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fredag 8 juni 2018

RNF189 (Kr.17q12), CARP-2, RFFL, RIFIFYLIN, Kaspaasisäätelijä-2

RNF189 (Kr.17q12), CARP-2, FRING, RIFIFYLIN

Also known as
CARP2; FRING; CARP-2; RNF189; RNF34L; RIFIFYLIN
Expression
Ubiquitous expression in thyroid (RPKM 18.0), esophagus (RPKM 12.3) and 25 other tissues See more
Orthologs mouse all

Related articles in PubMed

  1. Crystal structure of a FYVE-type zinc finger domain from the caspase regulator CARP2. Tibbetts MD, et al. Structure, 2004 Dec. PMID 15576038
  2. The N-terminal extension of UBE2E ubiquitin-conjugating enzymes limits chain assembly. Schumacher FR, et al. J Mol Biol, 2013 Nov 15. PMID 23871895
  3. CARPs are ubiquitin ligases that promote MDM2-independent p53 and phospho-p53ser20 degradation. Yang W, et al. J Biol Chem, 2007 Feb 2. PMID 17121812
See all (26) citations in PubMed
See citations in PubMed for homologs of this gene provided by HomoloGene

GeneRif

it is interesting to note that a human lncRNA does exist within the 5'-UTR intronic region of the human RFFL gene . Given the rat data, our study may serve as a translational foundation for considering this human lncRNA as a candidate regulator for cardiovascular diseases.
Preferred Names
E3 ubiquitin-protein ligase rififylin
Names
FYVE-RING finger protein SAKURA
RING finger and FYVE-like domain-containing protein 1
RING finger protein 189
RING-type E3 ubiquitin transferase rififylin
caspase 8 and 10 associated RING protein-2
caspase regulator CARP2
caspases-8 and -10-associated RING finger protein 2
ring finger and FYVE-like domain containing 1 (3) summary

Conserved domains

cd15770
Location:44 → 92
FYVE_CARP2; FYVE-like domain found in caspase regulator CARP2 and similar proteins
pfam13920
Location:312 → 356
zf-C3HC4_3; Zinc finger, C3HC4 type (RING finger)
pfam15439
Location:149 → 232
NYAP_N; Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter

Peptide sequence and history

https://www.ncbi.nlm.nih.gov/protein/NP_001017368.1
E3 ubiquitin-protein ligase rififylin [Homo sapiens]
NCBI Reference Sequence: NP_001017368.1
Identical Proteins FASTA Graphics



LOCUS       NP_001017368             363 aa            linear   PRI 08-APR-2018
DEFINITION  E3 ubiquitin-protein ligase rififylin [Homo sapiens].
ACCESSION   NP_001017368
VERSION     NP_001017368.1
DBSOURCE    REFSEQ: accession NM_001017368.1
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 363)
  AUTHORS   Cheng X, Waghulde H, Mell B, Morgan EE, Pruett-Miller SM and Joe B.
  TITLE     Positional cloning of quantitative trait nucleotides for blood
            pressure and cardiac QT-interval by targeted CRISPR/Cas9 editing of
            a novel long non-coding RNA
  JOURNAL   PLoS Genet. 13 (8), e1006961 (2017)
   PUBMED   28827789
  REMARK    GeneRIF: it is interesting to note that a human lncRNA does exist
            within the 5'-UTR intronic region of the human RFFL gene . Given
            the rat data, our study may serve as a translational foundation for
            considering this human lncRNA as a candidate regulator for
            cardiovascular diseases.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Gan X, Wang C, Patel M, Kreutz B, Zhou M, Kozasa T and Wu D.
  TITLE     Different Raf protein kinases mediate different signaling pathways
            to stimulate E3 ligase RFFL gene expression in cell migration
            regulation
  JOURNAL   J. Biol. Chem. 288 (47), 33978-33984 (2013)
   PUBMED   24114843
  REMARK    GeneRIF: EGF, which signals through CRAF, and an activated BRAF
            mutant also activate PKC and stimulate cell migration through
            up-regulating RFFL expression.
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Gan X, Wang J, Wang C, Sommer E, Kozasa T, Srinivasula S, Alessi D,
            Offermanns S, Simon MI and Wu D.
  TITLE     PRR5L degradation promotes mTORC2-mediated PKC-delta
            phosphorylation and cell migration downstream of Galpha12
  JOURNAL   Nat. Cell Biol. 14 (7), 686-696 (2012)
   PUBMED   22609986
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 363)
  AUTHORS   Lin ML, Lu YC, Su HL, Lin HT, Lee CC, Kang SE, Lai TC, Chung JG and
            Chen SS.
  TITLE     Destabilization of CARP mRNAs by aloe-emodin contributes to
            caspase-8-mediated p53-independent apoptosis of human carcinoma
            cells
  JOURNAL   J. Cell. Biochem. 112 (4), 1176-1191 (2011)
   PUBMED   21308745
  REMARK    GeneRIF: data indicate AE induces caspase-8-mediated activation of
            mitochondrial death pathways by decreasing the stability of CARP
            mRNAs in a p53-independent manner.
REFERENCE   5  (residues 1 to 363)
  AUTHORS   Shimada M, Miyagawa T, Kawashima M, Tanaka S, Honda Y, Honda M and
            Tokunaga K.
  TITLE     An approach based on a genome-wide association study reveals
            candidate loci for narcolepsy
  JOURNAL   Hum. Genet. 128 (4), 433-441 (2010)
   PUBMED   20677014
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 363)
  AUTHORS   Yang W, Rozan LM, McDonald ER 3rd, Navaraj A, Liu JJ, Matthew EM,
            Wang W, Dicker DT and El-Deiry WS.
  TITLE     CARPs are ubiquitin ligases that promote MDM2-independent p53 and
            phospho-p53ser20 degradation
  JOURNAL   J. Biol. Chem. 282 (5), 3273-3281 (2007)
   PUBMED   17121812
REFERENCE   7  (residues 1 to 363)
  AUTHORS   Tibbetts MD, Shiozaki EN, Gu L, McDonald ER 3rd, El-Deiry WS and
            Shi Y.
  TITLE     Crystal structure of a FYVE-type zinc finger domain from the
            caspase regulator CARP2
  JOURNAL   Structure 12 (12), 2257-2263 (2004)
   PUBMED   15576038
REFERENCE   8  (residues 1 to 363)
  AUTHORS   Coumailleau F, Das V, Alcover A, Raposo G, Vandormael-Pournin S, Le
            Bras S, Baldacci P, Dautry-Varsat A, Babinet C and Cohen-Tannoudji
            M.
  TITLE     Over-expression of Rififylin, a new RING finger and FYVE-like
            domain-containing protein, inhibits recycling from the endocytic
            recycling compartment
  JOURNAL   Mol. Biol. Cell 15 (10), 4444-4456 (2004)
   PUBMED   15229288
REFERENCE   9  (residues 1 to 363)
  AUTHORS   Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li
            J, Cohn MA, Cantley LC and Gygi SP.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   10 (residues 1 to 363)
  AUTHORS   McDonald ER 3rd and El-Deiry WS.
  TITLE     Suppression of caspase-8- and -10-associated RING proteins results
            in sensitization to death ligands and inhibition of tumor cell
            growth
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 101 (16), 6170-6175 (2004)
   PUBMED   15069192
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CR933651.1, CK001659.1 and BC028424.1.
            
            Transcript Variant: This variant (2) represents the shorter
            transcript but encodes the supported protein.
            
            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 :: CR933651.1, SRR1803611.198718.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q12"
     Protein         1..363
                     /product="E3 ubiquitin-protein ligase rififylin"
                     /EC_number="2.3.2.27"
                     /note="caspases-8 and -10-associated RING finger protein
                     2; FYVE-RING finger protein SAKURA; RING finger protein
                     189; caspase regulator CARP2; RING finger and FYVE-like
                     domain-containing protein 1; ring finger and FYVE-like
                     domain containing 1; caspase 8 and 10 associated RING
                     protein-2; RING-type E3 ubiquitin transferase rififylin"
                     /calculated_mol_wt=40383
     Region          44..92
                     /region_name="FYVE_CARP2"
                     /note="FYVE-like domain found in caspase regulator CARP2
                     and similar proteins; cd15770"
                     /db_xref="CDD:277309"
     Site            order(47,50,63,66,71,74,85,88)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:277309"
     Region          <149 ..="">232
                     /region_name="NYAP_N"
                     /note="Neuronal tyrosine-phosphorylated
                     phosphoinositide-3-kinase adapter; pfam15439"
                     /db_xref="CDD:292079"
     Site            226
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphoserine. {ECO:0000244|PubMed:19690332};
                     propagated from UniProtKB/Swiss-Prot (Q8WZ73.1)"
     Site            229
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphoserine. {ECO:0000244|PubMed:19690332,
                     ECO:0000244|PubMed:24275569}; propagated from
                     UniProtKB/Swiss-Prot (Q8WZ73.1)"
     Site            232
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphoserine. {ECO:0000250|UniProtKB:Q6ZQM0};
                     propagated from UniProtKB/Swiss-Prot (Q8WZ73.1)"
     Site            240
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphoserine. {ECO:0000250|UniProtKB:Q6ZQM0};
                     propagated from UniProtKB/Swiss-Prot (Q8WZ73.1)"
     Region          312..356
                     /region_name="zf-C3HC4_3"
                     /note="Zinc finger, C3HC4 type (RING finger); pfam13920"
                     /db_xref="CDD:290631"
     Site            order(316,319,331,333,337,340,347,350)
                     /site_type="other"
                     /note="cross-brace motif"
                     /db_xref="CDD:238093"
     CDS             1..363
                     /gene="RFFL"
                     /gene_synonym="CARP-2; CARP2; FRING; RIFIFYLIN; RNF189;
                     RNF34L"
                     /coded_by="NM_001017368.1:174..1265"
                     /db_xref="CCDS:CCDS11286.1"
                     /db_xref="GeneID:117584"
                     /db_xref="HGNC:HGNC:24821"
                     /db_xref="MIM:609735"
ORIGIN      
        1 mwatccnwfc ldgqpeevpp pqgarmqays npgyssfpsp tglepscksc gahfantark
       61 qtcldckknf cmtcssqvgn gprlcllcqr fratafqree lmkmkvkdlr dylslhdist
      121 emcrekeelv llvlgqqpvi sqedrtrast lspdfpeqqa fltqphssmv pptspnlpss
      181 saqatsvppa qvqenqqang hvsqdqeepv ylesvarvpa edetqsidse dsfvpgrras
      241 lsdltdledi egltvrqlke ilarnfvnyk gccekwelme rvtrlykdqk glqhlvsgae
      301 dqnggavpsg leenlckicm dspidcvlle cghmvtctkc gkrmnecpic rqyviravhv
      361 frs
//



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