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Protein

GTP-binding protein REM 1

Gene

Rem1

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

Functioni

Promotes endothelial cell sprouting and actin cytoskeletal reorganization (By similarity). May be involved in angiogenesis. May function in Ca2+ signaling.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi87 – 948GTPBy similarity
Nucleotide bindingi194 – 1974GTPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Calmodulin-binding, GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
GTP-binding protein REM 1
Alternative name(s):
Rad and Gem-like GTP-binding protein 1
Gene namesi
Name:Rem1
Synonyms:Rem
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1097696. Rem1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 297297GTP-binding protein REM 1PRO_0000122482Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei51 – 511PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO35929.
PaxDbiO35929.
PRIDEiO35929.

PTM databases

iPTMnetiO35929.
PhosphoSiteiO35929.

Expressioni

Tissue specificityi

High expression in cardiac muscle. Moderate expression in lung, skeletal muscle and kidney. Low levels in spleen and brain.

Inductioni

Repressed by lipopolysaccharide stimulation.

Gene expression databases

BgeeiO35929.
CleanExiMM_REM1.
ExpressionAtlasiO35929. baseline and differential.
GenevisibleiO35929. MM.

Interactioni

Subunit structurei

In vitro, interacts with calmodulin in a calcium-dependent manner (By similarity). Interacts 14-3-3 family members including YWHAE, YWHAH, YWHAQ, YWHAZ in a phosphorylation-dependent manner.By similarity1 Publication

Protein-protein interaction databases

MINTiMINT-101892.
STRINGi10090.ENSMUSP00000000369.

Structurei

3D structure databases

ProteinModelPortaliO35929.
SMRiO35929. Positions 79-246.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni267 – 28620Calmodulin-bindingAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi240 – 28748Arg-richAdd
BLAST

Sequence similaritiesi

Belongs to the small GTPase superfamily. RGK family.Curated

Phylogenomic databases

eggNOGiKOG0395. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00780000121849.
HOGENOMiHOG000246961.
HOVERGENiHBG104899.
InParanoidiO35929.
KOiK07847.
OMAiNNQRMAV.
OrthoDBiEOG7Q8CP8.
PhylomeDBiO35929.
TreeFamiTF314379.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR017358. Small_GTPase_GEM/REM/Rad.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERiPTHR24070. PTHR24070. 1 hit.
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PIRSFiPIRSF038017. GTP-binding_GEM. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51421. RAS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O35929-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLNTQQEAK TTLRRRASTP LPLSSRGHQP GRLCTAPSAP SQHPRLGQSV
60 70 80 90 100
SLNPPVRKPS PAQDGWSSES SDSEGSWEAL YRVVLLGDPG VGKTSLASLF
110 120 130 140 150
AEKQDRDPHE QLGGVYERTL SVDGEDTTLV VMDTWEAEKL DESWCQESCL
160 170 180 190 200
QAGSAYVIVY SIADRSSFES ASELRIQLRR THQANHVPII LVGNKADLAR
210 220 230 240 250
CREVSVEEGR ACAVVFDCKF IETSATLQHN VTELFEGVVR QLRLRRQDNA
260 270 280 290
APETPSPRRR ASLGQRARRF LARLTARSAR RRALKARSKS CHNLAVL
Length:297
Mass (Da):32,909
Last modified:January 1, 1998 - v1
Checksum:i4DCFFC50132C8262
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U91601 mRNA. Translation: AAB71639.1.
AK053133 mRNA. Translation: BAC35274.1.
AK084460 mRNA. Translation: BAC39190.1.
CCDSiCCDS16895.1.
RefSeqiNP_033073.1. NM_009047.5.
UniGeneiMm.8752.

Genome annotation databases

EnsembliENSMUST00000000369; ENSMUSP00000000369; ENSMUSG00000000359.
GeneIDi19700.
KEGGimmu:19700.
UCSCiuc008nfw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U91601 mRNA. Translation: AAB71639.1.
AK053133 mRNA. Translation: BAC35274.1.
AK084460 mRNA. Translation: BAC39190.1.
CCDSiCCDS16895.1.
RefSeqiNP_033073.1. NM_009047.5.
UniGeneiMm.8752.

3D structure databases

ProteinModelPortaliO35929.
SMRiO35929. Positions 79-246.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-101892.
STRINGi10090.ENSMUSP00000000369.

PTM databases

iPTMnetiO35929.
PhosphoSiteiO35929.

Proteomic databases

MaxQBiO35929.
PaxDbiO35929.
PRIDEiO35929.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000000369; ENSMUSP00000000369; ENSMUSG00000000359.
GeneIDi19700.
KEGGimmu:19700.
UCSCiuc008nfw.1. mouse.

Organism-specific databases

CTDi28954.
MGIiMGI:1097696. Rem1.

Phylogenomic databases

eggNOGiKOG0395. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00780000121849.
HOGENOMiHOG000246961.
HOVERGENiHBG104899.
InParanoidiO35929.
KOiK07847.
OMAiNNQRMAV.
OrthoDBiEOG7Q8CP8.
PhylomeDBiO35929.
TreeFamiTF314379.

Miscellaneous databases

PROiO35929.
SOURCEiSearch...

Gene expression databases

BgeeiO35929.
CleanExiMM_REM1.
ExpressionAtlasiO35929. baseline and differential.
GenevisibleiO35929. MM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR017358. Small_GTPase_GEM/REM/Rad.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERiPTHR24070. PTHR24070. 1 hit.
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PIRSFiPIRSF038017. GTP-binding_GEM. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51421. RAS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Rem is a new member of the Rad- and Gem/Kir Ras-related GTP-binding protein family repressed by lipopolysaccharide stimulation."
    Finlin B.S., Andres D.A.
    J. Biol. Chem. 272:21982-21988(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Testis.
  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.
    Tissue: Heart and Lung.
  3. "Phosphorylation-dependent association of the Ras-related GTP-binding protein Rem with 14-3-3 proteins."
    Finlin B.S., Andres D.A.
    Arch. Biochem. Biophys. 368:401-412(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH 14-3-3 PROTEINS.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney, Lung and Testis.

Entry informationi

Entry nameiREM1_MOUSE
AccessioniPrimary (citable) accession number: O35929
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: January 1, 1998
Last modified: July 6, 2016
This is version 124 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

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.