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Q9UKL3

- C8AP2_HUMAN

UniProt

Q9UKL3 - C8AP2_HUMAN

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Protein
CASP8-associated protein 2
Gene
CASP8AP2, FLASH, KIAA1315, RIP25
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.By similarity4 Publications

GO - Molecular functioni

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

GO - Biological processi

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

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
Synonyms:FLASH, KIAA1315, RIP25
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.3 Publications

GO - Cellular componenti

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

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 2
PRO_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-acetyllysine By 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.By similarity6 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. 12 interactions.
MINTiMINT-91616.
STRINGi9606.ENSP00000391210.

Structurei

Secondary structure

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.

Family & Domainsi

Region

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

Motif

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

Natural variant

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

Sequence conflict

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

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. 12 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

« Hide 'large scale' publications
  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 leukocyte.
  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: Brain.
  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: Skin and Testis.
  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: Placenta.
  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: June 11, 2014
This is version 98 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

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