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Protein

Enhancer of rudimentary homolog

Gene

Erh

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May have a role in the cell cycle.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle

Names & Taxonomyi

Protein namesi
Recommended name:
Enhancer of rudimentary homolog
Short name:
Mer
Gene namesi
Name:Erh
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:108089. Erh.

Subcellular locationi

GO - Cellular componenti

  • membrane Source: UniProtKB
  • methylosome Source: UniProtKB
  • midbody Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 104103Enhancer of rudimentary homologPRO_0000219352Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei11 – 111PhosphothreonineBy similarity
Cross-linki12 – 12Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP84089.
PaxDbiP84089.
PeptideAtlasiP84089.
PRIDEiP84089.
TopDownProteomicsiP84089.

PTM databases

iPTMnetiP84089.
PhosphoSiteiP84089.

Expressioni

Gene expression databases

BgeeiP84089.
CleanExiMM_ERH.
ExpressionAtlasiP84089. baseline.
GenevisibleiP84089. MM.

Interactioni

Subunit structurei

Homodimer (PubMed:15937287). Component of the methylosome, a 20S complex containing at least CLNS1A/pICln, PRMT5/SKB1, WDR77/MEP50, PRMT1 and ERH. Interacts with CHTOP (By similarity).By similarity1 Publication

Protein-protein interaction databases

BioGridi199505. 27 interactions.
IntActiP84089. 30 interactions.
MINTiMINT-4430981.
STRINGi10090.ENSMUSP00000021559.

Structurei

Secondary structure

1
104
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96Combined sources
Beta strandi11 – 144Combined sources
Beta strandi18 – 247Combined sources
Helixi25 – 4319Combined sources
Helixi54 – 6310Combined sources
Beta strandi64 – 7310Combined sources
Turni74 – 774Combined sources
Beta strandi78 – 825Combined sources
Helixi84 – 9613Combined sources
Turni97 – 993Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WWQNMR-A1-104[»]
1WZ7X-ray2.10A/B/C1-104[»]
ProteinModelPortaliP84089.
SMRiP84089. Positions 1-102.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP84089.

Family & Domainsi

Sequence similaritiesi

Belongs to the E(R) family.Curated

Phylogenomic databases

eggNOGiKOG1766. Eukaryota.
ENOG4111Z48. LUCA.
HOGENOMiHOG000246458.
HOVERGENiHBG000348.
InParanoidiP84089.
OrthoDBiEOG7H4DWR.
PhylomeDBiP84089.
TreeFamiTF314568.

Family and domain databases

InterProiIPR000781. Enh_rudimentary.
[Graphical view]
PANTHERiPTHR12373. PTHR12373. 1 hit.
PfamiPF01133. ER. 1 hit.
[Graphical view]
PIRSFiPIRSF016393. Enh_rudimentary. 1 hit.
ProDomiPD008105. Enh_rudimentary. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF143875. SSF143875. 1 hit.
PROSITEiPS01290. ER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P84089-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHTILLVQP TKRPEGRTYA DYESVNECME GVCKMYEEHL KRMNPNSPSI
60 70 80 90 100
TYDISQLFDF IDDLADLSCL VYRADTQTYQ PYNKDWIKEK IYVLLRRQAQ

QAGK
Length:104
Mass (Da):12,259
Last modified:August 16, 2004 - v1
Checksum:iC609AFF7F63E5279
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U66870 mRNA. Translation: AAC53105.1.
D73368 mRNA. Translation: BAA11118.1.
AK010451 mRNA. Translation: BAB26950.1.
AK080617 mRNA. Translation: BAC37960.1.
BC083141 mRNA. Translation: AAH83141.1.
CCDSiCCDS36483.1.
RefSeqiNP_031977.1. NM_007951.3.
UniGeneiMm.246551.
Mm.378913.

Genome annotation databases

EnsembliENSMUST00000021559; ENSMUSP00000021559; ENSMUSG00000021131.
GeneIDi13877.
KEGGimmu:13877.
UCSCiuc007oaz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U66870 mRNA. Translation: AAC53105.1.
D73368 mRNA. Translation: BAA11118.1.
AK010451 mRNA. Translation: BAB26950.1.
AK080617 mRNA. Translation: BAC37960.1.
BC083141 mRNA. Translation: AAH83141.1.
CCDSiCCDS36483.1.
RefSeqiNP_031977.1. NM_007951.3.
UniGeneiMm.246551.
Mm.378913.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WWQNMR-A1-104[»]
1WZ7X-ray2.10A/B/C1-104[»]
ProteinModelPortaliP84089.
SMRiP84089. Positions 1-102.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199505. 27 interactions.
IntActiP84089. 30 interactions.
MINTiMINT-4430981.
STRINGi10090.ENSMUSP00000021559.

PTM databases

iPTMnetiP84089.
PhosphoSiteiP84089.

Proteomic databases

EPDiP84089.
PaxDbiP84089.
PeptideAtlasiP84089.
PRIDEiP84089.
TopDownProteomicsiP84089.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000021559; ENSMUSP00000021559; ENSMUSG00000021131.
GeneIDi13877.
KEGGimmu:13877.
UCSCiuc007oaz.2. mouse.

Organism-specific databases

CTDi2079.
MGIiMGI:108089. Erh.

Phylogenomic databases

eggNOGiKOG1766. Eukaryota.
ENOG4111Z48. LUCA.
HOGENOMiHOG000246458.
HOVERGENiHBG000348.
InParanoidiP84089.
OrthoDBiEOG7H4DWR.
PhylomeDBiP84089.
TreeFamiTF314568.

Miscellaneous databases

EvolutionaryTraceiP84089.
PROiP84089.
SOURCEiSearch...

Gene expression databases

BgeeiP84089.
CleanExiMM_ERH.
ExpressionAtlasiP84089. baseline.
GenevisibleiP84089. MM.

Family and domain databases

InterProiIPR000781. Enh_rudimentary.
[Graphical view]
PANTHERiPTHR12373. PTHR12373. 1 hit.
PfamiPF01133. ER. 1 hit.
[Graphical view]
PIRSFiPIRSF016393. Enh_rudimentary. 1 hit.
ProDomiPD008105. Enh_rudimentary. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF143875. SSF143875. 1 hit.
PROSITEiPS01290. ER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The putative cell cycle gene, enhancer of rudimentary, encodes a highly conserved protein found in plants and animals."
    Gelsthorpe M., Pulumati M., McCallum C., Dang-Vu K., Tsubota S.I.
    Gene 186:189-195(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "cDNA cloning of a novel mouse protein 'Mer', a homologue of enhancer of rudimentary gene of Drosophila melanogaster."
    Kuwano Y., Kawamura T., Sugahara S., Watanabe H., Ogata K., Abo T.
    Biomed. Res. 17:305-309(1996)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ.
    Tissue: Thymus.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain cortex and Embryonic stem cell.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Bone and Limb.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  6. Cited for: STRUCTURE BY NMR.
  7. Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), SUBUNIT.

Entry informationi

Entry nameiERH_MOUSE
AccessioniPrimary (citable) accession number: P84089
Secondary accession number(s): P70659, Q14259
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: July 6, 2016
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.