Päivitys 3.5. 2018
TRIM60 , Kr.4q32.3, RNF 129, RNF 33 (C-IV SPRYPRY) FLJ35882
RING finger
motiivin, B-box2 domaanin, kaksi CC domaania ja B30.2 domaanin
omaava TRIM
TRIM60/RNF33 . Se
tekee interaktion kinesiini-2 perheenjäseniinin Kif3A ja Kif3B
motorisiin proteiineihin, kun ne ovat heterodimerisoituneena ja
kuljettavat kuormaa pitkin mikrotubulusta.Sen on havaittu tekevän
myös proteiini-DNA-interaktioita. Tällä geenillä on pseudogeenejä
ainakin 6 eri kromosomissa (mm. Y kromosomissa, jossa esiintyy trim
vain pseudogeeneineä).
Proteiiniksi asti
koodautuvaa geeniä TRIM60 eeniä esiintyy kahdessa kudoksessa:
testiksessä ja plasentassa (istukassa).
LÄHDE PubMed Gene:
https://www.ncbi.nlm.nih.gov/gene/166655
TRIM60.
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- RNF33; RNF129 Summary The protein encoded by this gene contains a RING finger domain, a motif present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions. Pseudogenes of this gene are located on more than six chromosomes including chromosome 4. Multiple alternatively spliced variants, encoding the same protein, have been identified. [provided by RefSeq, Jan 2013] Expression Low expression observed in reference dataset See more
Rakenne:
Conserved Domains
(5) summary
cd15828
Location:286 → 465
Location:286 → 465
SPRY_PRY_TRIM60;
PRY/SPRY domain of tripartite motif-binding protein 60 (TRIM60) also
known as RING finger protein 33 (RNF33)
pfam00643
Location:92 → 133
Location:92 → 133
zf-B_box; B-box zinc
finger
pfam15905
Location:139 → 260
Location:139 → 260
HMMR_N; Hyaluronan
mediated motility receptor N-terminal
cd16607
Location:13 → 59
Location:13 → 59
RING-HC_TRIM60_like_C-IV;
RING finger, HC subclass, found in tripartite motif-containing
proteins TRIM60, TRIM61 and similar proteins
cl26688
Location:16 → 105
Location:16 → 105
DWNN; DWNN domain
Aminohappoja 471.
(http://www.uniprot.org/uniprot/Q495X7
)
Tarkemmat domeenit:
https://www.ebi.ac.uk/interpro/protein/Q495X7
PubMed: tripartite motif-containing protein 60 [Homo sapiens]
NCBI Reference
Sequence: NP_001244954.1
LOCUS NP_001244954 471 aa linear PRI 03-OCT-2017 DEFINITION tripartite motif-containing protein 60 [Homo sapiens]. ACCESSION NP_001244954 VERSION NP_001244954.1 DBSOURCE REFSEQ: accession NM_001258025.1 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 471) AUTHORS Trynka G, Zhernakova A, Romanos J, Franke L, Hunt KA, Turner G, Bruinenberg M, Heap GA, Platteel M, Ryan AW, de Kovel C, Holmes GK, Howdle PD, Walters JR, Sanders DS, Mulder CJ, Mearin ML, Verbeek WH, Trimble V, Stevens FM, Kelleher D, Barisani D, Bardella MT, McManus R, van Heel DA and Wijmenga C. TITLE Coeliac disease-associated risk variants in TNFAIP3 and REL implicate altered NF-kappaB signalling JOURNAL Gut 58 (8), 1078-1083 (2009) PUBMED 19240061 REMARK GeneRIF: Observational study of gene-disease association. (HuGE Navigator) REFERENCE 2 (residues 1 to 471) AUTHORS Saurin AJ, Borden KL, Boddy MN and Freemont PS. TITLE Does this have a familiar RING? JOURNAL Trends Biochem. Sci. 21 (6), 208-214 (1996) PUBMED 8744354 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from AC106872.5 and BC100986.2. Summary: The protein encoded by this gene contains a RING finger domain, a motif present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions. Pseudogenes of this gene are located on more than six chromosomes including chromosome 4. Multiple alternatively spliced variants, encoding the same protein, have been identified. [provided by RefSeq, Jan 2013]. Transcript Variant: This variant (1) represents the longer transcript. Both variants 1 and 2 encode the same protein. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments. ##Evidence-Data-START## CDS exon combination :: AK093201.1, BX114353.1 [ECO:0000331] RNAseq introns :: mixed/partial sample support SAMEA1968968, SAMEA2142853 [ECO:0000350] ##Evidence-Data-END## FEATURES Location/Qualifiers source 1..471 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="4" /map="4q32.3" Protein 1..471 /product="tripartite motif-containing protein 60" /note="ring finger protein 33; ring finger protein 129" /calculated_mol_wt=54983 Region 13..59 /region_name="RING-HC_TRIM60_like_C-IV" /note="RING finger, HC subclass, found in tripartite motif-containing proteins TRIM60, TRIM61 and similar proteins; cd16607" /db_xref="CDD:319521" Region <16 ..105="" region_name="<b">"DWNN"16>
Artikkeleita PubMed . ”TRIM60 PROTEIN” (2)
TRIM60 assosioituu kinesiineihin
Association
of the testis-specific TRIM/RBCC protein RNF33/TRIM60 with the
cytoplasmic motor proteins KIF3A and KIF3B. Huang CJ, Huang CC,
Chang CC.Mol Cell Biochem. 2012 Jan;360(1-2):121-31. doi:
10.1007/s11010-011-1050-8. Epub 2011 Sep 11.
RNF33/TRIM60 geeni
on ajallisesti transkriboituna hiien alkiossa
preimplantaatiovaiheessa ennea kuin geeni blastokystivaiheessa
hiljentyy, mutta aikuisella koehiireellä geeni jälleen
transkriboituu testiksessä. Tässä artikkelin tutkimuksessa
tiedemiehet selvittivät TRIM60:n biologista funktiota ja niitä
proteiineja ,jotka assosioituvat TRIM60-proteiiniin. He selvittivät
interaktiodomeenit ja havaitsivat interaktion tekevät
moottoriproteiinit, heterodimeerinä esiintyvät proteiinit KIF3A ja
KIF3B kinesiini-2- perheestä, joiden tiedetään siirtävän
kuormaa pitkin mikrotubulusta. TRIM60-proteiinin RING ja Bbox sekä
PRYSPRY (B30.2) tekivät interaktion KIF3A-KIF2B-heterodimeerin
C-terminaaliseen päätyyn ja heterodimeerin moottoripääty oli
vapaana ja valmiina designtavaroiden kuljetukseen ja
liikkumiseen pitkin mikrotubulusta . Todennäköisesti TRIM60 myös
teki interaktion KIF3A-KIF3B heterodimeerin kanssa kinesiiniin
assosioituvasta soviteproteiinista 3 (KAP3 adaptorista )
riippumattakin Tässä työssä osoitetaan ensimmäsitä kertaa ,
että TRIM60 (RNF33) tekee interaktion kinesiinin molekulaariseen
moottoriin vaikuttaen osaltaan spesifisten kuormien kinesiinistä
riippuvaan mobilisaatioon hiiren testiksen mikrotubuluksissa .
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The Rnf33/Trim60 gene is temporally transcribed in the preimplantation embryo before being silenced at the blastocyst stage but Rnf33 expression is detected in adult testis of the mouse. The putative RNF33 protein is a tripartite motif (TRIM)/RBCC protein composed of a typical RING zinc finger, a B-box 2, two α-helical coiled-coil segments, and a B30.2 domain. As a first step towards the elucidation of the biologic function of RNF33, we aimed in this study to elucidate proteins that associate with RNF33. RNF33-interacting proteins were first derived by the yeast two-hybrid system followed by co-immunoprecipitation assays. Interacting domains were determined by deletion mapping in genetic and biochemical analyzes. RNF33 was shown to interact with the kinesin-2 family members 3A (KIF3A) and 3B (KIF3B) motor proteins in the heterodimeric form known to transport cargos along the microtubule. Domain mapping showed that the RB and B30.2 domains of RNF33 interacted with the respective carboxyl non-motor domains of KIF3A and KIF3B. Since RNF33 interacted with the carboxyl-terminal tail of the KIF3A-KIF3B heterodimer, the motor head section of KIF3A-KIF3B was free and available for association with designated cargo(s) and movement along the microtubule. Data also suggest that RNF33 most likely interacted with KIF3A-KIF3B independent of the adaptor kinesin-associated protein KAP3. This study is a first demonstration of a TRIM protein, namely RNF33, that interacts with the kinesin molecular motors possibly contributing to kinesin-dependent mobilization of specific cargo(s) along the microtubule in the testis of the mouse. PMID: 21909995 Similar articles
Nuclear
factor kappa B and tumor necrosis factor-alpha modulation of
transcription of the mouse testis- and pre-implantation
development-specific Rnf33/Trim60 gene.Choo KB, Hsu MC,
Tsai YH, Lin WY, Huang CJ.FEBS J. 2011 Mar;278(5):837-50. doi:
10.1111/j.1742-4658.2010.08002.x. Epub 2011 Feb 2.
NF-kB:n säätelemä
TRIM60- ilmenemä erityiseti Sertolin soluissa viittaa siihen, että
TRIM60:lla on ilmeistä osutta spermatogeneesissä kuten edellä
mainittiin osallistumisesta kinesiini-proteiinien suorittamaan
mikrotubuluksia myötäilevään kuljetukseen.
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Hence, demonstration of NF-κB-regulated Rnf33 expression in testicular cells, particularly in Sertoli cells, implicates functional involvement of the putative RNF33 protein in spermatogenesis through association of the RNF33 protein with the microtubule via interaction with kinesin motor proteins, as previously demonstrated [Huang et al., submitted]. PMID: 21205214 Free Article Similar articles
Related articles in PubMed TRIM60 GENE
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Complete sequencing and characterization of 21,243 full-length human cDNAs. Ota T, et al. Nat Genet, 2004 Jan. PMID 14702039 As a base for human transcriptome and functional genomics, we created the "full-length long Japan" (FLJ) collection of sequenced human cDNAs ” .. TRIM60 = FLJ358882
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