TRI16_MOUSE
ID TRI16_MOUSE Reviewed; 556 AA.
AC Q99PP9; Q7TPY6; Q8C332; Q8C6V0;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Tripartite motif-containing protein 16;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:O95361};
DE AltName: Full=E3 ubiquitin-protein ligase TRIM16;
DE AltName: Full=Estrogen-responsive B box protein;
GN Name=Trim16; Synonyms=Ebbp;
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 [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ;
RX PubMed=11919186; DOI=10.1074/jbc.m111233200;
RA Beer H.-D., Munding C., Dubois N., Mamie C., Hohl D., Werner S.;
RT "The estrogen-responsive B box protein: a novel regulator of keratinocyte
RT differentiation.";
RL J. Biol. Chem. 277:20740-20749(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Lung;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C3H/He; TISSUE=Osteoblast;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 345-556 (ISOFORMS 1/3).
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: E3 ubiquitin ligase that plays an essential role in the
CC organization of autophagic response and ubiquitination upon lysosomal
CC and phagosomal damages. Plays a role in the stress-induced biogenesis
CC and degradation of protein aggresomes by regulating the p62-KEAP1-NRF2
CC signaling and particularly by modulating the ubiquitination levels and
CC thus stability of NRF2. Acts as a scaffold protein and facilitates
CC autophagic degradation of protein aggregates by interacting with
CC p62/SQSTM, ATG16L1 and LC3B/MAP1LC3B. In turn, protects the cell
CC against oxidative stress-induced cell death as a consequence of
CC endomembrane damage. {ECO:0000250|UniProtKB:O95361}.
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:0000250|UniProtKB:O95361};
CC -!- SUBUNIT: Homodimerizes via its coiled-coil domain. Heterodimerizes with
CC MID1, TRIM24 and PML. Interacts with Galectin-3/LGALS3 in a ULK1-
CC dependent manner; this interaction mediates autophagy of damage
CC endomembranes. Interacts with BECN1. Interacts with ATG16L1. Interacts
CC with p62/SQSTM and LC3B/MAP1LC3B. {ECO:0000250|UniProtKB:O95361}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O95361}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q99PP9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99PP9-2; Sequence=VSP_009099, VSP_009100;
CC Name=3;
CC IsoId=Q99PP9-3; Sequence=VSP_009101;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in basal keratinocytes.
CC -!- PTM: Phosphorylated by ULK1. {ECO:0000250|UniProtKB:O95361}.
CC -!- PTM: Auto-ubiquitinates via its B-Boxes.
CC {ECO:0000250|UniProtKB:O95361}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AF449496; AAM46701.1; -; mRNA.
DR EMBL; AK053139; BAC35278.1; -; mRNA.
DR EMBL; AK087112; BAC39806.1; -; mRNA.
DR EMBL; BC052821; AAH52821.1; -; mRNA.
DR EMBL; AF220134; AAG53507.1; -; mRNA.
DR CCDS; CCDS24832.1; -. [Q99PP9-1]
DR RefSeq; NP_444399.2; NM_053169.2.
DR RefSeq; XP_006534643.1; XM_006534580.3. [Q99PP9-3]
DR AlphaFoldDB; Q99PP9; -.
DR SMR; Q99PP9; -.
DR BioGRID; 220447; 1.
DR STRING; 10090.ENSMUSP00000055542; -.
DR iPTMnet; Q99PP9; -.
DR PhosphoSitePlus; Q99PP9; -.
DR EPD; Q99PP9; -.
DR MaxQB; Q99PP9; -.
DR PaxDb; Q99PP9; -.
DR PeptideAtlas; Q99PP9; -.
DR PRIDE; Q99PP9; -.
DR ProteomicsDB; 259090; -. [Q99PP9-1]
DR ProteomicsDB; 259091; -. [Q99PP9-2]
DR ProteomicsDB; 259092; -. [Q99PP9-3]
DR Antibodypedia; 21540; 253 antibodies from 27 providers.
DR DNASU; 94092; -.
DR Ensembl; ENSMUST00000108703; ENSMUSP00000104343; ENSMUSG00000047821. [Q99PP9-3]
DR GeneID; 94092; -.
DR KEGG; mmu:94092; -.
DR UCSC; uc007jkc.1; mouse. [Q99PP9-1]
DR CTD; 10626; -.
DR MGI; MGI:2137356; Trim16.
DR VEuPathDB; HostDB:ENSMUSG00000047821; -.
DR eggNOG; ENOG502QRVY; Eukaryota.
DR GeneTree; ENSGT00940000161116; -.
DR HOGENOM; CLU_013137_0_2_1; -.
DR InParanoid; Q99PP9; -.
DR OrthoDB; 273204at2759; -.
DR PhylomeDB; Q99PP9; -.
DR BioGRID-ORCS; 94092; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Trim16; mouse.
DR PRO; PR:Q99PP9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q99PP9; protein.
DR Bgee; ENSMUSG00000047821; Expressed in triceps brachii and 158 other tissues.
DR ExpressionAtlas; Q99PP9; baseline and differential.
DR Genevisible; Q99PP9; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0016605; C:PML body; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0019966; F:interleukin-1 binding; ISO:MGI.
DR GO; GO:0032089; F:NACHT domain binding; ISO:MGI.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 2.60.120.920; -; 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 Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00589; PRY; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..556
FT /note="Tripartite motif-containing protein 16"
FT /id="PRO_0000056223"
FT DOMAIN 347..545
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 64..113
FT /note="B box-type 1"
FT ZN_FING 117..156
FT /note="B box-type 2"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 163..266
FT /evidence="ECO:0000255"
FT COILED 312..332
FT /evidence="ECO:0000255"
FT COMPBIAS 32..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95361"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95361"
FT VAR_SEQ 1..87
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009101"
FT VAR_SEQ 481..488
FT /note="VSPFRRLG -> AFMMTLLM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009099"
FT VAR_SEQ 489..556
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009100"
FT CONFLICT 33
FT /note="V -> A (in Ref. 2; BAC35278/BAC39806)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="L -> V (in Ref. 2; BAC35278/BAC39806)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="E -> EE (in Ref. 1; AAM46701)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="E -> K (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 481
FT /note="V -> A (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="D -> E (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 533
FT /note="N -> D (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 556 AA; 62943 MW; 1281F0FD6529B7A8 CRC64;
MAELDLIAPG PLTGVTAHPL APLGPDPVSA IPVEKEDADP LSKSGEETQE QGHDPAELGA
PGEEDQILCD FCLGASRVRA VKSCLTCMVN YCEEHLRPHQ ENSKLHSHQL TEPAKDQDLR
TCPAHHSPLV SFCHTHQQCI CQECGEGEHR GDSTVSLDAA RRNKEVDLRC MQLDLEQKLK
LNENAIARLQ ANHKSVLVSV SEVKVVAEEK FGELLAAVRK AQADVMVFLE EKEQAALNQV
NSIKTHLEHR SLEMEKSKQE LERLAAISNT VLFLEEYCKL KKTEDTASPS IYIGLKDKLS
GIRKVITDST LNLIQLLESY KEKLQEFSRE EEYDIRTQVS AIVQRKYRTS KPEPRTRDEF
LQYACDITFD PDTAHRYLRL QEDNRKVTNT TPWEHPYPDL PSRFLHWRQV LSQQSLYLHR
YYFEVELSGG GTYVGLTCKG IDRKGEERNS CISGNSFSWS IHWNGKEFTA WHSDTETPLK
VSPFRRLGIY VNFPGGILSF YGVEYDAMTL IHKFDCKFSE PVYAAFWLSK KENAIRIVDL
GEEPEKPAGS SVEAAP
