ID TRIM7_HUMAN Reviewed; 511 AA.
AC Q9C029; A2RUE4; D3DWR7; Q969F5; Q96F67; Q96J89; Q96J90;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2003, sequence version 2.
DT 27-MAR-2024, entry version 186.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM7 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:25851810};
DE AltName: Full=Glycogenin-interacting protein;
DE AltName: Full=RING finger protein 90;
DE AltName: Full=Tripartite motif-containing protein 7;
GN Name=TRIM7; Synonyms=GNIP, RNF90;
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] (ISOFORM 4).
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] (ISOFORMS 1; 2 AND 3), AND INTERACTION WITH GYG.
RC TISSUE=Skeletal muscle;
RX PubMed=11916970; DOI=10.1074/jbc.m201190200;
RA Skurat A.V., Dietrich A.D., Zhai L., Roach P.J.;
RT "GNIP, a novel protein that binds and activates glycogenin, the self-
RT glucosylating initiator of glycogen biosynthesis.";
RL J. Biol. Chem. 277:19331-19338(2002).
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] (ISOFORMS 1 AND 4), AND VARIANT
RP GLU-95.
RC TISSUE=Lung, and Salivary gland;
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 SUBUNIT, INTERACTION WITH GYG, TISSUE SPECIFICITY, AND DOMAIN.
RX PubMed=14984203; DOI=10.1016/j.abb.2003.11.017;
RA Zhai L., Dietrich A., Skurat A.V., Roach P.J.;
RT "Structure-function analysis of GNIP, the glycogenin-interacting protein.";
RL Arch. Biochem. Biophys. 421:236-242(2004).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBUNIT, INTERACTION WITH RNF187,
RP PHOSPHORYLATION AT SER-107 BY RPS6KA5, IDENTIFICATION BY MASS SPECTROMETRY,
RP AND MUTAGENESIS OF CYS-29; CYS-32; TRP-57 AND SER-107.
RX PubMed=25851810; DOI=10.1038/ncomms7782;
RA Chakraborty A., Diefenbacher M.E., Mylona A., Kassel O., Behrens A.;
RT "The E3 ubiquitin ligase Trim7 mediates c-Jun/AP-1 activation by Ras
RT signalling.";
RL Nat. Commun. 6:6782-6782(2015).
RN [7]
RP FUNCTION.
RX PubMed=32126128; DOI=10.1371/journal.ppat.1008387;
RA Yang B., Liu Y., Cui Y., Song D., Zhang G., Ma S., Liu Y., Chen M.,
RA Chen F., Wang H., Wang J.;
RT "RNF90 negatively regulates cellular antiviral responses by targeting MITA
RT for degradation.";
RL PLoS Pathog. 16:e1008387-e1008387(2020).
RN [8]
RP FUNCTION (MICROBIAL INFECTION), AND SUBCELLULAR LOCATION.
RX PubMed=32641828; DOI=10.1038/s41586-020-2457-8;
RA Giraldo M.I., Xia H., Aguilera-Aguirre L., Hage A., van Tol S., Shan C.,
RA Xie X., Sturdevant G.L., Robertson S.J., McNally K.L., Meade-White K.,
RA Azar S.R., Rossi S.L., Maury W., Woodson M., Ramage H., Johnson J.R.,
RA Krogan N.J., Morais M.C., Best S.M., Shi P.Y., Rajsbaum R.;
RT "Envelope protein ubiquitination drives entry and pathogenesis of Zika
RT virus.";
RL Nature 585:414-419(2020).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=32853985; DOI=10.1016/j.ebiom.2020.102955;
RA Zhou C., Zhang Z., Zhu X., Qian G., Zhou Y., Sun Y., Yu W., Wang J., Lu H.,
RA Lin F., Shen Z., Zheng S.;
RT "N6-Methyladenosine modification of the TRIM7 positively regulates
RT tumorigenesis and chemoresistance in osteosarcoma through ubiquitination of
RT BRMS1.";
RL EBioMedicine 59:102955-102955(2020).
RN [10]
RP FUNCTION, MUTAGENESIS OF CYS-29 AND CYS-32, AND SUBCELLULAR LOCATION.
RX PubMed=34062120; DOI=10.1016/j.cell.2021.04.047;
RA Fan W., Mar K.B., Sari L., Gaszek I.K., Cheng Q., Evers B.M., Shelton J.M.,
RA Wight-Carter M., Siegwart D.J., Lin M.M., Schoggins J.W.;
RT "TRIM7 inhibits enterovirus replication and promotes emergence of a viral
RT variant with increased pathogenicity.";
RL Cell 184:3410-3425(2021).
RN [11]
RP FUNCTION.
RX PubMed=36067704; DOI=10.1016/j.redox.2022.102451;
RA Li K., Chen B., Xu A., Shen J., Li K., Hao K., Hao R., Yang W., Jiang W.,
RA Zheng Y., Ge F., Wang Z.;
RT "TRIM7 modulates NCOA4-mediated ferritinophagy and ferroptosis in
RT glioblastoma cells.";
RL Redox Biol. 56:102451-102451(2022).
RN [12] {ECO:0007744|PDB:6UMA, ECO:0007744|PDB:6UMB}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 338-511, INTERACTION WITH GYG1,
RP AND MUTAGENESIS OF LEU-423; SER-499 AND CYS-501.
RX PubMed=33989636; DOI=10.1016/j.jbc.2021.100772;
RA Munoz Sosa C.J., Issoglio F.M., Carrizo M.E.;
RT "Crystal structure and mutational analysis of the human TRIM7 B30.2 domain
RT provide insights into the molecular basis of its binding to glycogenin-1.";
RL J. Biol. Chem. 296:100772-100772(2021).
RN [13] {ECO:0007744|PDB:7W0Q, ECO:0007744|PDB:7W0S, ECO:0007744|PDB:7W0T, ECO:0007744|PDB:7X6Y, ECO:0007744|PDB:7X6Z, ECO:0007744|PDB:7X70}
RP X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) OF 338-511, AND FUNCTION.
RX PubMed=35982226; DOI=10.1038/s41589-022-01128-x;
RA Liang X., Xiao J., Li X., Liu Y., Lu Y., Wen Y., Li Z., Che X., Ma Y.,
RA Zhang X., Zhang Y., Jian D., Wang P., Xuan C., Yu G., Li L., Zhang H.;
RT "A C-terminal glutamine recognition mechanism revealed by E3 ligase TRIM7
RT structures.";
RL Nat. Chem. Biol. 18:1214-1223(2022).
RN [14] {ECO:0007744|PDB:7Y3A, ECO:0007744|PDB:7Y3B, ECO:0007744|PDB:7Y3C}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 338-511, AND FUNCTION.
RX PubMed=35867826; DOI=10.1073/pnas.2203218119;
RA Ru Y., Yan X., Zhang B., Song L., Feng Q., Ye C., Zhou Z., Yang Z., Li Y.,
RA Zhang Z., Li Q., Mi W., Dong C.;
RT "C-terminal glutamine acts as a C-degron targeted by E3 ubiquitin ligase
RT TRIM7.";
RL Proc. Natl. Acad. Sci. U.S.A. 119:2203218119-2203218119(2022).
RN [15] {ECO:0007744|PDB:8A5L, ECO:0007744|PDB:8A5M, ECO:0007744|PDB:8A8X}
RP X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS) OF 342-511, FUNCTION, MUTAGENESIS OF
RP ASN-383; ARG-385; PHE-426 AND GLN-436, SUBUNIT, AND UBIQUITINATION.
RX PubMed=35893676; DOI=10.3390/v14081610;
RA Luptak J., Mallery D.L., Jahun A.S., Albecka A., Clift D., Ather O.,
RA Slodkowicz G., Goodfellow I., James L.C.;
RT "TRIM7 Restricts Coxsackievirus and Norovirus Infection by Detecting the C-
RT Terminal Glutamine Generated by 3C Protease Processing.";
RL Viruses 14:1610-1610(2022).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that have both tumor-promoting
CC and tumor-suppressing activities and functions in several biological
CC processes including innate immunity, regulation of ferroptosis as well
CC as cell proliferation and migration (PubMed:25851810, PubMed:32853985,
CC PubMed:34062120). Acts as an antiviral effector against multiple
CC viruses by targeting specific viral proteins for ubiquitination and
CC degradation including norovirus NTPase protein or SARS-CoV-2 NSP5 and
CC NSP8 proteins (PubMed:34062120, PubMed:35982226). Mechanistically,
CC recognizes the C-terminal glutamine-containing motif usually generated
CC by viral proteases that process the polyproteins and trigger their
CC ubiquitination and subsequent degradation (PubMed:35982226,
CC PubMed:35867826, PubMed:35893676). Mediates 'Lys-63'-linked
CC polyubiquitination and stabilization of the JUN coactivator RNF187 in
CC response to growth factor signaling via the MEK/ERK pathway, thereby
CC regulating JUN transactivation and cellular proliferation
CC (PubMed:25851810). Promotes the TLR4-mediated signaling activation
CC through its E3 ligase domain leading to production of pro-inflammatory
CC cytokines and type I interferon (By similarity). Also plays a negative
CC role in the regulation of exogenous cytosolic DNA virus-triggered
CC immune response. Mechanistically, enhances the 'Lys-48'-linked
CC ubiquitination of STING1 leading to its proteasome-dependent
CC degradation (PubMed:32126128). Mediates the ubiquitination of the SIN3-
CC HDAC chromatin remodeling complex component BRMS1 (PubMed:32853985).
CC Modulates NCOA4-mediated ferritinophagy and ferroptosis in glioblastoma
CC cells by ubiquitinating NCOA4, leading to its degradation
CC (PubMed:36067704). {ECO:0000250|UniProtKB:Q923T7,
CC ECO:0000269|PubMed:25851810, ECO:0000269|PubMed:32126128,
CC ECO:0000269|PubMed:32853985, ECO:0000269|PubMed:34062120,
CC ECO:0000269|PubMed:35867826, ECO:0000269|PubMed:35893676,
CC ECO:0000269|PubMed:35982226, ECO:0000269|PubMed:36067704}.
CC -!- FUNCTION: (Microbial infection) Promotes Zika virus replication by
CC mediating envelope protein E ubiquitination.
CC {ECO:0000269|PubMed:32641828}.
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:25851810};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:25851810}.
CC -!- SUBUNIT: Forms homodimers (PubMed:35893676). Interacts with GNIP2
CC (PubMed:14984203, PubMed:25851810). Interacts with GYG1
CC (PubMed:11916970, PubMed:14984203, PubMed:33989636). Interacts with
CC RNF187 (via C-terminus) (PubMed:25851810).
CC {ECO:0000269|PubMed:11916970, ECO:0000269|PubMed:14984203,
CC ECO:0000269|PubMed:25851810, ECO:0000269|PubMed:35893676}.
CC -!- INTERACTION:
CC Q9C029; P29972: AQP1; NbExp=3; IntAct=EBI-2813981, EBI-745213;
CC Q9C029; P50895: BCAM; NbExp=3; IntAct=EBI-2813981, EBI-10212133;
CC Q9C029; A0A2R8YD28: CDK13; NbExp=3; IntAct=EBI-2813981, EBI-22523896;
CC Q9C029; Q9Y281: CFL2; NbExp=3; IntAct=EBI-2813981, EBI-351218;
CC Q9C029; P07315: CRYGC; NbExp=3; IntAct=EBI-2813981, EBI-6875941;
CC Q9C029; Q9UBT7: CTNNAL1; NbExp=3; IntAct=EBI-2813981, EBI-514206;
CC Q9C029; P52657: GTF2A2; NbExp=3; IntAct=EBI-2813981, EBI-1045262;
CC Q9C029; Q9NWZ3: IRAK4; NbExp=3; IntAct=EBI-2813981, EBI-448378;
CC Q9C029; Q9UI95: MAD2L2; NbExp=3; IntAct=EBI-2813981, EBI-77889;
CC Q9C029; Q5VZE5: NAA35; NbExp=3; IntAct=EBI-2813981, EBI-9106478;
CC Q9C029; Q96AH0: NABP1; NbExp=3; IntAct=EBI-2813981, EBI-2889252;
CC Q9C029; Q7L8S5: OTUD6A; NbExp=3; IntAct=EBI-2813981, EBI-11960139;
CC Q9C029; P61019: RAB2A; NbExp=3; IntAct=EBI-2813981, EBI-752037;
CC Q9C029; Q13671: RIN1; NbExp=3; IntAct=EBI-2813981, EBI-366017;
CC Q9C029; P07998: RNASE1; NbExp=3; IntAct=EBI-2813981, EBI-2823523;
CC Q9C029; Q9UHP6: RSPH14; NbExp=3; IntAct=EBI-2813981, EBI-748350;
CC Q9C029; P57060: RWDD2B; NbExp=3; IntAct=EBI-2813981, EBI-724442;
CC Q9C029; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-2813981, EBI-747107;
CC Q9C029; Q8NBR0: TP53I13; NbExp=3; IntAct=EBI-2813981, EBI-11992976;
CC Q9C029; Q8TBZ6: TRMT10A; NbExp=3; IntAct=EBI-2813981, EBI-11059925;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:32853985}. Cytoplasm
CC {ECO:0000269|PubMed:32641828, ECO:0000269|PubMed:32853985,
CC ECO:0000269|PubMed:34062120}. Golgi apparatus
CC {ECO:0000269|PubMed:32641828}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=GNIP1;
CC IsoId=Q9C029-2; Sequence=Displayed;
CC Name=2; Synonyms=GNIP2;
CC IsoId=Q9C029-3; Sequence=VSP_009020;
CC Name=3; Synonyms=GNIP3;
CC IsoId=Q9C029-4; Sequence=VSP_009018, VSP_009019;
CC Name=4; Synonyms=TRIM7;
CC IsoId=Q9C029-1; Sequence=VSP_009021, VSP_009022;
CC -!- TISSUE SPECIFICITY: Skeletal muscle and placenta, at lower levels in
CC heart, brain and pancreas. Isoform 1 is widely expressed with high
CC level in testis, kidney and heart. {ECO:0000269|PubMed:14984203}.
CC -!- DOMAIN: The B30.2 domain mediates interaction with GYG1.
CC {ECO:0000269|PubMed:14984203}.
CC -!- DOMAIN: The coiled-coil region mediates homodimerization and
CC heterodimerization. {ECO:0000269|PubMed:14984203}.
CC -!- PTM: Phosphorylated at Ser-107 by RPS6KA5/MSK1, which stimulates the
CC ubiquitin ligase activity. {ECO:0000269|PubMed:25851810}.
CC -!- PTM: Auto-ubiquitinates via 'Lys-63'-linked polyubiquitination.
CC {ECO:0000269|PubMed:35893676}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AF220032; AAG53486.1; -; mRNA.
DR EMBL; AF396651; AAK85377.1; -; mRNA.
DR EMBL; AF396652; AAK85378.1; -; mRNA.
DR EMBL; AF396653; AAK85379.1; -; mRNA.
DR EMBL; AF396654; AAK85380.1; -; mRNA.
DR EMBL; AF396655; AAK85381.1; -; mRNA.
DR EMBL; CH471165; EAW53718.1; -; Genomic_DNA.
DR EMBL; CH471165; EAW53716.1; -; Genomic_DNA.
DR EMBL; CH471165; EAW53717.1; -; Genomic_DNA.
DR EMBL; CH471165; EAW53719.1; -; Genomic_DNA.
DR EMBL; BC011567; AAH11567.1; -; mRNA.
DR EMBL; BC080553; AAH80553.1; -; mRNA.
DR EMBL; BC132863; AAI32864.1; -; mRNA.
DR EMBL; BC132867; AAI32868.1; -; mRNA.
DR CCDS; CCDS43414.1; -. [Q9C029-4]
DR CCDS; CCDS4462.1; -. [Q9C029-2]
DR CCDS; CCDS4463.1; -. [Q9C029-3]
DR CCDS; CCDS4464.1; -. [Q9C029-1]
DR RefSeq; NP_203128.1; NM_033342.3. [Q9C029-1]
DR RefSeq; NP_976038.1; NM_203293.2. [Q9C029-2]
DR RefSeq; NP_976039.1; NM_203294.1. [Q9C029-3]
DR RefSeq; NP_976040.1; NM_203295.1. [Q9C029-3]
DR RefSeq; NP_976041.1; NM_203296.1. [Q9C029-3]
DR RefSeq; NP_976042.1; NM_203297.1. [Q9C029-4]
DR RefSeq; XP_016865392.1; XM_017009903.1.
DR RefSeq; XP_016865393.1; XM_017009904.1. [Q9C029-1]
DR PDB; 6UMA; X-ray; 1.60 A; A/B=338-511.
DR PDB; 6UMB; X-ray; 1.80 A; A/B=338-511.
DR PDB; 7OVX; X-ray; 1.70 A; A=342-511.
DR PDB; 7OW2; X-ray; 2.17 A; A/B/C/D=342-511.
DR PDB; 7W0Q; X-ray; 1.10 A; A=338-511.
DR PDB; 7W0S; X-ray; 1.40 A; B/C/E=338-511.
DR PDB; 7W0T; X-ray; 1.57 A; B/C/F=338-511.
DR PDB; 7X6Y; X-ray; 1.39 A; A=338-511.
DR PDB; 7X6Z; X-ray; 1.43 A; A=338-511.
DR PDB; 7X70; X-ray; 1.25 A; A=338-511.
DR PDB; 7Y3A; X-ray; 1.70 A; A/B/C=338-511.
DR PDB; 7Y3B; X-ray; 1.76 A; A=338-511.
DR PDB; 7Y3C; X-ray; 1.71 A; A=338-511.
DR PDB; 8A5L; X-ray; 1.62 A; A=342-511.
DR PDB; 8A5M; X-ray; 2.92 A; A/B=342-511.
DR PDB; 8A8X; X-ray; 2.37 A; A/C=342-511.
DR PDBsum; 6UMA; -.
DR PDBsum; 6UMB; -.
DR PDBsum; 7OVX; -.
DR PDBsum; 7OW2; -.
DR PDBsum; 7W0Q; -.
DR PDBsum; 7W0S; -.
DR PDBsum; 7W0T; -.
DR PDBsum; 7X6Y; -.
DR PDBsum; 7X6Z; -.
DR PDBsum; 7X70; -.
DR PDBsum; 7Y3A; -.
DR PDBsum; 7Y3B; -.
DR PDBsum; 7Y3C; -.
DR PDBsum; 8A5L; -.
DR PDBsum; 8A5M; -.
DR PDBsum; 8A8X; -.
DR AlphaFoldDB; Q9C029; -.
DR SMR; Q9C029; -.
DR BioGRID; 123579; 98.
DR IntAct; Q9C029; 35.
DR MINT; Q9C029; -.
DR STRING; 9606.ENSP00000274773; -.
DR iPTMnet; Q9C029; -.
DR PhosphoSitePlus; Q9C029; -.
DR BioMuta; TRIM7; -.
DR DMDM; 38605728; -.
DR EPD; Q9C029; -.
DR jPOST; Q9C029; -.
DR MassIVE; Q9C029; -.
DR MaxQB; Q9C029; -.
DR PaxDb; 9606-ENSP00000274773; -.
DR PeptideAtlas; Q9C029; -.
DR ProteomicsDB; 79946; -. [Q9C029-2]
DR ProteomicsDB; 79947; -. [Q9C029-1]
DR ProteomicsDB; 79948; -. [Q9C029-3]
DR ProteomicsDB; 79949; -. [Q9C029-4]
DR Pumba; Q9C029; -.
DR TopDownProteomics; Q9C029-2; -. [Q9C029-2]
DR Antibodypedia; 29710; 174 antibodies from 27 providers.
DR DNASU; 81786; -.
DR Ensembl; ENST00000274773.12; ENSP00000274773.7; ENSG00000146054.18. [Q9C029-2]
DR Ensembl; ENST00000334421.5; ENSP00000334666.5; ENSG00000146054.18. [Q9C029-1]
DR Ensembl; ENST00000393315.5; ENSP00000376991.1; ENSG00000146054.18. [Q9C029-3]
DR Ensembl; ENST00000393319.7; ENSP00000376994.3; ENSG00000146054.18. [Q9C029-4]
DR Ensembl; ENST00000422067.2; ENSP00000391458.2; ENSG00000146054.18. [Q9C029-3]
DR GeneID; 81786; -.
DR KEGG; hsa:81786; -.
DR MANE-Select; ENST00000274773.12; ENSP00000274773.7; NM_203293.3; NP_976038.1.
DR UCSC; uc003mmv.2; human. [Q9C029-2]
DR AGR; HGNC:16278; -.
DR CTD; 81786; -.
DR DisGeNET; 81786; -.
DR GeneCards; TRIM7; -.
DR HGNC; HGNC:16278; TRIM7.
DR HPA; ENSG00000146054; Tissue enhanced (brain, skeletal muscle, tongue).
DR MIM; 609315; gene.
DR neXtProt; NX_Q9C029; -.
DR OpenTargets; ENSG00000146054; -.
DR PharmGKB; PA38398; -.
DR VEuPathDB; HostDB:ENSG00000146054; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT01030000234669; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; Q9C029; -.
DR OMA; DMKMHIC; -.
DR OrthoDB; 3453019at2759; -.
DR PhylomeDB; Q9C029; -.
DR TreeFam; TF342569; -.
DR PathwayCommons; Q9C029; -.
DR SignaLink; Q9C029; -.
DR SIGNOR; Q9C029; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 81786; 17 hits in 1195 CRISPR screens.
DR ChiTaRS; TRIM7; human.
DR GenomeRNAi; 81786; -.
DR Pharos; Q9C029; Tbio.
DR PRO; PR:Q9C029; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9C029; Protein.
DR Bgee; ENSG00000146054; Expressed in vastus lateralis and 129 other cell types or tissues.
DR Genevisible; Q9C029; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProt.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0140374; P:antiviral innate immune response; IDA:UniProt.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR CDD; cd19762; Bbox2_TRIM7-like; 1.
DR CDD; cd16594; RING-HC_TRIM7-like_C-IV; 1.
DR CDD; cd13740; SPRY_PRY_TRIM7; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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; IPR000315; Znf_B-box.
DR InterPro; IPR020457; Znf_B-box_chordata.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR24103; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1.
DR PANTHER; PTHR24103:SF689; E3 UBIQUITIN-PROTEIN LIGASE TRIM7; 1.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF15227; zf-C3HC4_4; 1.
DR PRINTS; PR01406; BBOXZNFINGER.
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; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57850; RING/U-box; 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; Antiviral defense; Coiled coil;
KW Cytoplasm; Golgi apparatus; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..511
FT /note="E3 ubiquitin-protein ligase TRIM7"
FT /id="PRO_0000056204"
FT DOMAIN 324..511
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 29..82
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 125..166
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 166..263
FT /evidence="ECO:0000255"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 107
FT /note="Phosphoserine; by RPS6KA5"
FT /evidence="ECO:0000269|PubMed:25851810"
FT VAR_SEQ 1..208
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11916970"
FT /id="VSP_009020"
FT VAR_SEQ 1..182
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11916970"
FT /id="VSP_009018"
FT VAR_SEQ 183..206
FT /note="VLKKELEDCEVFRSTEKKESKELL -> MTQATGQMLCLHVQVPLQLLLLGQ
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11916970"
FT /id="VSP_009019"
FT VAR_SEQ 207..221
FT /note="KQMAAEQEKVGAEFQ -> VSQAPAGPPWDITEA (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11331580,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_009021"
FT VAR_SEQ 222..511
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11331580,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_009022"
FT VARIANT 18
FT /note="A -> S (in dbSNP:rs3857300)"
FT /id="VAR_017399"
FT VARIANT 73
FT /note="P -> S (in dbSNP:rs2770946)"
FT /id="VAR_017400"
FT VARIANT 95
FT /note="Q -> E (in dbSNP:rs2770945)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_017401"
FT VARIANT 258
FT /note="V -> A (in dbSNP:rs416574)"
FT /id="VAR_052125"
FT VARIANT 363
FT /note="G -> S (in dbSNP:rs254460)"
FT /id="VAR_052126"
FT MUTAGEN 29
FT /note="C->A: Abolishes ubiquitination and stabilization of
FT RNF187; when associated with A-32."
FT /evidence="ECO:0000269|PubMed:25851810,
FT ECO:0000269|PubMed:36067704"
FT MUTAGEN 32
FT /note="C->A: Abolishes ubiquitination and stabilization of
FT RNF187; when associated with A-29."
FT /evidence="ECO:0000269|PubMed:25851810,
FT ECO:0000269|PubMed:36067704"
FT MUTAGEN 57
FT /note="W->A: Abolishes ubiquitination and stabilization of
FT RNF187."
FT /evidence="ECO:0000269|PubMed:25851810"
FT MUTAGEN 107
FT /note="S->A: Abolishes phosphorylation by RPS6KA5/MSK1.
FT Reduced ubiquitination activity towards RNF187."
FT /evidence="ECO:0000269|PubMed:25851810"
FT MUTAGEN 383
FT /note="N->A: Complete loss of substrate binding."
FT /evidence="ECO:0000269|PubMed:35893676"
FT MUTAGEN 385
FT /note="R->A: Complete loss of substrate binding."
FT /evidence="ECO:0000269|PubMed:35893676"
FT MUTAGEN 423
FT /note="L->A: Complete loss of interaction with GYG1."
FT /evidence="ECO:0000269|PubMed:33989636"
FT MUTAGEN 426
FT /note="F->A: Complete loss of substrate binding."
FT /evidence="ECO:0000269|PubMed:35893676"
FT MUTAGEN 436
FT /note="Q->A: Complete loss of substrate binding."
FT /evidence="ECO:0000269|PubMed:35893676"
FT MUTAGEN 499
FT /note="S->A: Complete loss of interaction with GYG1."
FT /evidence="ECO:0000269|PubMed:33989636"
FT MUTAGEN 501
FT /note="C->A: Complete loss of interaction with GYG1."
FT /evidence="ECO:0000269|PubMed:33989636"
FT TURN 348..350
FT /evidence="ECO:0007829|PDB:7W0Q"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:7W0Q"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:7W0Q"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:8A5M"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:7W0Q"
FT STRAND 385..389
FT /evidence="ECO:0007829|PDB:7W0Q"
FT STRAND 392..403
FT /evidence="ECO:0007829|PDB:7W0Q"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:7W0Q"
FT STRAND 409..415
FT /evidence="ECO:0007829|PDB:7W0Q"
FT STRAND 421..423
FT /evidence="ECO:0007829|PDB:8A5L"
FT HELIX 428..430
FT /evidence="ECO:0007829|PDB:7W0Q"
FT STRAND 432..438
FT /evidence="ECO:0007829|PDB:7W0Q"
FT STRAND 441..444
FT /evidence="ECO:0007829|PDB:7W0Q"
FT STRAND 447..449
FT /evidence="ECO:0007829|PDB:7W0Q"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:7X70"
FT STRAND 459..466
FT /evidence="ECO:0007829|PDB:7W0Q"
FT TURN 467..470
FT /evidence="ECO:0007829|PDB:7W0Q"
FT STRAND 471..476
FT /evidence="ECO:0007829|PDB:7W0Q"
FT TURN 477..479
FT /evidence="ECO:0007829|PDB:7W0Q"
FT STRAND 482..487
FT /evidence="ECO:0007829|PDB:7W0Q"
FT STRAND 494..500
FT /evidence="ECO:0007829|PDB:7W0Q"
FT STRAND 502..504
FT /evidence="ECO:0007829|PDB:7X70"
FT STRAND 507..509
FT /evidence="ECO:0007829|PDB:7W0Q"
SQ SEQUENCE 511 AA; 56631 MW; 05C37C837A462597 CRC64;
MAAVGPRTGP GTGAEALALA AELQGEATCS ICLELFREPV SVECGHSFCR ACIGRCWERP
GAGSVGAATR APPFPLPCPQ CREPARPSQL RPNRQLAAVA TLLRRFSLPA AAPGEHGSQA
AAARAAAARC GQHGEPFKLY CQDDGRAICV VCDRAREHRE HAVLPLDEAV QEAKELLESR
LRVLKKELED CEVFRSTEKK ESKELLKQMA AEQEKVGAEF QALRAFLVEQ EGRLLGRLEE
LSREVAQKQN ENLAQLGVEI TQLSKLSSQI QETAQKPDLD FLQEFKSTLS RCSNVPGPKP
TTVSSEMKNK VWNVSLKTFV LKGMLKKFKE DLRGELEKEE KVELTLDPDT ANPRLILSLD
LKGVRLGERA QDLPNHPCRF DTNTRVLASC GFSSGRHHWE VEVGSKDGWA FGVARESVRR
KGLTPFTPEE GVWALQLNGG QYWAVTSPER SPLSCGHLSR VRVALDLEVG AVSFYAVEDM
RHLYTFRVNF QERVFPLFSV CSTGTYLRIW P
//
