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Q9Y4H4 (GPSM3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 106. 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:
G-protein-signaling modulator 3
Alternative name(s):
Activator of G-protein signaling 4
G18.1b
Protein G18
Gene names
Name:GPSM3
Synonyms:AGS4, C6orf9, G18
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length160 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Interacts with subunit of G(i) alpha proteins and regulates the activation of G(i) alpha proteins. Ref.1 Ref.8

Subcellular location

Cytoplasm Ref.1.

Tissue specificity

Expressed in heart, placenta, lung and liver. Ref.1

Domain

The GoLoco 1 and/or GoLoco 3 domains exhibit GDI activity towards GDP-bound G(i) alpha protein, but not the GoLoco 2 domain. Ref.8

Sequence similarities

Contains 3 GoLoco domains.

Ontologies

Keywords
   Cellular componentCytoplasm
   DomainRepeat
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGTPase regulator activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 160160G-protein-signaling modulator 3
PRO_0000233717

Regions

Domain62 – 8423GoLoco 1
Domain104 – 12623GoLoco 2
Domain132 – 15524GoLoco 3
Compositional bias16 – 4328Pro-rich

Amino acid modifications

Modified residue391Phosphoserine By similarity
Modified residue561Phosphoserine By similarity
Modified residue591Phosphoserine By similarity

Experimental info

Mutagenesis1211A → D: Restores G(i) alpha binding and GDI activity of the GoLoco 2 domain. Ref.8
Sequence conflict141Q → R Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9Y4H4 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 42B3D207D2C48428

FASTA16017,866
        10         20         30         40         50         60 
MEAERPQEEE DGEQGPPQDE EGWPPPNSTT RPWRSAPPSP PPPGTRHTAL GPRSASLLSL 

        70         80         90        100        110        120 
QTELLLDLVA EAQSRRLEEQ RATFYTPQNP SSLAPAPLRP LEDREQLYST ILSHQCQRME 

       130        140        150        160 
AQRSEPPLPP GGQELLELLL RVQGGGRMEE QRSRPPTHTC 

« Hide

References

« Hide 'large scale' references
[1]"Identification and characterization of AGS4: a protein containing three G-protein regulatory motifs that regulate the activation state of Gialpha."
Cao X., Cismowski M.J., Sato M., Blumer J.B., Lanier S.M.
J. Biol. Chem. 279:27567-27574(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Lung.
[2]"Characterisation of the novel gene G18, located in the class III region of the human major histocompatibility complex."
Kendall E., Campbell R.D.
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"A novel gene expressed in human adrenal gland."
Li Y., Fu S., Huang C., Jiang C., Ren S., Zhou J., Yu Y., Xu S., Wang Y., Fu G., Chen Z., Han Z.
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Adrenal gland.
[4]"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: Umbilical cord blood.
[5]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton 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].
[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: B-cell.
[8]"Guanine nucleotide dissociation inhibitor activity of the triple GoLoco motif protein G18: alanine-to-aspartate mutation restores function to an inactive second GoLoco motif."
Kimple R.J., Willard F.S., Hains M.D., Jones M.B., Nweke G.K., Siderovski D.P.
Biochem. J. 378:801-808(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ALA-121, DOMAIN.
[9]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ243937 mRNA. Translation: CAB51288.1.
AF155657 mRNA. Translation: AAF67476.1.
AK313922 mRNA. Translation: BAG36643.1.
AL662830 Genomic DNA. Translation: CAI17541.1.
AL662884 Genomic DNA. Translation: CAI18360.1.
AL845464 Genomic DNA. Translation: CAI41816.1.
BX284686 Genomic DNA. Translation: CAM26229.1.
BX927239 Genomic DNA. Translation: CAQ06601.1.
CR933878 Genomic DNA. Translation: CAQ09630.1.
CR812478 Genomic DNA. Translation: CAQ10705.1.
CH471081 Genomic DNA. Translation: EAX03620.1.
BC018724 mRNA. Translation: AAH18724.1.
CCDSCCDS34419.1.
RefSeqNP_001263430.1. NM_001276501.1.
NP_071390.1. NM_022107.1.
UniGeneHs.520046.

3D structure databases

ProteinModelPortalQ9Y4H4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122005. 3 interactions.
IntActQ9Y4H4. 1 interaction.
MINTMINT-1034681.
STRING9606.ENSP00000364180.

PTM databases

PhosphoSiteQ9Y4H4.

Polymorphism databases

DMDM74753502.

Proteomic databases

MaxQBQ9Y4H4.
PaxDbQ9Y4H4.
PRIDEQ9Y4H4.

Protocols and materials databases

DNASU63940.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375040; ENSP00000364180; ENSG00000213654.
ENST00000375043; ENSP00000364183; ENSG00000213654.
ENST00000383265; ENSP00000372752; ENSG00000206314.
ENST00000383269; ENSP00000372756; ENSG00000206314.
ENST00000414839; ENSP00000405026; ENSG00000236697.
ENST00000420041; ENSP00000413975; ENSG00000233490.
ENST00000424520; ENSP00000413430; ENSG00000237052.
ENST00000429209; ENSP00000392487; ENSG00000234243.
ENST00000432871; ENSP00000414939; ENSG00000234508.
ENST00000441705; ENSP00000396786; ENSG00000234243.
ENST00000445326; ENSP00000407538; ENSG00000234508.
ENST00000448684; ENSP00000403132; ENSG00000236697.
ENST00000453667; ENSP00000414024; ENSG00000233490.
ENST00000457070; ENSP00000410087; ENSG00000237052.
GeneID63940.
KEGGhsa:63940.
UCSCuc003oay.4. human.

Organism-specific databases

CTD63940.
GeneCardsGC06M032229.
GC06Mi32169.
GC06Mj32107.
GC06Ml32197.
GC06Mm32234.
GC06Mn32116.
GC06Mo32165.
HGNCHGNC:13945. GPSM3.
neXtProtNX_Q9Y4H4.
PharmGKBPA25940.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG77431.
HOGENOMHOG000232123.
HOVERGENHBG052882.
InParanoidQ9Y4H4.
KOK15838.
OMACQRIEAQ.
PhylomeDBQ9Y4H4.
TreeFamTF339136.

Gene expression databases

ArrayExpressQ9Y4H4.
BgeeQ9Y4H4.
CleanExHS_GPSM3.
GenevestigatorQ9Y4H4.

Family and domain databases

InterProIPR024800. G_prot_signal_mod_3.
IPR003109. GoLoco_motif.
[Graphical view]
PANTHERPTHR10098:SF99. PTHR10098:SF99. 1 hit.
PfamPF02188. GoLoco. 3 hits.
[Graphical view]
SMARTSM00390. GoLoco. 3 hits.
[Graphical view]
PROSITEPS50877. GOLOCO. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi63940.
NextBio65706.
PROQ9Y4H4.

Entry information

Entry nameGPSM3_HUMAN
AccessionPrimary (citable) accession number: Q9Y4H4
Secondary accession number(s): A2BFJ3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 106 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM