TRIM6 (Kr.11p15) , RNF89
TRIM6 geeni
sijaitsee useiden kr.11 TRIMgeenien kanssa klusterissa segmentissä 11p15.4. Sen
lokalisoituminen on tumaan ja funktiota ei ollut tarkasti ilmoitettu
vielä vuonna 2010. Geeni ilmenee eniten munuaisessa ja testiksessä
ja hieman myös 15 muussa kudoksessa. Alternatiivein pleissauksin
kirjoittuu useita variantteja. TRIM6:n osuutta on todettu
interferonivasteen (IFN-1) kehittämisessä . Muutama vakavia
tauteja aiheuttava virus on kaapannut TRIM6 -toiminta-alueen
avustamaan omaa replikaatiotaan ja kumomamaan TRIM6- välitteisen
antiviraalin interferonivasteen.
On havaittu , että
TRIM34 voi muodostaa fuusioproteiinin tämän TRIM6:n kanssa
interferonista riippuvalla geeniluennalla (Se on ”read through
RNF 21”(IFP1, IFN responsive finger protein1) , TRIM34 -TRIM6 ja
on saanut oman RNF nimen ja sisältää kaksi RING- domeenia
pisimmässä versiossaan).
- Gene TRIM6, RNF89
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- Summary The protein encoded by this gene is a member of the tripartite motif (TRIM) family. https://www.ncbi.nlm.nih.gov/gene/117854
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- The TRIM motif includes three zinc-binding domains, a RING, B-box type 1 and B-box type 2 domain, and a coiled-coil region. The protein localizes to the nucleus, but its specific function has not been identified. This gene is mapped to chromosome 11p15, where it resides within a TRIM gene cluster. Alternative splicing results in multiple transcript variants. A read-through transcript from this gene into the downstream TRIM34 gene has also been observed, which results in a fusion product from these neighboring family members. [provided by RefSeq, Oct 2010] Expression Broad expression in kidney (RPKM 10.6), testis (RPKM 6.4) and 15 other tissues See more
Rakennetietoa: konservoituneet domeenit ( variantti 1:stä isoformi 1)
Conserved Domains
(4) summary
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Location:121 → 161 - BBOX; B-Box-type zinc finger
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cd15823
Location:327 → 514 - SPRY_PRY_TRIM6; PRY/SPRY domain in tripartite motif-binding protein 6 (TRIM6), also known as RING finger protein 89 (RNF89)
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cl17238
Location:43 → 87 - RING; RING-finger (Really Interesting New Gene) domain, a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc; defined by the 'cross-brace' motif C-X2-C-X(9-39)-C-X(1-3)- H-X(2-3)-(N/C/H)-X2-C-X(4-48)C-X2-C; probably involved in ...
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cl23765
Location:170 → 287 - iSH2_PI3K_IA_R; Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunits
Kaapattu TRIM6: EBOV virusproteiini VP35
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The Host E3-Ubiquitin Ligase TRIM6 Ubiquitinates the Ebola Virus VP35 Protein and Promotes Virus Replication. Bharaj P, et al. J Virol, 2017 Sep 15. PMID 28679761, Free PMC Article . Ebolavirus kuuluu Filoviridae perheeseen ja on hyvin patogeeninen virus aiehutaten vaikeita verenvuotokuumeita ihmisessä ja järjestää epidemioita Saharan eteläisissä alueissa, Keski- ja Länsi-Afrikassa . EBOV genomi koodaa proteiinia VP35 ja se on virukselle tärkeä replikaatiossa viruspolymeraasin essentiellinä osana ja myös vahvana antagonistina isäntäkehon antivirusvaikutteiselle interferonille IFN-I- järjestelmälle. Tutkijat selvittivät että VP35 ubikitinoituu lysiiniin K309, joka sijaitsee sen IFN-antagonimsidomeenissa. Lisäksi he havaitsivat ,etä VP35 tekee interaktion E3 ubikitiiniligaasi TRIM6:n kanssa . Tutkijat ovat aiemmin osoittaneet, että TRIM6 edistää ankkuroimattomien K48-linkkiytyneiden polyubikitiiniketjujen synteesiä eikä ne ole kovalentisti littyneinä mihinkään proteiiniin ja niiden tarkoitus on indusoida tehokasta IFN-1-välitteistä antivirusvastetta. Johdonmukaisesti tämän tiedon mukaan myös Ebolan VP35 liittyy näihin polyubikitiiniketjuihin ja tekee tyhjäksi TRIM6:n yrittämän IFN-I induktion.Lisäksi tutkijat havaitsivat, että TRIM6 lisää Ebolaviruksen polymeraasin aktiivisuutta (minigenomi mentelmässä). TRIM6 poistogeenisissä soluissa infektoiva EBOV replikoitui vähemmän. Nämä tiedot viittaisivat siihen, että VP35 on kaapannut TRIM6:n, luonnollisen immuniteetin antivirustekijän ja asettanut sen edistämään EBOV replikaatiota ubikitinaatioillaan.
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Abstract Ebola virus (EBOV), a member of the Filoviridae family, is a highly pathogenic virus that causes severe hemorrhagic fever in humans and is responsible for epidemics throughout sub-Saharan, central, and West Africa. The EBOV genome encodes VP35, an important viral protein involved in virus replication by acting as an essential cofactor of the viral polymerase as well as a potent antagonist of the host antiviral type I interferon (IFN-I) system. By using mass spectrometry analysis and coimmunoprecipitation assays, we show here that VP35 is ubiquitinated on lysine 309 (K309), a residue located on its IFN antagonist domain. We also found that VP35 interacts with TRIM6, a member of the E3-ubiquitin ligase tripartite motif (TRIM) family. We recently reported that TRIM6 promotes the synthesis of unanchored K48-linked polyubiquitin chains, which are not covalently attached to any protein, to induce efficient antiviral IFN-I-mediated responses. Consistent with this notion, VP35 also associated noncovalently with polyubiquitin chains and inhibited TRIM6-mediated IFN-I induction. Intriguingly, we also found that TRIM6 enhances EBOV polymerase activity in a minigenome assay and TRIM6 knockout cells have reduced replication of infectious EBOV, suggesting that VP35 hijacks TRIM6 to promote EBOV replication through ubiquitination.
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Tämä työ antaa näyttöä TRIM6:n merkityksestä isäntäkehon tärkeänä solutekijänä, joka on alkanut edistää EBOV-replikaatiota. Tulevaiset tutkimukset keskittyvät siihen, olisiko TRIM6 mahdollinen kohde EBOV-infektion vastaisissa terapeuttisissa interventioissa. TÄRKEYS: EBOV kuuluu erittäin patogeenisten virusten perheeseen ja aiheuttaa vaikeita hemorrhagioita ihmisissä ja muissa imettäväisissä kortaliteetin ollessa korkea(40- 90%). koska se on kokrkeasti patogeeninen eikä vahvistettuja antiviraaleja lääkkeitä tai rokkotteita ole, EBOV on listattu kärkeen sekä väärinkäyttöriskiasteikkossa 1 että infektiotekijänä riksiluokkaa 4 (tier 1 select-agent risk group 4).
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Tärkeänä mekanismina EBOV-infektion vakavuudessa on se, että kumoaa luonnollisen immuniteetin vasteet eli etulinjan puolustuksen kehosta. EBOV proteiini VP35 antaa osuutensa patogeneesiin, koska se on viruspolymeraasin välttämätön kofaktori sekä lisäki luonnollisen immuuniteetin vahva antagonisti. Mutta ymmärretään aika niukasti, miten isäntäkehon tekijät säätävät VP35:n.
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Tämä artikkeli raportoi , kuinka isäntäkehon E3-ligaasi TRIM6 edistää VP35:n ubikitinaatiota ja tulee tärkeäksi viruksen tehokkaalle replikoitumiselle. TRIM6 pidetään uutena havaittuna isäntäkehotekijänä joka voi toimia mahdollisena kohteena kehitettäessä ebolaviruksen vastaisia antiviruslääkkeitä. Yksi tärkeä mekanismi Ebolavirusinfektion vakavuudessa on luonnollisen immuniteetin virusvasteen kumoaminen.
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Our work provides evidence that TRIM6 is an important host cellular factor that promotes EBOV replication, and future studies will focus on whether TRIM6 could be targeted for therapeutic intervention against EBOV infection. IMPORTANCE EBOV belongs to a family of highly pathogenic viruses that cause severe hemorrhagic fever in humans and other mammals with high mortality rates (40 to 90%). Because of its high pathogenicity and lack of licensed antivirals and vaccines, EBOV is listed as a tier 1 select-agent risk group 4 pathog responses. The EBOV VP35 protein contributes to pathogenesis, because it serves as an essential cofactor of the viral polymerase as well as a potent antagonist of innate immunity. However, how VP35 function is regulated by host cellular factors is poorly understood. Here, we report that the host E3-ubiquitin ligase TRIM6 promotes VP35 ubiquitination and is important for efficient virus replication. Therefore, our study identifies a new host factor, TRIM6, as a potential target in the development of antiviral drugs against EBOV. An important mechanism for the severity of EBOV infection is its suppression of innate immune
TRIM6-TRIM34 fuusioproteiini (RNF21) (IFP1=IFN responsive Fingerprotein 1)
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Molecular cloning of ring finger protein 21 (RNF21)/interferon-responsive finger protein (ifp1), which possesses two RING-B box-coiled coil domains in tandem. Orimo A, et al. Genomics, 2000 Oct 1. PMID 11013086 Genomics. 2000 Oct 1;69(1):143-9. (Suomennosta) (Tämä ilmeinen fuusioproteiini kahdesta RING- domeenista katsotaan eräässä luettelossa (RNF21) TRIM6-TRIM34 fuusioksi ja löytyy RNF haulla).
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On kloonattu molekulaarisesti RNF21/IFN-responsiivinen finger proteiini(IFP1) koko pituudeltaan Sillä on kolme isoformia. Pitkä muoto on RBCC-RBCC-B30.2 -domaaninen (fuusio) , keskimolekulaarinen muoto RBCC-B30.2 domaaninen ja lyhyt muoto RBCC- domaaninen. Keskimmäinen muoto säätyi ylös vahvasti interferonistimuluksesta. RNF21 katsotaan alavirran geeniksi, joka välittänee interferonin biologisia vasteita.
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Molecular cloning of ring finger protein 21 (RNF21)/interferon-responsive finger protein (ifp1), which possesses two RING-B box-coiled coil domains in tandem. Orimo A1, Tominaga N, et al. AbstractWe have cloned the full length of a novel cDNA, named ring finger protein 21 (RNF21), composed of the RING finger-B box-coiled coil (RBCC) domain and the B30.2 domain, which are characteristic of the RBCC-B30.2 family. As a structural feature, the RNF21 cDNA possessed at least three kinds of isoforms, due to alternative splicing, consisting of the long form with the RBCC-RBCC-B30.2 domain, the medium form with the RBCC-B30.2 domain, and the short form with only the RBCC domain. Moreover, respective transcripts corresponding to the three isoforms were detected in various human organs by reverse transcription-PCR and Northern blot analyses. Interestingly, the medium form of the RNF21 mRNA expressed most predominantly was dramatically up-regulated within 8-16 h by interferon stimulation of HeLa cells. These findings suggest that RNF21 is a downstream gene that may mediate interferon's biological action.
TRIM6 , TRIM34, TRIM5alfa sitoutuvat HIV-1 kapsidiin, mutta eivät pysty tekemään restriktiota
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Binding of the rhesus TRIM5α PRYSPRY domain to capsid is necessary but not sufficient for HIV-1 restriction. Yang Y, et al. Virology, 2014 Jan 5. PMID 24314652, Free PMC Article
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(Suom) TRIM6, TRIM34 ja TRIM5alfa sitoutuvat HIV-1 viruksen kapsidiin mutta eivät aiheutta restriktiota.
Miten NIPA-virus (NiV) on interferoniantagonisti? Uusia löytöjä : TRIM6 hajoitus NiV-M matrixproteiinilla
Nipavirusrelevanssi. http://www.who.int/csr/disease/nipah/en/
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Tehokkaasti replikoituakseen virukset ovat evolutionalisesti kehittäneet luonnollisen immuunivasteen kiertäviä ja välttäviä mekanismeja (evaasio). Nipah-virus kuuluu paramyxoviruksiin (henipa-virussukuun) ja on hyvin patogeeninen. Tunnetaan sen koodaavan neljää virusproteiinia (P/C/W/V) ja niillä on IFN-1-antagonistinen funktio. Tässä artikkelissa tutkijat raportoivat, että myös Nipa-viruksen matrixproteiini NiV_M voi estää IFN-1 interferonivasteen. Tämä matrixproteiini on virukselle tärkeä sen uusian osien koostumisessa ja uuden virionin silmukoitumisessa ulos isäntäsolusta.
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Kehoa puolustavaan IFN-I-interferonituotantoon tarvitaan monia signaloivia komponentteja ja niihin kuuluu IkB-kinaasi epsilon (IKKe). Aiemmin on kuvattu, miten TRIM6 (E3 ubikitiiniligaasi) katalysoi ankkuroimattomien K48-linkkiytyneiden polyubikitiiniketjujen muodostusta - ne eivät kiinnity kovalentisti mihinkään proteiiniin, mutta ne aktivoivat täysitehoisen IKKe- proteiinin, joka (osana signaaliketjua ) indusoi interferonituotannon (IFN-I) ja siitä seuraa eriasteista antivirusvastetta.
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Tutkimusryhmä osoitti, että Nipa-viruksen M-proteiini tekee interaktion TRIM6 E3 ligaasiin ja edistää sen hajoamista. Tästä on johdonmukainen seuraus, että niitä ankkuroimattomia K48-linkkiytyneitä ubikitiiniketjuja ilmenee yhä vähemmän IKKe;n saattamiseksi tehokkaaksi. Sen oligomerisaatio jää puutteelliseksi, se autofosforyloituu ja IFN-välitteinen antivirusvaste solussa heikkenee.
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For efficient replication, viruses have developed mechanisms to evade innate immune responses, including the antiviral type-I interferon (IFN-I) system. Nipah virus (NiV), a highly pathogenic member of the Paramyxoviridae family (genus Henipavirus), is known to encode for four P gene-derived viral proteins (P/C/W/V) with IFN-I antagonist functions. Here we report that NiV matrix protein (NiV-M), which is important for virus assembly and budding, can also inhibit IFN-I responses. IFN-I production requires activation of multiple signaling components including the IκB kinase epsilon (IKKε). We previously showed that the E3-ubiquitin ligase TRIM6 catalyzes the synthesis of unanchored K48-linked polyubiquitin chains, which are not covalently attached to any protein, and activate IKKε for induction of IFN-I mediated antiviral responses. Using co-immunoprecipitation assays and confocal microscopy we show here that the NiV-M protein interacts with TRIM6 and promotes TRIM6 degradation. Consequently, NiV-M expression results in reduced levels of unanchored K48-linked polyubiquitin chains associated with IKKε leading to impaired IKKε oligomerization, IKKε autophosphorylation and reduced IFN-mediated responses.
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Tämä interferoniantagonismi, mitä Nipaviruksen matrixproteiini (NiV-M) omaa, vaatii konservoituneen lysiinin(K258) kaksiosaisessa tumaan lokalisoivassa signaalissa (NLS)- joita löytyy eri henipa-viruksilta. Tästä johtuen interferonia IFNbeta voi estää mös seuraavien virusten amtrixproteiinit: Ghana virus, Hendra virus ja Cedar virus. Elävä NiV- virus ( mutta ei sensijaan M-proteiinivajeiset rekombinantit NiV) vähensi endogeenista TRIM6 proteiinin ilmenemistä Tutkijat mainitsevat, että ennen tätä tutkimusta ei ole raportoitu että myös paramyxovirusten matrixproteiini (M) osallistuvat luonnollisen immuunivasteen antagonisoimiseen. Tässä on raportoituna luonnollisen immuunijärjestelmän evaasiomekanismi, joka kohdistuu TRIM6- , IKKe- ja ankkuroimattomien polyubikitiiniketjujen molekyyleihin. Löydät laajentavat käsitystä virusten interferoniantagonismistrategioista ja samalla antavat vihjettä uusista kohteista terapeuttisten interventioiden kehittelyyn Nipavirusinfektioita vastaan.
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This IFN antagonist function of NiV-M requires a conserved lysine residue (K258) in the bipartite nuclear localization signal that is found in divergent henipaviruses. Consistent with this, the matrix proteins of Ghana, Hendra and Cedar viruses were also able to inhibit IFNβ induction. Live NiV infection, but not a recombinant NiV lacking the M protein, reduced the levels of endogenous TRIM6 protein expression. To our knowledge, matrix proteins of paramyxoviruses have never been reported to be involved in innate immune antagonism. We report here a novel mechanism of viral innate immune evasion by targeting TRIM6, IKKε and unanchored polyubiquitin chains. These findings expand the universe of viral IFN antagonism strategies and provide a new potential target for development of therapeutic interventions against NiV infections.
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Determinants
of the higher order association of the restriction factor TRIM5alpha
and other tripartite motif (TRIM) proteins. Li X, et al.
J Biol Chem, 2011 Aug 12. PMID 21680743, Free
PMC Article
GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?
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TRIM6 and the E2-ubiquitin conjugase UbE2K cooperated in the synthesis of unanchored K48-linked polyubiquitin chains, which activated IKKepsilon for subsequent STAT1 phosphorylation. Type I interferons (IFN-I) are essential antiviral cytokines produced upon microbial infection. IFN-I elicits this activity through the upregulation of hundreds of IFN-I-stimulated genes (ISGs). The full breadth of ISG induction demands activation of a number of cellular factors including the IκB kinase epsilon (IKKε). However, the mechanism of IKKε activation upon IFN receptor signaling has remained elusive. Here we show that TRIM6, a member of the E3-ubiquitin ligase tripartite motif (TRIM) family of proteins, interacted with IKKε and promoted induction of IKKε-dependent ISGs. TRIM6 and the E2-ubiquitin conjugase UbE2K cooperated in the synthesis of unanchored K48-linked polyubiquitin chains, which activated IKKε for subsequent STAT1 phosphorylation. Our work attributes a previously unrecognized activating role of K48-linked unanchored polyubiquitin chains in kinase activation and identifies the UbE2K-TRIM6-ubiquitin axis as critical for IFN signaling and antiviral response.
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heterologous
RING, B-box 2, and CC domains from related TRIM proteins can
functionally substitute for TRIM5alpha(rh) domains.
TRIM6 ja MYC, embryonaalisessa kantasolussa
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Trim6 interacts with MYC and maintain the pluripotency of
mouse embryonal stem cells(EC)
http://jcs.biologists.org/content/125/6/1544
- (Suomennosta) TRIM tekee interaktion MYC kanssa ja pitää
yllä hiiren embryonaalisten kantasolujen pluripotentiaalisuutta.
Muistiin 12.4. 2018
Alla on eräs TRIM6 rakenne, kyse on isoformista 3.
tripartite
motif-containing protein 6 isoform 3 [Homo sapiens]
NCBI Reference Sequence: NP_001185573.1Identical Proteins FASTA Graphics
LOCUS NP_001185573 313 aa linear PRI 05-MAR-2018 DEFINITION tripartite motif-containing protein 6 isoform 3 [Homo sapiens]. ACCESSION NP_001185573 VERSION NP_001185573.1 DBSOURCE REFSEQ: accession NM_001198644.1 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 313) AUTHORS Bharaj P, Atkins C, Luthra P, Giraldo MI, Dawes BE, Miorin L, Johnson JR, Krogan NJ, Basler CF, Freiberg AN and Rajsbaum R. TITLE The Host E3-Ubiquitin Ligase TRIM6 Ubiquitinates the Ebola Virus VP35 Protein and Promotes Virus Replication JOURNAL J. Virol. 91 (18), e00833-17 (2017) PUBMED 28679761 REMARK GeneRIF: Intriguingly, the authors also found that TRIM6 enhances ebola virus polymerase activity in a minigenome assay and TRIM6 knockout cells have reduced replication of infectious ebola virus, suggesting that VP35 hijacks TRIM6 to promote ebola virus replication through ubiquitination. Publication Status: Online-Only REFERENCE 2 (residues 1 to 313) AUTHORS Bharaj P, Wang YE, Dawes BE, Yun TE, Park A, Yen B, Basler CF, Freiberg AN, Lee B and Rajsbaum R. TITLE The Matrix Protein of Nipah Virus Targets the E3-Ubiquitin Ligase TRIM6 to Inhibit the IKKepsilon Kinase-Mediated Type-I IFN Antiviral Response JOURNAL PLoS Pathog. 12 (9), e1005880 (2016) PUBMED 27622505 REMARK GeneRIF: Live NiV infection, but not a recombinant NiV lacking the M protein, reduced the levels of endogenous TRIM6 protein expression. To our knowledge, matrix proteins of paramyxoviruses have never been reported to be involved in innate immune antagonism. We report here a novel mechanism of viral innate immune evasion by targeting TRIM6, IKKepsilon and unanchored polyubiquitin chains. Publication Status: Online-Only REFERENCE 3 (residues 1 to 313) 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 4 (residues 1 to 313) AUTHORS Rajsbaum R, Versteeg GA, Schmid S, Maestre AM, Belicha-Villanueva A, Martinez-Romero C, Patel JR, Morrison J, Pisanelli G, Miorin L, Laurent-Rolle M, Moulton HM, Stein DA, Fernandez-Sesma A, tenOever BR and Garcia-Sastre A. TITLE Unanchored K48-linked polyubiquitin synthesized by the E3-ubiquitin ligase TRIM6 stimulates the interferon-IKKepsilon kinase-mediated antiviral response JOURNAL Immunity 40 (6), 880-895 (2014) PUBMED 24882218 REMARK GeneRIF: TRIM6 and the E2-ubiquitin conjugase UbE2K cooperated in the synthesis of unanchored K48-linked polyubiquitin chains, which activated IKKepsilon for subsequent STAT1 phosphorylation. REFERENCE 5 (residues 1 to 313) AUTHORS Lauc G, Huffman JE, Pucic M, Zgaga L, Adamczyk B, Muzinic A, Novokmet M, Polasek O, Gornik O, Kristic J, Keser T, Vitart V, Scheijen B, Uh HW, Molokhia M, Patrick AL, McKeigue P, Kolcic I, Lukic IK, Swann O, van Leeuwen FN, Ruhaak LR, Houwing-Duistermaat JJ, Slagboom PE, Beekman M, de Craen AJ, Deelder AM, Zeng Q, Wang W, Hastie ND, Gyllensten U, Wilson JF, Wuhrer M, Wright AF, Rudd PM, Hayward C, Aulchenko Y, Campbell H and Rudan I. TITLE Loci associated with N-glycosylation of human immunoglobulin G show pleiotropy with autoimmune diseases and haematological cancers JOURNAL PLoS Genet. 9 (1), e1003225 (2013) PUBMED 23382691 REFERENCE 6 (residues 1 to 313) AUTHORS Li X, Gold B, O'hUigin C, Diaz-Griffero F, Song B, Si Z, Li Y, Yuan W, Stremlau M, Mische C, Javanbakht H, Scally M, Winkler C, Dean M and Sodroski J. TITLE Unique features of TRIM5alpha among closely related human TRIM family members JOURNAL Virology 360 (2), 419-433 (2007) PUBMED 17156811 REFERENCE 7 (residues 1 to 313) AUTHORS Li X, Li Y, Stremlau M, Yuan W, Song B, Perron M and Sodroski J. TITLE Functional replacement of the RING, B-box 2, and coiled-coil domains of tripartite motif 5alpha (TRIM5alpha) by heterologous TRIM domains JOURNAL J. Virol. 80 (13), 6198-6206 (2006) PUBMED 16775307 REMARK GeneRIF: heterologous RING, B-box 2, and CC domains from related TRIM proteins can functionally substitute for TRIM5alpha(rh) domains. REFERENCE 8 (residues 1 to 313) AUTHORS Woo JS, Imm JH, Min CK, Kim KJ, Cha SS and Oh BH. TITLE Structural and functional insights into the B30.2/SPRY domain JOURNAL EMBO J. 25 (6), 1353-1363 (2006) PUBMED 16498413 REFERENCE 9 (residues 1 to 313) 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 10 (residues 1 to 313) AUTHORS Orimo A, Tominaga N, Yoshimura K, Yamauchi Y, Nomura M, Sato M, Nogi Y, Suzuki M, Suzuki H, Ikeda K, Inoue S and Muramatsu M. TITLE Molecular cloning of ring finger protein 21 (RNF21)/interferon-responsive finger protein (ifp1), which possesses two RING-B box-coiled coil domains in tandem JOURNAL Genomics 69 (1), 143-149 (2000) PUBMED 11013086 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from AK290172.1, BC047564.1, DA401634.1, AK298301.1, AK316178.1, AK293295.1, AF220030.1 and AK023210.1. 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, B-box type 1 and B-box type 2 domain, and a coiled-coil region. The protein localizes to the nucleus, but its specific function has not been identified. This gene is mapped to chromosome 11p15, where it resides within a TRIM gene cluster. Alternative splicing results in multiple transcript variants. A read-through transcript from this gene into the downstream TRIM34 gene has also been observed, which results in a fusion product from these neighboring family members. [provided by RefSeq, Oct 2010]. Transcript Variant: This variant (3) lacks an alternate exon in the 5' coding region, and uses a downstream AUG start codon, compared to variant 1. The encoded isoform (3) has a shorter N-terminus, compared to isoform 1. Both variants 3 and 4 encode the same isoform. 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 :: AK298301.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968832, SAMEA1968968 [ECO:0000348] ##Evidence-Data-END## FEATURES Location/Qualifiers source 1..313 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="11" /map="11p15.4" Protein 1..313 /product="tripartite motif-containing protein 6 isoform 3" /EC_number="2.3.2.27" /note="RING finger protein 89; RING-type E3 ubiquitin transferase TRIM6" /calculated_mol_wt=36269 Region 124..311 /region_name="SPRY_PRY_TRIM6" /note="PRY/SPRY domain in tripartite motif-binding protein 6 (TRIM6), also known as RING finger protein 89 (RNF89); cd15823" /db_xref="CDD:293995" CDS 1..313 /gene="TRIM6" /gene_synonym="RNF89" /coded_by="NM_001198644.1:383..1324" /note="isoform 3 is encoded by transcript variant 3" /db_xref="CCDS:CCDS55738.1" /db_xref="GeneID:117854" /db_xref="HGNC:HGNC:16277" /db_xref="MIM:607564" ORIGIN 1 mepercriqt efnqlrnild rveqrelkkl eqeekkglri ieeaendlvh qtqslrelis 61 dlerrcqgst mellqdvsdv tersefwtlr kpealptklr smfrapdlkr mlrvcreltd 121 vqsywvdvtl nphtanlnlv laknrrqvrf vgakvsgpsc lekhydcsvl gsqhfssgkh 181 ywevdvakkt awilgvcsns lgptfsfnhf aqnhsaysry qpqsgywvig lqhnheyray 241 edsspsllls mtvpprrvgv fldyeagtvs fynvtnhgfp iytfskyyfp ttlcpyfnpc 301 ncvipmtlrr pss
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