Full text data of ASCC2
ASCC2
(ASC1P100)
[Confidence: low (only semi-automatic identification from reviews)]
Activating signal cointegrator 1 complex subunit 2 (ASC-1 complex subunit p100; Trip4 complex subunit p100)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Activating signal cointegrator 1 complex subunit 2 (ASC-1 complex subunit p100; Trip4 complex subunit p100)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9H1I8
ID ASCC2_HUMAN Reviewed; 757 AA.
AC Q9H1I8; B7Z8E0; F5H6J9; Q4TT54; Q8TAZ0; Q9H711; Q9H9D6;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 07-MAR-2006, sequence version 3.
DT 22-JAN-2014, entry version 100.
DE RecName: Full=Activating signal cointegrator 1 complex subunit 2;
DE AltName: Full=ASC-1 complex subunit p100;
DE AltName: Full=Trip4 complex subunit p100;
GN Name=ASCC2; Synonyms=ASC1P100;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE,
RP VARIANT GLN-509, AND INTERACTION WITH ASCC1 AND ASCC3.
RC TISSUE=Cervix carcinoma;
RX PubMed=12077347; DOI=10.1128/MCB.22.14.5203-5211.2002;
RA Jung D.-J., Sung H.-S., Goo Y.-W., Lee H.M., Park O.K., Jung S.-Y.,
RA Lim J., Kim H.-J., Lee S.-K., Kim T.S., Lee J.W., Lee Y.C.;
RT "Novel transcription coactivator complex containing activating signal
RT cointegrator 1.";
RL Mol. Cell. Biol. 22:5203-5211(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Colon, Teratocarcinoma, and Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-713, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa
RT cells and high confident phosphopeptide identification by cross-
RT validation of MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-713, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP INTERACTION WITH ALKHB3.
RX PubMed=22055184; DOI=10.1016/j.molcel.2011.08.039;
RA Dango S., Mosammaparast N., Sowa M.E., Xiong L.J., Wu F., Park K.,
RA Rubin M., Gygi S., Harper J.W., Shi Y.;
RT "DNA unwinding by ASCC3 helicase is coupled to ALKBH3-dependent DNA
RT alkylation repair and cancer cell proliferation.";
RL Mol. Cell 44:373-384(2011).
RN [9]
RP STRUCTURE BY NMR OF 463-525.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the CUE domain in the human activating signal
RT cointegrator 1 complex subunit 2 (ASCC2).";
RL Submitted (SEP-2006) to the PDB data bank.
CC -!- FUNCTION: Enhances NF-kappa-B, SRF and AP1 transactivation.
CC -!- SUBUNIT: Part of TRIP4 complex, that contains ASCC1, ASCC2 and
CC ASCC3. The TRIP4 complex interacts with ALKHB3.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9H1I8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H1I8-2; Sequence=VSP_011009, VSP_011010, VSP_011011;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q9H1I8-3; Sequence=VSP_045878, VSP_045879;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the ASCC2 family.
CC -!- SIMILARITY: Contains 1 CUE domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15089.1; Type=Erroneous initiation;
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DR EMBL; AY013289; AAG45475.1; -; mRNA.
DR EMBL; AK022886; BAB14293.1; -; mRNA.
DR EMBL; AK025241; BAB15089.1; ALT_INIT; mRNA.
DR EMBL; AK303257; BAH13926.1; -; mRNA.
DR EMBL; Z82171; CAI95602.1; -; Genomic_DNA.
DR EMBL; AC004882; CAI95602.1; JOINED; Genomic_DNA.
DR EMBL; BC025368; AAH25368.1; -; mRNA.
DR RefSeq; NP_001229835.1; NM_001242906.1.
DR RefSeq; NP_115580.2; NM_032204.4.
DR RefSeq; XP_005261832.1; XM_005261775.1.
DR RefSeq; XP_005261833.1; XM_005261776.1.
DR UniGene; Hs.731754; -.
DR PDB; 2DI0; NMR; -; A=463-525.
DR PDBsum; 2DI0; -.
DR ProteinModelPortal; Q9H1I8; -.
DR SMR; Q9H1I8; 463-525.
DR IntAct; Q9H1I8; 34.
DR MINT; MINT-1182192; -.
DR STRING; 9606.ENSP00000305502; -.
DR PhosphoSite; Q9H1I8; -.
DR DMDM; 92090990; -.
DR PaxDb; Q9H1I8; -.
DR PeptideAtlas; Q9H1I8; -.
DR PRIDE; Q9H1I8; -.
DR Ensembl; ENST00000307790; ENSP00000305502; ENSG00000100325.
DR Ensembl; ENST00000397771; ENSP00000380877; ENSG00000100325.
DR Ensembl; ENST00000542393; ENSP00000437570; ENSG00000100325.
DR GeneID; 84164; -.
DR KEGG; hsa:84164; -.
DR UCSC; uc011akr.2; human.
DR CTD; 84164; -.
DR GeneCards; GC22M030184; -.
DR HGNC; HGNC:24103; ASCC2.
DR HPA; HPA001439; -.
DR MIM; 614216; gene.
DR neXtProt; NX_Q9H1I8; -.
DR PharmGKB; PA134916940; -.
DR eggNOG; NOG245009; -.
DR HOGENOM; HOG000234347; -.
DR HOVERGEN; HBG050589; -.
DR InParanoid; Q9H1I8; -.
DR OMA; MPTILQV; -.
DR OrthoDB; EOG708VZP; -.
DR PhylomeDB; Q9H1I8; -.
DR ChiTaRS; ASCC2; human.
DR EvolutionaryTrace; Q9H1I8; -.
DR GeneWiki; ASCC2; -.
DR GenomeRNAi; 84164; -.
DR NextBio; 73512; -.
DR PRO; PR:Q9H1I8; -.
DR ArrayExpress; Q9H1I8; -.
DR Bgee; Q9H1I8; -.
DR CleanEx; HS_ASCC2; -.
DR Genevestigator; Q9H1I8; -.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR InterPro; IPR003892; CUE.
DR InterPro; IPR009060; UBA-like.
DR Pfam; PF02845; CUE; 1.
DR SMART; SM00546; CUE; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR PROSITE; PS51140; CUE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Phosphoprotein; Polymorphism;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1 757 Activating signal cointegrator 1 complex
FT subunit 2.
FT /FTId=PRO_0000064689.
FT DOMAIN 467 510 CUE.
FT MOD_RES 713 713 Phosphoserine.
FT VAR_SEQ 1 114 Missing (in isoform 2).
FT /FTId=VSP_011009.
FT VAR_SEQ 28 80 Missing (in isoform 3).
FT /FTId=VSP_045878.
FT VAR_SEQ 137 159 Missing (in isoform 3).
FT /FTId=VSP_045879.
FT VAR_SEQ 483 484 GE -> EK (in isoform 2).
FT /FTId=VSP_011010.
FT VAR_SEQ 485 757 Missing (in isoform 2).
FT /FTId=VSP_011011.
FT VARIANT 96 96 R -> C (in dbSNP:rs1894473).
FT /FTId=VAR_050675.
FT VARIANT 123 123 V -> I (in dbSNP:rs11549795).
FT /FTId=VAR_050676.
FT VARIANT 407 407 D -> H (in dbSNP:rs28265).
FT /FTId=VAR_025512.
FT VARIANT 423 423 P -> S (in dbSNP:rs36571).
FT /FTId=VAR_025513.
FT VARIANT 509 509 R -> Q (in dbSNP:rs4823054).
FT /FTId=VAR_019464.
FT VARIANT 546 546 D -> G (in dbSNP:rs34833047).
FT /FTId=VAR_050677.
FT VARIANT 588 588 E -> K (in dbSNP:rs34062345).
FT /FTId=VAR_050678.
FT VARIANT 639 639 R -> L (in dbSNP:rs6006259).
FT /FTId=VAR_025514.
FT CONFLICT 344 344 Q -> H (in Ref. 2; BAB15089).
FT CONFLICT 526 526 K -> N (in Ref. 2; BAB15089).
FT CONFLICT 586 586 R -> C (in Ref. 2; BAB15089).
FT CONFLICT 639 639 R -> G (in Ref. 2; BAH13926).
FT CONFLICT 645 645 P -> L (in Ref. 1; AAG45475).
FT CONFLICT 653 653 P -> L (in Ref. 1; AAG45475).
FT CONFLICT 661 661 D -> G (in Ref. 2; BAH13926).
FT CONFLICT 744 744 T -> I (in Ref. 2; BAH13926).
FT HELIX 466 478
FT HELIX 484 493
FT TURN 494 496
FT HELIX 498 506
FT TURN 512 516
SQ SEQUENCE 757 AA; 86360 MW; BB1DCE21E3068E64 CRC64;
MPALPLDQLQ ITHKDPKTGK LRTSPALHPE QKADRYFVLY KPPPKDNIPA LVEEYLERAT
FVANDLDWLL ALPHDKFWCQ VIFDETLQKC LDSYLRYVPR KFDEGVASAP EVVDMQKRLH
RSVFLTFLRM STHKESKDHF ISPSAFGEIL YNNFLFDIPK ILDLCVLFGK GNSPLLQKMI
GNIFTQQPSY YSDLDETLPT ILQVFSNILQ HCGLQGDGAN TTPQKLEERG RLTPSDMPLL
ELKDIVLYLC DTCTTLWAFL DIFPLACQTF QKHDFCYRLA SFYEAAIPEM ESAIKKRRLE
DSKLLGDLWQ RLSHSRKKLM EIFHIILNQI CLLPILESSC DNIQGFIEEF LQIFSSLLQE
KRFLRDYDAL FPVAEDISLL QQASSVLDET RTAYILQAVE SAWEGVDRRK ATDAKDPSVI
EEPNGEPNGV TVTAEAVSQA SSHPENSEEE ECMGAAAAVG PAMCGVELDS LISQVKDLLP
DLGEGFILAC LEYYHYDPEQ VINNILEERL APTLSQLDRN LDREMKPDPT PLLTSRHNVF
QNDEFDVFSR DSVDLSRVHK GKSTRKEENT RSLLNDKRAV AAQRQRYEQY SVVVEEVPLQ
PGESLPYHSV YYEDEYDDTY DGNQVGANDA DSDDELISRR PFTIPQVLRT KVPREGQEED
DDDEEDDADE EAPKPDHFVQ DPAVLREKAE ARRMAFLAKK GYRHDSSTAV AGSPRGHGQS
RETTQERRKK EANKATRANH NRRTMADRKR SKGMIPS
//
ID ASCC2_HUMAN Reviewed; 757 AA.
AC Q9H1I8; B7Z8E0; F5H6J9; Q4TT54; Q8TAZ0; Q9H711; Q9H9D6;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 07-MAR-2006, sequence version 3.
DT 22-JAN-2014, entry version 100.
DE RecName: Full=Activating signal cointegrator 1 complex subunit 2;
DE AltName: Full=ASC-1 complex subunit p100;
DE AltName: Full=Trip4 complex subunit p100;
GN Name=ASCC2; Synonyms=ASC1P100;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE,
RP VARIANT GLN-509, AND INTERACTION WITH ASCC1 AND ASCC3.
RC TISSUE=Cervix carcinoma;
RX PubMed=12077347; DOI=10.1128/MCB.22.14.5203-5211.2002;
RA Jung D.-J., Sung H.-S., Goo Y.-W., Lee H.M., Park O.K., Jung S.-Y.,
RA Lim J., Kim H.-J., Lee S.-K., Kim T.S., Lee J.W., Lee Y.C.;
RT "Novel transcription coactivator complex containing activating signal
RT cointegrator 1.";
RL Mol. Cell. Biol. 22:5203-5211(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Colon, Teratocarcinoma, and Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-713, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa
RT cells and high confident phosphopeptide identification by cross-
RT validation of MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-713, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP INTERACTION WITH ALKHB3.
RX PubMed=22055184; DOI=10.1016/j.molcel.2011.08.039;
RA Dango S., Mosammaparast N., Sowa M.E., Xiong L.J., Wu F., Park K.,
RA Rubin M., Gygi S., Harper J.W., Shi Y.;
RT "DNA unwinding by ASCC3 helicase is coupled to ALKBH3-dependent DNA
RT alkylation repair and cancer cell proliferation.";
RL Mol. Cell 44:373-384(2011).
RN [9]
RP STRUCTURE BY NMR OF 463-525.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the CUE domain in the human activating signal
RT cointegrator 1 complex subunit 2 (ASCC2).";
RL Submitted (SEP-2006) to the PDB data bank.
CC -!- FUNCTION: Enhances NF-kappa-B, SRF and AP1 transactivation.
CC -!- SUBUNIT: Part of TRIP4 complex, that contains ASCC1, ASCC2 and
CC ASCC3. The TRIP4 complex interacts with ALKHB3.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9H1I8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H1I8-2; Sequence=VSP_011009, VSP_011010, VSP_011011;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q9H1I8-3; Sequence=VSP_045878, VSP_045879;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the ASCC2 family.
CC -!- SIMILARITY: Contains 1 CUE domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15089.1; Type=Erroneous initiation;
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DR EMBL; AY013289; AAG45475.1; -; mRNA.
DR EMBL; AK022886; BAB14293.1; -; mRNA.
DR EMBL; AK025241; BAB15089.1; ALT_INIT; mRNA.
DR EMBL; AK303257; BAH13926.1; -; mRNA.
DR EMBL; Z82171; CAI95602.1; -; Genomic_DNA.
DR EMBL; AC004882; CAI95602.1; JOINED; Genomic_DNA.
DR EMBL; BC025368; AAH25368.1; -; mRNA.
DR RefSeq; NP_001229835.1; NM_001242906.1.
DR RefSeq; NP_115580.2; NM_032204.4.
DR RefSeq; XP_005261832.1; XM_005261775.1.
DR RefSeq; XP_005261833.1; XM_005261776.1.
DR UniGene; Hs.731754; -.
DR PDB; 2DI0; NMR; -; A=463-525.
DR PDBsum; 2DI0; -.
DR ProteinModelPortal; Q9H1I8; -.
DR SMR; Q9H1I8; 463-525.
DR IntAct; Q9H1I8; 34.
DR MINT; MINT-1182192; -.
DR STRING; 9606.ENSP00000305502; -.
DR PhosphoSite; Q9H1I8; -.
DR DMDM; 92090990; -.
DR PaxDb; Q9H1I8; -.
DR PeptideAtlas; Q9H1I8; -.
DR PRIDE; Q9H1I8; -.
DR Ensembl; ENST00000307790; ENSP00000305502; ENSG00000100325.
DR Ensembl; ENST00000397771; ENSP00000380877; ENSG00000100325.
DR Ensembl; ENST00000542393; ENSP00000437570; ENSG00000100325.
DR GeneID; 84164; -.
DR KEGG; hsa:84164; -.
DR UCSC; uc011akr.2; human.
DR CTD; 84164; -.
DR GeneCards; GC22M030184; -.
DR HGNC; HGNC:24103; ASCC2.
DR HPA; HPA001439; -.
DR MIM; 614216; gene.
DR neXtProt; NX_Q9H1I8; -.
DR PharmGKB; PA134916940; -.
DR eggNOG; NOG245009; -.
DR HOGENOM; HOG000234347; -.
DR HOVERGEN; HBG050589; -.
DR InParanoid; Q9H1I8; -.
DR OMA; MPTILQV; -.
DR OrthoDB; EOG708VZP; -.
DR PhylomeDB; Q9H1I8; -.
DR ChiTaRS; ASCC2; human.
DR EvolutionaryTrace; Q9H1I8; -.
DR GeneWiki; ASCC2; -.
DR GenomeRNAi; 84164; -.
DR NextBio; 73512; -.
DR PRO; PR:Q9H1I8; -.
DR ArrayExpress; Q9H1I8; -.
DR Bgee; Q9H1I8; -.
DR CleanEx; HS_ASCC2; -.
DR Genevestigator; Q9H1I8; -.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR InterPro; IPR003892; CUE.
DR InterPro; IPR009060; UBA-like.
DR Pfam; PF02845; CUE; 1.
DR SMART; SM00546; CUE; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR PROSITE; PS51140; CUE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Phosphoprotein; Polymorphism;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1 757 Activating signal cointegrator 1 complex
FT subunit 2.
FT /FTId=PRO_0000064689.
FT DOMAIN 467 510 CUE.
FT MOD_RES 713 713 Phosphoserine.
FT VAR_SEQ 1 114 Missing (in isoform 2).
FT /FTId=VSP_011009.
FT VAR_SEQ 28 80 Missing (in isoform 3).
FT /FTId=VSP_045878.
FT VAR_SEQ 137 159 Missing (in isoform 3).
FT /FTId=VSP_045879.
FT VAR_SEQ 483 484 GE -> EK (in isoform 2).
FT /FTId=VSP_011010.
FT VAR_SEQ 485 757 Missing (in isoform 2).
FT /FTId=VSP_011011.
FT VARIANT 96 96 R -> C (in dbSNP:rs1894473).
FT /FTId=VAR_050675.
FT VARIANT 123 123 V -> I (in dbSNP:rs11549795).
FT /FTId=VAR_050676.
FT VARIANT 407 407 D -> H (in dbSNP:rs28265).
FT /FTId=VAR_025512.
FT VARIANT 423 423 P -> S (in dbSNP:rs36571).
FT /FTId=VAR_025513.
FT VARIANT 509 509 R -> Q (in dbSNP:rs4823054).
FT /FTId=VAR_019464.
FT VARIANT 546 546 D -> G (in dbSNP:rs34833047).
FT /FTId=VAR_050677.
FT VARIANT 588 588 E -> K (in dbSNP:rs34062345).
FT /FTId=VAR_050678.
FT VARIANT 639 639 R -> L (in dbSNP:rs6006259).
FT /FTId=VAR_025514.
FT CONFLICT 344 344 Q -> H (in Ref. 2; BAB15089).
FT CONFLICT 526 526 K -> N (in Ref. 2; BAB15089).
FT CONFLICT 586 586 R -> C (in Ref. 2; BAB15089).
FT CONFLICT 639 639 R -> G (in Ref. 2; BAH13926).
FT CONFLICT 645 645 P -> L (in Ref. 1; AAG45475).
FT CONFLICT 653 653 P -> L (in Ref. 1; AAG45475).
FT CONFLICT 661 661 D -> G (in Ref. 2; BAH13926).
FT CONFLICT 744 744 T -> I (in Ref. 2; BAH13926).
FT HELIX 466 478
FT HELIX 484 493
FT TURN 494 496
FT HELIX 498 506
FT TURN 512 516
SQ SEQUENCE 757 AA; 86360 MW; BB1DCE21E3068E64 CRC64;
MPALPLDQLQ ITHKDPKTGK LRTSPALHPE QKADRYFVLY KPPPKDNIPA LVEEYLERAT
FVANDLDWLL ALPHDKFWCQ VIFDETLQKC LDSYLRYVPR KFDEGVASAP EVVDMQKRLH
RSVFLTFLRM STHKESKDHF ISPSAFGEIL YNNFLFDIPK ILDLCVLFGK GNSPLLQKMI
GNIFTQQPSY YSDLDETLPT ILQVFSNILQ HCGLQGDGAN TTPQKLEERG RLTPSDMPLL
ELKDIVLYLC DTCTTLWAFL DIFPLACQTF QKHDFCYRLA SFYEAAIPEM ESAIKKRRLE
DSKLLGDLWQ RLSHSRKKLM EIFHIILNQI CLLPILESSC DNIQGFIEEF LQIFSSLLQE
KRFLRDYDAL FPVAEDISLL QQASSVLDET RTAYILQAVE SAWEGVDRRK ATDAKDPSVI
EEPNGEPNGV TVTAEAVSQA SSHPENSEEE ECMGAAAAVG PAMCGVELDS LISQVKDLLP
DLGEGFILAC LEYYHYDPEQ VINNILEERL APTLSQLDRN LDREMKPDPT PLLTSRHNVF
QNDEFDVFSR DSVDLSRVHK GKSTRKEENT RSLLNDKRAV AAQRQRYEQY SVVVEEVPLQ
PGESLPYHSV YYEDEYDDTY DGNQVGANDA DSDDELISRR PFTIPQVLRT KVPREGQEED
DDDEEDDADE EAPKPDHFVQ DPAVLREKAE ARRMAFLAKK GYRHDSSTAV AGSPRGHGQS
RETTQERRKK EANKATRANH NRRTMADRKR SKGMIPS
//
MIM
614216
*RECORD*
*FIELD* NO
614216
*FIELD* TI
*614216 ACTIVATING SIGNAL COINTEGRATOR 1 COMPLEX, SUBUNIT 2; ASCC2
;;ASC1 COMPLEX, 100-KD SUBUNIT;;
read morep100
*FIELD* TX
CLONING
By sequencing peptides that copurified with the 650-kD ASC1 (TRIP4;
604501) complex from HeLa cells, followed by database analysis and
screening a HeLa cell cDNA library, Jung et al. (2002) cloned 2 splice
variants of ASCC2. The deduced full-length protein, p100, contains 756
amino acids. The shorter isoform, p100s, lacks 25 internal residues
compared with p100. Northern blot analysis detected variable expression
of an approximately 2.8-kb transcript in all tissues examined. P100
localized to nuclei of HeLa cells. Database analysis revealed orthologs
of p100 in mouse, fly, and frog, but not nematode.
GENE FUNCTION
Jung et al. (2002) identified a 650-kD protein complex containing ASC1,
p50 (ASCC1; 614215), p100, and p200 (ASCC3; 614217). Yeast 2-hybrid
analysis revealed that p100, but not p100s, interacted with ASC1.
Cotransfection of HeLa cells with p100 and ASC1, but not p100s and ASC1,
enhanced ASC1-mediated transactivation of NF-kappa-B (see 164011) and
AP1 (see 165160).
MAPPING
Hartz (2011) mapped the ASCC2 gene to chromosome 22q12.2 based on an
alignment of the ASCC2 sequence (GenBank GENBANK AK025241) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 9/6/2011.
2. Jung, D.-J.; Sung, H.-S.; Goo, Y.-W.; Lee, H. M.; Park, O. K.;
Jung, S.-Y.; Lim, J.; Kim, H.-J.; Lee, S.-K.; Kim, T. S.; Lee, J.
W.; Lee, Y. C.: Novel transcription coactivator complex containing
activating signal cointegrator 1. Molec. Cell. Biol. 22: 5203-5211,
2002.
*FIELD* CD
Patricia A. HJartz: 9/7/2011
*FIELD* ED
mgross: 09/07/2011
*RECORD*
*FIELD* NO
614216
*FIELD* TI
*614216 ACTIVATING SIGNAL COINTEGRATOR 1 COMPLEX, SUBUNIT 2; ASCC2
;;ASC1 COMPLEX, 100-KD SUBUNIT;;
read morep100
*FIELD* TX
CLONING
By sequencing peptides that copurified with the 650-kD ASC1 (TRIP4;
604501) complex from HeLa cells, followed by database analysis and
screening a HeLa cell cDNA library, Jung et al. (2002) cloned 2 splice
variants of ASCC2. The deduced full-length protein, p100, contains 756
amino acids. The shorter isoform, p100s, lacks 25 internal residues
compared with p100. Northern blot analysis detected variable expression
of an approximately 2.8-kb transcript in all tissues examined. P100
localized to nuclei of HeLa cells. Database analysis revealed orthologs
of p100 in mouse, fly, and frog, but not nematode.
GENE FUNCTION
Jung et al. (2002) identified a 650-kD protein complex containing ASC1,
p50 (ASCC1; 614215), p100, and p200 (ASCC3; 614217). Yeast 2-hybrid
analysis revealed that p100, but not p100s, interacted with ASC1.
Cotransfection of HeLa cells with p100 and ASC1, but not p100s and ASC1,
enhanced ASC1-mediated transactivation of NF-kappa-B (see 164011) and
AP1 (see 165160).
MAPPING
Hartz (2011) mapped the ASCC2 gene to chromosome 22q12.2 based on an
alignment of the ASCC2 sequence (GenBank GENBANK AK025241) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 9/6/2011.
2. Jung, D.-J.; Sung, H.-S.; Goo, Y.-W.; Lee, H. M.; Park, O. K.;
Jung, S.-Y.; Lim, J.; Kim, H.-J.; Lee, S.-K.; Kim, T. S.; Lee, J.
W.; Lee, Y. C.: Novel transcription coactivator complex containing
activating signal cointegrator 1. Molec. Cell. Biol. 22: 5203-5211,
2002.
*FIELD* CD
Patricia A. HJartz: 9/7/2011
*FIELD* ED
mgross: 09/07/2011