Q9UKL3 (C8AP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
CASP8-associated protein 2

Alternative name(s):
FLICE-associated huge protein

Gene names

Name:	CASP8AP2
Synonyms:	FLASH, KIAA1315, RIP25

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1982 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Nucleus › PML 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 process	Apoptosis Cell cycle Transcription Transcription regulation
Cellular component	Cytoplasm Mitochondrion Nucleus
Coding sequence diversity	Polymorphism
Molecular function	Activator Repressor
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Fas signaling pathway Inferred from mutant phenotype Ref.13. Source: UniProtKB 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-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	PML body Inferred from direct assay Ref.13. Source: UniProtKB mitochondrion Inferred from direct assay Ref.13. Source: UniProtKB
Molecular_function	DNA 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 transcription corepressor activity Inferred from direct assay Ref.10. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PIAS1	O75925	4	EBI-2339650,EBI-629434

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.18

Chain

2 – 1982

1981

CASP8-associated protein 2

PRO_0000076188

Regions

Region

1709 – 1982

274

NCOA2-binding Ref.10

Motif

1683 – 1687

5

SUMO interaction motif 1 (SIM); mediates the binding to polysumoylated substrates By similarity

Motif

1737 – 1741

5

SUMO interaction motif 2 (SIM); mediates the binding to polysumoylated substrates By similarity

Motif

1794 – 1798

5

SUMO interaction motif 3 (SIM); mediates the binding to polysumoylated substrates By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.18

Modified residue

20

1

Phosphoserine Ref.18

Cross-link

92

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.14

Cross-link

93

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.14

Natural variations

Natural variant

1659

1

P → S.
Corresponds to variant rs3799896 [ dbSNP | Ensembl ].

VAR_050700

Experimental info

Sequence conflict

278

1

L → S in AAD45537. Ref.2

Sequence conflict

362

1

D → E in AAH56685. Ref.7

Sequence conflict

638

1

L → P in AAD45537. Ref.2

Sequence conflict

668

1

M → T in AAD45537. Ref.2

Sequence conflict

861

1

N → S in AAD45537. Ref.2

Sequence conflict

1713

1

C → Y in AAD45537. Ref.2

Sequence conflict

1754

1

Missing in BAA92553. Ref.3

Sequence conflict

1832

1

S → P in BAA92067. Ref.8

Secondary structure

1

.

.

.

.

.

.

.

.

.

1982

Helix Strand Turn

Details...

Beta strand

1925 – 1927

3

Helix

1931 – 1943

13

Helix

1948 – 1958

11

Helix

1962 – 1977

16

Sequences

	Sequence		Length	Mass (Da)
	Q9UKL3 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: AF2B1A7798C19E39	FASTA	1,982	222,658
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE. 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.

IPI

IPI00100798.

RefSeq

NP_001131139.1. NM_001137667.1.
NP_001131140.1. NM_001137668.1.
NP_036247.1. NM_012115.3.

UniGene

Hs.558218.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2LR8	NMR	-	A	1916-1982	[»]

ProteinModelPortal

Q9UKL3.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-40986N.

IntAct

Q9UKL3. 8 interactions.

MINT

MINT-91616.

STRING

9606.ENSP00000391210.

PTM databases

PhosphoSite

Q9UKL3.

Polymorphism databases

DMDM

74721007.

Proteomic databases

PaxDb

Q9UKL3.

PRIDE

Q9UKL3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

9994.

KEGG

hsa:9994.

UCSC

uc003pnr.3. human.

Organism-specific databases

CTD

9994.

GeneCards

GC06P090539.

HGNC

HGNC:1510. CASP8AP2.

MIM

606880. gene.

neXtProt

NX_Q9UKL3.

PharmGKB

PA26093.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG42694.

HOVERGEN

HBG080371.

InParanoid

Q9UKL3.

Gene expression databases

CleanEx

HS_CASP8AP2.

Genevestigator

Q9UKL3.

Family and domain databases

Gene3D

1.10.10.60. 1 hit.

InterPro

IPR009057. Homeodomain-like.
[Graphical view]

SUPFAM

SSF46689. Homeodomain_like. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

CASP8AP2. human.

GenomeRNAi

9994.

NextBio

37755.

SOURCE

Search...

Entry information

Entry name

C8AP2_HUMAN

Accession

Primary (citable) accession number: Q9UKL3
Secondary accession number(s): A2RUB7 , 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:	May 29, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.