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P84090

- ERH_HUMAN

UniProt

P84090 - ERH_HUMAN

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Protein

Enhancer of rudimentary homolog

Gene
ERH
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

May have a role in the cell cycle.

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. nucleobase-containing compound metabolic process Source: ProtInc
  3. pyrimidine nucleoside metabolic process Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Cell cycle

Names & Taxonomyi

Protein namesi
Recommended name:
Enhancer of rudimentary homolog
Gene namesi
Name:ERH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:3447. ERH.

Subcellular locationi

GO - Cellular componenti

  1. midbody Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27859.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 104103Enhancer of rudimentary homologPRO_0000219351Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine3 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP84090.
PaxDbiP84090.
PeptideAtlasiP84090.
PRIDEiP84090.

PTM databases

PhosphoSiteiP84090.

Expressioni

Tissue specificityi

Expressed in all tissues examined.1 Publication

Gene expression databases

ArrayExpressiP84090.
BgeeiP84090.
CleanExiHS_ERH.
GenevestigatoriP84090.

Organism-specific databases

HPAiHPA002567.

Interactioni

Subunit structurei

Homodimer By similarity. Interacts with POLDIP3.1 Publication

Protein-protein interaction databases

BioGridi108390. 43 interactions.
DIPiDIP-42473N.
IntActiP84090. 22 interactions.
MINTiMINT-1217007.
STRINGi9606.ENSP00000216520.

Structurei

Secondary structure

1
104
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96
Helixi14 – 163
Beta strandi18 – 247
Helixi25 – 4319
Helixi54 – 6310
Beta strandi64 – 7310
Turni74 – 774
Beta strandi78 – 825
Helixi84 – 10017

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W9GX-ray2.00A/B1-104[»]
2NMLX-ray1.55A1-104[»]
ProteinModelPortaliP84090.
SMRiP84090. Positions 1-102.

Miscellaneous databases

EvolutionaryTraceiP84090.

Family & Domainsi

Sequence similaritiesi

Belongs to the E(R) family.

Phylogenomic databases

eggNOGiNOG317332.
HOGENOMiHOG000246458.
HOVERGENiHBG000348.
InParanoidiP84090.
OMAiHTIILLQ.
OrthoDBiEOG7H4DWR.
PhylomeDBiP84090.
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]
PROSITEiPS01290. ER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P84090-1 [UniParc]FASTAAdd to Basket

« Hide

MSHTILLVQP TKRPEGRTYA DYESVNECME GVCKMYEEHL KRMNPNSPSI    50
TYDISQLFDF IDDLADLSCL VYRADTQTYQ PYNKDWIKEK IYVLLRRQAQ 100
QAGK 104
Length:104
Mass (Da):12,259
Last modified:August 16, 2004 - v1
Checksum:iC609AFF7F63E5279
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D85758 mRNA. Translation: BAA12865.1.
U66871 mRNA. Translation: AAC51172.1.
BT006877 mRNA. Translation: AAP35523.1.
AK312186 mRNA. Translation: BAG35119.1.
CH471061 Genomic DNA. Translation: EAW80989.1.
BC014301 mRNA. Translation: AAH14301.1.
BC071709 mRNA. Translation: AAH71709.1.
CR450298 mRNA. Translation: CAG29294.1.
CR542178 mRNA. Translation: CAG46975.1.
CCDSiCCDS9794.1.
RefSeqiNP_004441.1. NM_004450.2.
UniGeneiHs.509791.

Genome annotation databases

EnsembliENST00000557016; ENSP00000451080; ENSG00000100632.
GeneIDi2079.
KEGGihsa:2079.
UCSCiuc001xlc.2. human.

Polymorphism databases

DMDMi51317296.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D85758 mRNA. Translation: BAA12865.1 .
U66871 mRNA. Translation: AAC51172.1 .
BT006877 mRNA. Translation: AAP35523.1 .
AK312186 mRNA. Translation: BAG35119.1 .
CH471061 Genomic DNA. Translation: EAW80989.1 .
BC014301 mRNA. Translation: AAH14301.1 .
BC071709 mRNA. Translation: AAH71709.1 .
CR450298 mRNA. Translation: CAG29294.1 .
CR542178 mRNA. Translation: CAG46975.1 .
CCDSi CCDS9794.1.
RefSeqi NP_004441.1. NM_004450.2.
UniGenei Hs.509791.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1W9G X-ray 2.00 A/B 1-104 [» ]
2NML X-ray 1.55 A 1-104 [» ]
ProteinModelPortali P84090.
SMRi P84090. Positions 1-102.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108390. 43 interactions.
DIPi DIP-42473N.
IntActi P84090. 22 interactions.
MINTi MINT-1217007.
STRINGi 9606.ENSP00000216520.

PTM databases

PhosphoSitei P84090.

Polymorphism databases

DMDMi 51317296.

Proteomic databases

MaxQBi P84090.
PaxDbi P84090.
PeptideAtlasi P84090.
PRIDEi P84090.

Protocols and materials databases

DNASUi 2079.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000557016 ; ENSP00000451080 ; ENSG00000100632 .
GeneIDi 2079.
KEGGi hsa:2079.
UCSCi uc001xlc.2. human.

Organism-specific databases

CTDi 2079.
GeneCardsi GC14M069846.
HGNCi HGNC:3447. ERH.
HPAi HPA002567.
MIMi 601191. gene.
neXtProti NX_P84090.
PharmGKBi PA27859.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG317332.
HOGENOMi HOG000246458.
HOVERGENi HBG000348.
InParanoidi P84090.
OMAi HTIILLQ.
OrthoDBi EOG7H4DWR.
PhylomeDBi P84090.
TreeFami TF314568.

Miscellaneous databases

ChiTaRSi ERH. human.
EvolutionaryTracei P84090.
GeneWikii ERH_(gene).
GenomeRNAii 2079.
NextBioi 8453.
PROi P84090.
SOURCEi Search...

Gene expression databases

ArrayExpressi P84090.
Bgeei P84090.
CleanExi HS_ERH.
Genevestigatori P84090.

Family and domain databases

InterProi IPR000781. Enh_rudimentary.
[Graphical view ]
PANTHERi PTHR12373. PTHR12373. 1 hit.
Pfami PF01133. ER. 1 hit.
[Graphical view ]
PIRSFi PIRSF016393. Enh_rudimentary. 1 hit.
ProDomi PD008105. Enh_rudimentary. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
PROSITEi PS01290. ER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and mapping of a novel human cDNA homologous to DROER, the enhancer of the Drosophila melanogaster rudimentary gene."
    Isomura M., Okui K., Fujiwara T., Shin S., Nakamura Y.
    Genomics 32:125-127(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. "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].
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: Kidney.
  8. Cited for: PROTEIN SEQUENCE OF 2-12 AND 74-88, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Mammary carcinoma and Ovarian carcinoma.
  9. Lubec G., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 18-34; 74-84 AND 91-96, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Fetal brain cortex.
  10. "Human enhancer of rudimentary is a molecular partner of PDIP46/SKAR, a protein interacting with DNA polymerase delta and S6K1 and regulating cell growth."
    Smyk A., Szuminska M., Uniewicz K.A., Graves L.M., Kozlowski P.
    FEBS J. 273:4728-4741(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH POLDIP3.
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Structure of the conserved transcriptional repressor enhancer of rudimentary homolog."
    Wan C., Tempel W., Liu Z.J., Wang B.C., Rose R.B.
    Biochemistry 44:5017-5023(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Entry informationi

Entry nameiERH_HUMAN
AccessioniPrimary (citable) accession number: P84090
Secondary accession number(s): B2R5H2, P70659, Q14259
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: July 9, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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