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FBX27_HUMAN
ID   FBX27_HUMAN             Reviewed;         283 AA.
AC   Q8NI29; Q96C87;
DT   09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=F-box only protein 27;
DE   AltName: Full=F-box/G-domain protein 5;
GN   Name=FBXO27; Synonyms=FBG5, FBX27;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=12383498; DOI=10.1016/s0378-1119(02)00867-3;
RA   Ilyin G.P., Serandour A.L., Pigeon C., Rialland M., Glaise D.,
RA   Guguen-Guillouzo C.;
RT   "A new subfamily of structurally related human F-box proteins.";
RL   Gene 296:11-20(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pancreas, and Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   SUGAR-BINDING, FUNCTION, INTERACTION WITH CUL1 AND SKP1, IDENTIFICATION IN
RP   SCF-COMPLEX, AND MUTAGENESIS OF 262-PHE-TRP-263.
RX   PubMed=18203720; DOI=10.1074/jbc.m709508200;
RA   Glenn K.A., Nelson R.F., Wen H.M., Mallinger A.J., Paulson H.L.;
RT   "Diversity in tissue expression, substrate binding, and SCF complex
RT   formation for a lectin family of ubiquitin ligases.";
RL   J. Biol. Chem. 283:12717-12729(2008).
CC   -!- FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box
CC       protein)-type E3 ubiquitin ligase complex. Able to recognize and bind
CC       denatured glycoproteins, which are modified with complex-type
CC       oligosaccharides. {ECO:0000269|PubMed:18203720}.
CC   -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex.
CC       Interacts with SKP1 and CUL1. {ECO:0000269|PubMed:18203720}.
CC   -!- INTERACTION:
CC       Q8NI29; P63208: SKP1; NbExp=3; IntAct=EBI-6425694, EBI-307486;
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in brain, heart and kidney.
CC       Expressed at lower levels in liver and lung.
CC       {ECO:0000269|PubMed:12383498}.
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DR   EMBL; AF436061; AAM27918.1; -; mRNA.
DR   EMBL; BC014527; AAH14527.1; -; mRNA.
DR   EMBL; BC030060; AAH30060.1; -; mRNA.
DR   CCDS; CCDS12527.1; -.
DR   RefSeq; NP_849142.1; NM_178820.4.
DR   AlphaFoldDB; Q8NI29; -.
DR   SMR; Q8NI29; -.
DR   BioGRID; 125992; 26.
DR   CORUM; Q8NI29; -.
DR   IntAct; Q8NI29; 4.
DR   STRING; 9606.ENSP00000292853; -.
DR   iPTMnet; Q8NI29; -.
DR   PhosphoSitePlus; Q8NI29; -.
DR   BioMuta; FBXO27; -.
DR   DMDM; 51338809; -.
DR   jPOST; Q8NI29; -.
DR   MassIVE; Q8NI29; -.
DR   MaxQB; Q8NI29; -.
DR   PaxDb; Q8NI29; -.
DR   PeptideAtlas; Q8NI29; -.
DR   PRIDE; Q8NI29; -.
DR   ProteomicsDB; 73819; -.
DR   Antibodypedia; 30249; 133 antibodies from 22 providers.
DR   DNASU; 126433; -.
DR   Ensembl; ENST00000292853.9; ENSP00000292853.3; ENSG00000161243.9.
DR   Ensembl; ENST00000509137.6; ENSP00000437662.1; ENSG00000161243.9.
DR   GeneID; 126433; -.
DR   KEGG; hsa:126433; -.
DR   MANE-Select; ENST00000292853.9; ENSP00000292853.3; NM_178820.5; NP_849142.1.
DR   UCSC; uc002okh.5; human.
DR   CTD; 126433; -.
DR   DisGeNET; 126433; -.
DR   GeneCards; FBXO27; -.
DR   HGNC; HGNC:18753; FBXO27.
DR   HPA; ENSG00000161243; Tissue enhanced (skin).
DR   MIM; 609099; gene.
DR   neXtProt; NX_Q8NI29; -.
DR   OpenTargets; ENSG00000161243; -.
DR   PharmGKB; PA38675; -.
DR   VEuPathDB; HostDB:ENSG00000161243; -.
DR   eggNOG; ENOG502RZA6; Eukaryota.
DR   GeneTree; ENSGT00940000161841; -.
DR   InParanoid; Q8NI29; -.
DR   OMA; NNVCLHV; -.
DR   OrthoDB; 922544at2759; -.
DR   PhylomeDB; Q8NI29; -.
DR   TreeFam; TF320527; -.
DR   PathwayCommons; Q8NI29; -.
DR   Reactome; R-HSA-8951664; Neddylation.
DR   Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SignaLink; Q8NI29; -.
DR   BioGRID-ORCS; 126433; 10 hits in 1119 CRISPR screens.
DR   ChiTaRS; FBXO27; human.
DR   GenomeRNAi; 126433; -.
DR   Pharos; Q8NI29; Tdark.
DR   PRO; PR:Q8NI29; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q8NI29; protein.
DR   Bgee; ENSG00000161243; Expressed in secondary oocyte and 100 other tissues.
DR   ExpressionAtlas; Q8NI29; baseline and differential.
DR   Genevisible; Q8NI29; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
DR   GO; GO:0006516; P:glycoprotein catabolic process; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:GOC.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR   InterPro; IPR007397; F-box-assoc_dom.
DR   InterPro; IPR036047; F-box-like_dom_sf.
DR   InterPro; IPR001810; F-box_dom.
DR   InterPro; IPR039752; F-box_only.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   PANTHER; PTHR12125; PTHR12125; 1.
DR   Pfam; PF00646; F-box; 1.
DR   Pfam; PF04300; FBA; 1.
DR   SMART; SM01198; FBA; 1.
DR   SMART; SM00256; FBOX; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF81383; SSF81383; 1.
DR   PROSITE; PS51114; FBA; 1.
DR   PROSITE; PS50181; FBOX; 1.
PE   1: Evidence at protein level;
KW   Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..283
FT                   /note="F-box only protein 27"
FT                   /id="PRO_0000119914"
FT   DOMAIN          23..70
FT                   /note="F-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT   DOMAIN          104..280
FT                   /note="FBA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00482"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         262..263
FT                   /note="FW->AA: Reduces interaction with glycosylated
FT                   concanavalin-A in vitro."
FT                   /evidence="ECO:0000269|PubMed:18203720"
FT   CONFLICT        8
FT                   /note="G -> C (in Ref. 1; AAM27918)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   283 AA;  31623 MW;  0A66E26971320B5F CRC64;
     MGASVSRGRA ARVPAPEPEP EEALDLSQLP PELLLVVLSH VPPRTLLGRC RQVCRGWRAL
     VDGQALWLLI LARDHGATGR ALLHLARSCQ SPARNARPCP LGRFCARRPI GRNLIRNPCG
     QEGLRKWMVQ HGGDGWVVEE NRTTVPGAPS QTCFVTSFSW CCKKQVLDLE EEGLWPELLD
     SGRIEICVSD WWGARHDSGC MYRLLVQLLD ANQTVLDKFS AVPDPIPQWN NNACLHVTHV
     FSNIKMGVRF VSFEHRGQDT QFWAGHYGAR VTNSSVIVRV RLS
 
 
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