Full text data of TRIM56
TRIM56
(RNF109)
[Confidence: low (only semi-automatic identification from reviews)]
E3 ubiquitin-protein ligase TRIM56; 6.3.2.- (RING finger protein 109; Tripartite motif-containing protein 56)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
E3 ubiquitin-protein ligase TRIM56; 6.3.2.- (RING finger protein 109; Tripartite motif-containing protein 56)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9BRZ2
ID TRI56_HUMAN Reviewed; 755 AA.
AC Q9BRZ2; Q6PJS5; Q86VT6; Q8N2H8; Q8NAC0; Q9H031;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 21-DEC-2004, sequence version 3.
DT 22-JAN-2014, entry version 105.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM56;
DE EC=6.3.2.-;
DE AltName: Full=RING finger protein 109;
DE AltName: Full=Tripartite motif-containing protein 56;
GN Name=TRIM56; Synonyms=RNF109;
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 [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 429-755 (ISOFORM 1).
RC TISSUE=Spleen, and Thyroid;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lymph, and Placenta;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 572-755 (ISOFORM 1).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475, AND MASS
RP SPECTROMETRY.
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 THR-418; THR-442 AND
RP SER-475, AND MASS SPECTROMETRY.
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).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates 'Lys-63'-
CC linked polyubiquitination of TMEM173/STING, thereby playing a key
CC role in innate immunity. TMEM173/STING 'Lys-63'-linked
CC ubiquitination activates the production of type I interferon IFN-
CC beta following detection of pathogen- and host-derived double-
CC stranded DNA (By similarity).
CC -!- SUBUNIT: Interacts with TMEM173/STING (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9BRZ2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BRZ2-2; Sequence=VSP_029111, VSP_029112;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q9BRZ2-3; Sequence=VSP_029109, VSP_029110;
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family.
CC -!- SIMILARITY: Contains 2 B box-type zinc fingers.
CC -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH11882.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=BAC11500.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AK075255; BAC11500.1; ALT_INIT; mRNA.
DR EMBL; AK092927; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC105446; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005847; AAH05847.3; -; mRNA.
DR EMBL; BC011882; AAH11882.1; ALT_INIT; mRNA.
DR EMBL; BC048194; AAH48194.1; -; mRNA.
DR EMBL; AL512757; CAC21676.1; -; mRNA.
DR RefSeq; NP_112223.1; NM_030961.1.
DR UniGene; Hs.521092; -.
DR ProteinModelPortal; Q9BRZ2; -.
DR SMR; Q9BRZ2; 7-89.
DR IntAct; Q9BRZ2; 6.
DR PhosphoSite; Q9BRZ2; -.
DR DMDM; 56749788; -.
DR PaxDb; Q9BRZ2; -.
DR PeptideAtlas; Q9BRZ2; -.
DR PRIDE; Q9BRZ2; -.
DR DNASU; 81844; -.
DR Ensembl; ENST00000306085; ENSP00000305161; ENSG00000169871.
DR GeneID; 81844; -.
DR KEGG; hsa:81844; -.
DR UCSC; uc003uxq.3; human.
DR CTD; 81844; -.
DR GeneCards; GC07P100728; -.
DR H-InvDB; HIX0006941; -.
DR HGNC; HGNC:19028; TRIM56.
DR HPA; HPA024358; -.
DR neXtProt; NX_Q9BRZ2; -.
DR PharmGKB; PA134958549; -.
DR eggNOG; NOG301641; -.
DR HOGENOM; HOG000154679; -.
DR HOVERGEN; HBG079280; -.
DR InParanoid; Q9BRZ2; -.
DR KO; K12026; -.
DR OMA; FPTRMPG; -.
DR OrthoDB; EOG76X5ZJ; -.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; TRIM56; human.
DR GenomeRNAi; 81844; -.
DR NextBio; 72142; -.
DR PRO; PR:Q9BRZ2; -.
DR ArrayExpress; Q9BRZ2; -.
DR Bgee; Q9BRZ2; -.
DR CleanEx; HS_TRIM56; -.
DR Genevestigator; Q9BRZ2; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0004842; F:ubiquitin-protein ligase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR GO; GO:0032608; P:interferon-beta production; ISS:UniProtKB.
DR GO; GO:0032481; P:positive regulation of type I interferon production; TAS:Reactome.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0034340; P:response to type I interferon; ISS:UniProtKB.
DR Gene3D; 2.120.10.30; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Antiviral defense; Coiled coil;
KW Complete proteome; Cytoplasm; Immunity; Innate immunity; Ligase;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1 755 E3 ubiquitin-protein ligase TRIM56.
FT /FTId=PRO_0000056288.
FT ZN_FING 21 60 RING-type.
FT ZN_FING 98 149 B box-type 1.
FT ZN_FING 164 205 B box-type 2.
FT COILED 216 314 Potential.
FT COMPBIAS 302 309 Poly-Ala.
FT COMPBIAS 459 464 Poly-Lys.
FT MOD_RES 418 418 Phosphothreonine.
FT MOD_RES 442 442 Phosphothreonine.
FT MOD_RES 475 475 Phosphoserine.
FT VAR_SEQ 259 269 AEGVLRALLAQ -> CLLRTESCKAE (in isoform
FT 3).
FT /FTId=VSP_029109.
FT VAR_SEQ 270 755 Missing (in isoform 3).
FT /FTId=VSP_029110.
FT VAR_SEQ 273 308 VLGQLRAHVEAAEEAARERLAELEGREQVARAAAAF -> N
FT HLNPGGGSCSELRSHHCTPAWVTRMKLHLKKKKKK (in
FT isoform 2).
FT /FTId=VSP_029111.
FT VAR_SEQ 309 755 Missing (in isoform 2).
FT /FTId=VSP_029112.
FT CONFLICT 230 230 L -> P (in Ref. 1; AK092927).
SQ SEQUENCE 755 AA; 81488 MW; CF72D0C8EC9F69E7 CRC64;
MVSHGSSPSL LEALSSDFLA CKICLEQLRA PKTLPCLHTY CQDCLAQLAD GGRVRCPECR
ETVPVPPEGV ASFKTNFFVN GLLDLVKARA CGDLRAGKPA CALCPLVGGT STGGPATARC
LDCADDLCQA CADGHRCTRQ THTHRVVDLV GYRAGWYDEE ARERQAAQCP QHPGEALRFL
CQPCSQLLCR ECRLDPHLDH PCLPLAEAVR ARRPGLEGLL AGVDNNLVEL EAARRVEKEA
LARLREQAAR VGTQVEEAAE GVLRALLAQK QEVLGQLRAH VEAAEEAARE RLAELEGREQ
VARAAAAFAR RVLSLGREAE ILSLEGAIAQ RLRQLQGCPW APGPAPCLLP QLELHPGLLD
KNCHLLRLSF EEQQPQKDGG KDGAGTQGGE ESQSRREDEP KTERQGGVQP QAGDGAQTPK
EEKAQTTREE GAQTLEEDRA QTPHEDGGPQ PHRGGRPNKK KKFKGRLKSI SREPSPALGP
NLDGSGLLPR PIFYCSFPTR MPGDKRSPRI TGLCPFGPRE ILVADEQNRA LKRFSLNGDY
KGTVPVPEGC SPCSVAALQS AVAFSASARL YLINPNGEVQ WRRALSLSQA SHAVAALPSG
DRVAVSVAGH VEVYNMEGSL ATRFIPGGKA SRGLRALVFL TTSPQGHFVG SDWQQNSVVI
CDGLGQVVGE YKGPGLHGCQ PGSVSVDKKG YIFLTLREVN KVVILDPKGS LLGDFLTAYH
GLEKPRVTTM VDGRYLVVSL SNGTIHIFRV RSPDS
//
ID TRI56_HUMAN Reviewed; 755 AA.
AC Q9BRZ2; Q6PJS5; Q86VT6; Q8N2H8; Q8NAC0; Q9H031;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 21-DEC-2004, sequence version 3.
DT 22-JAN-2014, entry version 105.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM56;
DE EC=6.3.2.-;
DE AltName: Full=RING finger protein 109;
DE AltName: Full=Tripartite motif-containing protein 56;
GN Name=TRIM56; Synonyms=RNF109;
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 [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 429-755 (ISOFORM 1).
RC TISSUE=Spleen, and Thyroid;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lymph, and Placenta;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 572-755 (ISOFORM 1).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475, AND MASS
RP SPECTROMETRY.
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 THR-418; THR-442 AND
RP SER-475, AND MASS SPECTROMETRY.
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).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates 'Lys-63'-
CC linked polyubiquitination of TMEM173/STING, thereby playing a key
CC role in innate immunity. TMEM173/STING 'Lys-63'-linked
CC ubiquitination activates the production of type I interferon IFN-
CC beta following detection of pathogen- and host-derived double-
CC stranded DNA (By similarity).
CC -!- SUBUNIT: Interacts with TMEM173/STING (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9BRZ2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BRZ2-2; Sequence=VSP_029111, VSP_029112;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q9BRZ2-3; Sequence=VSP_029109, VSP_029110;
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family.
CC -!- SIMILARITY: Contains 2 B box-type zinc fingers.
CC -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH11882.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=BAC11500.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AK075255; BAC11500.1; ALT_INIT; mRNA.
DR EMBL; AK092927; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC105446; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005847; AAH05847.3; -; mRNA.
DR EMBL; BC011882; AAH11882.1; ALT_INIT; mRNA.
DR EMBL; BC048194; AAH48194.1; -; mRNA.
DR EMBL; AL512757; CAC21676.1; -; mRNA.
DR RefSeq; NP_112223.1; NM_030961.1.
DR UniGene; Hs.521092; -.
DR ProteinModelPortal; Q9BRZ2; -.
DR SMR; Q9BRZ2; 7-89.
DR IntAct; Q9BRZ2; 6.
DR PhosphoSite; Q9BRZ2; -.
DR DMDM; 56749788; -.
DR PaxDb; Q9BRZ2; -.
DR PeptideAtlas; Q9BRZ2; -.
DR PRIDE; Q9BRZ2; -.
DR DNASU; 81844; -.
DR Ensembl; ENST00000306085; ENSP00000305161; ENSG00000169871.
DR GeneID; 81844; -.
DR KEGG; hsa:81844; -.
DR UCSC; uc003uxq.3; human.
DR CTD; 81844; -.
DR GeneCards; GC07P100728; -.
DR H-InvDB; HIX0006941; -.
DR HGNC; HGNC:19028; TRIM56.
DR HPA; HPA024358; -.
DR neXtProt; NX_Q9BRZ2; -.
DR PharmGKB; PA134958549; -.
DR eggNOG; NOG301641; -.
DR HOGENOM; HOG000154679; -.
DR HOVERGEN; HBG079280; -.
DR InParanoid; Q9BRZ2; -.
DR KO; K12026; -.
DR OMA; FPTRMPG; -.
DR OrthoDB; EOG76X5ZJ; -.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; TRIM56; human.
DR GenomeRNAi; 81844; -.
DR NextBio; 72142; -.
DR PRO; PR:Q9BRZ2; -.
DR ArrayExpress; Q9BRZ2; -.
DR Bgee; Q9BRZ2; -.
DR CleanEx; HS_TRIM56; -.
DR Genevestigator; Q9BRZ2; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0004842; F:ubiquitin-protein ligase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR GO; GO:0032608; P:interferon-beta production; ISS:UniProtKB.
DR GO; GO:0032481; P:positive regulation of type I interferon production; TAS:Reactome.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0034340; P:response to type I interferon; ISS:UniProtKB.
DR Gene3D; 2.120.10.30; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Antiviral defense; Coiled coil;
KW Complete proteome; Cytoplasm; Immunity; Innate immunity; Ligase;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1 755 E3 ubiquitin-protein ligase TRIM56.
FT /FTId=PRO_0000056288.
FT ZN_FING 21 60 RING-type.
FT ZN_FING 98 149 B box-type 1.
FT ZN_FING 164 205 B box-type 2.
FT COILED 216 314 Potential.
FT COMPBIAS 302 309 Poly-Ala.
FT COMPBIAS 459 464 Poly-Lys.
FT MOD_RES 418 418 Phosphothreonine.
FT MOD_RES 442 442 Phosphothreonine.
FT MOD_RES 475 475 Phosphoserine.
FT VAR_SEQ 259 269 AEGVLRALLAQ -> CLLRTESCKAE (in isoform
FT 3).
FT /FTId=VSP_029109.
FT VAR_SEQ 270 755 Missing (in isoform 3).
FT /FTId=VSP_029110.
FT VAR_SEQ 273 308 VLGQLRAHVEAAEEAARERLAELEGREQVARAAAAF -> N
FT HLNPGGGSCSELRSHHCTPAWVTRMKLHLKKKKKK (in
FT isoform 2).
FT /FTId=VSP_029111.
FT VAR_SEQ 309 755 Missing (in isoform 2).
FT /FTId=VSP_029112.
FT CONFLICT 230 230 L -> P (in Ref. 1; AK092927).
SQ SEQUENCE 755 AA; 81488 MW; CF72D0C8EC9F69E7 CRC64;
MVSHGSSPSL LEALSSDFLA CKICLEQLRA PKTLPCLHTY CQDCLAQLAD GGRVRCPECR
ETVPVPPEGV ASFKTNFFVN GLLDLVKARA CGDLRAGKPA CALCPLVGGT STGGPATARC
LDCADDLCQA CADGHRCTRQ THTHRVVDLV GYRAGWYDEE ARERQAAQCP QHPGEALRFL
CQPCSQLLCR ECRLDPHLDH PCLPLAEAVR ARRPGLEGLL AGVDNNLVEL EAARRVEKEA
LARLREQAAR VGTQVEEAAE GVLRALLAQK QEVLGQLRAH VEAAEEAARE RLAELEGREQ
VARAAAAFAR RVLSLGREAE ILSLEGAIAQ RLRQLQGCPW APGPAPCLLP QLELHPGLLD
KNCHLLRLSF EEQQPQKDGG KDGAGTQGGE ESQSRREDEP KTERQGGVQP QAGDGAQTPK
EEKAQTTREE GAQTLEEDRA QTPHEDGGPQ PHRGGRPNKK KKFKGRLKSI SREPSPALGP
NLDGSGLLPR PIFYCSFPTR MPGDKRSPRI TGLCPFGPRE ILVADEQNRA LKRFSLNGDY
KGTVPVPEGC SPCSVAALQS AVAFSASARL YLINPNGEVQ WRRALSLSQA SHAVAALPSG
DRVAVSVAGH VEVYNMEGSL ATRFIPGGKA SRGLRALVFL TTSPQGHFVG SDWQQNSVVI
CDGLGQVVGE YKGPGLHGCQ PGSVSVDKKG YIFLTLREVN KVVILDPKGS LLGDFLTAYH
GLEKPRVTTM VDGRYLVVSL SNGTIHIFRV RSPDS
//