TRI41_HUMAN
ID TRI41_HUMAN Reviewed; 630 AA.
AC Q8WV44; B3KNJ6; D3DWR9; Q5BKT0; Q7L484; Q96Q10; Q9BSL8;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM41 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:29760876, ECO:0000269|PubMed:29899090, ECO:0000269|PubMed:31979016};
DE AltName: Full=RING finger-interacting protein with C kinase {ECO:0000303|PubMed:17893151};
DE Short=RINCK {ECO:0000303|PubMed:17893151};
DE AltName: Full=Tripartite motif-containing protein 41;
GN Name=TRIM41 {ECO:0000303|PubMed:16022281, ECO:0000312|HGNC:HGNC:19013};
GN Synonyms=RINCK {ECO:0000303|PubMed:17893151};
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] (ISOFORMS 1 AND 2), AND SUBCELLULAR LOCATION.
RX PubMed=16022281; DOI=10.1007/s11033-004-6613-2;
RA Tanaka M., Fukuda Y., Mashima K., Hanai R.;
RT "Intracellular localization and domain organization of human TRIM41
RT proteins.";
RL Mol. Biol. Rep. 32:87-93(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 21-630 (ISOFORM 4).
RC TISSUE=Lung, Pancreas, and Uterus;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 80-630 (ISOFORM 2).
RX PubMed=11549288; DOI=10.1006/bbrc.2001.5580;
RA Kobayashi M., Hanai R.;
RT "M phase-specific association of human topoisomerase IIIbeta with
RT chromosomes.";
RL Biochem. Biophys. Res. Commun. 287:282-287(2001).
RN [8]
RP FUNCTION, ALTERNATIVE SPLICING (ISOFORMS 2 AND 4), TISSUE SPECIFICITY,
RP AUTOUBIQUITINATION, INTERACTION WITH PRKCA, AND MUTAGENESIS OF CYS-20.
RX PubMed=17893151; DOI=10.1074/jbc.m703320200;
RA Chen D., Gould C., Garza R., Gao T., Hampton R.Y., Newton A.C.;
RT "Amplitude control of protein kinase C by RINCK, a novel E3 ubiquitin
RT ligase.";
RL J. Biol. Chem. 282:33776-33787(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-447, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-84, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-256, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [12]
RP INTERACTION WITH NOD2, AND INDUCTION.
RX PubMed=27812135; DOI=10.1371/journal.pone.0165420;
RA Thiebaut R., Esmiol S., Lecine P., Mahfouz B., Hermant A., Nicoletti C.,
RA Parnis S., Perroy J., Borg J.P., Pascoe L., Hugot J.P., Ollendorff V.;
RT "Characterization and Genetic Analyses of New Genes Coding for NOD2
RT Interacting Proteins.";
RL PLoS ONE 11:E0165420-E0165420(2016).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=29760876; DOI=10.1186/s13578-018-0233-3;
RA Liu Z.S., Zhang Z.Y., Cai H., Zhao M., Mao J., Dai J., Xia T., Zhang X.M.,
RA Li T.;
RT "RINCK-mediated monoubiquitination of cGAS promotes antiviral innate immune
RT responses.";
RL Cell Biosci. 8:35-35(2018).
RN [14]
RP FUNCTION, PATHWAY, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RX PubMed=29899090; DOI=10.1128/jvi.00905-18;
RA Patil G., Zhao M., Song K., Hao W., Bouchereau D., Wang L., Li S.;
RT "TRIM41-Mediated Ubiquitination of Nucleoprotein Limits Influenza A Virus
RT Infection.";
RL J. Virol. 92:0-0(2018).
RN [15]
RP FUNCTION, PATHWAY, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RX PubMed=31979016; DOI=10.3390/v12020131;
RA Patil G., Xu L., Wu Y., Song K., Hao W., Hua F., Wang L., Li S.;
RT "TRIM41-Mediated Ubiquitination of Nucleoprotein Limits Vesicular
RT Stomatitis Virus Infection.";
RL Viruses 12:0-0(2020).
RN [16]
RP FUNCTION.
RX PubMed=33378676; DOI=10.1016/j.celrep.2020.108569;
RA Saha S., Sun Y., Huang S.N., Baechler S.A., Pongor L.S., Agama K., Jo U.,
RA Zhang H., Tse-Dinh Y.C., Pommier Y.;
RT "DNA and RNA Cleavage Complexes and Repair Pathway for TOP3B RNA- and DNA-
RT Protein Crosslinks.";
RL Cell Rep. 33:108569-108569(2020).
RN [17]
RP STRUCTURE BY NMR OF 214-263.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the ZF-b_box domain from human tripartite motif
RT protein 41.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: E3 ligase that plays essential roles in innate antiviral
CC response (PubMed:29760876, PubMed:29899090, PubMed:31979016). Directly
CC binds to influenza A virus or vesicular stomatitis virus nucleoproteins
CC and targets them for ubiquitination and proteasomal degradation,
CC thereby limiting viral infections (PubMed:29899090, PubMed:31979016).
CC Activates the innate antiviral response by catalyzing
CC monoubiquitination of CGAS, thereby activating CGAS (PubMed:29760876).
CC Also involved in innate antiviral response by mediating 'Lys-63'-linked
CC polyubiquitylation of BCL10 which in turn hubs NEMO for activation of
CC NF-kappa-B and IRF3 pathways (By similarity). Catalyzes the ubiquitin-
CC mediated degradation of other substrates including protein kinase C,
CC ZSCAN21 or TOP3B suggesting additional roles besides its function in
CC immune response (PubMed:17893151, PubMed:33378676).
CC {ECO:0000250|UniProtKB:Q5NCC3, ECO:0000269|PubMed:17893151,
CC ECO:0000269|PubMed:29760876, ECO:0000269|PubMed:29899090,
CC ECO:0000269|PubMed:31979016, ECO:0000269|PubMed:33378676}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:29760876,
CC ECO:0000269|PubMed:29899090, ECO:0000269|PubMed:31979016};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:29760876, ECO:0000269|PubMed:29899090,
CC ECO:0000269|PubMed:31979016}.
CC -!- SUBUNIT: Interacts with PRKCA (PubMed:17893151). Interacts with NOD2
CC (PubMed:27812135). Interacts with TRIM17; this interaction prevents
CC TRIM41 activity on ZSCAN2 (By similarity).
CC {ECO:0000250|UniProtKB:Q5NCC3, ECO:0000269|PubMed:17893151,
CC ECO:0000269|PubMed:27812135}.
CC -!- INTERACTION:
CC Q8WV44; Q8WTP8: AEN; NbExp=3; IntAct=EBI-725997, EBI-8637627;
CC Q8WV44; Q86SG2: ANKRD23; NbExp=3; IntAct=EBI-725997, EBI-5661893;
CC Q8WV44; Q9BXS5: AP1M1; NbExp=3; IntAct=EBI-725997, EBI-541426;
CC Q8WV44; P29972: AQP1; NbExp=3; IntAct=EBI-725997, EBI-745213;
CC Q8WV44; Q86UB2: BIVM; NbExp=3; IntAct=EBI-725997, EBI-12191873;
CC Q8WV44; Q13895: BYSL; NbExp=5; IntAct=EBI-725997, EBI-358049;
CC Q8WV44; D3DR40: C10orf4; NbExp=3; IntAct=EBI-725997, EBI-10176576;
CC Q8WV44; Q9H7E9: C8orf33; NbExp=3; IntAct=EBI-725997, EBI-715389;
CC Q8WV44; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-725997, EBI-3866279;
CC Q8WV44; Q96S94-5: CCNL2; NbExp=3; IntAct=EBI-725997, EBI-12024864;
CC Q8WV44; Q9C0F1: CEP44; NbExp=3; IntAct=EBI-725997, EBI-744115;
CC Q8WV44; O14647: CHD2; NbExp=4; IntAct=EBI-725997, EBI-1210503;
CC Q8WV44; P68400: CSNK2A1; NbExp=3; IntAct=EBI-725997, EBI-347804;
CC Q8WV44; P19784: CSNK2A2; NbExp=7; IntAct=EBI-725997, EBI-347451;
CC Q8WV44; Q92997: DVL3; NbExp=3; IntAct=EBI-725997, EBI-739789;
CC Q8WV44; Q08426: EHHADH; NbExp=7; IntAct=EBI-725997, EBI-2339219;
CC Q8WV44; Q86X51: EZHIP; NbExp=3; IntAct=EBI-725997, EBI-12827735;
CC Q8WV44; Q86V42: FAM124A; NbExp=3; IntAct=EBI-725997, EBI-744506;
CC Q8WV44; Q3B820: FAM161A; NbExp=3; IntAct=EBI-725997, EBI-719941;
CC Q8WV44; Q8IZU1: FAM9A; NbExp=3; IntAct=EBI-725997, EBI-8468186;
CC Q8WV44; Q96Q35-2: FLACC1; NbExp=3; IntAct=EBI-725997, EBI-11533409;
CC Q8WV44; O95995: GAS8; NbExp=3; IntAct=EBI-725997, EBI-1052570;
CC Q8WV44; Q9NWQ4: GPATCH2L; NbExp=3; IntAct=EBI-725997, EBI-5666657;
CC Q8WV44; Q9NWQ4-1: GPATCH2L; NbExp=3; IntAct=EBI-725997, EBI-11959863;
CC Q8WV44; O75564-2: JRK; NbExp=3; IntAct=EBI-725997, EBI-17181882;
CC Q8WV44; Q9H079: KATNBL1; NbExp=5; IntAct=EBI-725997, EBI-715394;
CC Q8WV44; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-725997, EBI-2125614;
CC Q8WV44; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-725997, EBI-10171774;
CC Q8WV44; P60411: KRTAP10-9; NbExp=5; IntAct=EBI-725997, EBI-10172052;
CC Q8WV44; Q9H213: MAGEH1; NbExp=3; IntAct=EBI-725997, EBI-473834;
CC Q8WV44; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-725997, EBI-348259;
CC Q8WV44; P50221: MEOX1; NbExp=3; IntAct=EBI-725997, EBI-2864512;
CC Q8WV44; P50222: MEOX2; NbExp=3; IntAct=EBI-725997, EBI-748397;
CC Q8WV44; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-725997, EBI-16439278;
CC Q8WV44; P55081: MFAP1; NbExp=3; IntAct=EBI-725997, EBI-1048159;
CC Q8WV44; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-725997, EBI-10172526;
CC Q8WV44; Q13875-3: MOBP; NbExp=3; IntAct=EBI-725997, EBI-12013470;
CC Q8WV44; Q9UBU8: MORF4L1; NbExp=3; IntAct=EBI-725997, EBI-399246;
CC Q8WV44; Q9UBU8-2: MORF4L1; NbExp=5; IntAct=EBI-725997, EBI-10288852;
CC Q8WV44; Q15014: MORF4L2; NbExp=3; IntAct=EBI-725997, EBI-399257;
CC Q8WV44; O43639: NCK2; NbExp=8; IntAct=EBI-725997, EBI-713635;
CC Q8WV44; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-725997, EBI-10302990;
CC Q8WV44; Q8IXK0: PHC2; NbExp=3; IntAct=EBI-725997, EBI-713786;
CC Q8WV44; Q9UIL8: PHF11; NbExp=3; IntAct=EBI-725997, EBI-2861403;
CC Q8WV44; Q9UPG8: PLAGL2; NbExp=3; IntAct=EBI-725997, EBI-2876622;
CC Q8WV44; Q9GZV8: PRDM14; NbExp=3; IntAct=EBI-725997, EBI-3957793;
CC Q8WV44; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-725997, EBI-1567797;
CC Q8WV44; P26045: PTPN3; NbExp=3; IntAct=EBI-725997, EBI-1047946;
CC Q8WV44; Q9H0K6: PUS7L; NbExp=3; IntAct=EBI-725997, EBI-5464419;
CC Q8WV44; Q9NYW8: RBAK; NbExp=3; IntAct=EBI-725997, EBI-1210429;
CC Q8WV44; D3DU92: RNPS1; NbExp=3; IntAct=EBI-725997, EBI-10176640;
CC Q8WV44; O60504: SORBS3; NbExp=3; IntAct=EBI-725997, EBI-741237;
CC Q8WV44; O75558: STX11; NbExp=3; IntAct=EBI-725997, EBI-714135;
CC Q8WV44; O43463: SUV39H1; NbExp=3; IntAct=EBI-725997, EBI-349968;
CC Q8WV44; Q8N0S2: SYCE1; NbExp=3; IntAct=EBI-725997, EBI-6872807;
CC Q8WV44; Q96C24: SYTL4; NbExp=3; IntAct=EBI-725997, EBI-747142;
CC Q8WV44; Q15560: TCEA2; NbExp=3; IntAct=EBI-725997, EBI-710310;
CC Q8WV44; Q8N8B7-2: TCEANC; NbExp=5; IntAct=EBI-725997, EBI-11955057;
CC Q8WV44; Q08117: TLE5; NbExp=3; IntAct=EBI-725997, EBI-717810;
CC Q8WV44; Q08117-2: TLE5; NbExp=5; IntAct=EBI-725997, EBI-11741437;
CC Q8WV44; P19237: TNNI1; NbExp=3; IntAct=EBI-725997, EBI-746692;
CC Q8WV44; O95985: TOP3B; NbExp=4; IntAct=EBI-725997, EBI-373403;
CC Q8WV44; Q9Y577: TRIM17; NbExp=4; IntAct=EBI-725997, EBI-743894;
CC Q8WV44; Q8WV44: TRIM41; NbExp=5; IntAct=EBI-725997, EBI-725997;
CC Q8WV44; O43167: ZBTB24; NbExp=6; IntAct=EBI-725997, EBI-744471;
CC Q8WV44; Q9HCK0: ZBTB26; NbExp=5; IntAct=EBI-725997, EBI-3918996;
CC Q8WV44; O15060: ZBTB39; NbExp=3; IntAct=EBI-725997, EBI-9995672;
CC Q8WV44; P10074: ZBTB48; NbExp=4; IntAct=EBI-725997, EBI-744864;
CC Q8WV44; Q96BR9: ZBTB8A; NbExp=4; IntAct=EBI-725997, EBI-742740;
CC Q8WV44; Q8N3Z6: ZCCHC7; NbExp=3; IntAct=EBI-725997, EBI-7265024;
CC Q8WV44; Q6P2D0: ZFP1; NbExp=3; IntAct=EBI-725997, EBI-2555749;
CC Q8WV44; Q6ZN57: ZFP2; NbExp=6; IntAct=EBI-725997, EBI-7236323;
CC Q8WV44; Q9NTW7: ZFP64; NbExp=7; IntAct=EBI-725997, EBI-711679;
CC Q8WV44; Q9UDW3: ZMAT5; NbExp=3; IntAct=EBI-725997, EBI-7850213;
CC Q8WV44; P58317: ZNF121; NbExp=3; IntAct=EBI-725997, EBI-1228269;
CC Q8WV44; P52741: ZNF134; NbExp=3; IntAct=EBI-725997, EBI-18054945;
CC Q8WV44; P52744: ZNF138; NbExp=3; IntAct=EBI-725997, EBI-10746567;
CC Q8WV44; P52744-2: ZNF138; NbExp=3; IntAct=EBI-725997, EBI-10213071;
CC Q8WV44; P49910: ZNF165; NbExp=3; IntAct=EBI-725997, EBI-741694;
CC Q8WV44; Q9BSG1: ZNF2; NbExp=3; IntAct=EBI-725997, EBI-8489229;
CC Q8WV44; Q9P2Y4: ZNF219; NbExp=3; IntAct=EBI-725997, EBI-3937106;
CC Q8WV44; P15622-3: ZNF250; NbExp=9; IntAct=EBI-725997, EBI-10177272;
CC Q8WV44; Q9BRH9: ZNF251; NbExp=3; IntAct=EBI-725997, EBI-7254491;
CC Q8WV44; P17031: ZNF26; NbExp=3; IntAct=EBI-725997, EBI-2841331;
CC Q8WV44; O14978: ZNF263; NbExp=5; IntAct=EBI-725997, EBI-744493;
CC Q8WV44; O43296: ZNF264; NbExp=4; IntAct=EBI-725997, EBI-4395808;
CC Q8WV44; Q14C61: ZNF264; NbExp=3; IntAct=EBI-725997, EBI-2826570;
CC Q8WV44; Q14584: ZNF266; NbExp=6; IntAct=EBI-725997, EBI-7115319;
CC Q8WV44; Q9NSD4: ZNF275; NbExp=6; IntAct=EBI-725997, EBI-17263125;
CC Q8WV44; Q9HBT8: ZNF286A; NbExp=3; IntAct=EBI-725997, EBI-10754950;
CC Q8WV44; Q9P2F9: ZNF319; NbExp=3; IntAct=EBI-725997, EBI-11993110;
CC Q8WV44; Q86UD4: ZNF329; NbExp=4; IntAct=EBI-725997, EBI-7233259;
CC Q8WV44; Q6P1L6: ZNF343; NbExp=3; IntAct=EBI-725997, EBI-10252492;
CC Q8WV44; Q8TD17: ZNF398; NbExp=3; IntAct=EBI-725997, EBI-8643207;
CC Q8WV44; Q9H9D4: ZNF408; NbExp=4; IntAct=EBI-725997, EBI-347633;
CC Q8WV44; Q8TAU3: ZNF417; NbExp=8; IntAct=EBI-725997, EBI-740727;
CC Q8WV44; Q8NDP4: ZNF439; NbExp=3; IntAct=EBI-725997, EBI-747580;
CC Q8WV44; Q14592: ZNF460; NbExp=3; IntAct=EBI-725997, EBI-2555738;
CC Q8WV44; Q8WTR7: ZNF473; NbExp=5; IntAct=EBI-725997, EBI-751409;
CC Q8WV44; Q96MX3: ZNF48; NbExp=3; IntAct=EBI-725997, EBI-12006434;
CC Q8WV44; Q9ULM2: ZNF490; NbExp=7; IntAct=EBI-725997, EBI-1105370;
CC Q8WV44; Q6ZNH5: ZNF497; NbExp=3; IntAct=EBI-725997, EBI-10486136;
CC Q8WV44; Q8TF50: ZNF526; NbExp=3; IntAct=EBI-725997, EBI-11035148;
CC Q8WV44; Q9H707: ZNF552; NbExp=3; IntAct=EBI-725997, EBI-2555731;
CC Q8WV44; Q8TBZ8: ZNF564; NbExp=3; IntAct=EBI-725997, EBI-10273713;
CC Q8WV44; Q86XF7: ZNF575; NbExp=3; IntAct=EBI-725997, EBI-14069183;
CC Q8WV44; Q96SQ5: ZNF587; NbExp=6; IntAct=EBI-725997, EBI-6427977;
CC Q8WV44; Q9UEG4: ZNF629; NbExp=3; IntAct=EBI-725997, EBI-9977294;
CC Q8WV44; Q5T619: ZNF648; NbExp=3; IntAct=EBI-725997, EBI-11985915;
CC Q8WV44; Q96CK0: ZNF653; NbExp=3; IntAct=EBI-725997, EBI-12217757;
CC Q8WV44; Q8N720: ZNF655; NbExp=3; IntAct=EBI-725997, EBI-625509;
CC Q8WV44; Q9BS34: ZNF670; NbExp=6; IntAct=EBI-725997, EBI-745276;
CC Q8WV44; Q5VV52: ZNF691; NbExp=3; IntAct=EBI-725997, EBI-720883;
CC Q8WV44; Q9H7X3: ZNF696; NbExp=3; IntAct=EBI-725997, EBI-11090299;
CC Q8WV44; Q9NQZ8: ZNF71; NbExp=8; IntAct=EBI-725997, EBI-7138235;
CC Q8WV44; Q6PK81: ZNF773; NbExp=3; IntAct=EBI-725997, EBI-2686307;
CC Q8WV44; O75290: ZNF780A; NbExp=3; IntAct=EBI-725997, EBI-13335739;
CC Q8WV44; Q8NCA9: ZNF784; NbExp=3; IntAct=EBI-725997, EBI-7138303;
CC Q8WV44; Q3KQV3: ZNF792; NbExp=3; IntAct=EBI-725997, EBI-10240849;
CC Q8WV44; Q9Y2P0: ZNF835; NbExp=6; IntAct=EBI-725997, EBI-5667516;
CC Q8WV44; Q96EG3: ZNF837; NbExp=3; IntAct=EBI-725997, EBI-11962574;
CC Q8WV44; Q9H4T2: ZSCAN16; NbExp=3; IntAct=EBI-725997, EBI-723596;
CC Q8WV44; Q9Y5A6: ZSCAN21; NbExp=3; IntAct=EBI-725997, EBI-10281938;
CC Q8WV44; Q16670: ZSCAN26; NbExp=3; IntAct=EBI-725997, EBI-3920053;
CC Q8WV44; Q9H6F0; NbExp=3; IntAct=EBI-725997, EBI-10307481;
CC Q8WV44; C5E522: NP; Xeno; NbExp=3; IntAct=EBI-725997, EBI-12583355;
CC Q8WV44; P03466: NP; Xeno; NbExp=5; IntAct=EBI-725997, EBI-2547640;
CC Q8WV44; Q1K9H2: NP; Xeno; NbExp=3; IntAct=EBI-725997, EBI-6050688;
CC Q8WV44; Q5EP28: NP; Xeno; NbExp=3; IntAct=EBI-725997, EBI-12582202;
CC Q8WV44-2; P68403-2: Prkcb; Xeno; NbExp=3; IntAct=EBI-726015, EBI-397092;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16022281,
CC ECO:0000269|PubMed:29899090, ECO:0000269|PubMed:31979016}. Nucleus
CC {ECO:0000269|PubMed:16022281, ECO:0000269|PubMed:29899090,
CC ECO:0000269|PubMed:31979016}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=TRIM41a, TRIM41alpha;
CC IsoId=Q8WV44-1; Sequence=Displayed;
CC Name=2; Synonyms=TRIM41b, TRIM41beta, RINCK1;
CC IsoId=Q8WV44-2; Sequence=VSP_010395, VSP_010396;
CC Name=3;
CC IsoId=Q8WV44-3; Sequence=VSP_012515;
CC Name=4; Synonyms=RINCK2;
CC IsoId=Q8WV44-4; Sequence=VSP_012516, VSP_012517;
CC -!- TISSUE SPECIFICITY: Expressed in multiple tissues with the highest
CC levels in heart and skeletal muscle. {ECO:0000269|PubMed:17893151}.
CC -!- INDUCTION: Down-regulated by muramyl-dipeptide and lipopolysaccharide.
CC {ECO:0000269|PubMed:27812135}.
CC -!- PTM: Auto-ubiquitinated. {ECO:0000269|PubMed:17893151}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AB100366; BAD07472.1; -; mRNA.
DR EMBL; AB100367; BAD07473.1; -; mRNA.
DR EMBL; AF258579; AAG23782.1; -; mRNA.
DR EMBL; CR457349; CAG33630.1; -; mRNA.
DR EMBL; AK027601; BAG51358.1; -; mRNA.
DR EMBL; CH471165; EAW53712.1; -; Genomic_DNA.
DR EMBL; CH471165; EAW53708.1; -; Genomic_DNA.
DR EMBL; CH471165; EAW53709.1; -; Genomic_DNA.
DR EMBL; BC004956; AAH04956.1; -; mRNA.
DR EMBL; BC009762; AAH09762.2; -; mRNA.
DR EMBL; BC018765; AAH18765.2; -; mRNA.
DR EMBL; BC071887; AAH71887.1; -; mRNA.
DR EMBL; BC090953; AAH90953.1; -; mRNA.
DR EMBL; AB063180; BAB70617.1; -; mRNA.
DR CCDS; CCDS4465.1; -. [Q8WV44-2]
DR CCDS; CCDS4466.1; -. [Q8WV44-1]
DR RefSeq; NP_291027.3; NM_033549.4. [Q8WV44-1]
DR RefSeq; NP_963921.1; NM_201627.2. [Q8WV44-2]
DR PDB; 2EGM; NMR; -; A=214-263.
DR PDBsum; 2EGM; -.
DR AlphaFoldDB; Q8WV44; -.
DR SMR; Q8WV44; -.
DR BioGRID; 124780; 229.
DR IntAct; Q8WV44; 180.
DR MINT; Q8WV44; -.
DR STRING; 9606.ENSP00000320869; -.
DR MoonDB; Q8WV44; Predicted.
DR iPTMnet; Q8WV44; -.
DR PhosphoSitePlus; Q8WV44; -.
DR BioMuta; TRIM41; -.
DR DMDM; 116242826; -.
DR EPD; Q8WV44; -.
DR jPOST; Q8WV44; -.
DR MassIVE; Q8WV44; -.
DR MaxQB; Q8WV44; -.
DR PaxDb; Q8WV44; -.
DR PeptideAtlas; Q8WV44; -.
DR PRIDE; Q8WV44; -.
DR ProteomicsDB; 74747; -. [Q8WV44-1]
DR ProteomicsDB; 74748; -. [Q8WV44-2]
DR ProteomicsDB; 74749; -. [Q8WV44-3]
DR ProteomicsDB; 74750; -. [Q8WV44-4]
DR Antibodypedia; 17930; 218 antibodies from 26 providers.
DR DNASU; 90933; -.
DR Ensembl; ENST00000315073.10; ENSP00000320869.5; ENSG00000146063.20. [Q8WV44-1]
DR Ensembl; ENST00000351937.9; ENSP00000336749.6; ENSG00000146063.20. [Q8WV44-2]
DR GeneID; 90933; -.
DR KEGG; hsa:90933; -.
DR MANE-Select; ENST00000315073.10; ENSP00000320869.5; NM_033549.5; NP_291027.3.
DR UCSC; uc003mnd.3; human. [Q8WV44-1]
DR CTD; 90933; -.
DR DisGeNET; 90933; -.
DR GeneCards; TRIM41; -.
DR HGNC; HGNC:19013; TRIM41.
DR HPA; ENSG00000146063; Tissue enhanced (brain).
DR MIM; 610530; gene.
DR neXtProt; NX_Q8WV44; -.
DR OpenTargets; ENSG00000146063; -.
DR PharmGKB; PA134918519; -.
DR VEuPathDB; HostDB:ENSG00000146063; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000154294; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; Q8WV44; -.
DR OMA; WDTPMRE; -.
DR OrthoDB; 423686at2759; -.
DR PhylomeDB; Q8WV44; -.
DR TreeFam; TF342569; -.
DR PathwayCommons; Q8WV44; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q8WV44; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 90933; 17 hits in 1120 CRISPR screens.
DR ChiTaRS; TRIM41; human.
DR EvolutionaryTrace; Q8WV44; -.
DR GeneWiki; TRIM41; -.
DR GenomeRNAi; 90933; -.
DR Pharos; Q8WV44; Tbio.
DR PRO; PR:Q8WV44; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q8WV44; protein.
DR Bgee; ENSG00000146063; Expressed in C1 segment of cervical spinal cord and 178 other tissues.
DR ExpressionAtlas; Q8WV44; baseline and differential.
DR Genevisible; Q8WV44; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:UniProtKB.
DR GO; GO:0071225; P:cellular response to muramyl dipeptide; IMP:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR CDD; cd13741; SPRY_PRY_TRIM41; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006574; PRY.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR042828; TRIM41_SPRY_PRY.
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; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00589; PRY; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 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 3D-structure; Alternative splicing; Coiled coil; Cytoplasm;
KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..630
FT /note="E3 ubiquitin-protein ligase TRIM41"
FT /id="PRO_0000056262"
FT DOMAIN 413..630
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 20..61
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 222..263
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 51..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 264..373
FT /evidence="ECO:0000255"
FT COMPBIAS 51..76
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..166
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 249
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 255
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 84
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CROSSLNK 256
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT VAR_SEQ 1..420
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15498874, ECO:0000303|Ref.3"
FT /id="VSP_012515"
FT VAR_SEQ 381
FT /note="D -> V (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012516"
FT VAR_SEQ 382..630
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012517"
FT VAR_SEQ 490..518
FT /note="VEVGGRRGWAVGAARESTHHKEKVGPGGS -> EPKEPSWPPAQPSLTYYVC
FT PTDRPEFSFT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11549288,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:16022281"
FT /id="VSP_010395"
FT VAR_SEQ 519..630
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11549288,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:16022281"
FT /id="VSP_010396"
FT VARIANT 78
FT /note="A -> T (in dbSNP:rs6601178)"
FT /id="VAR_027914"
FT VARIANT 438
FT /note="D -> G (in dbSNP:rs2241371)"
FT /id="VAR_027915"
FT MUTAGEN 20
FT /note="C->A: Abolishes E3 ligase activity."
FT /evidence="ECO:0000269|PubMed:17893151"
FT CONFLICT 276
FT /note="G -> E (in Ref. 1; BAD07472/BAD07473 and 5;
FT BAB70617)"
FT /evidence="ECO:0000305"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:2EGM"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:2EGM"
FT TURN 239..242
FT /evidence="ECO:0007829|PDB:2EGM"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:2EGM"
FT HELIX 247..251
FT /evidence="ECO:0007829|PDB:2EGM"
FT HELIX 253..256
FT /evidence="ECO:0007829|PDB:2EGM"
SQ SEQUENCE 630 AA; 71670 MW; 8E704CBEAB928BF5 CRC64;
MAAVAMTPNP VQTLQEEAVC AICLDYFTDP VSIGCGHNFC RVCVTQLWGG EDEEDRDELD
REEEEEDGEE EEVEAVGAGA GWDTPMRDED YEGDMEEEVE EEEEGVFWTS GMSRSSWDNM
DYVWEEEDEE EDLDYYLGDM EEEDLRGEDE EDEEEVLEEV EEEDLDPVTP LPPPPAPRRC
FTCPQCRKSF PRRSFRPNLQ LANMVQVIRQ MHPTPGRGSR VTDQGICPKH QEALKLFCEV
DEEAICVVCR ESRSHKQHSV VPLEEVVQEY KAKLQGHVEP LRKHLEAVQK MKAKEERRVT
ELKSQMKSEL AAVASEFGRL TRFLAEEQAG LERRLREMHE AQLGRAGAAA SRLAEQAAQL
SRLLAEAQER SQQGGLRLLQ DIKETFNRCE EVQLQPPEVW SPDPCQPHSH DFLTDAIVRK
MSRMFCQAAR VDLTLDPDTA HPALMLSPDR RGVRLAERRQ EVADHPKRFS ADCCVLGAQG
FRSGRHYWEV EVGGRRGWAV GAARESTHHK EKVGPGGSSV GSGDASSSRH HHRRRRLHLP
QQPLLQREVW CVGTNGKRYQ AQSSTEQTLL SPSEKPRRFG VYLDYEAGRL GFYNAETLAH
VHTFSAAFLG ERVFPFFRVL SKGTRIKLCP
