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Q9UKL3 (C8AP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CASP8-associated protein 2
Alternative name(s):
FLICE-associated huge protein
Gene names
Name:CASP8AP2
Synonyms:FLASH, KIAA1315, RIP25
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1982 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10 Ref.11 Ref.12 Ref.13 UniProtKB Q9WUF3

Subunit structure

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. Ref.10 Ref.11 Ref.12 Ref.13 Ref.16 Ref.19 UniProtKB Q9WUF3

Subcellular location

Cytoplasm. Nucleus. NucleusPML body. Mitochondrion. Note: Exported from the nucleus to the mitochondria upon FAS activation. Ref.10 Ref.12 Ref.13

Induction

By TNF which induces strong nuclear localization. Ref.10

Sequence caution

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.

Ontologies

Keywords
   Biological processApoptosis
Cell cycle
Transcription
Transcription regulation
   Cellular componentCytoplasm
Mitochondrion
Nucleus
   Coding sequence diversityPolymorphism
   Molecular functionActivator
Repressor
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFas signaling pathway

Inferred from mutant phenotype Ref.13. Source: UniProtKB

activation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from mutant phenotype Ref.13. Source: UniProtKB

apoptotic signaling pathway

Traceable author statement PubMed 10235259. Source: ProtInc

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to mechanical stimulus

Inferred from expression pattern PubMed 19593445. Source: UniProtKB

extrinsic apoptotic signaling pathway via death domain receptors

Inferred from mutant phenotype Ref.13. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

signal transduction

Traceable author statement PubMed 10235259. Source: ProtInc

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentPML body

Inferred from direct assay Ref.13. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.10Ref.13. Source: UniProtKB

mitochondrion

Inferred from direct assay Ref.13. Source: UniProtKB

nucleus

Inferred from direct assay Ref.10. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: InterPro

SUMO polymer binding

Inferred from direct assay Ref.19. Source: UniProtKB

cysteine-type endopeptidase activator activity involved in apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

death receptor binding

Traceable author statement PubMed 10235259. Source: ProtInc

peptidase activator activity involved in apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.10Ref.11Ref.13. Source: UniProtKB

transcription corepressor activity

Inferred from direct assay Ref.10. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.18
Chain2 – 19821981CASP8-associated protein 2
PRO_0000076188

Regions

Region1709 – 1982274NCOA2-binding Ref.10
Motif1683 – 16875SUMO interaction motif 1 (SIM); mediates the binding to polysumoylated substrates By similarity
Motif1737 – 17415SUMO interaction motif 2 (SIM); mediates the binding to polysumoylated substrates By similarity
Motif1794 – 17985SUMO interaction motif 3 (SIM); mediates the binding to polysumoylated substrates By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.18
Modified residue201Phosphoserine Ref.18
Modified residue13431N6-acetyllysine By similarity
Cross-link92Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.14
Cross-link93Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.14

Natural variations

Natural variant16591P → S.
Corresponds to variant rs3799896 [ dbSNP | Ensembl ].
VAR_050700

Experimental info

Sequence conflict2781L → S in AAD45537. Ref.2
Sequence conflict3621D → E in AAH56685. Ref.7
Sequence conflict6381L → P in AAD45537. Ref.2
Sequence conflict6681M → T in AAD45537. Ref.2
Sequence conflict8611N → S in AAD45537. Ref.2
Sequence conflict17131C → Y in AAD45537. Ref.2
Sequence conflict17541Missing in BAA92553. Ref.3
Sequence conflict18321S → P in BAA92067. Ref.8

Secondary structure

......... 1982
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9UKL3 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: AF2B1A7798C19E39

FASTA1,982222,658
        10         20         30         40         50         60 
MAADDDNGDG TSLFDVFSAS PLKNNDEGSL DIYAGLDSAV SDSASKSCVP SRNCLDLYEE 

        70         80         90        100        110        120 
ILTEEGTAKE ATYNDLQVEY GKCQLQMKEL MKKFKEIQTQ NFSLINENQS LKKNISALIK 

       130        140        150        160        170        180 
TARVEINRKD EEISNLHQRL SEFPHFRNNH KTARTFDTVK TKDLKSRSPH LDDCSKTDHR 

       190        200        210        220        230        240 
AKSDVSKDVH HSTSLPNLEK EGKPHSDKRS TSHLPTSVEK HCTNGVWSRS HYQVGEGSSN 

       250        260        270        280        290        300 
EDSRRGRKDI RHSQFNRGTE RVRKDLSTGC GDGEPRILEA SQRLQGHPEK YGKGEPKTES 

       310        320        330        340        350        360 
KSSKFKSNSD SDYKGERINS SWEKETPGER SHSRVDSQSD KKLERQSERS QNINRKEVKS 

       370        380        390        400        410        420 
QDKEERKVDQ KPKSVVKDQD HWRRSERASL PHSKNEITFS HNSSKYHLEE RRGWEDCKRD 

       430        440        450        460        470        480 
KSVNSHSFQD GRCPSSLSNS RTHKNIDSKE VDAMHQWENT PLKAERHRTE DKRKREQESK 

       490        500        510        520        530        540 
EENRHIRNEK RVPTEHLQKT NKETKKTTTD LKKQNEPKTD KGEVLDNGVS EGADNKELAM 

       550        560        570        580        590        600 
KAESGPNETK NKDLKLSFMK KLNLTLSPAK KQPVSQDNQH KITDIPKSSG VCDSESSMQV 

       610        620        630        640        650        660 
KTVAYVPSIS EHILGEAAVS EHTMGETKST LLEPKVALLA VTEPRIGISE TNKEDENSLL 

       670        680        690        700        710        720 
VRSVDNTMHC EEPICGTETS FPSPMEIQQT ESLFPSTGMK QTINNGRAAA PVVMDVLQTD 

       730        740        750        760        770        780 
VSQNFGLELD TKRNDNSDYC GISEGMEMKV ALSTTVSETT ESILQPSIEE ADILPIMLSE 

       790        800        810        820        830        840 
DNNPKFEPSV IVTPLVESKS CHLEPCLPKE TLDSSLQQTE LMDHRMATGE TNSVYHDDDN 

       850        860        870        880        890        900 
SVLSIDLNHL RPIPEAISPL NSPVRPVAKV LRNESPPQVP VYNNSHKDVF LPNSAHSTSK 

       910        920        930        940        950        960 
SQSDLNKENQ KPIYKSDKCT EADTCKNSPL DELEEGEIRS DSETSKPQES FEKNSKRRVS 

       970        980        990       1000       1010       1020 
ADVRKSKTIP RRGKSTVCLD KDSRKTHVRI HQTNNKWNKR PDKSSRSSKT EKKDKVMSTS 

      1030       1040       1050       1060       1070       1080 
SLEKIVPIIA VPSSEQEIMH MLRMIRKHVR KNYMKFKAKF SLIQFHRIIE SAILSFTSLI 

      1090       1100       1110       1120       1130       1140 
KHLNLHKISK SVTTLQKNLC DIIESKLKQV KKNGIVDRLF EQQLPDMKKK LWKFVDDQLD 

      1150       1160       1170       1180       1190       1200 
YLFAKLKKIL VCDSKSFGRD SDEGKLEKTS KQNAQYSNSQ KRSVDNSNRE LLKEKLSKSE 

      1210       1220       1230       1240       1250       1260 
DPVHYKSLVG CKKSEENYQD QNNSSINTVK HDIKKNFNIC FDNIKNSQSE ERSLEVHCPS 

      1270       1280       1290       1300       1310       1320 
TPKSEKNEGS SIEDAQTSQH ATLKPERSFE ILTEQQASSL TFNLVSDAQM GEIFKSLLQG 

      1330       1340       1350       1360       1370       1380 
SDLLDSSVNC TEKSEWELKT PEKQLLETLK CESIPACTTE ELVSGVASPC PKMISDDNWS 

      1390       1400       1410       1420       1430       1440 
LLSSEKGPSL SSGLSLPVHP DVLDESCMFE VSTNLPLSKD NVCSVEKSKP CVSSILLEDL 

      1450       1460       1470       1480       1490       1500 
AVSLTVPSPL KSDGHLSFLK PDMSSSSTPE EVISAHFSED ALLEEEDASE QDIHLALESD 

      1510       1520       1530       1540       1550       1560 
NSSSKSSCSS SWTSRSVAPG FQYHPNLPMH AVIMEKSNDH FIVKIRRATP STSSGLKQSM 

      1570       1580       1590       1600       1610       1620 
MPDELLTSLP RHGKEADEGP EKEYISCQNT VFKSVEELEN SNKNVDGSKS THEEQSSMIQ 

      1630       1640       1650       1660       1670       1680 
TQVPDIYEFL KDASDKMGHS DEVADECFKL HQVWETKVPE SIEELPSMEE ISHSVGEHLP 

      1690       1700       1710       1720       1730       1740 
NTYVDLTKDP VTETKNLGEF IEVTVLHIDQ LGCSGGNLNQ SAQILDNSLQ ADTVGAFIDL 

      1750       1760       1770       1780       1790       1800 
TQDASSEAKS EGNHPALAVE DLGCGVIQVD EDNCKEEKAQ VANRPLKCIV EETYIDLTTE 

      1810       1820       1830       1840       1850       1860 
SPSSCEVKKD ELKSEPGSNC DNSELPGTLH NSHKKRRNIS DLNHPHKKQR KETDLTNKEK 

      1870       1880       1890       1900       1910       1920 
TKKPTQDSCE NTEAHQKKAS KKKAPPVTKD PSSLKATPGI KDSSAALATS TSLSAKNVIK 

      1930       1940       1950       1960       1970       1980 
KKGEIIILWT RNDDREILLE CQKRGPSFKT FAYLAAKLDK NPNQVSERFQ QLMKLFEKSK 


CR 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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. expand/collapse author list , 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]"Apoptosis. Searching for FLASH domains."
Koonin E.V., Aravind L., Hofmann K., Tschopp J., Dixit V.M.
Nature 401:662-662(1999) [PubMed] [Europe PMC] [Abstract]
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]"FLASH is required for histone transcription and S-phase progression."
Barcaroli D., Bongiorno-Borbone L., Terrinoni A., Hofmann T.G., Rossi M., Knight R.A., Matera A.G., Melino G., De Laurenzi V.
Proc. Natl. Acad. Sci. U.S.A. 103:14808-14812(2006) [PubMed] [Europe PMC] [Abstract]
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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001131139.1. NM_001137667.1.
NP_001131140.1. NM_001137668.1.
NP_036247.1. NM_012115.3.
UniGeneHs.558218.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LR8NMR-A1916-1982[»]
ProteinModelPortalQ9UKL3.
SMRQ9UKL3. Positions 1916-1982.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115315. 18 interactions.
DIPDIP-40986N.
IntActQ9UKL3. 12 interactions.
MINTMINT-91616.
STRING9606.ENSP00000391210.

PTM databases

PhosphoSiteQ9UKL3.

Polymorphism databases

DMDM74721007.

Proteomic databases

MaxQBQ9UKL3.
PaxDbQ9UKL3.
PRIDEQ9UKL3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID9994.
KEGGhsa:9994.
UCSCuc003pnr.3. human.

Organism-specific databases

CTD9994.
GeneCardsGC06P090539.
HGNCHGNC:1510. CASP8AP2.
MIM606880. gene.
neXtProtNX_Q9UKL3.
PharmGKBPA26093.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG42694.
HOVERGENHBG080371.
InParanoidQ9UKL3.
PhylomeDBQ9UKL3.

Gene expression databases

CleanExHS_CASP8AP2.
GenevestigatorQ9UKL3.

Family and domain databases

Gene3D1.10.10.60. 1 hit.
InterProIPR009057. Homeodomain-like.
[Graphical view]
SUPFAMSSF46689. SSF46689. 1 hit.
ProtoNetSearch...

Other

ChiTaRSCASP8AP2. human.
GeneWikiCASP8AP2.
GenomeRNAi9994.
NextBio37755.
PROQ9UKL3.
SOURCESearch...

Entry information

Entry nameC8AP2_HUMAN
AccessionPrimary (citable) accession number: Q9UKL3
Secondary accession number(s): A2RUB7 expand/collapse secondary AC list , E1P553, Q6PH76, Q7LCQ7, Q86YD9, Q9NUQ4, Q9NZV9, Q9P2N1, Q9Y563
Entry history
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 statusReviewed (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.

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM