TRIM5_HUMAN
ID TRIM5_HUMAN Reviewed; 493 AA.
AC Q9C035; A6NGQ1; A8WFA8; D3DQS8; D3DQS9; G3GJY1; Q2MLV4; Q2MLV8; Q2MLV9;
AC Q2MLW1; Q2MLW3; Q2MLW4; Q2MLW6; Q2MLW7; Q2MLX1; Q2MLX2; Q2MLX3; Q2MLX5;
AC Q2MLY3; Q2MLY4; Q2V6Q6; Q6GX26; Q8WU46; Q96SR5; Q9C031; Q9C032; Q9C033;
AC Q9C034;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Tripartite motif-containing protein 5;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 88;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM5 {ECO:0000305};
GN Name=TRIM5; Synonyms=RNF88;
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 ALPHA; BETA; GAMMA; DELTA AND
RP EPSILON), AND VARIANT GLN-136.
RX PubMed=11331580; DOI=10.1093/emboj/20.9.2140;
RA Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L.,
RA Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A., Minucci S.,
RA Pelicci P.G., Ballabio A.;
RT "The tripartite motif family identifies cell compartments.";
RL EMBO J. 20:2140-2151(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
RX PubMed=15249690; DOI=10.1073/pnas.0402876101;
RA Yap M.W., Nisole S., Lynch C., Stoye J.P.;
RT "Trim5alpha protein restricts both HIV-1 and murine leukemia virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:10786-10791(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM ALPHA), AND VARIANTS TYR-43 AND
RP ASP-249.
RX PubMed=16401428; DOI=10.1016/j.cub.2005.11.045;
RA Sawyer S.L., Wu L.I., Akey J.M., Emerman M., Malik H.S.;
RT "High-frequency persistence of an impaired allele of the retroviral defense
RT gene TRIM5alpha in humans.";
RL Curr. Biol. 16:95-100(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-136, FUNCTION, AUTOUBIQUITINATION,
RP UBIQUITINATION BY TRIM21, AND MUTAGENESIS OF CYS-15.
RC TISSUE=Brain;
RX PubMed=18312418; DOI=10.1111/j.1742-4658.2008.06313.x;
RA Yamauchi K., Wada K., Tanji K., Tanaka M., Kamitani T.;
RT "Ubiquitination of E3 ubiquitin ligase TRIM5 alpha and its potential
RT role.";
RL FEBS J. 275:1540-1555(2008).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM EPSILON), ALTERNATIVE SPLICING, AND
RP FUNCTION.
RX PubMed=21632761; DOI=10.1128/jvi.00648-11;
RA Battivelli E., Migraine J., Lecossier D., Matsuoka S., Perez-Bercoff D.,
RA Saragosti S., Clavel F., Hance A.J.;
RT "Modulation of TRIM5alpha activity in human cells by alternatively spliced
RT TRIM5 isoforms.";
RL J. Virol. 85:7828-7835(2011).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA), AND VARIANT
RP GLN-136.
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-31; TYR-43; TYR-58;
RP GLU-110; PHE-112; GLN-136; ASP-249; TYR-419; SER-467 AND LEU-479.
RG NIEHS SNPs program;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GAMMA).
RC TISSUE=Rhabdomyosarcoma;
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 [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BTBD1 AND BTBD2.
RX PubMed=12878161; DOI=10.1016/s0014-4827(03)00187-3;
RA Xu L., Yang L., Moitra P.K., Hashimoto K., Rallabhandi P., Kaul S.,
RA Meroni G., Jensen J.P., Weissman A.M., D'Arpa P.;
RT "BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the RBCC/tripartite
RT motif protein, TRIM5delta.";
RL Exp. Cell Res. 288:84-93(2003).
RN [12]
RP FUNCTION (ISOFORM ALPHA).
RX PubMed=16474118; DOI=10.1128/jvi.80.5.2100-2105.2006;
RA Passerini L.D., Keckesova Z., Towers G.J.;
RT "Retroviral restriction factors Fv1 and TRIM5alpha act independently and
RT can compete for incoming virus before reverse transcription.";
RL J. Virol. 80:2100-2105(2006).
RN [13]
RP MUTAGENESIS OF ARG-332.
RX PubMed=16809279; DOI=10.1128/jvi.00270-06;
RA Li Y., Li X., Stremlau M., Lee M., Sodroski J.;
RT "Removal of arginine 332 allows human TRIM5alpha to bind human
RT immunodeficiency virus capsids and to restrict infection.";
RL J. Virol. 80:6738-6744(2006).
RN [14]
RP FUNCTION (ISOFORM ALPHA).
RX PubMed=16643975; DOI=10.1016/j.virol.2006.03.015;
RA Stremlau M., Song B., Javanbakht H., Perron M., Sodroski J.;
RT "Cyclophilin A: an auxiliary but not necessary cofactor for TRIM5alpha
RT restriction of HIV-1.";
RL Virology 351:112-120(2006).
RN [15]
RP REVIEW.
RX PubMed=16956947; DOI=10.1128/jvi.01519-06;
RA Luban J.;
RT "Cyclophilin A, TRIM5, and resistance to human immunodeficiency virus type
RT 1 infection.";
RL J. Virol. 81:1054-1061(2007).
RN [16]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH TRIM6 AND TRIM34.
RX PubMed=17156811; DOI=10.1016/j.virol.2006.10.035;
RA Li X., Gold B., O'hUigin C., Diaz-Griffero F., Song B., Si Z., Li Y.,
RA Yuan W., Stremlau M., Mische C., Javanbakht H., Scally M., Winkler C.,
RA Dean M., Sodroski J.;
RT "Unique features of TRIM5alpha among closely related human TRIM family
RT members.";
RL Virology 360:419-433(2007).
RN [17]
RP INTERACTION WITH HSPA1A/B.
RX PubMed=20053985; DOI=10.1074/jbc.m109.040618;
RA Hwang C.Y., Holl J., Rajan D., Lee Y., Kim S., Um M., Kwon K.S., Song B.;
RT "Hsp70 interacts with the retroviral restriction factor TRIM5alpha and
RT assists the folding of TRIM5alpha.";
RL J. Biol. Chem. 285:7827-7837(2010).
RN [18]
RP INTERACTION WITH SQSTM1, AND SUBCELLULAR LOCATION.
RX PubMed=20357094; DOI=10.1128/jvi.02412-09;
RA O'Connor C., Pertel T., Gray S., Robia S.L., Bakowska J.C., Luban J.,
RA Campbell E.M.;
RT "p62/sequestosome-1 associates with and sustains the expression of
RT retroviral restriction factor TRIM5alpha.";
RL J. Virol. 84:5997-6006(2010).
RN [19]
RP REVIEW, AND PROTEASOMAL DEGRADATION.
RX PubMed=21247355; DOI=10.1089/aid.2010.0367;
RA Sastri J., Campbell E.M.;
RT "Recent insights into the mechanism and consequences of TRIM5alpha
RT retroviral restriction.";
RL AIDS Res. Hum. Retroviruses 27:231-238(2011).
RN [20]
RP REVIEW.
RX PubMed=21575904; DOI=10.1016/j.chom.2011.05.003;
RA Tareen S.U., Emerman M.;
RT "Trim5 TAKes on pattern recognition.";
RL Cell Host Microbe 9:349-350(2011).
RN [21]
RP INTERACTION WITH TRIM6 AND TRIM34.
RX PubMed=21680743; DOI=10.1074/jbc.m111.260406;
RA Li X., Yeung D.F., Fiegen A.M., Sodroski J.;
RT "Determinants of the higher order association of the restriction factor
RT TRIM5alpha and other tripartite motif (TRIM) proteins.";
RL J. Biol. Chem. 286:27959-27970(2011).
RN [22]
RP REVIEW.
RX PubMed=21512569; DOI=10.1038/472305a;
RA Aiken C., Joyce S.;
RT "Immunology: TRIM5 does double duty.";
RL Nature 472:305-306(2011).
RN [23]
RP FUNCTION, AND INTERACTION WITH MAP3K7/TAK1; TAB2 AND TAB3.
RX PubMed=21512573; DOI=10.1038/nature09976;
RA Pertel T., Hausmann S., Morger D., Zueger S., Guerra J., Lascano J.,
RA Reinhard C., Santoni F.A., Uchil P.D., Chatel L., Bisiaux A., Albert M.L.,
RA Strambio-De-Castillia C., Mothes W., Pizzato M., Gruetter M.G., Luban J.;
RT "TRIM5 is an innate immune sensor for the retrovirus capsid lattice.";
RL Nature 472:361-365(2011).
RN [24]
RP REVIEW.
RX PubMed=21572451; DOI=10.1038/nrmicro2582;
RA Jermy A.;
RT "Antiviral immunity: TRIM5 moonlights as a pattern recognition receptor.";
RL Nat. Rev. Microbiol. 9:398-398(2011).
RN [25]
RP INTERACTION WITH PSMC2.
RX PubMed=22078707; DOI=10.1186/1742-4690-8-93;
RA Lukic Z., Hausmann S., Sebastian S., Rucci J., Sastri J., Robia S.L.,
RA Luban J., Campbell E.M.;
RT "TRIM5alpha associates with proteasomal subunits in cells while in complex
RT with HIV-1 virions.";
RL Retrovirology 8:93-93(2011).
RN [26]
RP FUNCTION.
RX PubMed=21035162; DOI=10.1016/j.virol.2010.09.018;
RA Tareen S.U., Emerman M.;
RT "Human Trim5alpha has additional activities that are uncoupled from
RT retroviral capsid recognition.";
RL Virology 409:113-120(2011).
RN [27]
RP REVIEW.
RX PubMed=21866272; DOI=10.3390/v3071204;
RA de Silva S., Wu L.;
RT "TRIM5 acts as more than a retroviral restriction factor.";
RL Viruses 3:1204-1209(2011).
RN [28]
RP REVIEW.
RX PubMed=22482711; DOI=10.1016/j.coviro.2012.02.003;
RA Gruetter M.G., Luban J.;
RT "TRIM5 structure, HIV-1 capsid recognition, and innate immune signaling.";
RL Curr. Opin. Virol. 2:142-150(2012).
RN [29]
RP REVIEW, AND FUNCTION.
RX PubMed=22291694; DOI=10.3389/fmicb.2012.00013;
RA Nakayama E.E., Shioda T.;
RT "TRIM5alpha and species tropism of HIV/SIV.";
RL Front. Microbiol. 3:13-13(2012).
RN [30]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [32]
RP FUNCTION, INTERACTION WITH ULK1; SQSTM1; GABARAP; GABARAPL1; GABARAPL2;
RP MAP1LC3A; MAP1LC3C AND BECN1, AND SUBCELLULAR LOCATION.
RX PubMed=25127057; DOI=10.1016/j.devcel.2014.06.013;
RA Mandell M.A., Jain A., Arko-Mensah J., Chauhan S., Kimura T., Dinkins C.,
RA Silvestri G., Munch J., Kirchhoff F., Simonsen A., Wei Y., Levine B.,
RA Johansen T., Deretic V.;
RT "TRIM proteins regulate autophagy and can target autophagic substrates by
RT direct recognition.";
RL Dev. Cell 30:394-409(2014).
RN [33]
RP IDENTIFICATION BY 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 [34]
RP STRUCTURE BY NMR OF 1-78.
RX PubMed=21734049; DOI=10.1128/jvi.00497-11;
RA Lienlaf M., Hayashi F., Di Nunzio F., Tochio N., Kigawa T., Yokoyama S.,
RA Diaz-Griffero F.;
RT "Contribution of E3-ubiquitin ligase activity to HIV-1 restriction by
RT TRIM5alpha(rh): structure of the RING domain of TRIM5alpha.";
RL J. Virol. 85:8725-8737(2011).
RN [35]
RP STRUCTURE BY NMR OF 86-129.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the b-box domain from tripartite motif-containing
RT protein 5.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Capsid-specific restriction factor that prevents infection
CC from non-host-adapted retroviruses. Blocks viral replication early in
CC the life cycle, after viral entry but before reverse transcription. In
CC addition to acting as a capsid-specific restriction factor, also acts
CC as a pattern recognition receptor that activates innate immune
CC signaling in response to the retroviral capsid lattice. Binding to the
CC viral capsid triggers its E3 ubiquitin ligase activity, and in concert
CC with the heterodimeric ubiquitin conjugating enzyme complex UBE2V1-
CC UBE2N (also known as UBC13-UEV1A complex) generates 'Lys-63'-linked
CC polyubiquitin chains, which in turn are catalysts in the
CC autophosphorylation of the MAP3K7/TAK1 complex (includes TAK1, TAB2,
CC and TAB3). Activation of the MAP3K7/TAK1 complex by autophosphorylation
CC results in the induction and expression of NF-kappa-B and MAPK-
CC responsive inflammatory genes, thereby leading to an innate immune
CC response in the infected cell. Restricts infection by N-tropic murine
CC leukemia virus (N-MLV), equine infectious anemia virus (EIAV), simian
CC immunodeficiency virus of macaques (SIVmac), feline immunodeficiency
CC virus (FIV), and bovine immunodeficiency virus (BIV) (PubMed:17156811).
CC Plays a role in regulating autophagy through activation of autophagy
CC regulator BECN1 by causing its dissociation from its inhibitors BCL2
CC and TAB2 (PubMed:25127057). Also plays a role in autophagy by acting as
CC a selective autophagy receptor which recognizes and targets HIV-1
CC capsid protein p24 for autophagic destruction (PubMed:25127057).
CC {ECO:0000269|PubMed:12878161, ECO:0000269|PubMed:17156811,
CC ECO:0000269|PubMed:18312418, ECO:0000269|PubMed:21035162,
CC ECO:0000269|PubMed:21512573, ECO:0000269|PubMed:21632761,
CC ECO:0000269|PubMed:22291694, ECO:0000269|PubMed:25127057}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Can form homodimers and homotrimers. In addition to lower-
CC order dimerization, also exhibits a higher-order multimerization and
CC both low- and high-order multimerizations are essential for its
CC restriction activity. Isoform Delta interacts with BTBD1 and BTBD2.
CC Interacts with PSMC4, PSMC5, PSMD7 and HSPA8/HSC70 (By similarity).
CC Interacts (via B30.2/SPRY domain) with HSPA1A/B. Interacts with PSMC2,
CC MAP3K7/TAK1, TAB2 and TAB3 (PubMed:21512573, PubMed:22078707).
CC Interacts with SQSTM1 (PubMed:20357094, PubMed:25127057). Interacts
CC with TRIM6 and TRIM34 (PubMed:21680743, PubMed:17156811). Interacts
CC with ULK1 (phosphorylated form), GABARAP, GABARAPL1, GABARAPL2,
CC MAP1LC3A, MAP1LC3C and BECN1 (PubMed:25127057). {ECO:0000250,
CC ECO:0000269|PubMed:12878161, ECO:0000269|PubMed:17156811,
CC ECO:0000269|PubMed:20053985, ECO:0000269|PubMed:20357094,
CC ECO:0000269|PubMed:21512573, ECO:0000269|PubMed:21680743,
CC ECO:0000269|PubMed:22078707, ECO:0000269|PubMed:25127057}.
CC -!- INTERACTION:
CC Q9C035; O95863: SNAI1; NbExp=3; IntAct=EBI-924214, EBI-1045459;
CC Q9C035; Q13049: TRIM32; NbExp=2; IntAct=EBI-924214, EBI-742790;
CC Q9C035; Q9C035: TRIM5; NbExp=3; IntAct=EBI-924214, EBI-924214;
CC Q9C035-1; Q2Y080; Xeno; NbExp=3; IntAct=EBI-924230, EBI-924086;
CC Q9C035-3; Q08426: EHHADH; NbExp=3; IntAct=EBI-12840050, EBI-2339219;
CC Q9C035-3; P13473-2: LAMP2; NbExp=3; IntAct=EBI-12840050, EBI-21591415;
CC Q9C035-3; Q5T2T1: MPP7; NbExp=3; IntAct=EBI-12840050, EBI-2514004;
CC Q9C035-3; Q8N3F0: MTURN; NbExp=3; IntAct=EBI-12840050, EBI-11980301;
CC Q9C035-3; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-12840050, EBI-741158;
CC Q9C035-3; O43765: SGTA; NbExp=3; IntAct=EBI-12840050, EBI-347996;
CC Q9C035-3; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-12840050, EBI-2623095;
CC Q9C035-3; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-12840050, EBI-10241197;
CC Q9C035-3; P57075-2: UBASH3A; NbExp=3; IntAct=EBI-12840050, EBI-7353612;
CC Q9C035-3; P61086: UBE2K; NbExp=6; IntAct=EBI-12840050, EBI-473850;
CC Q9C035-3; P07947: YES1; NbExp=3; IntAct=EBI-12840050, EBI-515331;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25127057}. Nucleus
CC {ECO:0000250|UniProtKB:Q0PF16}. Note=Predominantly localizes in
CC cytoplasmic bodies (PubMed:12878161, PubMed:20357094). Localization may
CC be influenced by the coexpression of other TRIM proteins, hence partial
CC nuclear localization is observed in the presence of TRIM22 or TRIM27
CC (By similarity). In cytoplasmic bodies, colocalizes with proteasomal
CC subunits and SQSTM1 (By similarity). {ECO:0000250|UniProtKB:Q0PF16,
CC ECO:0000269|PubMed:12878161, ECO:0000269|PubMed:20357094,
CC ECO:0000269|PubMed:25127057}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=Alpha;
CC IsoId=Q9C035-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=Q9C035-2; Sequence=VSP_009010, VSP_009011;
CC Name=Gamma;
CC IsoId=Q9C035-3; Sequence=VSP_009012, VSP_009013;
CC Name=Delta;
CC IsoId=Q9C035-4; Sequence=VSP_009014, VSP_009015;
CC Name=Epsilon; Synonyms=Kappa;
CC IsoId=Q9C035-5; Sequence=VSP_009016, VSP_009017;
CC Name=Iota;
CC IsoId=Q9C035-6; Sequence=VSP_044095, VSP_044096;
CC -!- DOMAIN: The B box-type zinc finger domain and the coiled-coil domain
CC contribute to the higher and low order multimerization respectively
CC which is essential for restriction activity (PubMed:22482711). The
CC coiled coil domain is important for higher order multimerization by
CC promoting the initial dimerization (By similarity).
CC {ECO:0000250|UniProtKB:Q0PF16, ECO:0000269|PubMed:22482711}.
CC -!- DOMAIN: The B30.2/SPRY domain acts as a capsid recognition domain.
CC Polymorphisms in this domain explain the observed species-specific
CC differences among orthologs (PubMed:22482711).
CC {ECO:0000269|PubMed:22482711}.
CC -!- DOMAIN: The RING-type zinc finger domain confers E3 ubiquitin ligase
CC activity and is essential for retrovirus restriction activity,
CC autoubiquitination and higher-order multimerization.
CC {ECO:0000269|PubMed:22482711}.
CC -!- PTM: Degraded in a proteasome-independent fashion in the absence of
CC viral infection but in a proteasome-dependent fashion following
CC exposure to restriction sensitive virus.
CC -!- PTM: Autoubiquitinated in a RING finger- and UBE2D2-dependent manner.
CC Monoubiquitinated by TRIM21. Deubiquitinated by Yersinia YopJ.
CC Ubiquitination may not lead to proteasomal degradation.
CC {ECO:0000269|PubMed:18312418}.
CC -!- MISCELLANEOUS: [Isoform Beta]: Probable artifact. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform Iota]: Has dominant-negative activity against
CC TRIM5alpha. Does not inhibit HIV-1 replication. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/trim5/";
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DR EMBL; AF220025; AAG53479.1; -; mRNA.
DR EMBL; AF220026; AAG53480.1; -; mRNA.
DR EMBL; AF220027; AAG53481.1; -; mRNA.
DR EMBL; AF220028; AAG53482.1; -; mRNA.
DR EMBL; AF220029; AAG53483.1; -; mRNA.
DR EMBL; AY625000; AAT48101.1; -; mRNA.
DR EMBL; DQ301444; ABC00997.1; -; Genomic_DNA.
DR EMBL; DQ301445; ABC00998.1; -; Genomic_DNA.
DR EMBL; DQ301446; ABC00999.1; -; Genomic_DNA.
DR EMBL; DQ301447; ABC01000.1; -; Genomic_DNA.
DR EMBL; DQ301448; ABC01001.1; -; Genomic_DNA.
DR EMBL; DQ301449; ABC01002.1; -; Genomic_DNA.
DR EMBL; DQ301450; ABC01003.1; -; Genomic_DNA.
DR EMBL; DQ301451; ABC01004.1; -; Genomic_DNA.
DR EMBL; DQ301452; ABC01005.1; -; Genomic_DNA.
DR EMBL; DQ301453; ABC01006.1; -; Genomic_DNA.
DR EMBL; DQ301454; ABC01007.1; -; Genomic_DNA.
DR EMBL; DQ301455; ABC01008.1; -; Genomic_DNA.
DR EMBL; DQ301456; ABC01009.1; -; Genomic_DNA.
DR EMBL; DQ301457; ABC01010.1; -; Genomic_DNA.
DR EMBL; DQ301458; ABC01011.1; -; Genomic_DNA.
DR EMBL; DQ301459; ABC01012.1; -; Genomic_DNA.
DR EMBL; DQ301460; ABC01013.1; -; Genomic_DNA.
DR EMBL; DQ301461; ABC01014.1; -; Genomic_DNA.
DR EMBL; DQ301462; ABC01015.1; -; Genomic_DNA.
DR EMBL; DQ301463; ABC01016.1; -; Genomic_DNA.
DR EMBL; DQ301464; ABC01017.1; -; Genomic_DNA.
DR EMBL; DQ301465; ABC01018.1; -; Genomic_DNA.
DR EMBL; DQ301466; ABC01019.1; -; Genomic_DNA.
DR EMBL; DQ301467; ABC01020.1; -; Genomic_DNA.
DR EMBL; DQ301468; ABC01021.1; -; Genomic_DNA.
DR EMBL; DQ301469; ABC01022.1; -; Genomic_DNA.
DR EMBL; DQ301470; ABC01023.1; -; Genomic_DNA.
DR EMBL; DQ301471; ABC01024.1; -; Genomic_DNA.
DR EMBL; DQ301472; ABC01025.1; -; Genomic_DNA.
DR EMBL; DQ301473; ABC01026.1; -; Genomic_DNA.
DR EMBL; DQ301474; ABC01027.1; -; Genomic_DNA.
DR EMBL; DQ301475; ABC01028.1; -; Genomic_DNA.
DR EMBL; DQ301476; ABC01029.1; -; Genomic_DNA.
DR EMBL; DQ301477; ABC01030.1; -; Genomic_DNA.
DR EMBL; DQ301478; ABC01031.1; -; Genomic_DNA.
DR EMBL; DQ301479; ABC01032.1; -; Genomic_DNA.
DR EMBL; DQ301480; ABC01033.1; -; Genomic_DNA.
DR EMBL; DQ288685; ABB90543.1; -; mRNA.
DR EMBL; JF928461; AEN14475.1; -; mRNA.
DR EMBL; JF928462; AEN14476.1; -; mRNA.
DR EMBL; AK027593; BAB55218.1; -; mRNA.
DR EMBL; AC015691; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471064; EAW68771.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68772.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68774.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68775.1; -; Genomic_DNA.
DR EMBL; EU260465; ABW96352.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68776.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68777.1; -; Genomic_DNA.
DR EMBL; BC021258; AAH21258.1; -; mRNA.
DR CCDS; CCDS31392.1; -. [Q9C035-4]
DR CCDS; CCDS31393.1; -. [Q9C035-1]
DR CCDS; CCDS31394.1; -. [Q9C035-3]
DR RefSeq; NP_149023.2; NM_033034.2. [Q9C035-1]
DR RefSeq; NP_149083.2; NM_033092.2. [Q9C035-3]
DR RefSeq; NP_149084.2; NM_033093.2. [Q9C035-4]
DR RefSeq; XP_005253240.1; XM_005253183.2. [Q9C035-1]
DR RefSeq; XP_005253241.1; XM_005253184.2. [Q9C035-4]
DR RefSeq; XP_011518729.1; XM_011520427.1. [Q9C035-5]
DR PDB; 2ECV; NMR; -; A=1-78.
DR PDB; 2YRG; NMR; -; A=86-129.
DR PDBsum; 2ECV; -.
DR PDBsum; 2YRG; -.
DR AlphaFoldDB; Q9C035; -.
DR BMRB; Q9C035; -.
DR SMR; Q9C035; -.
DR BioGRID; 124491; 84.
DR ELM; Q9C035; -.
DR IntAct; Q9C035; 38.
DR STRING; 9606.ENSP00000369373; -.
DR MoonDB; Q9C035; Predicted.
DR iPTMnet; Q9C035; -.
DR PhosphoSitePlus; Q9C035; -.
DR BioMuta; TRIM5; -.
DR DMDM; 38605459; -.
DR EPD; Q9C035; -.
DR jPOST; Q9C035; -.
DR MassIVE; Q9C035; -.
DR MaxQB; Q9C035; -.
DR PaxDb; Q9C035; -.
DR PeptideAtlas; Q9C035; -.
DR PRIDE; Q9C035; -.
DR ProteomicsDB; 79952; -. [Q9C035-1]
DR ProteomicsDB; 79953; -. [Q9C035-2]
DR ProteomicsDB; 79954; -. [Q9C035-3]
DR ProteomicsDB; 79955; -. [Q9C035-4]
DR ProteomicsDB; 79956; -. [Q9C035-5]
DR Antibodypedia; 4609; 508 antibodies from 40 providers.
DR DNASU; 85363; -.
DR Ensembl; ENST00000380027.5; ENSP00000369366.1; ENSG00000132256.20. [Q9C035-4]
DR Ensembl; ENST00000380034.8; ENSP00000369373.3; ENSG00000132256.20. [Q9C035-1]
DR Ensembl; ENST00000396847.7; ENSP00000380058.3; ENSG00000132256.20. [Q9C035-3]
DR Ensembl; ENST00000433961.5; ENSP00000393052.1; ENSG00000132256.20. [Q9C035-5]
DR Ensembl; ENST00000684655.1; ENSP00000507420.1; ENSG00000132256.20. [Q9C035-1]
DR GeneID; 85363; -.
DR KEGG; hsa:85363; -.
DR MANE-Select; ENST00000380034.8; ENSP00000369373.3; NM_033034.3; NP_149023.2.
DR UCSC; uc001mbm.3; human. [Q9C035-1]
DR CTD; 85363; -.
DR DisGeNET; 85363; -.
DR GeneCards; TRIM5; -.
DR HGNC; HGNC:16276; TRIM5.
DR HPA; ENSG00000132256; Low tissue specificity.
DR MIM; 608487; gene.
DR neXtProt; NX_Q9C035; -.
DR OpenTargets; ENSG00000132256; -.
DR PharmGKB; PA38109; -.
DR VEuPathDB; HostDB:ENSG00000132256; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000154647; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; Q9C035; -.
DR OMA; LTNFNYC; -.
DR OrthoDB; 740493at2759; -.
DR PhylomeDB; Q9C035; -.
DR TreeFam; TF338674; -.
DR BRENDA; 2.3.2.27; 2681.
DR PathwayCommons; Q9C035; -.
DR Reactome; R-HSA-877300; Interferon gamma signaling.
DR SignaLink; Q9C035; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 85363; 8 hits in 1118 CRISPR screens.
DR ChiTaRS; TRIM5; human.
DR EvolutionaryTrace; Q9C035; -.
DR GeneWiki; TRIM5alpha; -.
DR GenomeRNAi; 85363; -.
DR Pharos; Q9C035; Tbio.
DR PRO; PR:Q9C035; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9C035; protein.
DR Bgee; ENSG00000132256; Expressed in sural nerve and 154 other tissues.
DR ExpressionAtlas; Q9C035; baseline and differential.
DR Genevisible; Q9C035; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0038187; F:pattern recognition receptor activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:ARUK-UCL.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0002218; P:activation of innate immune response; IDA:UniProtKB.
DR GO; GO:0006914; P:autophagy; IDA:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; TAS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; IDA:UniProtKB.
DR GO; GO:0010508; P:positive regulation of autophagy; IBA:GO_Central.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IMP:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0031664; P:regulation of lipopolysaccharide-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; IMP:UniProtKB.
DR GO; GO:0046596; P:regulation of viral entry into host cell; IBA:GO_Central.
DR GO; GO:0044790; P:suppression of viral release by host; IDA:UniProtKB.
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; IPR003877; SPRY_dom.
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; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00336; BBOX; 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; Acetylation; Alternative splicing; Antiviral defense;
KW Autophagy; Coiled coil; Cytoplasm; Host-virus interaction; Immunity;
KW Innate immunity; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..493
FT /note="Tripartite motif-containing protein 5"
FT /id="PRO_0000056201"
FT DOMAIN 281..493
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 15..59
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 90..132
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 185..198
FT /note="Required for interaction with GABARAP and for
FT autophagy"
FT /evidence="ECO:0000250|UniProtKB:Q0PF16"
FT COILED 130..241
FT /evidence="ECO:0000255"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 249..271
FT /note="GVDGVIKRTENVTLKKPETFPKN -> DGERDLEEARNFSKKSKESVSSS
FT (in isoform Epsilon)"
FT /evidence="ECO:0000303|PubMed:11331580,
FT ECO:0000303|PubMed:21632761"
FT /id="VSP_009016"
FT VAR_SEQ 249..257
FT /note="GVDGVIKRT -> VKSGKKPEH (in isoform Iota)"
FT /evidence="ECO:0000305"
FT /id="VSP_044095"
FT VAR_SEQ 258..493
FT /note="Missing (in isoform Iota)"
FT /evidence="ECO:0000305"
FT /id="VSP_044096"
FT VAR_SEQ 272..493
FT /note="Missing (in isoform Epsilon)"
FT /evidence="ECO:0000303|PubMed:11331580,
FT ECO:0000303|PubMed:21632761"
FT /id="VSP_009017"
FT VAR_SEQ 299..347
FT /note="VDVTVAPNNISCAVISEDKRQVSSPKPQIIYGARGTRYQTFVNFNYCTG ->
FT GKEKSHYHKPPCGLSLLLSLSFRILCSLLGSCFKIYDSPSKTHITYPSL (in
FT isoform Gamma)"
FT /evidence="ECO:0000303|PubMed:11331580,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_009012"
FT VAR_SEQ 299..326
FT /note="VDVTVAPNNISCAVISEDKRQVSSPKPQ -> GWSAMARSRFTATSTSQIQA
FT ILLPQPPK (in isoform Delta)"
FT /evidence="ECO:0000303|PubMed:11331580"
FT /id="VSP_009014"
FT VAR_SEQ 327..493
FT /note="Missing (in isoform Delta)"
FT /evidence="ECO:0000303|PubMed:11331580"
FT /id="VSP_009015"
FT VAR_SEQ 348..493
FT /note="Missing (in isoform Gamma)"
FT /evidence="ECO:0000303|PubMed:11331580,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_009013"
FT VAR_SEQ 390..400
FT /note="NENYQPKYGYW -> KRFMILLPRHT (in isoform Beta)"
FT /evidence="ECO:0000303|PubMed:11331580"
FT /id="VSP_009010"
FT VAR_SEQ 401..493
FT /note="Missing (in isoform Beta)"
FT /evidence="ECO:0000303|PubMed:11331580"
FT /id="VSP_009011"
FT VARIANT 31
FT /note="G -> S (in dbSNP:rs59896509)"
FT /evidence="ECO:0000269|Ref.9"
FT /id="VAR_060707"
FT VARIANT 43
FT /note="H -> Y (in dbSNP:rs3740996)"
FT /evidence="ECO:0000269|PubMed:16401428, ECO:0000269|Ref.9"
FT /id="VAR_017397"
FT VARIANT 58
FT /note="C -> Y (in dbSNP:rs61432120)"
FT /evidence="ECO:0000269|Ref.9"
FT /id="VAR_060708"
FT VARIANT 110
FT /note="G -> E (in dbSNP:rs56348930)"
FT /evidence="ECO:0000269|Ref.9"
FT /id="VAR_060709"
FT VARIANT 112
FT /note="V -> F (in dbSNP:rs11601507)"
FT /evidence="ECO:0000269|Ref.9"
FT /id="VAR_030154"
FT VARIANT 136
FT /note="R -> Q (in dbSNP:rs10838525)"
FT /evidence="ECO:0000269|PubMed:11331580,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:18312418,
FT ECO:0000269|Ref.9"
FT /id="VAR_017398"
FT VARIANT 249
FT /note="G -> D (in dbSNP:rs11038628)"
FT /evidence="ECO:0000269|PubMed:16401428, ECO:0000269|Ref.9"
FT /id="VAR_030155"
FT VARIANT 419
FT /note="H -> Y (in dbSNP:rs28381981)"
FT /evidence="ECO:0000269|Ref.9"
FT /id="VAR_030156"
FT VARIANT 467
FT /note="C -> S (in dbSNP:rs59218593)"
FT /evidence="ECO:0000269|Ref.9"
FT /id="VAR_060710"
FT VARIANT 479
FT /note="P -> L (in dbSNP:rs7104422)"
FT /evidence="ECO:0000269|Ref.9"
FT /id="VAR_030157"
FT MUTAGEN 15
FT /note="C->A: Abolishes E3 ligase activity."
FT /evidence="ECO:0000269|PubMed:18312418"
FT MUTAGEN 332
FT /note="R->A,G,H,P,Q,S: Increases strongly cell restriction
FT against HIV-1 and SIVmac infection."
FT /evidence="ECO:0000269|PubMed:16809279"
FT MUTAGEN 332
FT /note="R->D,E,L: Increases strongly cell restriction
FT against HIV-1 infection."
FT /evidence="ECO:0000269|PubMed:16809279"
FT MUTAGEN 332
FT /note="R->K: No effect on HIV-1 and SIVmac infection."
FT /evidence="ECO:0000269|PubMed:16809279"
FT CONFLICT 76
FT /note="I -> L (in Ref. 2; BAB55218)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="L -> P (in Ref. 2; BAB55218)"
FT /evidence="ECO:0000305"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:2ECV"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:2ECV"
FT HELIX 38..45
FT /evidence="ECO:0007829|PDB:2ECV"
FT TURN 46..50
FT /evidence="ECO:0007829|PDB:2ECV"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:2ECV"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:2ECV"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:2YRG"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:2YRG"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:2YRG"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:2YRG"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:2YRG"
FT HELIX 115..118
FT /evidence="ECO:0007829|PDB:2YRG"
FT TURN 121..125
FT /evidence="ECO:0007829|PDB:2YRG"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:2YRG"
SQ SEQUENCE 493 AA; 56338 MW; 8E61AAFD508AF6C0 CRC64;
MASGILVNVK EEVTCPICLE LLTQPLSLDC GHSFCQACLT ANHKKSMLDK GESSCPVCRI
SYQPENIRPN RHVANIVEKL REVKLSPEGQ KVDHCARHGE KLLLFCQEDG KVICWLCERS
QEHRGHHTFL TEEVAREYQV KLQAALEMLR QKQQEAEELE ADIREEKASW KTQIQYDKTN
VLADFEQLRD ILDWEESNEL QNLEKEEEDI LKSLTNSETE MVQQTQSLRE LISDLEHRLQ
GSVMELLQGV DGVIKRTENV TLKKPETFPK NQRRVFRAPD LKGMLEVFRE LTDVRRYWVD
VTVAPNNISC AVISEDKRQV SSPKPQIIYG ARGTRYQTFV NFNYCTGILG SQSITSGKHY
WEVDVSKKTA WILGVCAGFQ PDAMCNIEKN ENYQPKYGYW VIGLEEGVKC SAFQDSSFHT
PSVPFIVPLS VIICPDRVGV FLDYEACTVS FFNITNHGFL IYKFSHCSFS QPVFPYLNPR
KCGVPMTLCS PSS
