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P55040 (GEM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
GTP-binding protein GEM
Alternative name(s):
GTP-binding mitogen-induced T-cell protein
RAS-like protein KIR
Gene names
Name:GEM
Synonyms:KIR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length296 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Could be a regulatory protein, possibly participating in receptor-mediated signal transduction at the plasma membrane. Has guanine nucleotide-binding activity but undetectable intrinsic GTPase activity.

Subunit structure

Interacts with calmodulin in a Ca2+-dependent manner. Binds ROCK1. Ref.6 Ref.7

Subcellular location

Cell membrane; Peripheral membrane protein; Cytoplasmic side.

Tissue specificity

Most abundant in thymus, spleen, kidney, lung, and testis. Less abundant in heart, brain, liver and skeletal muscle.

Induction

By mitogens.

Post-translational modification

Phosphorylated on tyrosine residues.

Sequence similarities

Belongs to the small GTPase superfamily. RGK family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TRIM23P364063EBI-744104,EBI-740098

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 296296GTP-binding protein GEM
PRO_0000122475

Regions

Nucleotide binding82 – 898GTP By similarity
Nucleotide binding191 – 1944GTP By similarity
Region266 – 28520Calmodulin-binding By similarity

Natural variations

Natural variant431R → G.
Corresponds to variant rs2170363 [ dbSNP | Ensembl ].
VAR_020097

Experimental info

Sequence conflict1591I → V in AAC50067. Ref.2
Sequence conflict174 – 1752QL → HV in AAC50067. Ref.2

Secondary structure

................................. 296
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P55040 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: B7BB3F2CA96D338F

FASTA29633,949
        10         20         30         40         50         60 
MTLNNVTMRQ GTVGMQPQQQ RWSIPADGRH LMVQKEPHQY SHRNRHSATP EDHCRRSWSS 

        70         80         90        100        110        120 
DSTDSVISSE SGNTYYRVVL IGEQGVGKST LANIFAGVHD SMDSDCEVLG EDTYERTLMV 

       130        140        150        160        170        180 
DGESATIILL DMWENKGENE WLHDHCMQVG DAYLIVYSIT DRASFEKASE LRIQLRRARQ 

       190        200        210        220        230        240 
TEDIPIILVG NKSDLVRCRE VSVSEGRACA VVFDCKFIET SAAVQHNVKE LFEGIVRQVR 

       250        260        270        280        290 
LRRDSKEKNE RRLAYQKRKE SMPRKARRFW GKIVAKNNKN MAFKLKSKSC HDLSVL 

« Hide

References

« Hide 'large scale' references
[1]"Gem: an induced, immediate early protein belonging to the Ras family."
Maguire J., Santoro T., Jensen P., Siebenlist U., Yewdell J., Kelly K.
Science 265:241-244(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Peripheral blood.
[2]"Transcriptional activation of a ras-like gene (kir) by oncogenic tyrosine kinases."
Cohen L., Mohr R., Chen Y.-Y., Huang M., Kato R., Dorin D., Tamanoi F., Goga A., Afar D., Rosenberg N., Witte O.
Proc. Natl. Acad. Sci. U.S.A. 91:12448-12452(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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. expand/collapse author list , 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].
Tissue: Amygdala.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: Testis.
[6]"Rad and Rad-related GTPases interact with calmodulin and calmodulin-dependent protein kinase II."
Moyers J.S., Bilan P.J., Zhu J., Kahn C.R.
J. Biol. Chem. 272:11832-11839(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CALMODULIN.
[7]"The GTP binding proteins Gem and Rad are negative regulators of the Rho-Rho kinase pathway."
Ward Y., Yap S.-F., Ravichandran V., Matsumura F., Ito M., Spinelli B., Kelly K.
J. Cell Biol. 157:291-302(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ROCK1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U10550 mRNA. Translation: AAA64911.1.
U13052 mRNA. Translation: AAC50067.1.
AK314017 mRNA. Translation: BAG36728.1.
CH471060 Genomic DNA. Translation: EAW91709.1.
BC022010 mRNA. Translation: AAH22010.1.
IPIIPI00022710.
PIRA54575.
I38745.
RefSeqNP_005252.1. NM_005261.3.
NP_859053.1. NM_181702.2.
UniGeneHs.654463.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CJWX-ray2.10A/B74-261[»]
2G3YX-ray2.40A62-249[»]
2HT6X-ray2.40A/B71-243[»]
ProteinModelPortalP55040.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-41587N.
IntActP55040. 13 interactions.
MINTMINT-1468979.
STRING9606.ENSP00000297596.

PTM databases

PhosphoSiteP55040.

Polymorphism databases

DMDM1707896.

Proteomic databases

PaxDbP55040.
PRIDEP55040.

Protocols and materials databases

DNASU2669.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000297596; ENSP00000297596; ENSG00000164949.
ENST00000396194; ENSP00000379497; ENSG00000164949.
GeneID2669.
KEGGhsa:2669.
UCSCuc003ygi.3. human.

Organism-specific databases

CTD2669.
GeneCardsGC08M095330.
HGNCHGNC:4234. GEM.
HPAHPA024798.
MIM600164. gene.
neXtProtNX_P55040.
PharmGKBPA28645.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000246961.
HOVERGENHBG104899.
InParanoidP55040.
KOK07846.
OMAAPEDHCR.
OrthoDBEOG49KFR5.
PhylomeDBP55040.

Gene expression databases

ArrayExpressP55040.
BgeeP55040.
CleanExHS_GEM.
GenevestigatorP55040.
GermOnlineENSG00000164949. Homo sapiens.

Family and domain databases

InterProIPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR017358. Small_GTPase_GEM/REM/Rad.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERPTHR24070. PTHR24070. 1 hit.
PfamPF00071. Ras. 1 hit.
[Graphical view]
PIRSFPIRSF038017. GTP-binding_GEM. 1 hit.
PRINTSPR00449. RASTRNSFRMNG.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51421. RAS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP55040.
GenomeRNAi2669.
NextBio10532.
SOURCESearch...

Entry information

Entry nameGEM_HUMAN
AccessionPrimary (citable) accession number: P55040
Secondary accession number(s): B2RA31
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 1, 2013
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families