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Q9CZU4

- ERAL1_MOUSE

UniProt

Q9CZU4 - ERAL1_MOUSE

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Protein

GTPase Era, mitochondrial

Gene

Eral1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

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).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi120 – 1278GTPSequence Analysis
Nucleotide bindingi167 – 1715GTPSequence Analysis
Nucleotide bindingi236 – 2394GTPSequence Analysis

GO - Molecular functioni

  1. GTP binding Source: UniProtKB-KW
  2. poly(A) RNA binding Source: Ensembl
  3. ribosomal small subunit binding Source: UniProtKB
  4. rRNA binding Source: UniProtKB

GO - Biological processi

  1. ribosomal small subunit assembly Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Ribosome biogenesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding, RNA-binding, rRNA-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Eral1
Synonyms:Mera
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:1889295. Eral1.

Subcellular locationi

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

GO - Cellular componenti

  1. actin cytoskeleton Source: Ensembl
  2. intermediate filament cytoskeleton Source: Ensembl
  3. mitochondrial inner membrane Source: UniProtKB-KW
  4. mitochondrial matrix Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2020MitochondrionSequence AnalysisAdd
BLAST
Chaini21 – 437417GTPase Era, mitochondrialPRO_0000180082Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei173 – 1731PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9CZU4.
PRIDEiQ9CZU4.

PTM databases

PhosphoSiteiQ9CZU4.

Expressioni

Gene expression databases

BgeeiQ9CZU4.
CleanExiMM_ERAL1.
GenevestigatoriQ9CZU4.

Structurei

3D structure databases

ProteinModelPortaliQ9CZU4.
SMRiQ9CZU4. Positions 112-436.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini112 – 330219Era-type GAdd
BLAST
Domaini360 – 43778KH type-2Add
BLAST

Sequence similaritiesi

Contains 1 KH type-2 domain.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1159.
GeneTreeiENSGT00390000013800.
HOGENOMiHOG000245598.
HOVERGENiHBG051495.
InParanoidiQ9CZU4.
OMAiHDNAQIV.
OrthoDBiEOG7XWPNP.
PhylomeDBiQ9CZU4.
TreeFamiTF321650.

Family and domain databases

Gene3Di3.30.300.20. 1 hit.
3.40.50.300. 2 hits.
HAMAPiMF_00367. GTPase_Era.
InterProiIPR005662. 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]
PfamiPF01926. MMR_HSR1. 1 hit.
[Graphical view]
PRINTSiPR00326. GTP1OBG.
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF54814. SSF54814. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51713. G_ERA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9CZU4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAPRRYCAG LVRALLGARQ VGSHAGREWL APPGCLLGNQ ARCVSCVVGS
60 70 80 90 100
TFSGPLLASA SSRYGQDSAL DRILGFSQPD SSLVPSVPAV SVHRDEQNLL
110 120 130 140 150
LVHTPDMPEN PRVLRVVLLG APNAGKSTLS NQLLGRKVFP VSKKVHTTRC
160 170 180 190 200
QALGVITEKE TQVILLDTPG IISPVKQKRH HLERSLLEDP WTSMESADLV
210 220 230 240 250
VVLVDVSDKW TRSRLNPQVL QCLTKFSQVP SILVLNKVDC LKQKSVLLEL
260 270 280 290 300
TAALTEGVVN GKKLNIKQAL RSRSSTHCPG PETEGPNAHS VRNPQRIGWP
310 320 330 340 350
YFQEIFMLSA LNNKDVNTLK QYLLTQAQPG PWEFHSGVLT SQTPEEICAN
360 370 380 390 400
KIREKLLEYL PEEVPYGVQQ KTVIWEEGPS GELVIQQNLL VPKESHVRIL
410 420 430
IGQKGLLISQ IAQEVGRDLM DIFHCDVLIR LSVKLLK
Length:437
Mass (Da):48,187
Last modified:June 1, 2001 - v1
Checksum:iD6118FD53DC9A7E1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti154 – 1541G → W in BAB56113. (PubMed:11733036)Curated
Sequence conflicti407 – 4071L → S in AAH68271. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS48856.1.
RefSeqiNP_071708.2. NM_022313.2.
UniGeneiMm.21096.

Genome annotation databases

EnsembliENSMUST00000021183; ENSMUSP00000021183; ENSMUSG00000020832.
GeneIDi57837.
KEGGimmu:57837.
UCSCiuc007kia.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS48856.1.
RefSeqi NP_071708.2. NM_022313.2.
UniGenei Mm.21096.

3D structure databases

ProteinModelPortali Q9CZU4.
SMRi Q9CZU4. Positions 112-436.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q9CZU4.

Proteomic databases

MaxQBi Q9CZU4.
PRIDEi Q9CZU4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000021183 ; ENSMUSP00000021183 ; ENSMUSG00000020832 .
GeneIDi 57837.
KEGGi mmu:57837.
UCSCi uc007kia.2. mouse.

Organism-specific databases

CTDi 26284.
MGIi MGI:1889295. Eral1.

Phylogenomic databases

eggNOGi COG1159.
GeneTreei ENSGT00390000013800.
HOGENOMi HOG000245598.
HOVERGENi HBG051495.
InParanoidi Q9CZU4.
OMAi HDNAQIV.
OrthoDBi EOG7XWPNP.
PhylomeDBi Q9CZU4.
TreeFami TF321650.

Miscellaneous databases

NextBioi 314014.
PROi Q9CZU4.
SOURCEi Search...

Gene expression databases

Bgeei Q9CZU4.
CleanExi MM_ERAL1.
Genevestigatori Q9CZU4.

Family and domain databases

Gene3Di 3.30.300.20. 1 hit.
3.40.50.300. 2 hits.
HAMAPi MF_00367. GTPase_Era.
InterProi IPR005662. 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 ]
Pfami PF01926. MMR_HSR1. 1 hit.
[Graphical view ]
PRINTSi PR00326. GTP1OBG.
SUPFAMi SSF52540. SSF52540. 2 hits.
SSF54814. SSF54814. 1 hit.
TIGRFAMsi TIGR00231. small_GTP. 1 hit.
PROSITEi PS51713. G_ERA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiERAL1_MOUSE
AccessioniPrimary (citable) accession number: Q9CZU4
Secondary accession number(s): Q6NV78, Q8VE60, Q925U1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: June 1, 2001
Last modified: October 29, 2014
This is version 102 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

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3