TRIML_MOUSE
ID TRIML_MOUSE Reviewed; 470 AA.
AC Q8BVP1;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Probable E3 ubiquitin-protein ligase TRIML1;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIML1 {ECO:0000305};
DE AltName: Full=Tripartite motif family-like protein 1;
GN Name=Triml1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP FUNCTION, INTERACTION WITH USP5, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=19156909; DOI=10.1002/mrd.20997;
RA Tian L., Wu X., Lin Y., Liu Z., Xiong F., Han Z., Zhou Y., Zeng Q.,
RA Wang Y., Deng J., Chen H.;
RT "Characterization and potential function of a novel pre-implantation
RT embryo-specific RING finger protein: TRIML1.";
RL Mol. Reprod. Dev. 76:656-664(2009).
CC -!- FUNCTION: Probable E3 ubiquitin-protein ligase which plays an important
CC role in blastocyst development. Involved in progression of blastocyst
CC stage and subsequent embryo development. {ECO:0000269|PubMed:19156909}.
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:0000269|PubMed:19156909}.
CC -!- TISSUE SPECIFICITY: Testis. {ECO:0000269|PubMed:19156909}.
CC -!- DEVELOPMENTAL STAGE: Expressed from two-cell to blastocyst stage of
CC embryo development. {ECO:0000269|PubMed:19156909}.
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DR EMBL; AK077092; BAC36608.1; -; mRNA.
DR CCDS; CCDS22266.1; -.
DR RefSeq; NP_808410.1; NM_177742.4.
DR AlphaFoldDB; Q8BVP1; -.
DR SMR; Q8BVP1; -.
DR STRING; 10090.ENSMUSP00000050267; -.
DR iPTMnet; Q8BVP1; -.
DR PhosphoSitePlus; Q8BVP1; -.
DR PaxDb; Q8BVP1; -.
DR PRIDE; Q8BVP1; -.
DR ProteomicsDB; 258848; -.
DR Antibodypedia; 29145; 125 antibodies from 19 providers.
DR DNASU; 244448; -.
DR Ensembl; ENSMUST00000059692; ENSMUSP00000050267; ENSMUSG00000031651.
DR GeneID; 244448; -.
DR KEGG; mmu:244448; -.
DR UCSC; uc009lnz.1; mouse.
DR CTD; 339976; -.
DR MGI; MGI:2687279; Triml1.
DR VEuPathDB; HostDB:ENSMUSG00000031651; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000154582; -.
DR HOGENOM; CLU_013137_0_0_1; -.
DR InParanoid; Q8BVP1; -.
DR OMA; GHSFCLM; -.
DR OrthoDB; 423686at2759; -.
DR PhylomeDB; Q8BVP1; -.
DR TreeFam; TF338674; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 244448; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Triml1; mouse.
DR PRO; PR:Q8BVP1; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8BVP1; protein.
DR Bgee; ENSMUSG00000031651; Expressed in spermatid and 10 other tissues.
DR Genevisible; Q8BVP1; MM.
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 1: Evidence at protein level;
KW Coiled coil; Developmental protein; Metal-binding; Reference proteome;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..470
FT /note="Probable E3 ubiquitin-protein ligase TRIML1"
FT /id="PRO_0000274599"
FT DOMAIN 273..470
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 22..63
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT COILED 135..170
FT /evidence="ECO:0000255"
FT COILED 196..235
FT /evidence="ECO:0000255"
SQ SEQUENCE 470 AA; 53787 MW; 41906582DFE64BD7 CRC64;
MSNHEKMSTT DLMENLREEL TCFICLDYFS SPVTTECGHS FCLMCLLKSW EEHNTPLSCP
ECWRTLGAPH FQANERLGRL ANIGRQLRSQ VLQSEDEQSI CGRMPGPSWV FSDDEQSVIN
VSPPSQGTNK ACFSSEAEEQ HKEKLQDIIN ILRKKKKEVQ AILNHEKERV MLCKEETKTC
KQVVVSEYMK MHQFLKEEEQ LQLQLLEREE KANMKKLREN EIQLTQQIRR LGKMIGRIES
TCQNLTLESF EEVKGAMDRY ESLLFQSPET TITELSLCHI TGMREMLRKF STDITLDPAT
ANAYLLLSED LKSVRYGGTR QQLPDNPERF DQSATVLGAQ IFTCGRHYWE VEVGKKTEWE
VGICKDSVNR KGNLPKPPGD LFSLIGLKIG DDYSLWVSSP LKGQHVREPV HKVGVFLDYD
SGHIAFYNAT DESLIYSFPP TPFHEALRPI FSPCLPNEGT NTDPLIICHI
