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torsdag 29 mars 2018

TRIM60 (Kr.4q32.8), RNF33, RNF129.(C_IV PRYSPRY)

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.

  • 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
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
zf-B_box; B-box zinc finger
pfam15905
Location:139 → 260
HMMR_N; Hyaluronan mediated motility receptor N-terminal
cd16607
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
DWNN; DWNN domain


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"
/note="DWNN domain; cl26688" /db_xref="CDD:331509" Region 16..56 /region_name="RING-HC finger (C3HC4-type)" /note="RING-HC finger (C3HC4-type) [structural motif]" /db_xref="CDD:319521" Site order(16,19,31,33,36,39,53,56) /site_type="other" /note="Zn binding site [ion binding]" /db_xref="CDD:319521" Region 92..133 /region_name="zf-B_box" /note="B-box zinc finger; pfam00643" /db_xref="CDD:306989" Site order(97,100,119,125) /site_type="other" /note="Zn2+ binding site [ion binding]" /db_xref="CDD:237988" Region <139 ..260="" b="">region_name="HMMR_N" /note="Hyaluronan mediated motility receptor N-terminal; pfam15905" /db_xref="CDD:318177" Region 286..465 /region_name="SPRY_PRY_TRIM60" /note="PRY/SPRY domain of tripartite motif-binding protein 60 (TRIM60) also known as RING finger protein 33 (RNF33); cd15828" /db_xref="CDD:294000" CDS 1..471 /gene="TRIM60" /gene_synonym="RNF129; RNF33" /coded_by="NM_001258025.1:345..1760" /db_xref="CCDS:CCDS3808.1" /db_xref="GeneID:166655" /db_xref="HGNC:HGNC:21162" ORIGIN 1 mefvtalvnl qeesscpicl eylkdpvtin cghnfcrscl svswkdlddt fpcpvcrfcf 61 pyksfrrnpq lrnlteiakq lqirrskrkr qkenamcekh nqfltlfcvk dleilctqcs 121 fstkhqkhyi cpikkaasyh reilegslep lrnniervek viilqgsksv elkkkveykr 181 eeinsefeqi rlflqneqem ilrqiqdeem nilaklnenl velsdyvstl khllrevegk 241 svqsnlellt qaksmhhkyq nlkcpelfsf rltkygfslp pqysgldrii kpfqvdvild 301 lntahpqllv sedrkavrye rkkrnicydp rrfyvcpavl gsqrfssgrh ywevevgnkp 361 kwilgvcqdc llrnwqdqps vlggfwaigr ymksgyvasg pkttqllpvv kpskigifld 421 yelgdlsfyn mndrsilytf ndcfteavwp yfytgtdsep lkicsvsdse r //

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 .

  • 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
Select item 212052142.
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.
  • 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

  1. 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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