TRI45_HUMAN
ID TRI45_HUMAN Reviewed; 580 AA.
AC Q9H8W5; Q53GN0; Q5T2K4; Q5T2K5; Q8IYV6;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Tripartite motif-containing protein 45;
DE AltName: Full=RING finger protein 99;
GN Name=TRIM45; Synonyms=RNF99;
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 1), VARIANT THR-496, FUNCTION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryonic heart;
RX PubMed=15351693; DOI=10.1016/j.bbrc.2004.08.048;
RA Wang Y., Li Y., Qi X., Yuan W., Ai J., Zhu C., Cao L., Yang H., Liu F.,
RA Wu X., Liu M.;
RT "TRIM45, a novel human RBCC/TRIM protein, inhibits transcriptional
RT activities of ElK-1 and AP-1.";
RL Biochem. Biophys. Res. Commun. 323:9-16(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-496.
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 MRNA], AND VARIANTS TYR-375 AND THR-496.
RC TISSUE=Kidney;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT THR-496.
RC TISSUE=Testis;
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 [6]
RP STRUCTURE BY NMR OF 396-501.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the filamin domain from human tripartite motif
RT protein 45.";
RL Submitted (DEC-2006) to the PDB data bank.
CC -!- FUNCTION: May act as a transcriptional repressor in mitogen-activated
CC protein kinase signaling pathway. {ECO:0000269|PubMed:15351693}.
CC -!- INTERACTION:
CC Q9H8W5-2; Q9BTE6-2: AARSD1; NbExp=3; IntAct=EBI-11993364, EBI-9357295;
CC Q9H8W5-2; P60520: GABARAPL2; NbExp=3; IntAct=EBI-11993364, EBI-720116;
CC Q9H8W5-2; Q9BTT4: MED10; NbExp=3; IntAct=EBI-11993364, EBI-394354;
CC Q9H8W5-2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-11993364, EBI-16439278;
CC Q9H8W5-2; Q13148: TARDBP; NbExp=3; IntAct=EBI-11993364, EBI-372899;
CC Q9H8W5-2; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-11993364, EBI-529518;
CC Q9H8W5-2; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-11993364, EBI-11139477;
CC Q9H8W5-2; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-11993364, EBI-1105213;
CC Q9H8W5-2; Q96E35: ZMYND19; NbExp=3; IntAct=EBI-11993364, EBI-746595;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15351693}. Nucleus
CC {ECO:0000269|PubMed:15351693}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H8W5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H8W5-2; Sequence=VSP_012000;
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle, brain, heart and
CC pancreas. {ECO:0000269|PubMed:15351693}.
CC -!- DEVELOPMENTAL STAGE: Expressed in brain, lung, skeletal muscle, heart
CC and intestine in 80-day old embryo. {ECO:0000269|PubMed:15351693}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AY669488; AAT76864.1; -; mRNA.
DR EMBL; AK023243; BAB14484.1; -; mRNA.
DR EMBL; AK222901; BAD96621.1; -; mRNA.
DR EMBL; AL391476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034943; AAH34943.1; -; mRNA.
DR CCDS; CCDS44200.1; -. [Q9H8W5-2]
DR CCDS; CCDS893.1; -. [Q9H8W5-1]
DR RefSeq; NP_001139107.1; NM_001145635.1. [Q9H8W5-2]
DR RefSeq; NP_079464.2; NM_025188.3. [Q9H8W5-1]
DR PDB; 2DS4; NMR; -; A=396-501.
DR PDBsum; 2DS4; -.
DR AlphaFoldDB; Q9H8W5; -.
DR SMR; Q9H8W5; -.
DR BioGRID; 123205; 29.
DR IntAct; Q9H8W5; 12.
DR STRING; 9606.ENSP00000256649; -.
DR iPTMnet; Q9H8W5; -.
DR PhosphoSitePlus; Q9H8W5; -.
DR BioMuta; TRIM45; -.
DR DMDM; 90110721; -.
DR EPD; Q9H8W5; -.
DR MassIVE; Q9H8W5; -.
DR PaxDb; Q9H8W5; -.
DR PeptideAtlas; Q9H8W5; -.
DR PRIDE; Q9H8W5; -.
DR ProteomicsDB; 81250; -. [Q9H8W5-1]
DR ProteomicsDB; 81251; -. [Q9H8W5-2]
DR Antibodypedia; 33887; 241 antibodies from 21 providers.
DR DNASU; 80263; -.
DR Ensembl; ENST00000256649.9; ENSP00000256649.4; ENSG00000134253.10. [Q9H8W5-1]
DR Ensembl; ENST00000369464.7; ENSP00000358476.3; ENSG00000134253.10. [Q9H8W5-2]
DR GeneID; 80263; -.
DR KEGG; hsa:80263; -.
DR MANE-Select; ENST00000256649.9; ENSP00000256649.4; NM_025188.4; NP_079464.2.
DR UCSC; uc001egz.3; human. [Q9H8W5-1]
DR CTD; 80263; -.
DR DisGeNET; 80263; -.
DR GeneCards; TRIM45; -.
DR HGNC; HGNC:19018; TRIM45.
DR HPA; ENSG00000134253; Tissue enhanced (skeletal).
DR MIM; 609318; gene.
DR neXtProt; NX_Q9H8W5; -.
DR OpenTargets; ENSG00000134253; -.
DR PharmGKB; PA134873644; -.
DR VEuPathDB; HostDB:ENSG00000134253; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000154334; -.
DR HOGENOM; CLU_013137_14_8_1; -.
DR InParanoid; Q9H8W5; -.
DR OMA; TRCPLCM; -.
DR OrthoDB; 489543at2759; -.
DR PhylomeDB; Q9H8W5; -.
DR TreeFam; TF324196; -.
DR PathwayCommons; Q9H8W5; -.
DR Reactome; R-HSA-877300; Interferon gamma signaling.
DR SignaLink; Q9H8W5; -.
DR BioGRID-ORCS; 80263; 9 hits in 1121 CRISPR screens.
DR EvolutionaryTrace; Q9H8W5; -.
DR GeneWiki; TRIM45; -.
DR GenomeRNAi; 80263; -.
DR Pharos; Q9H8W5; Tbio.
DR PRO; PR:Q9H8W5; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9H8W5; protein.
DR Bgee; ENSG00000134253; Expressed in secondary oocyte and 157 other tissues.
DR ExpressionAtlas; Q9H8W5; baseline and differential.
DR Genevisible; Q9H8W5; HS.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0060348; P:bone development; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR InterPro; IPR001298; Filamin/ABP280_rpt.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
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; PF00630; Filamin; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00557; IG_FLMN; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS50194; FILAMIN_REPEAT; 1.
DR PROSITE; PS50119; ZF_BBOX; 2.
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; Metal-binding;
KW Nucleus; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..580
FT /note="Tripartite motif-containing protein 45"
FT /id="PRO_0000056266"
FT REPEAT 394..497
FT /note="Filamin"
FT ZN_FING 29..98
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 130..176
FT /note="B box-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 186..227
FT /note="B box-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 281..335
FT /evidence="ECO:0000255"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT VAR_SEQ 390..407
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012000"
FT VARIANT 353
FT /note="R -> Q (in dbSNP:rs34863850)"
FT /id="VAR_044128"
FT VARIANT 375
FT /note="C -> Y (in dbSNP:rs749902)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_019931"
FT VARIANT 413
FT /note="R -> Q (in dbSNP:rs3738413)"
FT /id="VAR_019932"
FT VARIANT 496
FT /note="M -> T (in dbSNP:rs1289658)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15351693, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.3"
FT /id="VAR_019933"
FT TURN 399..401
FT /evidence="ECO:0007829|PDB:2DS4"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:2DS4"
FT TURN 407..410
FT /evidence="ECO:0007829|PDB:2DS4"
FT STRAND 411..413
FT /evidence="ECO:0007829|PDB:2DS4"
FT STRAND 418..423
FT /evidence="ECO:0007829|PDB:2DS4"
FT STRAND 429..431
FT /evidence="ECO:0007829|PDB:2DS4"
FT STRAND 439..447
FT /evidence="ECO:0007829|PDB:2DS4"
FT STRAND 454..458
FT /evidence="ECO:0007829|PDB:2DS4"
FT STRAND 461..470
FT /evidence="ECO:0007829|PDB:2DS4"
FT STRAND 472..485
FT /evidence="ECO:0007829|PDB:2DS4"
FT STRAND 492..498
FT /evidence="ECO:0007829|PDB:2DS4"
SQ SEQUENCE 580 AA; 64359 MW; 44DFADF69D598682 CRC64;
MSENRKPLLG FVSKLTSGTA LGNSGKTHCP LCLGLFKAPR LLPCLHTVCT TCLEQLEPFS
VVDIRGGDSD TSSEGSIFQE LKPRSLQSQI GILCPVCDAQ VDLPMGGVKA LTIDHLAVND
VMLESLRGEG QGLVCDLCND REVEKRCQTC KANLCHFCCQ AHRRQKKTTY HTMVDLKDLK
GYSRIGKPIL CPVHPAEELR LFCEFCDRPV CQDCVVGEHR EHPCDFTSNV IHKHGDSVWE
LLKGTQPHVE ALEEALAQIH IINSALQKRV EAVAADVRTF SEGYIKAIEE HRDKLLKQLE
DIRAQKENSL QLQKAQLEQL LADMRTGVEF TEHLLTSGSD LEILITKRVV VERLRKLNKV
QYSTRPGVND KIRFCPQEKA GQCRGYEIYG TINTKEVDPA KCVLQGEDLH RAREKQTASF
TLLCKDAAGE IMGRGGDNVQ VAVVPKDKKD SPVRTMVQDN KDGTYYISYT PKEPGVYTVW
VCIKEQHVQG SPFTVMVRRK HRPHSGVFHC CTFCSSGGQK TARCACGGTM PGGYLGCGHG
HKGHPGHPHW SCCGKFNEKS ECTWTGGQSA PRSLLRTVAL
