ERH_HUMAN
ID ERH_HUMAN Reviewed; 104 AA.
AC P84090; B2R5H2; P70659; Q14259;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Enhancer of rudimentary homolog;
GN Name=ERH;
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=8786099; DOI=10.1006/geno.1996.0086;
RA Isomura M., Okui K., Fujiwara T., Shin S., Nakamura Y.;
RT "Cloning and mapping of a novel human cDNA homologous to DROER, the
RT enhancer of the Drosophila melanogaster rudimentary gene.";
RL Genomics 32:125-127(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9074495; DOI=10.1016/s0378-1119(96)00701-9;
RA Gelsthorpe M., Pulumati M., McCallum C., Dang-Vu K., Tsubota S.I.;
RT "The putative cell cycle gene, enhancer of rudimentary, encodes a highly
RT conserved protein found in plants and animals.";
RL Gene 186:189-195(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [8]
RP PROTEIN SEQUENCE OF 2-12 AND 74-88, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Mammary carcinoma, and Ovarian carcinoma;
RA Bienvenut W.V., Matallanas D., Cooper W.N., Lilla S., von Kriegsheim A.,
RA Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP PROTEIN SEQUENCE OF 18-34; 74-84 AND 91-96, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [10]
RP INTERACTION WITH POLDIP3.
RX PubMed=16984396; DOI=10.1111/j.1742-4658.2006.05477.x;
RA Smyk A., Szuminska M., Uniewicz K.A., Graves L.M., Kozlowski P.;
RT "Human enhancer of rudimentary is a molecular partner of PDIP46/SKAR, a
RT protein interacting with DNA polymerase delta and S6K1 and regulating cell
RT growth.";
RL FEBS J. 273:4728-4741(2006).
RN [11]
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 [12]
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 [13]
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=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=23145069; DOI=10.1371/journal.pone.0049059;
RA Krzyzanowski M.K., Kozlowska E., Kozlowski P.;
RT "Identification and Functional Analysis of the erh1(+) Gene Encoding
RT Enhancer of Rudimentary Homolog from the Fission Yeast Schizosaccharomyces
RT pombe.";
RL PLoS ONE 7:E49059-E49059(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-11, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [16]
RP INTERACTION WITH CHTOP, AND IDENTIFICATION IN THE METHYLOSOME COMPLEX WITH
RP PRMT1; PRMT5 AND WDR77.
RX PubMed=25284789; DOI=10.1016/j.celrep.2014.08.071;
RA Takai H., Masuda K., Sato T., Sakaguchi Y., Suzuki T., Suzuki T.,
RA Koyama-Nasu R., Nasu-Nishimura Y., Katou Y., Ogawa H., Morishita Y.,
RA Kozuka-Hata H., Oyama M., Todo T., Ino Y., Mukasa A., Saito N.,
RA Toyoshima C., Shirahige K., Akiyama T.;
RT "5-Hydroxymethylcytosine plays a critical role in glioblastomagenesis by
RT recruiting the CHTOP-methylosome complex.";
RL Cell Rep. 9:48-60(2014).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-12, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [18]
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).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-12, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=15794639; DOI=10.1021/bi047785w;
RA Wan C., Tempel W., Liu Z.J., Wang B.C., Rose R.B.;
RT "Structure of the conserved transcriptional repressor enhancer of
RT rudimentary homolog.";
RL Biochemistry 44:5017-5023(2005).
CC -!- FUNCTION: May have a role in the cell cycle.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with POLDIP3. Component
CC of the methylosome, a 20S complex containing at least CLNS1A/pICln,
CC PRMT5/SKB1, WDR77/MEP50, PRMT1 and ERH (PubMed:25284789). Interacts
CC with CHTOP (PubMed:25284789). {ECO:0000250|UniProtKB:P84089,
CC ECO:0000269|PubMed:16984396, ECO:0000269|PubMed:25284789}.
CC -!- INTERACTION:
CC P84090; P27449: ATP6V0C; NbExp=3; IntAct=EBI-711389, EBI-721179;
CC P84090; Q9H3R5: CENPH; NbExp=3; IntAct=EBI-711389, EBI-1003700;
CC P84090; Q9Y3Y2: CHTOP; NbExp=4; IntAct=EBI-711389, EBI-347794;
CC P84090; Q9Y3Y2-3: CHTOP; NbExp=5; IntAct=EBI-711389, EBI-11984237;
CC P84090; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-711389, EBI-3867333;
CC P84090; P60900: PSMA6; NbExp=3; IntAct=EBI-711389, EBI-357793;
CC P84090; P62318: SNRPD3; NbExp=3; IntAct=EBI-711389, EBI-372789;
CC P84090; Q5VWN6: TASOR2; NbExp=6; IntAct=EBI-711389, EBI-745958;
CC P84090; Q5VWN6-2: TASOR2; NbExp=3; IntAct=EBI-711389, EBI-10172380;
CC P84090; Q96BW1: UPRT; NbExp=3; IntAct=EBI-711389, EBI-742943;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23145069}.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined.
CC {ECO:0000269|PubMed:8786099}.
CC -!- SIMILARITY: Belongs to the E(R) family. {ECO:0000305}.
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DR EMBL; D85758; BAA12865.1; -; mRNA.
DR EMBL; U66871; AAC51172.1; -; mRNA.
DR EMBL; BT006877; AAP35523.1; -; mRNA.
DR EMBL; AK312186; BAG35119.1; -; mRNA.
DR EMBL; CH471061; EAW80989.1; -; Genomic_DNA.
DR EMBL; BC014301; AAH14301.1; -; mRNA.
DR EMBL; BC071709; AAH71709.1; -; mRNA.
DR EMBL; CR450298; CAG29294.1; -; mRNA.
DR EMBL; CR542178; CAG46975.1; -; mRNA.
DR CCDS; CCDS9794.1; -.
DR RefSeq; NP_004441.1; NM_004450.2.
DR PDB; 1W9G; X-ray; 2.00 A; A/B=1-104.
DR PDB; 2NML; X-ray; 1.55 A; A=1-104.
DR PDB; 7CNC; X-ray; 1.60 A; A=1-104.
DR PDBsum; 1W9G; -.
DR PDBsum; 2NML; -.
DR PDBsum; 7CNC; -.
DR AlphaFoldDB; P84090; -.
DR SMR; P84090; -.
DR BioGRID; 108390; 172.
DR CORUM; P84090; -.
DR DIP; DIP-42473N; -.
DR IntAct; P84090; 69.
DR MINT; P84090; -.
DR STRING; 9606.ENSP00000451080; -.
DR GlyGen; P84090; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P84090; -.
DR PhosphoSitePlus; P84090; -.
DR SwissPalm; P84090; -.
DR BioMuta; ERH; -.
DR DMDM; 51317296; -.
DR EPD; P84090; -.
DR jPOST; P84090; -.
DR MassIVE; P84090; -.
DR MaxQB; P84090; -.
DR PaxDb; P84090; -.
DR PeptideAtlas; P84090; -.
DR PRIDE; P84090; -.
DR ProteomicsDB; 57749; -.
DR TopDownProteomics; P84090; -.
DR Antibodypedia; 117; 256 antibodies from 27 providers.
DR DNASU; 2079; -.
DR Ensembl; ENST00000557016.6; ENSP00000451080.1; ENSG00000100632.11.
DR GeneID; 2079; -.
DR KEGG; hsa:2079; -.
DR MANE-Select; ENST00000557016.6; ENSP00000451080.1; NM_004450.3; NP_004441.1.
DR UCSC; uc001xlc.3; human.
DR CTD; 2079; -.
DR DisGeNET; 2079; -.
DR GeneCards; ERH; -.
DR HGNC; HGNC:3447; ERH.
DR HPA; ENSG00000100632; Low tissue specificity.
DR MIM; 601191; gene.
DR neXtProt; NX_P84090; -.
DR OpenTargets; ENSG00000100632; -.
DR PharmGKB; PA27859; -.
DR VEuPathDB; HostDB:ENSG00000100632; -.
DR eggNOG; KOG1766; Eukaryota.
DR GeneTree; ENSGT00390000003316; -.
DR HOGENOM; CLU_125703_1_0_1; -.
DR InParanoid; P84090; -.
DR OMA; RTWSDYE; -.
DR OrthoDB; 1512482at2759; -.
DR PhylomeDB; P84090; -.
DR TreeFam; TF314568; -.
DR PathwayCommons; P84090; -.
DR SignaLink; P84090; -.
DR BioGRID-ORCS; 2079; 782 hits in 1046 CRISPR screens.
DR ChiTaRS; ERH; human.
DR EvolutionaryTrace; P84090; -.
DR GeneWiki; ERH_(gene); -.
DR GenomeRNAi; 2079; -.
DR Pharos; P84090; Tbio.
DR PRO; PR:P84090; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P84090; protein.
DR Bgee; ENSG00000100632; Expressed in seminal vesicle and 217 other tissues.
DR ExpressionAtlas; P84090; baseline and differential.
DR Genevisible; P84090; HS.
DR GO; GO:0034709; C:methylosome; IDA:UniProtKB.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0008327; F:methyl-CpG binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; TAS:ProtInc.
DR GO; GO:0006213; P:pyrimidine nucleoside metabolic process; TAS:ProtInc.
DR Gene3D; 3.30.2260.10; -; 1.
DR InterPro; IPR035912; EHR_sf.
DR InterPro; IPR000781; ERH.
DR PANTHER; PTHR12373; PTHR12373; 1.
DR Pfam; PF01133; ER; 1.
DR PIRSF; PIRSF016393; Enh_rudimentary; 1.
DR SUPFAM; SSF143875; SSF143875; 1.
DR PROSITE; PS01290; ER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell cycle; Direct protein sequencing;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:25944712"
FT CHAIN 2..104
FT /note="Enhancer of rudimentary homolog"
FT /id="PRO_0000219351"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:25944712"
FT MOD_RES 11
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 12
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:2NML"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:2NML"
FT STRAND 18..24
FT /evidence="ECO:0007829|PDB:2NML"
FT HELIX 25..43
FT /evidence="ECO:0007829|PDB:2NML"
FT HELIX 54..63
FT /evidence="ECO:0007829|PDB:2NML"
FT STRAND 64..73
FT /evidence="ECO:0007829|PDB:2NML"
FT TURN 74..77
FT /evidence="ECO:0007829|PDB:2NML"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:2NML"
FT HELIX 84..100
FT /evidence="ECO:0007829|PDB:2NML"
SQ SEQUENCE 104 AA; 12259 MW; C609AFF7F63E5279 CRC64;
MSHTILLVQP TKRPEGRTYA DYESVNECME GVCKMYEEHL KRMNPNSPSI TYDISQLFDF
IDDLADLSCL VYRADTQTYQ PYNKDWIKEK IYVLLRRQAQ QAGK
