Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9UKL3

- C8AP2_HUMAN

UniProt

Q9UKL3 - C8AP2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

CASP8-associated protein 2

Gene

CASP8AP2

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.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. SUMO polymer binding Source: UniProtKB
  6. 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
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
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
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 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 – 19273Combined sources
Helixi1931 – 194313Combined sources
Helixi1948 – 195811Combined sources
Helixi1962 – 197716Combined sources

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

        10         20         30         40         50
MAADDDNGDG TSLFDVFSAS PLKNNDEGSL DIYAGLDSAV SDSASKSCVP
60 70 80 90 100
SRNCLDLYEE ILTEEGTAKE ATYNDLQVEY GKCQLQMKEL MKKFKEIQTQ
110 120 130 140 150
NFSLINENQS LKKNISALIK TARVEINRKD EEISNLHQRL SEFPHFRNNH
160 170 180 190 200
KTARTFDTVK TKDLKSRSPH LDDCSKTDHR AKSDVSKDVH HSTSLPNLEK
210 220 230 240 250
EGKPHSDKRS TSHLPTSVEK HCTNGVWSRS HYQVGEGSSN EDSRRGRKDI
260 270 280 290 300
RHSQFNRGTE RVRKDLSTGC GDGEPRILEA SQRLQGHPEK YGKGEPKTES
310 320 330 340 350
KSSKFKSNSD SDYKGERINS SWEKETPGER SHSRVDSQSD KKLERQSERS
360 370 380 390 400
QNINRKEVKS QDKEERKVDQ KPKSVVKDQD HWRRSERASL PHSKNEITFS
410 420 430 440 450
HNSSKYHLEE RRGWEDCKRD KSVNSHSFQD GRCPSSLSNS RTHKNIDSKE
460 470 480 490 500
VDAMHQWENT PLKAERHRTE DKRKREQESK EENRHIRNEK RVPTEHLQKT
510 520 530 540 550
NKETKKTTTD LKKQNEPKTD KGEVLDNGVS EGADNKELAM KAESGPNETK
560 570 580 590 600
NKDLKLSFMK KLNLTLSPAK KQPVSQDNQH KITDIPKSSG VCDSESSMQV
610 620 630 640 650
KTVAYVPSIS EHILGEAAVS EHTMGETKST LLEPKVALLA VTEPRIGISE
660 670 680 690 700
TNKEDENSLL VRSVDNTMHC EEPICGTETS FPSPMEIQQT ESLFPSTGMK
710 720 730 740 750
QTINNGRAAA PVVMDVLQTD VSQNFGLELD TKRNDNSDYC GISEGMEMKV
760 770 780 790 800
ALSTTVSETT ESILQPSIEE ADILPIMLSE DNNPKFEPSV IVTPLVESKS
810 820 830 840 850
CHLEPCLPKE TLDSSLQQTE LMDHRMATGE TNSVYHDDDN SVLSIDLNHL
860 870 880 890 900
RPIPEAISPL NSPVRPVAKV LRNESPPQVP VYNNSHKDVF LPNSAHSTSK
910 920 930 940 950
SQSDLNKENQ KPIYKSDKCT EADTCKNSPL DELEEGEIRS DSETSKPQES
960 970 980 990 1000
FEKNSKRRVS ADVRKSKTIP RRGKSTVCLD KDSRKTHVRI HQTNNKWNKR
1010 1020 1030 1040 1050
PDKSSRSSKT EKKDKVMSTS SLEKIVPIIA VPSSEQEIMH MLRMIRKHVR
1060 1070 1080 1090 1100
KNYMKFKAKF SLIQFHRIIE SAILSFTSLI KHLNLHKISK SVTTLQKNLC
1110 1120 1130 1140 1150
DIIESKLKQV KKNGIVDRLF EQQLPDMKKK LWKFVDDQLD YLFAKLKKIL
1160 1170 1180 1190 1200
VCDSKSFGRD SDEGKLEKTS KQNAQYSNSQ KRSVDNSNRE LLKEKLSKSE
1210 1220 1230 1240 1250
DPVHYKSLVG CKKSEENYQD QNNSSINTVK HDIKKNFNIC FDNIKNSQSE
1260 1270 1280 1290 1300
ERSLEVHCPS TPKSEKNEGS SIEDAQTSQH ATLKPERSFE ILTEQQASSL
1310 1320 1330 1340 1350
TFNLVSDAQM GEIFKSLLQG SDLLDSSVNC TEKSEWELKT PEKQLLETLK
1360 1370 1380 1390 1400
CESIPACTTE ELVSGVASPC PKMISDDNWS LLSSEKGPSL SSGLSLPVHP
1410 1420 1430 1440 1450
DVLDESCMFE VSTNLPLSKD NVCSVEKSKP CVSSILLEDL AVSLTVPSPL
1460 1470 1480 1490 1500
KSDGHLSFLK PDMSSSSTPE EVISAHFSED ALLEEEDASE QDIHLALESD
1510 1520 1530 1540 1550
NSSSKSSCSS SWTSRSVAPG FQYHPNLPMH AVIMEKSNDH FIVKIRRATP
1560 1570 1580 1590 1600
STSSGLKQSM MPDELLTSLP RHGKEADEGP EKEYISCQNT VFKSVEELEN
1610 1620 1630 1640 1650
SNKNVDGSKS THEEQSSMIQ TQVPDIYEFL KDASDKMGHS DEVADECFKL
1660 1670 1680 1690 1700
HQVWETKVPE SIEELPSMEE ISHSVGEHLP NTYVDLTKDP VTETKNLGEF
1710 1720 1730 1740 1750
IEVTVLHIDQ LGCSGGNLNQ SAQILDNSLQ ADTVGAFIDL TQDASSEAKS
1760 1770 1780 1790 1800
EGNHPALAVE DLGCGVIQVD EDNCKEEKAQ VANRPLKCIV EETYIDLTTE
1810 1820 1830 1840 1850
SPSSCEVKKD ELKSEPGSNC DNSELPGTLH NSHKKRRNIS DLNHPHKKQR
1860 1870 1880 1890 1900
KETDLTNKEK TKKPTQDSCE NTEAHQKKAS KKKAPPVTKD PSSLKATPGI
1910 1920 1930 1940 1950
KDSSAALATS TSLSAKNVIK KKGEIIILWT RNDDREILLE CQKRGPSFKT
1960 1970 1980
FAYLAAKLDK NPNQVSERFQ QLMKLFEKSK CR
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

« 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 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 29, 2014
This is version 100 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