TRIML_HUMAN
ID TRIML_HUMAN Reviewed; 468 AA.
AC Q8N9V2; Q96BE5;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Probable E3 ubiquitin-protein ligase TRIML1;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 209;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIML1 {ECO:0000305};
DE AltName: Full=Tripartite motif family-like protein 1;
GN Name=TRIML1; Synonyms=RNF209;
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 [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [4]
RP VARIANT [LARGE SCALE ANALYSIS] HIS-21.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Probable E3 ubiquitin-protein ligase which plays an important
CC role in blastocyst development. {ECO:0000250|UniProtKB:Q8BVP1}.
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: Interacts with USP5. {ECO:0000250|UniProtKB:Q8BVP1}.
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DR EMBL; AK093499; BAC04185.1; -; mRNA.
DR EMBL; AC138781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015684; AAH15684.1; -; mRNA.
DR EMBL; BC113860; AAI13861.1; -; mRNA.
DR EMBL; BC114469; AAI14470.1; -; mRNA.
DR CCDS; CCDS3851.1; -.
DR RefSeq; NP_848651.2; NM_178556.4.
DR AlphaFoldDB; Q8N9V2; -.
DR SMR; Q8N9V2; -.
DR BioGRID; 130974; 5.
DR IntAct; Q8N9V2; 2.
DR STRING; 9606.ENSP00000327738; -.
DR iPTMnet; Q8N9V2; -.
DR PhosphoSitePlus; Q8N9V2; -.
DR BioMuta; TRIML1; -.
DR DMDM; 74729772; -.
DR EPD; Q8N9V2; -.
DR MassIVE; Q8N9V2; -.
DR PaxDb; Q8N9V2; -.
DR PeptideAtlas; Q8N9V2; -.
DR PRIDE; Q8N9V2; -.
DR ProteomicsDB; 72587; -.
DR Antibodypedia; 29145; 125 antibodies from 19 providers.
DR DNASU; 339976; -.
DR Ensembl; ENST00000332517.4; ENSP00000327738.3; ENSG00000184108.8.
DR GeneID; 339976; -.
DR KEGG; hsa:339976; -.
DR MANE-Select; ENST00000332517.4; ENSP00000327738.3; NM_178556.5; NP_848651.2.
DR UCSC; uc003izm.2; human.
DR CTD; 339976; -.
DR DisGeNET; 339976; -.
DR GeneCards; TRIML1; -.
DR HGNC; HGNC:26698; TRIML1.
DR HPA; ENSG00000184108; Tissue enriched (testis).
DR neXtProt; NX_Q8N9V2; -.
DR OpenTargets; ENSG00000184108; -.
DR PharmGKB; PA162407030; -.
DR VEuPathDB; HostDB:ENSG00000184108; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000154582; -.
DR HOGENOM; CLU_013137_0_0_1; -.
DR InParanoid; Q8N9V2; -.
DR OMA; GHSFCLM; -.
DR OrthoDB; 423686at2759; -.
DR PhylomeDB; Q8N9V2; -.
DR TreeFam; TF338674; -.
DR PathwayCommons; Q8N9V2; -.
DR SignaLink; Q8N9V2; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 339976; 7 hits in 1104 CRISPR screens.
DR GenomeRNAi; 339976; -.
DR Pharos; Q8N9V2; Tdark.
DR PRO; PR:Q8N9V2; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q8N9V2; protein.
DR Bgee; ENSG00000184108; Expressed in left testis and 17 other tissues.
DR Genevisible; Q8N9V2; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0010508; P:positive regulation of autophagy; IBA:GO_Central.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IBA:GO_Central.
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:0032880; P:regulation of protein localization; IBA:GO_Central.
DR GO; GO:0046596; P:regulation of viral entry into host cell; IBA:GO_Central.
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; 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 PRINTS; PR01407; BUTYPHLNCDUF.
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; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Developmental protein; Metal-binding; Reference proteome;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..468
FT /note="Probable E3 ubiquitin-protein ligase TRIML1"
FT /id="PRO_0000274598"
FT DOMAIN 267..468
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 16..57
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT COILED 133..158
FT /evidence="ECO:0000255"
FT COILED 184..237
FT /evidence="ECO:0000255"
FT VARIANT 21
FT /note="D -> H (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035963"
FT VARIANT 132
FT /note="E -> K (in dbSNP:rs13131525)"
FT /id="VAR_052145"
SQ SEQUENCE 468 AA; 53002 MW; 66F9E2DABC5C96B8 CRC64;
MSTADLMENL REELTCFICL DYFSSPVTTE CGHSFCLVCL LRSWEEHNTP LSCPECWRTL
EGPHFQSNER LGRLASIARQ LRSQVLQSED EQGSYGRMPT TAKALSDDEQ GGSAFVAQSH
GANRVHLSSE AEEHHREKLQ EILNLLRVRR KEAQAVLTHE KERVKLCQEE TKTCKQVVVS
EYMKMHQFLK EEEQLQLQLL EQEEKENMRK LRNNEIKLTQ QIRSLSKMIA QIESSSQSSA
FESLEEVRGA LERSEPLLLQ CPEATTTELS LCRITGMKEM LRKFSTEITL DPATANAYLV
LSEDLKSVKY GGSRQQLPDN PERFDQSATV LGTQIFTSGR HYWEVEVGNK TEWEVGICKD
SVSRKGNLPK PPGDLFSLIG LKIGDDYSLW VSSPLKGQHV REPVCKVGVF LDYESGHIAF
YNGTDESLIY SFPQASFQEA LRPIFSPCLP NEGTNTDPLT ICSLNSHV
