TRIM17 (Kr.1q42.13)
Tämän TRIM17
rakenteeseen kuuluu RING, Bbox1 , Bbox2 ja Coiled-Coil domaanit.
Proteiini lokalisoituu sytoplasmakappaleisiin. Proteiinia ilmenee
miltei yksinomaan testiksessä ja funktio oli tuntematon
vielä 2008. Monia vaihtoehtoisia transkripteja pleissautuu. Geeniä
ilmenee myös pernassa ja 11 muussa kudoksessa. Viime vuosien löytöjä
TRIM17:n funktiosta on sen osallistuminen solunjakautumisen
koneiston jäteproteiinien degradaatioon, nämä jäänteet ovat
tunnettuja autofagian kohteena olevia proteiineja. Monet
alternatiivisti pleissautuvat variantit saattavat tehostaa tällaista
funktiota. TRIM17 osallistuu myös neuronaaliseen apotoosiin
vuorovaikuttamalla NFATc3 resiprokaaliseen säätelyyn.8Tästä on mainitaa aiemin)
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https://www.ncbi.nlm.nih.gov/gene/51127
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- Also known as RBCC; terf; RNF16. Summary The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The protein localizes to cytoplasmic bodies. The protein is expressed almost exclusively in the testis, but its function is unknown. Multiple alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Jul 2008] Expression Biased expression in testis (RPKM 5.7), spleen (RPKM 1.3) and 11 other tissues See more
Rakenteesta. Konservoidut domeenit.
BBOX; B-Box-type zinc finger; zinc binding domain (CHC3H2); often
present in combination with other motifs, like RING zinc finger, NHL
motif, coiled-coil or RFP domain in functionally unrelated proteins,
most likely mediating protein-protein interaction.
cd15812
Location:296 → 472
Location:296 → 472
SPRY_PRY_TRIM17;
PRY/SPRY domain of tripartite motif-binding protein 17 (TRIM17), also
known as testis RING finger protein (terf)
RING-HC_TRIM17_C-IV;
RING finger, HC subclass, found in tripartite motif-containing
protein TRIM17 and similar proteins
Location:13 → 66
Location:13 → 66
Rakenne, isoformi 1
GenPept
E3 ubiquitin-protein
ligase TRIM17 isoform 1 [Homo sapiens]
NCBI Reference Sequence: NP_001020111.1Identical Proteins FASTA Graphics
LOCUS NP_001020111 477 aa linear PRI 11-FEB-2018 DEFINITION E3 ubiquitin-protein ligase TRIM17 isoform 1 [Homo sapiens]. ACCESSION NP_001020111 VERSION NP_001020111.1 DBSOURCE REFSEQ: accession NM_001024940.2 KEYWORDS RefSeq. SOURCE Homo sapiens (human) ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 477) AUTHORS Mandell MA, Jain A, Kumar S, Castleman MJ, Anwar T, Eskelinen EL, Johansen T, Prekeris R and Deretic V. TITLE TRIM17 contributes to autophagy of midbodies while actively sparing other targets from degradation JOURNAL J. Cell. Sci. 129 (19), 3562-3573 (2016) PUBMED 27562068 REMARK GeneRIF: TRIM17 promoted the removal of midbodies, remnants of the cell division machinery that are known autophagy targets. Erratum:[J Cell Sci. 2017 Mar 15;130(6):1194. PMID: 28298613] REFERENCE 2 (residues 1 to 477) AUTHORS Yang X, Coulombe-Huntington J, Kang S, Sheynkman GM, Hao T, Richardson A, Sun S, Yang F, Shen YA, Murray RR, Spirohn K, Begg BE, Duran-Frigola M, MacWilliams A, Pevzner SJ, Zhong Q, Trigg SA, Tam S, Ghamsari L, Sahni N, Yi S, Rodriguez MD, Balcha D, Tan G, Costanzo M, Andrews B, Boone C, Zhou XJ, Salehi-Ashtiani K, Charloteaux B, Chen AA, Calderwood MA, Aloy P, Roth FP, Hill DE, Iakoucheva LM, Xia Y and Vidal M. TITLE Widespread Expansion of Protein Interaction Capabilities by Alternative Splicing JOURNAL Cell 164 (4), 805-817 (2016) PUBMED 26871637 REFERENCE 3 (residues 1 to 477) AUTHORS Mojsa B, Mora S, Bossowski JP, Lassot I and Desagher S. TITLE Control of neuronal apoptosis by reciprocal regulation of NFATc3 and Trim17 JOURNAL Cell Death Differ. 22 (2), 274-286 (2015) PUBMED 25215946 REMARK GeneRIF: NFATc3 interacted in a SUMO-dependent manner with Trim17, an E3 ubiquitin ligase necessary for neuronal apoptosis REFERENCE 4 (residues 1 to 477) AUTHORS Mandell MA, Jain A, Arko-Mensah J, Chauhan S, Kimura T, Dinkins C, Silvestri G, Munch J, Kirchhoff F, Simonsen A, Wei Y, Levine B, Johansen T and Deretic V. TITLE TRIM proteins regulate autophagy and can target autophagic substrates by direct recognition JOURNAL Dev. Cell 30 (4), 394-409 (2014) PUBMED 25127057 REFERENCE 5 (residues 1 to 477) AUTHORS Woodsmith J, Jenn RC and Sanderson CM. TITLE Systematic analysis of dimeric E3-RING interactions reveals increased combinatorial complexity in human ubiquitination networks JOURNAL Mol. Cell Proteomics 11 (7), M111.016162 (2012) PUBMED 22493164 REFERENCE 6 (residues 1 to 477) AUTHORS Urano T, Usui T, Takeda S, Ikeda K, Okada A, Ishida Y, Iwayanagi T, Otomo J, Ouchi Y and Inoue S. TITLE TRIM44 interacts with and stabilizes terf, a TRIM ubiquitin E3 ligase JOURNAL Biochem. Biophys. Res. Commun. 383 (2), 263-268 (2009) PUBMED 19358823 REMARK GeneRIF: terf interacts with TRIM44;TRIM44 inhibited ubiquitination of terf, and thus stabilized the protein. REFERENCE 7 (residues 1 to 477) AUTHORS Aurino S, Piluso G, Saccone V, Cacciottolo M, D'Amico F, Dionisi M, Totaro A, Belsito A, Di Vicino U and Nigro V. TITLE Candidate-gene testing for orphan limb-girdle muscular dystrophies JOURNAL Acta Myol 27, 90-97 (2008) PUBMED 19472918 REMARK GeneRIF: Observational study of gene-disease association. (HuGE Navigator) REFERENCE 8 (residues 1 to 477) AUTHORS Reymond A, Meroni G, Fantozzi A, Merla G, Cairo S, Luzi L, Riganelli D, Zanaria E, Messali S, Cainarca S, Guffanti A, Minucci S, Pelicci PG and Ballabio A. TITLE The tripartite motif family identifies cell compartments JOURNAL EMBO J. 20 (9), 2140-2151 (2001) PUBMED 11331580 REFERENCE 9 (residues 1 to 477) AUTHORS Ogawa S, Saito T, Matsuda Y, Seki N, Hayashi A, Orimo A, Hosoi T, Ouchi Y, Muramatsu M, Hori T and Inoue S. TITLE Chromosome mapping of RNF16 and rnf16, human, mouse and rat genes coding for testis RING finger protein (terf), a member of the RING finger family JOURNAL Cytogenet. Cell Genet. 89 (1-2), 56-58 (2000) PUBMED 10894938 REFERENCE 10 (residues 1 to 477) AUTHORS Ogawa S, Goto W, Orimo A, Hosoi T, Ouchi Y, Muramatsu M and Inoue S. TITLE Molecular cloning of a novel RING finger-B box-coiled coil (RBCC) protein, terf, expressed in the testis JOURNAL Biochem. Biophys. Res. Commun. 251 (2), 515-519 (1998) PUBMED 9792805 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from DA270450.1, BC033788.1 and AW770403.1. Summary: The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The protein localizes to cytoplasmic bodies. The protein is expressed almost exclusively in the testis, but its function is unknown. Multiple alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Jul 2008]. Transcript Variant: This variant (2) lacks a segment in the 5' UTR, as compared to variant 1. Variants 1 and 2 encode the same isoform (1). Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BC023999.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1968189, SAMEA1968540 [ECO:0000350] ##Evidence-Data-END## FEATURES Location/Qualifiers source 1..477 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="1" /map="1q42.13" Protein 1..477 /product="E3 ubiquitin-protein ligase TRIM17 isoform 1" /EC_number="2.3.2.27" /note="ring finger protein 16; RING finger protein terf; testis RING finger protein; E3 ubiquitin-protein ligase TRIM17; tripartite motif-containing protein 17; RING-type E3 ubiquitin transferase TRIM17" /calculated_mol_wt=54287 Region 13..66 /region_name="RING-HC_TRIM17_C-IV" /note="RING finger, HC subclass, found in tripartite motif-containing protein TRIM17 and similar proteins; cd16595" /db_xref="CDD:319509" Region 16..65 /region_name="RING-HC finger (C3HC4-type)" /note="RING-HC finger (C3HC4-type) [structural motif]" /db_xref="CDD:319509" Site order(16,19,31,33,36,39,62,65) /site_type="other" /note="Zn binding site [ion binding]" /db_xref="CDD:319509" Region 97..134 /region_name="BBOX" /note="B-Box-type zinc finger; zinc binding domain (CHC3H2); often present in combination with other motifs, like RING zinc finger, NHL motif, coiled-coil or RFP domain in functionally unrelated proteins, most likely mediating protein-protein interaction; cd00021" /db_xref="CDD:237988" Site order(99,102,121,127) /site_type="other" /note="Zn2+ binding site [ion binding]" /db_xref="CDD:237988" Region 296..472 /region_name="SPRY_PRY_TRIM17" /note="PRY/SPRY domain of tripartite motif-binding protein 17 (TRIM17), also known as testis RING finger protein (terf); cd15812" /db_xref="CDD:293984" CDS 1..477 /gene="TRIM17" /gene_synonym="RBCC; RNF16; terf" /coded_by="NM_001024940.2:350..1783" /note="isoform 1 is encoded by transcript variant 2" /db_xref="CCDS:CCDS1571.1" /db_xref="GeneID:51127" /db_xref="HGNC:HGNC:13430" /db_xref="MIM:606123" ORIGIN 1 meavelarkl qeeatcsicl dyftdpvmtt cghnfcraci qlswekargk kgrrkrkgsf 61 pcpecremsp qrnllpnrll tkvaemaqqh pglqkqdlcq ehheplklfc qkdqspicvv 121 cresrehrlh rvlpaeeavq gyklkleedm eylreqitrt gnlqareeqs laewqgkvke 181 rrerivlefe kmnlylveee qrllqalete eeetasrlre svacldrqgh slellllqle 241 erstqgplqm lqdmkeplsr knnvsvqcpe vapptrprtv crvpgqievl rgfledvvpd 301 atsaypylll yesrqrrylg sspegsgfcs kdrfvaypca vgqtafssgr hywevgmnit 361 gdalwalgvc rdnvsrkdrv pkcpengfwv vqlskgtkyl stfsaltpvm lmeppshmgi 421 fldfeagevs fysvsdgshl htysqatfpg plqpffclga pksgqmvist vtmwvkg //
