Full text data of TRAFD1
TRAFD1
(FLN29)
[Confidence: low (only semi-automatic identification from reviews)]
TRAF-type zinc finger domain-containing protein 1 (Protein FLN29)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
TRAF-type zinc finger domain-containing protein 1 (Protein FLN29)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O14545
ID TRAD1_HUMAN Reviewed; 582 AA.
AC O14545; A8K5L6;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JAN-1998, sequence version 1.
DT 22-JAN-2014, entry version 112.
DE RecName: Full=TRAF-type zinc finger domain-containing protein 1;
DE AltName: Full=Protein FLN29;
GN Name=TRAFD1; Synonyms=FLN29;
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].
RC TISSUE=Brain;
RA Nezu J.;
RT "TRAF interacting Zn finger protein.";
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
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 MRNA].
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 [4]
RP FUNCTION, AND INTERACTION WITH TRAF6.
RX PubMed=16221674; DOI=10.1074/jbc.M508221200;
RA Mashima R., Saeki K., Aki D., Minoda Y., Takaki H., Sanada T.,
RA Kobayashi T., Aburatani H., Yamanashi Y., Yoshimura A.;
RT "FLN29, a novel interferon- and LPS-inducible gene acting as a
RT negative regulator of toll-like receptor signaling.";
RL J. Biol. Chem. 280:41289-41297(2005).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327; SER-415 AND
RP SER-470, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327 AND SER-415, AND
RP MASS 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 [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326; SER-327 AND
RP SER-415, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP STRUCTURE BY NMR OF 78-139 IN COMPLEX WITH ZINC IONS.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the ZF-TRAF domain of FLN29 gene product.";
RL Submitted (JUN-2006) to the PDB data bank.
CC -!- FUNCTION: Negative feedback regulator that controls excessive
CC innate immune responses. Regulates both Toll-like receptor 4
CC (TLR4) and DDX58/RIG1-like helicases (RLH) pathways. May inhibit
CC the LTR pathway by direct interaction with TRAF6 and attenuation
CC of NF-kappa-B activation. May negatively regulate the RLH pathway
CC downstream from MAVS and upstream of NF-kappa-B and IRF3 (By
CC similarity).
CC -!- SUBUNIT: Interacts with MAVS, TICAM1, TRAF1, TRAF2, TRAF3 (By
CC similarity). Interacts with TRAF6.
CC -!- SIMILARITY: Contains 1 TRAF-type zinc finger.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB007447; BAA22541.1; -; mRNA.
DR EMBL; BC003553; AAH03553.1; -; mRNA.
DR EMBL; AK291331; BAF84020.1; -; mRNA.
DR RefSeq; NP_001137378.1; NM_001143906.1.
DR RefSeq; NP_006691.1; NM_006700.2.
DR UniGene; Hs.5148; -.
DR PDB; 2D9K; NMR; -; A=78-139.
DR PDBsum; 2D9K; -.
DR ProteinModelPortal; O14545; -.
DR SMR; O14545; 6-40, 78-139.
DR IntAct; O14545; 7.
DR STRING; 9606.ENSP00000257604; -.
DR PhosphoSite; O14545; -.
DR PaxDb; O14545; -.
DR PeptideAtlas; O14545; -.
DR PRIDE; O14545; -.
DR DNASU; 10906; -.
DR Ensembl; ENST00000257604; ENSP00000257604; ENSG00000135148.
DR Ensembl; ENST00000412615; ENSP00000396526; ENSG00000135148.
DR GeneID; 10906; -.
DR KEGG; hsa:10906; -.
DR UCSC; uc001tto.3; human.
DR CTD; 10906; -.
DR GeneCards; GC12P112563; -.
DR HGNC; HGNC:24808; TRAFD1.
DR HPA; HPA039254; -.
DR HPA; HPA039266; -.
DR MIM; 613197; gene.
DR neXtProt; NX_O14545; -.
DR PharmGKB; PA142670704; -.
DR eggNOG; NOG75133; -.
DR HOGENOM; HOG000154674; -.
DR HOVERGEN; HBG094084; -.
DR InParanoid; O14545; -.
DR OMA; HEETECP; -.
DR OrthoDB; EOG76473W; -.
DR PhylomeDB; O14545; -.
DR ChiTaRS; TRAFD1; human.
DR EvolutionaryTrace; O14545; -.
DR GeneWiki; TRAFD1; -.
DR GenomeRNAi; 10906; -.
DR NextBio; 41423; -.
DR PRO; PR:O14545; -.
DR ArrayExpress; O14545; -.
DR Bgee; O14545; -.
DR CleanEx; HS_TRAFD1; -.
DR Genevestigator; O14545; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045824; P:negative regulation of innate immune response; ISS:UniProtKB.
DR GO; GO:0034097; P:response to cytokine stimulus; IEA:Ensembl.
DR InterPro; IPR015880; Znf_C2H2-like.
DR SMART; SM00355; ZnF_C2H2; 1.
DR PROSITE; PS50145; ZF_TRAF; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Metal-binding;
KW Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 582 TRAF-type zinc finger domain-containing
FT protein 1.
FT /FTId=PRO_0000278457.
FT ZN_FING 27 103 TRAF-type.
FT COMPBIAS 577 582 Poly-Glu.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 326 326 Phosphoserine.
FT MOD_RES 327 327 Phosphoserine.
FT MOD_RES 415 415 Phosphoserine.
FT MOD_RES 470 470 Phosphoserine.
FT CONFLICT 138 138 E -> V (in Ref. 2; BAF84020).
FT STRAND 91 93
FT HELIX 99 111
FT STRAND 113 115
FT STRAND 117 119
FT STRAND 122 124
FT HELIX 127 129
FT HELIX 131 134
SQ SEQUENCE 582 AA; 64841 MW; 4937682988851AC0 CRC64;
MAEFLDDQET RLCDNCKKEI PVFNFTIHEI HCQRNIGMCP TCKEPFPKSD METHMAAEHC
QVTCKCNKKL EKRLLKKHEE TECPLRLAVC QHCDLELSIL KLKEHEDYCG ARTELCGNCG
RNVLVKDLKT HPEVCGREGE EKRNEVAIPP NAYDESWGQD GIWIASQLLR QIEALDPPMR
LPRRPLRAFE SDVFHNRTTN QRNITAQVSI QNNLFEEQER QERNRGQQPP KEGGEESANL
DFMLALSLQN EGQASSVAEQ DFWRAVCEAD QSHGGPRSLS DIKGAADEIM LPCEFCEELY
PEELLIDHQT SCNPSRALPS LNTGSSSPRG VEEPDVIFQN FLQQAASNQL DSLMGLSNSH
PVEESIIIPC EFCGVQLEEE VLFHHQDQCD QRPATATNHV TEGIPRLDSQ PQETSPELPR
RRVRHQGDLS SGYLDDTKQE TANGPTSCLP PSRPINNMTA TYNQLSRSTS GPRPGCQPSS
PCVPKLSNSD SQDIQGRNRD SQNGAIAPGH VSVIRPPQNL YPENIVPSFS PGPSGRYGAS
GRSEGGRNSR VTPAAANYRS RTAKAKPSKQ QGAGDAEEEE EE
//
ID TRAD1_HUMAN Reviewed; 582 AA.
AC O14545; A8K5L6;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JAN-1998, sequence version 1.
DT 22-JAN-2014, entry version 112.
DE RecName: Full=TRAF-type zinc finger domain-containing protein 1;
DE AltName: Full=Protein FLN29;
GN Name=TRAFD1; Synonyms=FLN29;
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].
RC TISSUE=Brain;
RA Nezu J.;
RT "TRAF interacting Zn finger protein.";
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
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 MRNA].
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 [4]
RP FUNCTION, AND INTERACTION WITH TRAF6.
RX PubMed=16221674; DOI=10.1074/jbc.M508221200;
RA Mashima R., Saeki K., Aki D., Minoda Y., Takaki H., Sanada T.,
RA Kobayashi T., Aburatani H., Yamanashi Y., Yoshimura A.;
RT "FLN29, a novel interferon- and LPS-inducible gene acting as a
RT negative regulator of toll-like receptor signaling.";
RL J. Biol. Chem. 280:41289-41297(2005).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327; SER-415 AND
RP SER-470, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327 AND SER-415, AND
RP MASS 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 [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326; SER-327 AND
RP SER-415, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP STRUCTURE BY NMR OF 78-139 IN COMPLEX WITH ZINC IONS.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the ZF-TRAF domain of FLN29 gene product.";
RL Submitted (JUN-2006) to the PDB data bank.
CC -!- FUNCTION: Negative feedback regulator that controls excessive
CC innate immune responses. Regulates both Toll-like receptor 4
CC (TLR4) and DDX58/RIG1-like helicases (RLH) pathways. May inhibit
CC the LTR pathway by direct interaction with TRAF6 and attenuation
CC of NF-kappa-B activation. May negatively regulate the RLH pathway
CC downstream from MAVS and upstream of NF-kappa-B and IRF3 (By
CC similarity).
CC -!- SUBUNIT: Interacts with MAVS, TICAM1, TRAF1, TRAF2, TRAF3 (By
CC similarity). Interacts with TRAF6.
CC -!- SIMILARITY: Contains 1 TRAF-type zinc finger.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB007447; BAA22541.1; -; mRNA.
DR EMBL; BC003553; AAH03553.1; -; mRNA.
DR EMBL; AK291331; BAF84020.1; -; mRNA.
DR RefSeq; NP_001137378.1; NM_001143906.1.
DR RefSeq; NP_006691.1; NM_006700.2.
DR UniGene; Hs.5148; -.
DR PDB; 2D9K; NMR; -; A=78-139.
DR PDBsum; 2D9K; -.
DR ProteinModelPortal; O14545; -.
DR SMR; O14545; 6-40, 78-139.
DR IntAct; O14545; 7.
DR STRING; 9606.ENSP00000257604; -.
DR PhosphoSite; O14545; -.
DR PaxDb; O14545; -.
DR PeptideAtlas; O14545; -.
DR PRIDE; O14545; -.
DR DNASU; 10906; -.
DR Ensembl; ENST00000257604; ENSP00000257604; ENSG00000135148.
DR Ensembl; ENST00000412615; ENSP00000396526; ENSG00000135148.
DR GeneID; 10906; -.
DR KEGG; hsa:10906; -.
DR UCSC; uc001tto.3; human.
DR CTD; 10906; -.
DR GeneCards; GC12P112563; -.
DR HGNC; HGNC:24808; TRAFD1.
DR HPA; HPA039254; -.
DR HPA; HPA039266; -.
DR MIM; 613197; gene.
DR neXtProt; NX_O14545; -.
DR PharmGKB; PA142670704; -.
DR eggNOG; NOG75133; -.
DR HOGENOM; HOG000154674; -.
DR HOVERGEN; HBG094084; -.
DR InParanoid; O14545; -.
DR OMA; HEETECP; -.
DR OrthoDB; EOG76473W; -.
DR PhylomeDB; O14545; -.
DR ChiTaRS; TRAFD1; human.
DR EvolutionaryTrace; O14545; -.
DR GeneWiki; TRAFD1; -.
DR GenomeRNAi; 10906; -.
DR NextBio; 41423; -.
DR PRO; PR:O14545; -.
DR ArrayExpress; O14545; -.
DR Bgee; O14545; -.
DR CleanEx; HS_TRAFD1; -.
DR Genevestigator; O14545; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045824; P:negative regulation of innate immune response; ISS:UniProtKB.
DR GO; GO:0034097; P:response to cytokine stimulus; IEA:Ensembl.
DR InterPro; IPR015880; Znf_C2H2-like.
DR SMART; SM00355; ZnF_C2H2; 1.
DR PROSITE; PS50145; ZF_TRAF; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Metal-binding;
KW Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 582 TRAF-type zinc finger domain-containing
FT protein 1.
FT /FTId=PRO_0000278457.
FT ZN_FING 27 103 TRAF-type.
FT COMPBIAS 577 582 Poly-Glu.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 326 326 Phosphoserine.
FT MOD_RES 327 327 Phosphoserine.
FT MOD_RES 415 415 Phosphoserine.
FT MOD_RES 470 470 Phosphoserine.
FT CONFLICT 138 138 E -> V (in Ref. 2; BAF84020).
FT STRAND 91 93
FT HELIX 99 111
FT STRAND 113 115
FT STRAND 117 119
FT STRAND 122 124
FT HELIX 127 129
FT HELIX 131 134
SQ SEQUENCE 582 AA; 64841 MW; 4937682988851AC0 CRC64;
MAEFLDDQET RLCDNCKKEI PVFNFTIHEI HCQRNIGMCP TCKEPFPKSD METHMAAEHC
QVTCKCNKKL EKRLLKKHEE TECPLRLAVC QHCDLELSIL KLKEHEDYCG ARTELCGNCG
RNVLVKDLKT HPEVCGREGE EKRNEVAIPP NAYDESWGQD GIWIASQLLR QIEALDPPMR
LPRRPLRAFE SDVFHNRTTN QRNITAQVSI QNNLFEEQER QERNRGQQPP KEGGEESANL
DFMLALSLQN EGQASSVAEQ DFWRAVCEAD QSHGGPRSLS DIKGAADEIM LPCEFCEELY
PEELLIDHQT SCNPSRALPS LNTGSSSPRG VEEPDVIFQN FLQQAASNQL DSLMGLSNSH
PVEESIIIPC EFCGVQLEEE VLFHHQDQCD QRPATATNHV TEGIPRLDSQ PQETSPELPR
RRVRHQGDLS SGYLDDTKQE TANGPTSCLP PSRPINNMTA TYNQLSRSTS GPRPGCQPSS
PCVPKLSNSD SQDIQGRNRD SQNGAIAPGH VSVIRPPQNL YPENIVPSFS PGPSGRYGAS
GRSEGGRNSR VTPAAANYRS RTAKAKPSKQ QGAGDAEEEE EE
//
MIM
613197
*RECORD*
*FIELD* NO
613197
*FIELD* TI
*613197 TRAF-TYPE ZINC FINGER DOMAIN-CONTAINING 1; TRAFD1
;;FLN29
*FIELD* TX
DESCRIPTION
read more
The innate immune system confers host defense against viral and
microbial infection, and TRAFD1 is a negative feedback regulator that
controls excessive immune responses (Sanada et al., 2008).
CLONING
Using microarray analysis to identify genes upregulated in mouse
macrophages by lipopolysaccharide (LPS), followed by RT-PCR of human
HEK293 cells and the mouse RAW macrophage line, Mashima et al. (2005)
cloned human and mouse TRAFD1, which they called FLN29. The deduced
human and mouse proteins contain 582 and 576 amino acids, respectively.
TRAFD1 has an N-terminal RING finger domain, followed by a zinc finger
domain, and TRAF-N and TRAF-C domains. Northern blot analysis of mouse
tissues showed expression skeletal muscle, brain, kidney, spleen, and
bone marrow.
GENE FUNCTION
Mashima et al. (2005) found that the expression of Fln29 was upregulated
in mouse RAW cells by LPS, IFN-beta (IFNB; 147640), and IFN-gamma (IFNG;
147570). Use of Stat1 (600555)-deficient mouse bone marrow-derived
macrophages and mouse embryonic fibroblasts (MEFs) showed that Stat1 was
required for Fln29 upregulation by LPS and IFNB. Exogenous
overexpression of Fln29 in LPS-pretreated RAW cells resulted in the
suppression of TLR4 (603030)-mediated NF-kappa B (see 164011) and
activation of MAP kinase (see MAPK1, 176948). Small interfering
RNA-induced downregulation of Fln29 reversed these effects and increased
the production of nitrous oxide. Fln29 inhibited Toll-like receptor
(TLR) signaling by interacting directly with Traf6 (602355). Mashima et
al. (2005) concluded that FLN29 is activated by STAT1 and functions as a
negative feedback regulator of TLR signaling downstream of TRAF6.
By immunoprecipitation of transfected HEK293 cells, Sanada et al. (2008)
found that mouse Fln29 interacted with IPS1 (MAVS; 609676), TRIF
(TICAM1; 607601), TRAF1 (601711), TRAF2 (601895), and TRAF3 (601896).
Overexpression of mouse Fln29 inhibited IPS1-dependent IRF3 (603734)
activation.
MAPPING
Hartz (2009) mapped the TRAFD1 gene to chromosome 12q24.13 based on an
alignment of the TRAFD1 sequence (GenBank GENBANK AB007447) with the
genomic sequence (GRCh37).
ANIMAL MODEL
Sanada et al. (2008) found that Fln29 -/- mice were born at the expected
mendelian ratio and showed no gross developmental abnormalities.
However, they mounted an exaggerated response to LPS and to poly(I:C), a
synthetic double-stranded RNA that stimulates both the Toll-like
receptor and RIGI (DDX58; 609631)-like helicase (RLH) response pathways.
Bone marrow-derived dendritic cells from Fln29 -/- animals, but not
wildtype animals, showed augmented LPS-induced activation of Ikk (see
CHUK, 600664) and Jnk (see MAPK8, 601158). Mutant mice were
significantly more sensitive than wildtype mice to poly(I:C)-induced
septic shock. They suffered more severe hepatic damage and showed
elevated serum Il6 (147620) levels. Finally, Fln29 -/- MEFs were more
resistant to vesicular stomatitis virus (VSV) cytopathic effects, with
lower virus titer than in wildtype MEFs due to reduced VSV replication.
Sanada et al. (2008) concluded that FLN29 is a negative regulator of
both TLR- and RLH-mediated innate immune responses.
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 12/28/2009.
2. Mashima, R.; Saeki, K.; Aki, D.; Minoda, Y.; Takaki, H.; Sanada,
T.; Kobayashi, T.; Aburatani, H.; Yamanashi, Y.; Yoshimura, A.: FLN29,
a novel interferon- and LPS-inducible gene acting as a negative regulator
of Toll-like receptor signaling. J. Biol. Chem. 280: 41289-41297,
2005.
3. Sanada, T.; Takaesu, G.; Mashima, R.; Yoshida, R.; Kobayashi, T.;
Yoshimura, A.: FLN29 deficiency reveals its negative regulatory role
in the Toll-like receptor (TLR) and retinoic acid-inducible gene 1
(RIG-I)-like helicase signaling pathway. J. Biol. Chem. 283: 33858-33864,
2008.
*FIELD* CD
Patricia A. Hartz: 12/29/2009
*FIELD* ED
wwang: 12/29/2009
*RECORD*
*FIELD* NO
613197
*FIELD* TI
*613197 TRAF-TYPE ZINC FINGER DOMAIN-CONTAINING 1; TRAFD1
;;FLN29
*FIELD* TX
DESCRIPTION
read more
The innate immune system confers host defense against viral and
microbial infection, and TRAFD1 is a negative feedback regulator that
controls excessive immune responses (Sanada et al., 2008).
CLONING
Using microarray analysis to identify genes upregulated in mouse
macrophages by lipopolysaccharide (LPS), followed by RT-PCR of human
HEK293 cells and the mouse RAW macrophage line, Mashima et al. (2005)
cloned human and mouse TRAFD1, which they called FLN29. The deduced
human and mouse proteins contain 582 and 576 amino acids, respectively.
TRAFD1 has an N-terminal RING finger domain, followed by a zinc finger
domain, and TRAF-N and TRAF-C domains. Northern blot analysis of mouse
tissues showed expression skeletal muscle, brain, kidney, spleen, and
bone marrow.
GENE FUNCTION
Mashima et al. (2005) found that the expression of Fln29 was upregulated
in mouse RAW cells by LPS, IFN-beta (IFNB; 147640), and IFN-gamma (IFNG;
147570). Use of Stat1 (600555)-deficient mouse bone marrow-derived
macrophages and mouse embryonic fibroblasts (MEFs) showed that Stat1 was
required for Fln29 upregulation by LPS and IFNB. Exogenous
overexpression of Fln29 in LPS-pretreated RAW cells resulted in the
suppression of TLR4 (603030)-mediated NF-kappa B (see 164011) and
activation of MAP kinase (see MAPK1, 176948). Small interfering
RNA-induced downregulation of Fln29 reversed these effects and increased
the production of nitrous oxide. Fln29 inhibited Toll-like receptor
(TLR) signaling by interacting directly with Traf6 (602355). Mashima et
al. (2005) concluded that FLN29 is activated by STAT1 and functions as a
negative feedback regulator of TLR signaling downstream of TRAF6.
By immunoprecipitation of transfected HEK293 cells, Sanada et al. (2008)
found that mouse Fln29 interacted with IPS1 (MAVS; 609676), TRIF
(TICAM1; 607601), TRAF1 (601711), TRAF2 (601895), and TRAF3 (601896).
Overexpression of mouse Fln29 inhibited IPS1-dependent IRF3 (603734)
activation.
MAPPING
Hartz (2009) mapped the TRAFD1 gene to chromosome 12q24.13 based on an
alignment of the TRAFD1 sequence (GenBank GENBANK AB007447) with the
genomic sequence (GRCh37).
ANIMAL MODEL
Sanada et al. (2008) found that Fln29 -/- mice were born at the expected
mendelian ratio and showed no gross developmental abnormalities.
However, they mounted an exaggerated response to LPS and to poly(I:C), a
synthetic double-stranded RNA that stimulates both the Toll-like
receptor and RIGI (DDX58; 609631)-like helicase (RLH) response pathways.
Bone marrow-derived dendritic cells from Fln29 -/- animals, but not
wildtype animals, showed augmented LPS-induced activation of Ikk (see
CHUK, 600664) and Jnk (see MAPK8, 601158). Mutant mice were
significantly more sensitive than wildtype mice to poly(I:C)-induced
septic shock. They suffered more severe hepatic damage and showed
elevated serum Il6 (147620) levels. Finally, Fln29 -/- MEFs were more
resistant to vesicular stomatitis virus (VSV) cytopathic effects, with
lower virus titer than in wildtype MEFs due to reduced VSV replication.
Sanada et al. (2008) concluded that FLN29 is a negative regulator of
both TLR- and RLH-mediated innate immune responses.
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 12/28/2009.
2. Mashima, R.; Saeki, K.; Aki, D.; Minoda, Y.; Takaki, H.; Sanada,
T.; Kobayashi, T.; Aburatani, H.; Yamanashi, Y.; Yoshimura, A.: FLN29,
a novel interferon- and LPS-inducible gene acting as a negative regulator
of Toll-like receptor signaling. J. Biol. Chem. 280: 41289-41297,
2005.
3. Sanada, T.; Takaesu, G.; Mashima, R.; Yoshida, R.; Kobayashi, T.;
Yoshimura, A.: FLN29 deficiency reveals its negative regulatory role
in the Toll-like receptor (TLR) and retinoic acid-inducible gene 1
(RIG-I)-like helicase signaling pathway. J. Biol. Chem. 283: 33858-33864,
2008.
*FIELD* CD
Patricia A. Hartz: 12/29/2009
*FIELD* ED
wwang: 12/29/2009