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Protein

G-protein-signaling modulator 1

Gene

GPSM1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  1. GDP-dissociation inhibitor activity Source: InterPro

GO - Biological processi

  1. cell differentiation Source: UniProtKB-KW
  2. nervous system development Source: UniProtKB-KW
  3. regulation of G-protein coupled receptor protein signaling pathway Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Neurogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
G-protein-signaling modulator 1
Alternative name(s):
Activator of G-protein signaling 3
Gene namesi
Name:GPSM1
Synonyms:AGS3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:17858. GPSM1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB-SubCell
  2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  3. Golgi apparatus Source: HPA
  4. Golgi membrane Source: UniProtKB-SubCell
  5. nucleoplasm Source: HPA
  6. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134986171.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 675675G-protein-signaling modulator 1PRO_0000252402Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei413 – 4131Phosphoserine1 Publication
Modified residuei471 – 4711Phosphoserine1 Publication
Modified residuei492 – 4921Phosphoserine1 Publication
Modified residuei493 – 4931Phosphoserine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ86YR5.
PaxDbiQ86YR5.
PRIDEiQ86YR5.

PTM databases

PhosphoSiteiQ86YR5.

Expressioni

Tissue specificityi

Expressed in intestinal cells.1 Publication

Gene expression databases

BgeeiQ86YR5.
CleanExiHS_GPSM1.
GenevestigatoriQ86YR5.

Organism-specific databases

HPAiHPA042199.

Interactioni

Subunit structurei

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.By similarity2 Publications

Protein-protein interaction databases

BioGridi117539. 23 interactions.
IntActiQ86YR5. 5 interactions.
MINTiMINT-1453185.
STRINGi9606.ENSP00000392828.

Structurei

3D structure databases

ProteinModelPortaliQ86YR5.
SMRiQ86YR5. Positions 26-567, 595-650.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati28 – 6134TPR 1Add
BLAST
Repeati66 – 9934TPR 2Add
BLAST
Repeati106 – 13934TPR 3Add
BLAST
Repeati146 – 18136TPR 4Add
BLAST
Repeati183 – 20220TPR 5Add
BLAST
Repeati209 – 24234TPR 6Add
BLAST
Repeati249 – 28234TPR 7Add
BLAST
Repeati289 – 32234TPR 8Add
BLAST
Repeati329 – 36234TPR 9Add
BLAST
Domaini495 – 51723GoLoco 1PROSITE-ProRule annotationAdd
BLAST
Domaini548 – 57023GoLoco 2PROSITE-ProRule annotationAdd
BLAST
Domaini596 – 61823GoLoco 3PROSITE-ProRule annotationAdd
BLAST
Domaini630 – 65223GoLoco 4PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 509509Mediates association with membranesBy similarityAdd
BLAST
Regioni364 – 487124Interaction with STK11/LKB1By similarityAdd
BLAST

Domaini

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.By similarity

Sequence similaritiesi

Belongs to the GPSM family.Curated
Contains 4 GoLoco domains.PROSITE-ProRule annotation
Contains 9 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiCOG0457.
GeneTreeiENSGT00530000063126.
HOGENOMiHOG000231543.
HOVERGENiHBG051823.
InParanoidiQ86YR5.
KOiK15839.
OMAiLEREQNG.
OrthoDBiEOG7WHH8W.
PhylomeDBiQ86YR5.
TreeFamiTF328344.

Family and domain databases

Gene3Di1.25.40.10. 2 hits.
InterProiIPR024804. G_prot_signal_mod_1.
IPR003109. GoLoco_motif.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERiPTHR10098:SF36. PTHR10098:SF36. 1 hit.
PfamiPF02188. GoLoco. 4 hits.
PF00515. TPR_1. 1 hit.
PF13176. TPR_7. 1 hit.
[Graphical view]
SMARTiSM00390. GoLoco. 4 hits.
SM00028. TPR. 6 hits.
[Graphical view]
PROSITEiPS50877. GOLOCO. 4 hits.
PS50005. TPR. 6 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q86YR5-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAGPAPPVAD ELPGPAARRL YSRMEASCLE LALEGERLCK AGDFKTGVAF
60 70 80 90 100
FEAAVQVGTE DLKTLSAIYS QLGNAYFYLK EHGRALEYHK HDLLLARTIG
110 120 130 140 150
DRMGEAKASG NLGNTLKVLG RFDEAAVCCQ RHLSIAQEQG DKVGEARALY
160 170 180 190 200
NIGNVYHAKG KQLSWNAANA TQDPGHLPPD VRETLCKASE FYERNLSLVK
210 220 230 240 250
ELGDRAAQGR AYGNLGNTHY LLGNFTEATT FHKERLAIAK EFGDKAAERR
260 270 280 290 300
AYSNLGNAHV FLGRFDVAAE YYKKTLQLSR QLRDQAVEAQ ACYSLGNTYT
310 320 330 340 350
LLQDYERAAE YHLRHLLIAQ ELADRVGEGR ACWSLGNAYV SMGRPAQALT
360 370 380 390 400
FAKKHLQISQ EIGDRHGELT ARMNVAQLQL VLGRLTSPAA SEKPDLAGYE
410 420 430 440 450
AQGARPKRTQ RLSAETWDLL RLPLEREQNG DSHHSGDWRG PSRDSLPLPV
460 470 480 490 500
RSRKYQEGPD AERRPREGSH SPLDSADVRV HVPRTSIPRA PSSDEECFFD
510 520 530 540 550
LLTKFQSSRM DDQRCPLDDG QAGAAEATAA PTLEDRIAQP SMTASPQTEE
560 570 580 590 600
FFDLIASSQS RRLDDQRASV GSLPGLRITH SNAGHLRGHG EPQEPGDDFF
610 620 630 640 650
NMLIKYQSSR IDDQRCPPPD VLPRGPTMPD EDFFSLIQRV QAKRMDEQRV
660 670
DLAGGPEQGA GGPPEPQQQC QPGAS
Length:675
Mass (Da):74,510
Last modified:April 19, 2010 - v2
Checksum:i27EB86667EEC1951
GO
Isoform 2 (identifier: Q86YR5-2) [UniParc]FASTAAdd to basket

Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     1-509: Missing.

Note: Minor isoform.

Show »
Length:166
Mass (Da):18,024
Checksum:iB0009DE5201BD2BD
GO
Isoform 3 (identifier: Q86YR5-3) [UniParc]FASTAAdd to basket

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.

Show »
Length:457
Mass (Da):49,685
Checksum:i4493B11B5D9986DC
GO
Isoform 4 (identifier: Q86YR5-4) [UniParc]FASTAAdd to basket

Also known as: FL

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

Note: Major isoform.

Show »
Length:652
Mass (Da):72,136
Checksum:iFF690E5EC1999611
GO

Sequence cautioni

The sequence AAH09979.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH17353.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAB55951.1 differs from that shown. Reason: Frameshift at position 657. Curated
The sequence CAI19339.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 509509Missing in isoform 2. 1 PublicationVSP_020937Add
BLAST
Alternative sequencei1 – 2323Missing in isoform 4. 1 PublicationVSP_039028Add
BLAST
Alternative sequencei404 – 45754ARPKR…RKYQE → EFQGCGGVLLPTGTDRIRSC GGVGSRPGQHGGGGSRQKMA PTSQFFLASGTAQA in isoform 3. 1 PublicationVSP_020938Add
BLAST
Alternative sequencei458 – 675218Missing in isoform 3. 1 PublicationVSP_020939Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS48055.1. [Q86YR5-1]
CCDS48056.1. [Q86YR5-2]
CCDS6996.2. [Q86YR5-3]
PIRiT17261.
RefSeqiNP_001139110.2. NM_001145638.2.
NP_001139111.1. NM_001145639.1. [Q86YR5-2]
NP_001186932.1. NM_001200003.1. [Q86YR5-2]
NP_056412.5. NM_015597.5.
UniGeneiHs.239370.

Genome annotation databases

EnsembliENST00000291775; ENSP00000291775; ENSG00000160360. [Q86YR5-2]
ENST00000392944; ENSP00000376673; ENSG00000160360. [Q86YR5-2]
ENST00000429455; ENSP00000390705; ENSG00000160360. [Q86YR5-2]
GeneIDi26086.
KEGGihsa:26086.
UCSCiuc004chc.3. human. [Q86YR5-3]
uc004chd.2. human. [Q86YR5-1]
uc004che.2. human. [Q86YR5-2]

Polymorphism databases

DMDMi294862435.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS48055.1. [Q86YR5-1]
CCDS48056.1. [Q86YR5-2]
CCDS6996.2. [Q86YR5-3]
PIRiT17261.
RefSeqiNP_001139110.2. NM_001145638.2.
NP_001139111.1. NM_001145639.1. [Q86YR5-2]
NP_001186932.1. NM_001200003.1. [Q86YR5-2]
NP_056412.5. NM_015597.5.
UniGeneiHs.239370.

3D structure databases

ProteinModelPortaliQ86YR5.
SMRiQ86YR5. Positions 26-567, 595-650.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117539. 23 interactions.
IntActiQ86YR5. 5 interactions.
MINTiMINT-1453185.
STRINGi9606.ENSP00000392828.

PTM databases

PhosphoSiteiQ86YR5.

Polymorphism databases

DMDMi294862435.

Proteomic databases

MaxQBiQ86YR5.
PaxDbiQ86YR5.
PRIDEiQ86YR5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000291775; ENSP00000291775; ENSG00000160360. [Q86YR5-2]
ENST00000392944; ENSP00000376673; ENSG00000160360. [Q86YR5-2]
ENST00000429455; ENSP00000390705; ENSG00000160360. [Q86YR5-2]
GeneIDi26086.
KEGGihsa:26086.
UCSCiuc004chc.3. human. [Q86YR5-3]
uc004chd.2. human. [Q86YR5-1]
uc004che.2. human. [Q86YR5-2]

Organism-specific databases

CTDi26086.
GeneCardsiGC09P139221.
HGNCiHGNC:17858. GPSM1.
HPAiHPA042199.
MIMi609491. gene.
neXtProtiNX_Q86YR5.
PharmGKBiPA134986171.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0457.
GeneTreeiENSGT00530000063126.
HOGENOMiHOG000231543.
HOVERGENiHBG051823.
InParanoidiQ86YR5.
KOiK15839.
OMAiLEREQNG.
OrthoDBiEOG7WHH8W.
PhylomeDBiQ86YR5.
TreeFamiTF328344.

Miscellaneous databases

ChiTaRSiGPSM1. human.
GeneWikiiGPSM1.
GenomeRNAii26086.
NextBioi48007.
PROiQ86YR5.
SOURCEiSearch...

Gene expression databases

BgeeiQ86YR5.
CleanExiHS_GPSM1.
GenevestigatoriQ86YR5.

Family and domain databases

Gene3Di1.25.40.10. 2 hits.
InterProiIPR024804. G_prot_signal_mod_1.
IPR003109. GoLoco_motif.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERiPTHR10098:SF36. PTHR10098:SF36. 1 hit.
PfamiPF02188. GoLoco. 4 hits.
PF00515. TPR_1. 1 hit.
PF13176. TPR_7. 1 hit.
[Graphical view]
SMARTiSM00390. GoLoco. 4 hits.
SM00028. TPR. 6 hits.
[Graphical view]
PROSITEiPS50877. GOLOCO. 4 hits.
PS50005. TPR. 6 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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 (OCT-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.
    , 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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. 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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Tissue: Fetal brain and Rhabdomyosarcoma.
  5. 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(1999) [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(2002) [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(2005) [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(2007) [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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  11. 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(2008) [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(2008) [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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGPSM1_HUMAN
AccessioniPrimary (citable) accession number: Q86YR5
Secondary accession number(s): A9Z1X4
, B1B0W3, Q86SR5, Q969T1, Q9UFS8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 16, 2006
Last sequence update: April 19, 2010
Last modified: February 3, 2015
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.