TRI59_HUMAN
ID TRI59_HUMAN Reviewed; 403 AA.
AC Q8IWR1; A8K5G9; D3DNL9;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Tripartite motif-containing protein 59;
DE AltName: Full=RING finger protein 104;
DE AltName: Full=Tumor suppressor TSBF-1;
GN Name=TRIM59; Synonyms=RNF104, TRIM57, TSBF1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Gong L., Wu K.;
RT "Identification and characterization of TSBF-1, a novel gene encoding a
RT tumor suppressor with ring finger domain.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP CHARACTERIZATION OF ISOFORM IFT80-L, AND TISSUE SPECIFICITY.
RX PubMed=18601909; DOI=10.1016/j.bbrc.2008.06.085;
RA Huang W., Kane J.K., Li M.D.;
RT "Identification and characterization of a long isoform of human IFT80,
RT IFT80-L.";
RL Biochem. Biophys. Res. Commun. 373:653-658(2008).
CC -!- FUNCTION: May serve as a multifunctional regulator for innate immune
CC signaling pathways. {ECO:0000250|UniProtKB:Q922Y2}.
CC -!- SUBUNIT: Interacts with ECSIT. {ECO:0000250|UniProtKB:Q922Y2}.
CC -!- INTERACTION:
CC Q8IWR1; Q7Z3H0-1: ANKRD33; NbExp=3; IntAct=EBI-10262539, EBI-16746154;
CC Q8IWR1; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-10262539, EBI-2548012;
CC Q8IWR1; O14493: CLDN4; NbExp=3; IntAct=EBI-10262539, EBI-9316372;
CC Q8IWR1; Q14232: EIF2B1; NbExp=3; IntAct=EBI-10262539, EBI-491065;
CC Q8IWR1; Q3SY46: KRTAP13-3; NbExp=3; IntAct=EBI-10262539, EBI-10241252;
CC Q8IWR1; A8MW99: MEI4; NbExp=3; IntAct=EBI-10262539, EBI-19944212;
CC Q8IWR1; P52815: MRPL12; NbExp=3; IntAct=EBI-10262539, EBI-358272;
CC Q8IWR1; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-10262539, EBI-10172876;
CC Q8IWR1; Q8IXM6: NRM; NbExp=7; IntAct=EBI-10262539, EBI-10262547;
CC Q8IWR1; Q9Y342: PLLP; NbExp=3; IntAct=EBI-10262539, EBI-3919291;
CC Q8IWR1; Q86WH2: RASSF3; NbExp=3; IntAct=EBI-10262539, EBI-2845202;
CC Q8IWR1; Q96IW7: SEC22A; NbExp=5; IntAct=EBI-10262539, EBI-8652744;
CC Q8IWR1; Q5SQN1: SNAP47; NbExp=3; IntAct=EBI-10262539, EBI-10244848;
CC Q8IWR1; Q8N2K1: UBE2J2; NbExp=3; IntAct=EBI-10262539, EBI-2340110;
CC Q8IWR1; Q96FI0: UBE2W; NbExp=3; IntAct=EBI-10262539, EBI-10285774;
CC Q8IWR1; Q9UEU0: VTI1B; NbExp=9; IntAct=EBI-10262539, EBI-723716;
CC Q8IWR1; Q8IVQ6: ZDHHC21; NbExp=3; IntAct=EBI-10262539, EBI-2849773;
CC Q8IWR1; Q8N966: ZDHHC22; NbExp=8; IntAct=EBI-10262539, EBI-10268111;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q922Y2}; Single-pass membrane protein
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8IWR1-1; Sequence=Displayed;
CC Name=IFT80-L;
CC IsoId=Q9P2H3-3; Sequence=External;
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AY159379; AAN86853.1; -; mRNA.
DR EMBL; AK291284; BAF83973.1; -; mRNA.
DR EMBL; CH471052; EAW78635.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78636.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78637.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78638.1; -; Genomic_DNA.
DR EMBL; BC109259; AAI09260.1; -; mRNA.
DR EMBL; BC109260; AAI09261.1; -; mRNA.
DR CCDS; CCDS3190.1; -. [Q8IWR1-1]
DR RefSeq; NP_775107.1; NM_173084.2. [Q8IWR1-1]
DR AlphaFoldDB; Q8IWR1; -.
DR BioGRID; 130421; 52.
DR IntAct; Q8IWR1; 27.
DR STRING; 9606.ENSP00000311219; -.
DR iPTMnet; Q8IWR1; -.
DR PhosphoSitePlus; Q8IWR1; -.
DR BioMuta; TRIM59; -.
DR DMDM; 74714421; -.
DR jPOST; Q8IWR1; -.
DR MassIVE; Q8IWR1; -.
DR MaxQB; Q8IWR1; -.
DR PaxDb; Q8IWR1; -.
DR PeptideAtlas; Q8IWR1; -.
DR PRIDE; Q8IWR1; -.
DR ProteomicsDB; 70884; -.
DR Antibodypedia; 18518; 180 antibodies from 27 providers.
DR DNASU; 286827; -.
DR Ensembl; ENST00000309784.9; ENSP00000311219.4; ENSG00000213186.8. [Q8IWR1-1]
DR GeneID; 286827; -.
DR KEGG; hsa:286827; -.
DR MANE-Select; ENST00000309784.9; ENSP00000311219.4; NM_173084.3; NP_775107.1.
DR UCSC; uc003fdm.4; human. [Q8IWR1-1]
DR CTD; 286827; -.
DR DisGeNET; 286827; -.
DR GeneCards; TRIM59; -.
DR HGNC; HGNC:30834; TRIM59.
DR HPA; ENSG00000213186; Tissue enhanced (brain).
DR MIM; 616148; gene.
DR neXtProt; NX_Q8IWR1; -.
DR OpenTargets; ENSG00000213186; -.
DR PharmGKB; PA134899610; -.
DR VEuPathDB; HostDB:ENSG00000213186; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000160146; -.
DR InParanoid; Q8IWR1; -.
DR OMA; ILCHTLY; -.
DR OrthoDB; 635534at2759; -.
DR PhylomeDB; Q8IWR1; -.
DR TreeFam; TF331669; -.
DR PathwayCommons; Q8IWR1; -.
DR SignaLink; Q8IWR1; -.
DR SIGNOR; Q8IWR1; -.
DR BioGRID-ORCS; 286827; 8 hits in 1118 CRISPR screens.
DR GenomeRNAi; 286827; -.
DR Pharos; Q8IWR1; Tbio.
DR PRO; PR:Q8IWR1; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q8IWR1; protein.
DR Bgee; ENSG00000213186; Expressed in oocyte and 155 other tissues.
DR ExpressionAtlas; Q8IWR1; baseline and differential.
DR Genevisible; Q8IWR1; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IMP:MGI.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; IEA:Ensembl.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR027370; Znf-RING_LisH.
DR InterPro; IPR000315; Znf_B-box.
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; PF13445; zf-RING_UBOX; 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; Coiled coil; Endoplasmic reticulum; Membrane;
KW Metal-binding; Reference proteome; Transmembrane; Transmembrane helix;
KW Zinc; Zinc-finger.
FT CHAIN 1..403
FT /note="Tripartite motif-containing protein 59"
FT /id="PRO_0000249679"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 10..60
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 92..134
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 163..246
FT /evidence="ECO:0000255"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
SQ SEQUENCE 403 AA; 47114 MW; 5C32183E7633F45D CRC64;
MHNFEEELTC PICYSIFEDP RVLPCSHTFC RNCLENILQA SGNFYIWRPL RIPLKCPNCR
SITEIAPTGI ESLPVNFALR AIIEKYQQED HPDIVTCPEH YRQPLNVYCL LDKKLVCGHC
LTIGQHHGHP IDDLQSAYLK EKDTPQKLLE QLTDTHWTDL THLIEKLKEQ KSHSEKMIQG
DKEAVLQYFK ELNDTLEQKK KSFLTALCDV GNLINQEYTP QIERMKEIRE QQLELMALTI
SLQEESPLKF LEKVDDVRQH VQILKQRPLP EVQPVEIYPR VSKILKEEWS RTEIGQIKNV
LIPKMKISPK RMSCSWPGKD EKEVEFLKIL NIVVVTLISV ILMSILFFNQ HIITFLSEIT
LIWFSEASLS VYQSLSNSLH KVKNILCHIF YLLKEFVWKI VSH
