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Q86YR5 (GPSM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
G-protein-signaling modulator 1
Alternative name(s):
Activator of G-protein signaling 3
Gene names
Name:GPSM1
Synonyms:AGS3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length675 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Guanine nucleotide dissociation inhibitor (GDI) which functions as a receptor-independent activator of heterotrimeric G-protein signaling. Keeps G(i/o) alpha subunit in its GDP-bound form thus uncoupling heterotrimeric G-proteins signaling from G protein-coupled receptors. Controls spindle orientation and asymmetric cell fate of cerebral cortical progenitors. May also be involved in macroautophagy in intestinal cells. May play a role in drug addiction. Ref.6 Ref.7

Subunit structure

Interacts with GNAI1, GNAI2 and GNAI3 preferentially in their GDP-bound state. May also interact with GNAO1. Interacts with STK11/LKB1 and MACF1 By similarity. Interacts with INSC/inscuteable and FRMPD1. Ref.8 Ref.9

Subcellular location

Cytoplasmcytosol. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cell membrane; Peripheral membrane protein; Cytoplasmic side Ref.7 Ref.9.

Tissue specificity

Expressed in intestinal cells. Ref.7

Domain

The GoLoco domains mediate interaction with G(i/o) alpha By similarity. The GoLoco domains are essential for the GDI activity toward G(i/o) alpha.

Post-translational modification

Phosphorylation regulates interaction with G(i/o) alpha By similarity.

Sequence similarities

Belongs to the GPSM family.

Contains 4 GoLoco domains.

Contains 9 TPR repeats.

Sequence caution

The sequence AAH09979.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAH17353.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAB55951.1 differs from that shown. Reason: Frameshift at position 657.

The sequence CAI19339.1 differs from that shown. Reason: Erroneous gene model prediction.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q86YR5-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q86YR5-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     1-509: Missing.
Note: Minor isoform.
Isoform 3 (identifier: Q86YR5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     404-457: ARPKRTQRLS...LPVRSRKYQE → EFQGCGGVLL...FFLASGTAQA
     458-675: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q86YR5-4)

Also known as: FL;

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: Missing.
Note: Major isoform.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 675675G-protein-signaling modulator 1
PRO_0000252402

Regions

Repeat28 – 6134TPR 1
Repeat66 – 9934TPR 2
Repeat106 – 13934TPR 3
Repeat146 – 18136TPR 4
Repeat183 – 20220TPR 5
Repeat209 – 24234TPR 6
Repeat249 – 28234TPR 7
Repeat289 – 32234TPR 8
Repeat329 – 36234TPR 9
Domain495 – 51723GoLoco 1
Domain548 – 57023GoLoco 2
Domain596 – 61823GoLoco 3
Domain630 – 65223GoLoco 4
Region1 – 509509Mediates association with membranes By similarity
Region364 – 487124Interaction with STK11/LKB1 By similarity

Amino acid modifications

Modified residue4131Phosphoserine Ref.13
Modified residue4711Phosphoserine Ref.11
Modified residue4921Phosphoserine Ref.11
Modified residue4931Phosphoserine Ref.11

Natural variations

Alternative sequence1 – 509509Missing in isoform 2.
VSP_020937
Alternative sequence1 – 2323Missing in isoform 4.
VSP_039028
Alternative sequence404 – 45754ARPKR…RKYQE → EFQGCGGVLLPTGTDRIRSC GGVGSRPGQHGGGGSRQKMA PTSQFFLASGTAQA in isoform 3.
VSP_020938
Alternative sequence458 – 675218Missing in isoform 3.
VSP_020939

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 20, 2010. Version 2.
Checksum: 27EB86667EEC1951

FASTA67574,510
        10         20         30         40         50         60 
MAGPAPPVAD ELPGPAARRL YSRMEASCLE LALEGERLCK AGDFKTGVAF FEAAVQVGTE 

        70         80         90        100        110        120 
DLKTLSAIYS QLGNAYFYLK EHGRALEYHK HDLLLARTIG DRMGEAKASG NLGNTLKVLG 

       130        140        150        160        170        180 
RFDEAAVCCQ RHLSIAQEQG DKVGEARALY NIGNVYHAKG KQLSWNAANA TQDPGHLPPD 

       190        200        210        220        230        240 
VRETLCKASE FYERNLSLVK ELGDRAAQGR AYGNLGNTHY LLGNFTEATT FHKERLAIAK 

       250        260        270        280        290        300 
EFGDKAAERR AYSNLGNAHV FLGRFDVAAE YYKKTLQLSR QLRDQAVEAQ ACYSLGNTYT 

       310        320        330        340        350        360 
LLQDYERAAE YHLRHLLIAQ ELADRVGEGR ACWSLGNAYV SMGRPAQALT FAKKHLQISQ 

       370        380        390        400        410        420 
EIGDRHGELT ARMNVAQLQL VLGRLTSPAA SEKPDLAGYE AQGARPKRTQ RLSAETWDLL 

       430        440        450        460        470        480 
RLPLEREQNG DSHHSGDWRG PSRDSLPLPV RSRKYQEGPD AERRPREGSH SPLDSADVRV 

       490        500        510        520        530        540 
HVPRTSIPRA PSSDEECFFD LLTKFQSSRM DDQRCPLDDG QAGAAEATAA PTLEDRIAQP 

       550        560        570        580        590        600 
SMTASPQTEE FFDLIASSQS RRLDDQRASV GSLPGLRITH SNAGHLRGHG EPQEPGDDFF 

       610        620        630        640        650        660 
NMLIKYQSSR IDDQRCPPPD VLPRGPTMPD EDFFSLIQRV QAKRMDEQRV DLAGGPEQGA 

       670 
GGPPEPQQQC QPGAS 

« Hide

Isoform 2 (Short) [UniParc].

Checksum: B0009DE5201BD2BD
Show »

FASTA16618,024
Isoform 3 [UniParc].

Checksum: 4493B11B5D9986DC
Show »

FASTA45749,685
Isoform 4 (FL) [UniParc].

Checksum: FF690E5EC1999611
Show »

FASTA65272,136

References

« Hide 'large scale' references
[1]"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
Cismowski M.J., Kopatz S.A., Puhl H.L. III, Sharma S.V., Aronstam R.S.
Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Brain.
[2]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]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].
[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] (ISOFORMS 2 AND 3).
Tissue: Fetal brain and Rhabdomyosarcoma.
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 315-675 (ISOFORM 1).
Tissue: Mammary cancer.
[6]"AGS3 inhibits GDP dissociation from galpha subunits of the Gi family and rhodopsin-dependent activation of transducin."
Natochin M., Lester B., Peterson Y.K., Bernard M.L., Lanier S.M., Artemyev N.O.
J. Biol. Chem. 275:40981-40985(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"The G-protein regulator AGS3 controls an early event during macroautophagy in human intestinal HT-29 cells."
Pattingre S., de Vries L., Bauvy C., Chantret I., Cluzeaud F., Ogier-Denis E., Vandewalle A., Codogno P.
J. Biol. Chem. 278:20995-21002(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, ALTERNATIVE SPLICING, SUBCELLULAR LOCATION.
[8]"Two forms of human Inscuteable-related protein that links Par3 to the Pins homologues LGN and AGS3."
Izaki T., Kamakura S., Kohjima M., Sumimoto H.
Biochem. Biophys. Res. Commun. 341:1001-1006(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH INSC.
[9]"The PDZ and band 4.1 containing protein Frmpd1 regulates the subcellular location of activator of G-protein signaling 3 and its interaction with G-proteins."
An N., Blumer J.B., Bernard M.L., Lanier S.M.
J. Biol. Chem. 283:24718-24728(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FRMPD1, SUBCELLULAR LOCATION.
[10]"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-471; SER-492 AND SER-493, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY173053 mRNA. Translation: AAO17260.1.
BX649589 Genomic DNA. Translation: CAI19338.1.
BX649589 Genomic DNA. Translation: CAI19339.1. Sequence problems.
BX649589 Genomic DNA. Translation: CAM27654.1.
CH471090 Genomic DNA. Translation: EAW88216.1.
BC009979 mRNA. Translation: AAH09979.1. Different initiation.
BC017353 mRNA. Translation: AAH17353.1. Different initiation.
BC048343 mRNA. Translation: AAH48343.1.
AL117478 mRNA. Translation: CAB55951.1. Frameshift.
PIRT17261.
RefSeqNP_001139110.2. NM_001145638.2.
NP_001139111.1. NM_001145639.1.
NP_001186932.1. NM_001200003.1.
NP_056412.5. NM_015597.5.
UniGeneHs.239370.

3D structure databases

ProteinModelPortalQ86YR5.
SMRQ86YR5. Positions 24-650.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117539. 14 interactions.
IntActQ86YR5. 5 interactions.
MINTMINT-1453185.
STRING9606.ENSP00000392828.

PTM databases

PhosphoSiteQ86YR5.

Polymorphism databases

DMDM294862435.

Proteomic databases

PaxDbQ86YR5.
PRIDEQ86YR5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000291775; ENSP00000291775; ENSG00000160360. [Q86YR5-2]
ENST00000354753; ENSP00000346797; ENSG00000160360. [Q86YR5-4]
ENST00000392944; ENSP00000376673; ENSG00000160360. [Q86YR5-2]
ENST00000392945; ENSP00000376674; ENSG00000160360. [Q86YR5-3]
ENST00000429455; ENSP00000390705; ENSG00000160360. [Q86YR5-2]
ENST00000440944; ENSP00000392828; ENSG00000160360. [Q86YR5-1]
ENST00000562213; ENSP00000457891; ENSG00000260789. [Q86YR5-2]
ENST00000563222; ENSP00000456621; ENSG00000260789. [Q86YR5-2]
ENST00000563430; ENSP00000454556; ENSG00000260789. [Q86YR5-4]
GeneID26086.
KEGGhsa:26086.
UCSCuc004chc.3. human. [Q86YR5-3]
uc004chd.2. human. [Q86YR5-1]
uc004che.2. human. [Q86YR5-2]

Organism-specific databases

CTD26086.
GeneCardsGC09P139221.
HGNCHGNC:17858. GPSM1.
HPAHPA042199.
MIM609491. gene.
neXtProtNX_Q86YR5.
PharmGKBPA134986171.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0457.
HOGENOMHOG000231543.
HOVERGENHBG051823.
InParanoidQ86YR5.
KOK15839.
OMALEREQNG.
OrthoDBEOG7WHH8W.
PhylomeDBQ86YR5.
TreeFamTF328344.

Gene expression databases

BgeeQ86YR5.
CleanExHS_GPSM1.
GenevestigatorQ86YR5.

Family and domain databases

Gene3D1.25.40.10. 2 hits.
InterProIPR024804. G_prot_signal_mod_1.
IPR003109. GoLoco_motif.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERPTHR10098:SF36. PTHR10098:SF36. 1 hit.
PfamPF02188. GoLoco. 4 hits.
PF00515. TPR_1. 1 hit.
PF13176. TPR_7. 1 hit.
[Graphical view]
SMARTSM00390. GoLoco. 4 hits.
SM00028. TPR. 6 hits.
[Graphical view]
PROSITEPS50877. GOLOCO. 4 hits.
PS50005. TPR. 6 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGPSM1. human.
GeneWikiGPSM1.
GenomeRNAi26086.
NextBio48007.
PROQ86YR5.
SOURCESearch...

Entry information

Entry nameGPSM1_HUMAN
AccessionPrimary (citable) accession number: Q86YR5
Secondary accession number(s): A9Z1X4 expand/collapse secondary AC list , B1B0W3, Q86SR5, Q969T1, Q9UFS8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: April 20, 2010
Last modified: April 16, 2014
This is version 96 of the entry and version 2 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

MIM cross-references

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

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM