ERH_MOUSE
ID ERH_MOUSE Reviewed; 104 AA.
AC P84089; P70659; Q14259;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Enhancer of rudimentary homolog;
DE Short=Mer;
GN Name=Erh;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Thymus;
RA Kuwano Y., Kawamura T., Sugahara S., Watanabe H., Ogata K., Abo T.;
RT "cDNA cloning of a novel mouse protein 'Mer', a homologue of enhancer of
RT rudimentary gene of Drosophila melanogaster.";
RL Biomed. Res. 17:305-309(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, and Embryonic stem cell;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone, and Limb;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP STRUCTURE BY NMR.
RX PubMed=16211485; DOI=10.1007/s10858-005-7959-z;
RA Li H., Inoue M., Yabuki T., Aoki M., Seki E., Matsuda T., Nunokawa E.,
RA Motoda Y., Kobayashi A., Terada T., Shirouzu M., Koshiba S., Lin Y.J.,
RA Guntert P., Suzuki H., Hayashizaki Y., Kigawa T., Yokoyama S.;
RT "Solution structure of the mouse enhancer of rudimentary protein reveals a
RT novel fold.";
RL J. Biomol. NMR 32:329-334(2005).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND SUBUNIT.
RX PubMed=15937287; DOI=10.1110/ps.051484505;
RA Arai R., Kukimoto-Niino M., Uda-Tochio H., Morita S., Uchikubo-Kamo T.,
RA Akasaka R., Etou Y., Hayashizaki Y., Kigawa T., Terada T., Shirouzu M.,
RA Yokoyama S.;
RT "Crystal structure of an enhancer of rudimentary homolog (ERH) at 2.1
RT Angstroms resolution.";
RL Protein Sci. 14:1888-1893(2005).
CC -!- FUNCTION: May have a role in the cell cycle.
CC -!- SUBUNIT: Homodimer (PubMed:15937287). Component of the methylosome, a
CC 20S complex containing at least CLNS1A/pICln, PRMT5/SKB1, WDR77/MEP50,
CC PRMT1 and ERH. Interacts with CHTOP (By similarity).
CC {ECO:0000250|UniProtKB:P84090, ECO:0000269|PubMed:15937287}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P84090}.
CC -!- SIMILARITY: Belongs to the E(R) family. {ECO:0000305}.
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DR EMBL; U66870; AAC53105.1; -; mRNA.
DR EMBL; D73368; BAA11118.1; -; mRNA.
DR EMBL; AK010451; BAB26950.1; -; mRNA.
DR EMBL; AK080617; BAC37960.1; -; mRNA.
DR EMBL; BC083141; AAH83141.1; -; mRNA.
DR CCDS; CCDS36483.1; -.
DR RefSeq; NP_031977.1; NM_007951.4.
DR PDB; 1WWQ; NMR; -; A=1-104.
DR PDB; 1WZ7; X-ray; 2.10 A; A/B/C=1-104.
DR PDBsum; 1WWQ; -.
DR PDBsum; 1WZ7; -.
DR AlphaFoldDB; P84089; -.
DR SMR; P84089; -.
DR BioGRID; 199505; 44.
DR IntAct; P84089; 33.
DR MINT; P84089; -.
DR STRING; 10090.ENSMUSP00000021559; -.
DR iPTMnet; P84089; -.
DR PhosphoSitePlus; P84089; -.
DR SwissPalm; P84089; -.
DR EPD; P84089; -.
DR jPOST; P84089; -.
DR PaxDb; P84089; -.
DR PeptideAtlas; P84089; -.
DR PRIDE; P84089; -.
DR ProteomicsDB; 275884; -.
DR TopDownProteomics; P84089; -.
DR DNASU; 13877; -.
DR Ensembl; ENSMUST00000021559; ENSMUSP00000021559; ENSMUSG00000021131.
DR Ensembl; ENSMUST00000080152; ENSMUSP00000147411; ENSMUSG00000063412.
DR GeneID; 13877; -.
DR KEGG; mmu:13877; -.
DR UCSC; uc007oaz.2; mouse.
DR CTD; 2079; -.
DR MGI; MGI:108089; Erh.
DR VEuPathDB; HostDB:ENSMUSG00000021131; -.
DR VEuPathDB; HostDB:ENSMUSG00000063412; -.
DR eggNOG; KOG1766; Eukaryota.
DR GeneTree; ENSGT00390000003316; -.
DR HOGENOM; CLU_125703_1_0_1; -.
DR InParanoid; P84089; -.
DR OMA; RTWSDYE; -.
DR OrthoDB; 1512482at2759; -.
DR PhylomeDB; P84089; -.
DR TreeFam; TF314568; -.
DR BioGRID-ORCS; 13877; 27 hits in 71 CRISPR screens.
DR ChiTaRS; Erh; mouse.
DR EvolutionaryTrace; P84089; -.
DR PRO; PR:P84089; -.
DR Proteomes; UP000000589; Chromosome 12.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P84089; protein.
DR Bgee; ENSMUSG00000021131; Expressed in yolk sac and 186 other tissues.
DR ExpressionAtlas; P84089; baseline and differential.
DR Genevisible; P84089; MM.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0034709; C:methylosome; ISS:UniProtKB.
DR GO; GO:0030496; C:midbody; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:UniProtKB.
DR GO; GO:0008327; F:methyl-CpG binding; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB.
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; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P84090"
FT CHAIN 2..104
FT /note="Enhancer of rudimentary homolog"
FT /id="PRO_0000219352"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P84090"
FT MOD_RES 11
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P84090"
FT CROSSLNK 12
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P84090"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:1WZ7"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:1WZ7"
FT STRAND 18..24
FT /evidence="ECO:0007829|PDB:1WZ7"
FT HELIX 25..43
FT /evidence="ECO:0007829|PDB:1WZ7"
FT HELIX 54..63
FT /evidence="ECO:0007829|PDB:1WZ7"
FT STRAND 64..73
FT /evidence="ECO:0007829|PDB:1WZ7"
FT TURN 74..77
FT /evidence="ECO:0007829|PDB:1WZ7"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:1WZ7"
FT HELIX 84..96
FT /evidence="ECO:0007829|PDB:1WZ7"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:1WZ7"
SQ SEQUENCE 104 AA; 12259 MW; C609AFF7F63E5279 CRC64;
MSHTILLVQP TKRPEGRTYA DYESVNECME GVCKMYEEHL KRMNPNSPSI TYDISQLFDF
IDDLADLSCL VYRADTQTYQ PYNKDWIKEK IYVLLRRQAQ QAGK
