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REEP3_HUMAN
ID   REEP3_HUMAN             Reviewed;         255 AA.
AC   Q6NUK4; Q5JQR5; Q5QGT2; Q6PEW8; Q6PJY4;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Receptor expression-enhancing protein 3;
GN   Name=REEP3; Synonyms=C10orf74;
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] (ISOFORM 2).
RX   PubMed=15550249; DOI=10.1016/j.cell.2004.11.021;
RA   Saito H., Kubota M., Roberts R.W., Chi Q., Matsunami H.;
RT   "RTP family members induce functional expression of mammalian odorant
RT   receptors.";
RL   Cell 119:679-691(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Placenta, and Uterus;
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   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=16720576; DOI=10.1074/jbc.m513637200;
RA   Behrens M., Bartelt J., Reichling C., Winnig M., Kuhn C., Meyerhof W.;
RT   "Members of RTP and REEP gene families influence functional bitter taste
RT   receptor expression.";
RL   J. Biol. Chem. 281:20650-20659(2006).
RN   [5]
RP   IDENTIFICATION.
RX   PubMed=17290275; DOI=10.1038/sj.ejhg.5201785;
RA   Castermans D., Vermeesch J.R., Fryns J.P., Steyaert J.G., Van de Ven W.J.,
RA   Creemers J.W., Devriendt K.;
RT   "Identification and characterization of the TRIP8 and REEP3 genes on
RT   chromosome 10q21.3 as novel candidate genes for autism.";
RL   Eur. J. Hum. Genet. 15:422-431(2007).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-201 AND SER-210, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [8]
RP   FUNCTION.
RX   PubMed=23911198; DOI=10.1016/j.devcel.2013.06.016;
RA   Schlaitz A.L., Thompson J., Wong C.C., Yates J.R. III, Heald R.;
RT   "REEP3/4 ensure endoplasmic reticulum clearance from metaphase chromatin
RT   and proper nuclear envelope architecture.";
RL   Dev. Cell 26:315-323(2013).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
CC   -!- FUNCTION: Microtubule-binding protein required to ensure proper cell
CC       division and nuclear envelope reassembly by sequestering the
CC       endoplasmic reticulum away from chromosomes during mitosis. Probably
CC       acts by clearing the endoplasmic reticulum membrane from metaphase
CC       chromosomes. {ECO:0000269|PubMed:23911198}.
CC   -!- INTERACTION:
CC       Q6NUK4; Q5BVD1: TTMP; NbExp=3; IntAct=EBI-7545786, EBI-10243654;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6NUK4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6NUK4-2; Sequence=VSP_016634, VSP_016635;
CC   -!- TISSUE SPECIFICITY: Expressed in circumvallate papillae.
CC       {ECO:0000269|PubMed:16720576}.
CC   -!- SIMILARITY: Belongs to the DP1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH10040.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR   EMBL; AY562241; AAT70686.1; -; mRNA.
DR   EMBL; AC022022; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL607062; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC010040; AAH10040.1; ALT_SEQ; mRNA.
DR   EMBL; BC057832; AAH57832.1; -; mRNA.
DR   EMBL; BC068557; AAH68557.1; -; mRNA.
DR   CCDS; CCDS44411.1; -. [Q6NUK4-1]
DR   RefSeq; NP_001001330.1; NM_001001330.2. [Q6NUK4-1]
DR   AlphaFoldDB; Q6NUK4; -.
DR   BioGRID; 128676; 33.
DR   IntAct; Q6NUK4; 12.
DR   MINT; Q6NUK4; -.
DR   STRING; 9606.ENSP00000362863; -.
DR   iPTMnet; Q6NUK4; -.
DR   PhosphoSitePlus; Q6NUK4; -.
DR   BioMuta; REEP3; -.
DR   DMDM; 74736808; -.
DR   EPD; Q6NUK4; -.
DR   jPOST; Q6NUK4; -.
DR   MassIVE; Q6NUK4; -.
DR   MaxQB; Q6NUK4; -.
DR   PaxDb; Q6NUK4; -.
DR   PeptideAtlas; Q6NUK4; -.
DR   PRIDE; Q6NUK4; -.
DR   ProteomicsDB; 66687; -. [Q6NUK4-1]
DR   ProteomicsDB; 66688; -. [Q6NUK4-2]
DR   Antibodypedia; 45181; 82 antibodies from 21 providers.
DR   DNASU; 221035; -.
DR   Ensembl; ENST00000373758.5; ENSP00000362863.4; ENSG00000165476.14. [Q6NUK4-1]
DR   GeneID; 221035; -.
DR   KEGG; hsa:221035; -.
DR   MANE-Select; ENST00000373758.5; ENSP00000362863.4; NM_001001330.3; NP_001001330.1.
DR   CTD; 221035; -.
DR   DisGeNET; 221035; -.
DR   GeneCards; REEP3; -.
DR   HGNC; HGNC:23711; REEP3.
DR   HPA; ENSG00000165476; Low tissue specificity.
DR   MIM; 609348; gene.
DR   neXtProt; NX_Q6NUK4; -.
DR   OpenTargets; ENSG00000165476; -.
DR   PharmGKB; PA134863406; -.
DR   VEuPathDB; HostDB:ENSG00000165476; -.
DR   eggNOG; KOG1726; Eukaryota.
DR   GeneTree; ENSGT00940000158794; -.
DR   HOGENOM; CLU_028431_0_1_1; -.
DR   InParanoid; Q6NUK4; -.
DR   OMA; DLTISWF; -.
DR   PhylomeDB; Q6NUK4; -.
DR   TreeFam; TF314177; -.
DR   PathwayCommons; Q6NUK4; -.
DR   SignaLink; Q6NUK4; -.
DR   BioGRID-ORCS; 221035; 5 hits in 1043 CRISPR screens.
DR   ChiTaRS; REEP3; human.
DR   GenomeRNAi; 221035; -.
DR   Pharos; Q6NUK4; Tbio.
DR   PRO; PR:Q6NUK4; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; Q6NUK4; protein.
DR   Bgee; ENSG00000165476; Expressed in palpebral conjunctiva and 191 other tissues.
DR   ExpressionAtlas; Q6NUK4; baseline and differential.
DR   Genevisible; Q6NUK4; HS.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0071782; C:endoplasmic reticulum tubular network; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071786; P:endoplasmic reticulum tubular network organization; IBA:GO_Central.
DR   GO; GO:0007084; P:mitotic nuclear membrane reassembly; IMP:UniProtKB.
DR   GO; GO:0006998; P:nuclear envelope organization; IMP:UniProtKB.
DR   InterPro; IPR004345; TB2_DP1_HVA22.
DR   PANTHER; PTHR12300; PTHR12300; 1.
DR   Pfam; PF03134; TB2_DP1_HVA22; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell cycle; Cell division; Endoplasmic reticulum;
KW   Membrane; Microtubule; Mitosis; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..255
FT                   /note="Receptor expression-enhancing protein 3"
FT                   /id="PRO_0000101826"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          158..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         201
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         210
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   VAR_SEQ         140..170
FT                   /note="SQGAITERLRSFSMHDLTTIQGDEPVGQRPY -> VIVHLPF (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15550249"
FT                   /id="VSP_016634"
FT   VAR_SEQ         171..255
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15550249"
FT                   /id="VSP_016635"
FT   VARIANT         171
FT                   /note="Q -> R (in dbSNP:rs10995569)"
FT                   /id="VAR_048926"
SQ   SEQUENCE   255 AA;  29264 MW;  83E4D6E153DDE3EB CRC64;
     MVSWMISRAV VLVFGMLYPA YYSYKAVKTK NVKEYVRWMM YWIVFALYTV IETVADQTVA
     WFPLYYELKI AFVIWLLSPY TKGASLIYRK FLHPLLSSKE REIDDYIVQA KERGYETMVN
     FGRQGLNLAA TAAVTAAVKS QGAITERLRS FSMHDLTTIQ GDEPVGQRPY QPLPEAKKKS
     KPAPSESAGY GIPLKDGDEK TDEEAEGPYS DNEMLTHKGL RRSQSMKSVK TTKGRKEVRY
     GSLKYKVKKR PQVYF
 
 
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