoptotic signaling pathway via death domain receptors Source: UniProtKB
    6. Fas signaling pathway Source: UniProtKB
    7. regulation of transcription, DNA-templated Source: UniProtKB-KW
    8. signal transduction Source: ProtInc
    9. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Apoptosis, Cell cycle, Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    CASP8-associated protein 2
    Alternative name(s):
    FLICE-associated huge protein
    Gene namesi
    Name:CASP8AP2Imported
    Synonyms:FLASH, KIAA1315Imported, RIP25Imported
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Unplaced

    Organism-specific databases

    HGNCiHGNC:1510. CASP8AP2.

    Subcellular locationi

    Cytoplasm. Nucleus. NucleusPML body. Mitochondrion
    Note: Exported from the nucleus to the mitochondria upon FAS activation.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. mitochondrion Source: UniProtKB
    3. nucleus Source: UniProtKB
    4. PML body Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26093.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 19821981CASP8-associated protein 2PRO_0000076188Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei20 – 201Phosphoserine1 Publication
    Cross-linki92 – 92Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki93 – 93Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei1343 – 13431N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9UKL3.
    PaxDbiQ9UKL3.
    PRIDEiQ9UKL3.

    PTM databases

    PhosphoSiteiQ9UKL3.

    Expressioni

    Inductioni

    By TNF which induces strong nuclear localization.1 Publication

    Gene expression databases

    CleanExiHS_CASP8AP2.
    GenevestigatoriQ9UKL3.

    Interactioni

    Subunit structurei

    Self-associates. Component of the death-inducing signaling complex (DISC) with CASP8, FADD and FAS. Interacts with NCOA2 and NCOA3. Interacts with SRRT. Interacts with TRAF2. Interacts with NPAT. Interacts (via SIM domains) with SUMO1 and SUMO2. Interacts with SP100; may negatively regulate CASP8AP2 export from the nucleus to the cytoplasm.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CASP8Q147903EBI-2339650,EBI-78060
    PIAS1O759254EBI-2339650,EBI-629434
    SP100P234975EBI-2339650,EBI-751145
    TP73O15350-12EBI-2339650,EBI-389619

    Protein-protein interaction databases

    BioGridi115315. 18 interactions.
    DIPiDIP-40986N.
    IntActiQ9UKL3. 13 interactions.
    MINTiMINT-91616.
    STRINGi9606.ENSP00000391210.

    Structurei

    Secondary structure

    1
    1982
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1925 – 19273
    Helixi1931 – 194313
    Helixi1948 – 195811
    Helixi1962 – 197716

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2LR8NMR-A1916-1982[»]
    ProteinModelPortaliQ9UKL3.
    SMRiQ9UKL3. Positions 1916-1982.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1709 – 1982274NCOA2-binding1 PublicationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1683 – 16875SUMO interaction motif 1 (SIM); mediates the binding to polysumoylated substratesBy similarity
    Motifi1737 – 17415SUMO interaction motif 2 (SIM); mediates the binding to polysumoylated substratesBy similarity
    Motifi1794 – 17985SUMO interaction motif 3 (SIM); mediates the binding to polysumoylated substratesBy similarity

    Phylogenomic databases

    eggNOGiNOG42694.
    HOVERGENiHBG080371.
    InParanoidiQ9UKL3.
    PhylomeDBiQ9UKL3.

    Family and domain databases

    Gene3Di1.10.10.60. 1 hit.
    InterProiIPR009057. Homeodomain-like.
    [Graphical view]
    SUPFAMiSSF46689. SSF46689. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q9UKL3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAADDDNGDG TSLFDVFSAS PLKNNDEGSL DIYAGLDSAV SDSASKSCVP     50
    SRNCLDLYEE ILTEEGTAKE ATYNDLQVEY GKCQLQMKEL MKKFKEIQTQ 100
    NFSLINENQS LKKNISALIK TARVEINRKD EEISNLHQRL SEFPHFRNNH 150
    KTARTFDTVK TKDLKSRSPH LDDCSKTDHR AKSDVSKDVH HSTSLPNLEK 200
    EGKPHSDKRS TSHLPTSVEK HCTNGVWSRS HYQVGEGSSN EDSRRGRKDI 250
    RHSQFNRGTE RVRKDLSTGC GDGEPRILEA SQRLQGHPEK YGKGEPKTES 300
    KSSKFKSNSD SDYKGERINS SWEKETPGER SHSRVDSQSD KKLERQSERS 350
    QNINRKEVKS QDKEERKVDQ KPKSVVKDQD HWRRSERASL PHSKNEITFS 400
    HNSSKYHLEE RRGWEDCKRD KSVNSHSFQD GRCPSSLSNS RTHKNIDSKE 450
    VDAMHQWENT PLKAERHRTE DKRKREQESK EENRHIRNEK RVPTEHLQKT 500
    NKETKKTTTD LKKQNEPKTD KGEVLDNGVS EGADNKELAM KAESGPNETK 550
    NKDLKLSFMK KLNLTLSPAK KQPVSQDNQH KITDIPKSSG VCDSESSMQV 600
    KTVAYVPSIS EHILGEAAVS EHTMGETKST LLEPKVALLA VTEPRIGISE 650
    TNKEDENSLL VRSVDNTMHC EEPICGTETS FPSPMEIQQT ESLFPSTGMK 700
    QTINNGRAAA PVVMDVLQTD VSQNFGLELD TKRNDNSDYC GISEGMEMKV 750
    ALSTTVSETT ESILQPSIEE ADILPIMLSE DNNPKFEPSV IVTPLVESKS 800
    CHLEPCLPKE TLDSSLQQTE LMDHRMATGE TNSVYHDDDN SVLSIDLNHL 850
    RPIPEAISPL NSPVRPVAKV LRNESPPQVP VYNNSHKDVF LPNSAHSTSK 900
    SQSDLNKENQ KPIYKSDKCT EADTCKNSPL DELEEGEIRS DSETSKPQES 950
    FEKNSKRRVS ADVRKSKTIP RRGKSTVCLD KDSRKTHVRI HQTNNKWNKR 1000
    PDKSSRSSKT EKKDKVMSTS SLEKIVPIIA VPSSEQEIMH MLRMIRKHVR 1050
    KNYMKFKAKF SLIQFHRIIE SAILSFTSLI KHLNLHKISK SVTTLQKNLC 1100
    DIIESKLKQV KKNGIVDRLF EQQLPDMKKK LWKFVDDQLD YLFAKLKKIL 1150
    VCDSKSFGRD SDEGKLEKTS KQNAQYSNSQ KRSVDNSNRE LLKEKLSKSE 1200
    DPVHYKSLVG CKKSEENYQD QNNSSINTVK HDIKKNFNIC FDNIKNSQSE 1250
    ERSLEVHCPS TPKSEKNEGS SIEDAQTSQH ATLKPERSFE ILTEQQASSL 1300
    TFNLVSDAQM GEIFKSLLQG SDLLDSSVNC TEKSEWELKT PEKQLLETLK 1350
    CESIPACTTE ELVSGVASPC PKMISDDNWS LLSSEKGPSL SSGLSLPVHP 1400
    DVLDESCMFE VSTNLPLSKD NVCSVEKSKP CVSSILLEDL AVSLTVPSPL 1450
    KSDGHLSFLK PDMSSSSTPE EVISAHFSED ALLEEEDASE QDIHLALESD 1500
    NSSSKSSCSS SWTSRSVAPG FQYHPNLPMH AVIMEKSNDH FIVKIRRATP 1550
    STSSGLKQSM MPDELLTSLP RHGKEADEGP EKEYISCQNT VFKSVEELEN 1600
    SNKNVDGSKS THEEQSSMIQ TQVPDIYEFL KDASDKMGHS DEVADECFKL 1650
    HQVWETKVPE SIEELPSMEE ISHSVGEHLP NTYVDLTKDP VTETKNLGEF 1700
    IEVTVLHIDQ LGCSGGNLNQ SAQILDNSLQ ADTVGAFIDL TQDASSEAKS 1750
    EGNHPALAVE DLGCGVIQVD EDNCKEEKAQ VANRPLKCIV EETYIDLTTE 1800
    SPSSCEVKKD ELKSEPGSNC DNSELPGTLH NSHKKRRNIS DLNHPHKKQR 1850
    KETDLTNKEK TKKPTQDSCE NTEAHQKKAS KKKAPPVTKD PSSLKATPGI 1900
    KDSSAALATS TSLSAKNVIK KKGEIIILWT RNDDREILLE CQKRGPSFKT 1950
    FAYLAAKLDK NPNQVSERFQ QLMKLFEKSK CR 1982
    Length:1,982
    Mass (Da):222,658
    Last modified:May 1, 2000 - v1
    Checksum:iAF2B1A7798C19E39
    GO

    Sequence cautioni

    The sequence AAH56685.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence starting in position 364.
    The sequence BAA92067.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti278 – 2781L → S in AAD45537. 1 PublicationCurated
    Sequence conflicti362 – 3621D → E in AAH56685. (PubMed:15489334)Curated
    Sequence conflicti638 – 6381L → P in AAD45537. 1 PublicationCurated
    Sequence conflicti668 – 6681M → T in AAD45537. 1 PublicationCurated
    Sequence conflicti861 – 8611N → S in AAD45537. 1 PublicationCurated
    Sequence conflicti1713 – 17131C → Y in AAD45537. 1 PublicationCurated
    Sequence conflicti1754 – 17541Missing in BAA92553. (PubMed:10718198)Curated
    Sequence conflicti1832 – 18321S → P in BAA92067. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1659 – 16591P → S.
    Corresponds to variant rs3799896 [ dbSNP | Ensembl ].
    VAR_050700

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF154415 mRNA. Translation: AAF03367.1.
    AF164678 mRNA. Translation: AAD45537.2.
    AB037736 mRNA. Translation: BAA92553.2.
    AL353692 Genomic DNA. No translation available.
    CH471051 Genomic DNA. Translation: EAW48540.1.
    CH471051 Genomic DNA. Translation: EAW48542.1.
    CH471051 Genomic DNA. Translation: EAW48544.1.
    BC042577 mRNA. Translation: AAH42577.1.
    BC056685 mRNA. Translation: AAH56685.1. Sequence problems.
    BC132828 mRNA. Translation: AAI32829.1.
    BC132830 mRNA. Translation: AAI32831.1.
    AK002070 mRNA. Translation: BAA92067.1. Different initiation.
    AF165161 mRNA. Translation: AAD45157.1.
    RefSeqiNP_001131139.1. NM_001137667.1.
    NP_001131140.1. NM_001137668.1.
    NP_036247.1. NM_012115.3.
    UniGeneiHs.558218.

    Genome annotation databases

    GeneIDi9994.
    KEGGihsa:9994.
    UCSCiuc003pnr.3. human.

    Polymorphism databases

    DMDMi74721007.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF154415 mRNA. Translation: AAF03367.1 .
    AF164678 mRNA. Translation: AAD45537.2 .
    AB037736 mRNA. Translation: BAA92553.2 .
    AL353692 Genomic DNA. No translation available.
    CH471051 Genomic DNA. Translation: EAW48540.1 .
    CH471051 Genomic DNA. Translation: EAW48542.1 .
    CH471051 Genomic DNA. Translation: EAW48544.1 .
    BC042577 mRNA. Translation: AAH42577.1 .
    BC056685 mRNA. Translation: AAH56685.1 . Sequence problems.
    BC132828 mRNA. Translation: AAI32829.1 .
    BC132830 mRNA. Translation: AAI32831.1 .
    AK002070 mRNA. Translation: BAA92067.1 . Different initiation.
    AF165161 mRNA. Translation: AAD45157.1 .
    RefSeqi NP_001131139.1. NM_001137667.1.
    NP_001131140.1. NM_001137668.1.
    NP_036247.1. NM_012115.3.
    UniGenei Hs.558218.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2LR8 NMR - A 1916-1982 [» ]
    ProteinModelPortali Q9UKL3.
    SMRi Q9UKL3. Positions 1916-1982.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115315. 18 interactions.
    DIPi DIP-40986N.
    IntActi Q9UKL3. 13 interactions.
    MINTi MINT-91616.
    STRINGi 9606.ENSP00000391210.

    PTM databases

    PhosphoSitei Q9UKL3.

    Polymorphism databases

    DMDMi 74721007.

    Proteomic databases

    MaxQBi Q9UKL3.
    PaxDbi Q9UKL3.
    PRIDEi Q9UKL3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 9994.
    KEGGi hsa:9994.
    UCSCi uc003pnr.3. human.

    Organism-specific databases

    CTDi 9994.
    GeneCardsi GC06P090539.
    HGNCi HGNC:1510. CASP8AP2.
    MIMi 606880. gene.
    neXtProti NX_Q9UKL3.
    PharmGKBi PA26093.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG42694.
    HOVERGENi HBG080371.
    InParanoidi Q9UKL3.
    PhylomeDBi Q9UKL3.

    Miscellaneous databases

    ChiTaRSi CASP8AP2. human.
    GeneWikii CASP8AP2.
    GenomeRNAii 9994.
    NextBioi 37755.
    PROi Q9UKL3.
    SOURCEi Search...

    Gene expression databases

    CleanExi HS_CASP8AP2.
    Genevestigatori Q9UKL3.

    Family and domain databases

    Gene3Di 1.10.10.60. 1 hit.
    InterProi IPR009057. Homeodomain-like.
    [Graphical view ]
    SUPFAMi SSF46689. SSF46689. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Reply: searching for FLASH domains."
      Kimura T., Imai Y., Yonehara S.
      Nature 401:662-663(1999)
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: T-cell.
    2. "RIP25, a human homolog of Mus musculus FLASH, is involved in IL-2 signaling."
      Yan M.D., Sun L.Y., Liu X.Y., Zheng Z.C.
      Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Peripheral blood leukocyteImported.
    3. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
      DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: BrainImported.
    4. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    5. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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].
      Tissue: SkinImported and TestisImported.
    8. "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.
      , 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] OF 1478-1982.
      Tissue: PlacentaImported.
    9. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 714-1982.
    10. "Tumor necrosis factor alpha receptor- and Fas-associated FLASH inhibit transcriptional activity of the glucocorticoid receptor by binding to and interfering with its interaction with p160 type nuclear receptor coactivators."
      Kino T., Chrousos G.P.
      J. Biol. Chem. 278:3023-3029(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NCOA2, SUBCELLULAR LOCATION, INDUCTION.
    11. "FLASH interacts with p160 coactivator subtypes and differentially suppresses transcriptional activity of steroid hormone receptors."
      Kino T., Ichijo T., Chrousos G.P.
      J. Steroid Biochem. Mol. Biol. 92:357-363(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NCOA3.
    12. Cited for: FUNCTION, INTERACTION WITH NPAT, SUBCELLULAR LOCATION.
    13. "FLASH links the CD95 signaling pathway to the cell nucleus and nuclear bodies."
      Milovic-Holm K., Krieghoff E., Jensen K., Will H., Hofmann T.G.
      EMBO J. 26:391-401(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN FAS-MEDIATED APOPTOSIS, INTERACTION WITH CASP8 AND SP100, SUBCELLULAR LOCATION.
    14. "Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
      Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
      Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-92 AND LYS-93.
      Tissue: Mammary cancer.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    16. "Interaction of FLASH with arsenite resistance protein 2 is involved in cell cycle progression at S phase."
      Kiriyama M., Kobayashi Y., Saito M., Ishikawa F., Yonehara S.
      Mol. Cell. Biol. 29:4729-4741(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SRRT.
    17. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "PolySUMO-binding proteins identified through a string search."
      Sun H., Hunter T.
      J. Biol. Chem. 287:42071-42083(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF REPEAT SUMO-INTERACTING MOTIF, INTERACTION WITH SUMO1 AND SUMO2.
    20. "Solution NMR structure of CASP8-associated protein 2 from Homo sapiens, Northeast structural genomics consortium (NESG) target HR8150A."
      Northeast structural genomics consortium (NESG)
      Submitted (JUN-2012) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 1916-1982.

    Entry informationi

    Entry nameiC8AP2_HUMAN
    AccessioniPrimary (citable) accession number: Q9UKL3
    Secondary accession number(s): A2RUB7
    , E1P553, Q6PH76, Q7LCQ7, Q86YD9, Q9NUQ4, Q9NZV9, Q9P2N1, Q9Y563
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 99 of the entry and version 1 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    External Data

    Dasty 3