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Q9CZU4 (ERAL1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
GTPase Era, mitochondrial

Short name=M-ERA
Alternative name(s):
Conserved ERA-like GTPase
Short name=CEGA
ERA-W
ERA-like protein 1
Gene names
Name:Eral1
Synonyms:Mera
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length437 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Probable GTPase that plays a role in the mitochondrial ribosomal small subunit assembly. Specifically binds the 12S mitochondrial rRNA (12S mt-rRNA) to a 33 nucleotide section delineating the 3' terminal stem-loop region. May act as a chaperone that protects the 12S mt-rRNA on the 28S mitoribosomal subunit during ribosomal small subunit assembly By similarity. HAMAP-Rule MF_00367

Subcellular location

Mitochondrion matrix By similarity. Mitochondrion inner membrane; Peripheral membrane protein By similarity. Note: Localizes on the matrix side on the mitochondrial inner membrane By similarity. HAMAP-Rule MF_00367

Sequence similarities

Belongs to the Era/MnmE GTP-binding protein family. Era subfamily.

Contains 1 G (guanine nucleotide-binding) domain.

Contains 1 KH type-2 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2020Mitochondrion Potential
Chain21 – 437417GTPase Era, mitochondrial HAMAP-Rule MF_00367
PRO_0000180082

Regions

Domain125 – 237113G
Domain360 – 43778KH type-2
Nucleotide binding120 – 1278GTP Potential
Nucleotide binding167 – 1715GTP Potential
Nucleotide binding236 – 2394GTP Potential

Amino acid modifications

Modified residue1731Phosphoserine By similarity

Experimental info

Sequence conflict1541G → W in BAB56113. Ref.1
Sequence conflict4071L → S in AAH68271. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9CZU4 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: D6118FD53DC9A7E1

FASTA43748,187
        10         20         30         40         50         60 
MAAPRRYCAG LVRALLGARQ VGSHAGREWL APPGCLLGNQ ARCVSCVVGS TFSGPLLASA 

        70         80         90        100        110        120 
SSRYGQDSAL DRILGFSQPD SSLVPSVPAV SVHRDEQNLL LVHTPDMPEN PRVLRVVLLG 

       130        140        150        160        170        180 
APNAGKSTLS NQLLGRKVFP VSKKVHTTRC QALGVITEKE TQVILLDTPG IISPVKQKRH 

       190        200        210        220        230        240 
HLERSLLEDP WTSMESADLV VVLVDVSDKW TRSRLNPQVL QCLTKFSQVP SILVLNKVDC 

       250        260        270        280        290        300 
LKQKSVLLEL TAALTEGVVN GKKLNIKQAL RSRSSTHCPG PETEGPNAHS VRNPQRIGWP 

       310        320        330        340        350        360 
YFQEIFMLSA LNNKDVNTLK QYLLTQAQPG PWEFHSGVLT SQTPEEICAN KIREKLLEYL 

       370        380        390        400        410        420 
PEEVPYGVQQ KTVIWEEGPS GELVIQQNLL VPKESHVRIL IGQKGLLISQ IAQEVGRDLM 

       430 
DIFHCDVLIR LSVKLLK 

« Hide

References

« Hide 'large scale' references
[1]"Mammalian homologue of E. coli Ras-like GTPase (ERA) is a possible apoptosis regulator with RNA binding activity."
Akiyama T., Gohda J., Shibata S., Nomura Y., Azuma S., Ohmori Y., Sugano S., Arai H., Yamamoto T., Inoue J.
Genes Cells 6:987-1001(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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. expand/collapse author list , 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.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[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].
Strain: 129/Sv X 129SvCp and Czech II.
Tissue: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB049389 mRNA. Translation: BAB56113.1.
AK012155 mRNA. Translation: BAB28065.1.
AL669840 Genomic DNA. Translation: CAI25706.1.
BC019728 mRNA. Translation: AAH19728.1.
BC068271 mRNA. Translation: AAH68271.1.
RefSeqNP_071708.2. NM_022313.2.
UniGeneMm.21096.

3D structure databases

ProteinModelPortalQ9CZU4.
SMRQ9CZU4. Positions 94-436.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ9CZU4.

Proteomic databases

PRIDEQ9CZU4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021183; ENSMUSP00000021183; ENSMUSG00000020832.
GeneID57837.
KEGGmmu:57837.
UCSCuc007kia.2. mouse.

Organism-specific databases

CTD26284.
MGIMGI:1889295. Eral1.

Phylogenomic databases

eggNOGCOG1159.
GeneTreeENSGT00390000013800.
HOGENOMHOG000245598.
HOVERGENHBG051495.
InParanoidQ8VE60.
OMATTTRNIS.
OrthoDBEOG7XWPNP.
PhylomeDBQ9CZU4.
TreeFamTF321650.

Gene expression databases

BgeeQ9CZU4.
CleanExMM_ERAL1.
GenevestigatorQ9CZU4.

Family and domain databases

Gene3D3.30.300.20. 1 hit.
3.40.50.300. 2 hits.
HAMAPMF_00367. GTPase_Era.
InterProIPR005662. GTP-bd_Era.
IPR006073. GTP_binding_domain.
IPR015946. KH_dom-like_a/b.
IPR009019. KH_prok-type.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
[Graphical view]
PfamPF01926. MMR_HSR1. 1 hit.
[Graphical view]
PRINTSPR00326. GTP1OBG.
SUPFAMSSF52540. SSF52540. 2 hits.
SSF54814. SSF54814. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
ProtoNetSearch...

Other

NextBio314014.
PROQ9CZU4.
SOURCESearch...

Entry information

Entry nameERAL1_MOUSE
AccessionPrimary (citable) accession number: Q9CZU4
Secondary accession number(s): Q6NV78, Q8VE60, Q925U1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot