RER1_HUMAN
ID RER1_HUMAN Reviewed; 196 AA.
AC O15258; O95322;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Protein RER1;
GN Name=RER1;
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].
RC TISSUE=Mammary cancer;
RX PubMed=9309388;
RA Fuellekrug J., Boehm J., Roettger S., Nilsson T., Mieskes G., Schmitt H.;
RT "Human Rer1 is localized to the Golgi apparatus and complements the
RT deletion of the homologous Rer1 protein of Saccharomyces cerevisiae.";
RL Eur. J. Cell Biol. 74:31-40(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Barrow I.K.-P., Boguski M.S., Touchman J.W., Spencer F.;
RT "Full-insert sequence of mapped XREF EST.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND SER-95, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND IDENTIFICATION BY
RP 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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-6 AND SER-95, CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND IDENTIFICATION BY
RP 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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-6; SER-10 AND SER-95,
RP AND 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).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP ACETYLATION AT SER-2, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=25489052; DOI=10.1093/hmg/ddu611;
RA Myklebust L.M., Van Damme P., Stoeve S.I., Doerfel M.J., Abboud A.,
RA Kalvik T.V., Grauffel C., Jonckheere V., Wu Y., Swensen J., Kaasa H.,
RA Liszczak G., Marmorstein R., Reuter N., Lyon G.J., Gevaert K., Arnesen T.;
RT "Biochemical and cellular analysis of Ogden syndrome reveals downstream Nt-
RT acetylation defects.";
RL Hum. Mol. Genet. 24:1956-1976(2015).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Involved in the retrieval of endoplasmic reticulum membrane
CC proteins from the early Golgi compartment. {ECO:0000250}.
CC -!- INTERACTION:
CC O15258; P57086: SCAND1; NbExp=3; IntAct=EBI-716910, EBI-745846;
CC O15258; Q17RD7: SYT16; NbExp=3; IntAct=EBI-716910, EBI-10238936;
CC O15258; O43516-4: WIPF1; NbExp=3; IntAct=EBI-716910, EBI-12052927;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane
CC protein.
CC -!- SIMILARITY: Belongs to the RER1 family. {ECO:0000305}.
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DR EMBL; AJ001421; CAA04754.1; -; mRNA.
DR EMBL; AF091071; AAC72940.1; -; mRNA.
DR EMBL; BC004965; AAH04965.1; -; mRNA.
DR CCDS; CCDS41232.1; -.
DR RefSeq; NP_008964.3; NM_007033.4.
DR RefSeq; XP_006710369.1; XM_006710306.2.
DR RefSeq; XP_011538844.1; XM_011540542.1.
DR RefSeq; XP_011538845.1; XM_011540543.1.
DR RefSeq; XP_016855622.1; XM_017000133.1.
DR RefSeq; XP_016855623.1; XM_017000134.1.
DR RefSeq; XP_016855624.1; XM_017000135.1.
DR AlphaFoldDB; O15258; -.
DR BioGRID; 116262; 129.
DR IntAct; O15258; 27.
DR MINT; O15258; -.
DR STRING; 9606.ENSP00000475168; -.
DR TCDB; 9.B.82.1.2; the endoplasmic reticulum retrieval protein1 (putative heavy metal transporter) (rer1) family.
DR GlyGen; O15258; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O15258; -.
DR MetOSite; O15258; -.
DR PhosphoSitePlus; O15258; -.
DR SwissPalm; O15258; -.
DR BioMuta; RER1; -.
DR EPD; O15258; -.
DR jPOST; O15258; -.
DR MassIVE; O15258; -.
DR PaxDb; O15258; -.
DR PeptideAtlas; O15258; -.
DR PRIDE; O15258; -.
DR ProteomicsDB; 48544; -.
DR Antibodypedia; 26719; 101 antibodies from 27 providers.
DR DNASU; 11079; -.
DR Ensembl; ENST00000488353.2; ENSP00000464222.1; ENSG00000157916.20.
DR Ensembl; ENST00000605895.6; ENSP00000475168.1; ENSG00000157916.20.
DR GeneID; 11079; -.
DR KEGG; hsa:11079; -.
DR MANE-Select; ENST00000605895.6; ENSP00000475168.1; NM_007033.5; NP_008964.3.
DR CTD; 11079; -.
DR DisGeNET; 11079; -.
DR GeneCards; RER1; -.
DR HGNC; HGNC:30309; RER1.
DR HPA; ENSG00000157916; Low tissue specificity.
DR neXtProt; NX_O15258; -.
DR OpenTargets; ENSG00000157916; -.
DR PharmGKB; PA134901074; -.
DR VEuPathDB; HostDB:ENSG00000157916; -.
DR eggNOG; KOG1688; Eukaryota.
DR GeneTree; ENSGT00510000047137; -.
DR InParanoid; O15258; -.
DR OMA; WYIVAYS; -.
DR OrthoDB; 1458086at2759; -.
DR PhylomeDB; O15258; -.
DR TreeFam; TF300029; -.
DR PathwayCommons; O15258; -.
DR SignaLink; O15258; -.
DR BioGRID-ORCS; 11079; 86 hits in 1084 CRISPR screens.
DR ChiTaRS; RER1; human.
DR GenomeRNAi; 11079; -.
DR Pharos; O15258; Tbio.
DR PRO; PR:O15258; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O15258; protein.
DR Bgee; ENSG00000157916; Expressed in lower esophagus mucosa and 208 other tissues.
DR ExpressionAtlas; O15258; baseline and differential.
DR Genevisible; O15258; HS.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:GOC.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0030173; C:integral component of Golgi membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:GOC.
DR GO; GO:0033130; F:acetylcholine receptor binding; IEA:Ensembl.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0006621; P:protein retention in ER lumen; IBA:GO_Central.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0071340; P:skeletal muscle acetylcholine-gated channel clustering; IEA:Ensembl.
DR InterPro; IPR004932; Rer1.
DR PANTHER; PTHR10743; PTHR10743; 1.
DR Pfam; PF03248; Rer1; 1.
DR PIRSF; PIRSF016013; AtER_Rer1p; 1.
PE 1: Evidence at protein level;
KW Acetylation; Golgi apparatus; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25489052,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..196
FT /note="Protein RER1"
FT /id="PRO_0000207589"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:25489052,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT CONFLICT 123..196
FT /note="HAATKGILVAMVCTFFDAFNVPVFWPILVMYFIMLFCITMKRQIKHMIKYRY
FT IPFTHGKRRYRGKEDAGKAFAS -> DASVCGDGRCSCKAGGGRQCPVLAADAALTFSP
FT HLKACGYQGHPCGYGLYFLRRFQRPGVLADSGDVLHHALLYHDEEANQAHD (in
FT Ref. 2; AAC72940)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 196 AA; 22958 MW; 0FF7F3CDC9F88A69 CRC64;
MSEGDSVGES VHGKPSVVYR FFTRLGQIYQ SWLDKSTPYT AVRWVVTLGL SFVYMIRVYL
LQGWYIVTYA LGIYHLNLFI AFLSPKVDPS LMEDSDDGPS LPTKQNEEFR PFIRRLPEFK
FWHAATKGIL VAMVCTFFDA FNVPVFWPIL VMYFIMLFCI TMKRQIKHMI KYRYIPFTHG
KRRYRGKEDA GKAFAS
