GPSM1_HUMAN - dbPTM
GPSM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GPSM1_HUMAN
UniProt AC Q86YR5
Protein Name G-protein-signaling modulator 1
Gene Name GPSM1
Organism Homo sapiens (Human).
Sequence Length 675
Subcellular Localization Cytoplasm, cytosol. Endoplasmic reticulum membrane
Peripheral membrane protein
Cytoplasmic side. Golgi apparatus membrane
Peripheral membrane protein
Cytoplasmic side. Cell membrane
Peripheral membrane protein
Cytoplasmic side.
Protein Description 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..
Protein Sequence MAGPAPPVADELPGPAARRLYSRMEASCLELALEGERLCKAGDFKTGVAFFEAAVQVGTEDLKTLSAIYSQLGNAYFYLKEHGRALEYHKHDLLLARTIGDRMGEAKASGNLGNTLKVLGRFDEAAVCCQRHLSIAQEQGDKVGEARALYNIGNVYHAKGKQLSWNAANATQDPGHLPPDVRETLCKASEFYERNLSLVKELGDRAAQGRAYGNLGNTHYLLGNFTEATTFHKERLAIAKEFGDKAAERRAYSNLGNAHVFLGRFDVAAEYYKKTLQLSRQLRDQAVEAQACYSLGNTYTLLQDYERAAEYHLRHLLIAQELADRVGEGRACWSLGNAYVSMGRPAQALTFAKKHLQISQEIGDRHGELTARMNVAQLQLVLGRLTSPAASEKPDLAGYEAQGARPKRTQRLSAETWDLLRLPLEREQNGDSHHSGDWRGPSRDSLPLPVRSRKYQEGPDAERRPREGSHSPLDSADVRVHVPRTSIPRAPSSDEECFFDLLTKFQSSRMDDQRCPLDDGQAGAAEATAAPTLEDRIAQPSMTASPQTEEFFDLIASSQSRRLDDQRASVGSLPGLRITHSNAGHLRGHGEPQEPGDDFFNMLIKYQSSRIDDQRCPPPDVLPRGPTMPDEDFFSLIQRVQAKRMDEQRVDLAGGPEQGAGGPPEPQQQCQPGAS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
22PhosphorylationPAARRLYSRMEASCL
HHHHHHHHHHHHHHH		29.7324719451
40UbiquitinationLEGERLCKAGDFKTG
HCCHHHHHCCCCHHH		61.06-
45UbiquitinationLCKAGDFKTGVAFFE
HHHCCCCHHHHHHHH		49.46-
88PhosphorylationEHGRALEYHKHDLLL
HCCCCHHHHHHHHHH		19.6129496907
90UbiquitinationGRALEYHKHDLLLAR
CCCHHHHHHHHHHEE		37.60-
107UbiquitinationGDRMGEAKASGNLGN
HHHHHCHHHCCCCCH		38.4921906983
107 (in isoform 3)Ubiquitination-38.4921890473
107 (in isoform 1)Ubiquitination-38.4921890473
117UbiquitinationGNLGNTLKVLGRFDE
CCCCHHHHHCCCCHH		33.1221890473
117MalonylationGNLGNTLKVLGRFDE
CCCCHHHHHCCCCHH		33.1226320211
134PhosphorylationVCCQRHLSIAQEQGD
HHHHHHHHHHHHHHC		15.1128857561
142 (in isoform 3)Ubiquitination-59.9921890473
142UbiquitinationIAQEQGDKVGEARAL
HHHHHHCHHHHHHHH		59.9921906983
142 (in isoform 1)Ubiquitination-59.9921890473
150PhosphorylationVGEARALYNIGNVYH
HHHHHHHEEECCEEE		12.0725884760
156PhosphorylationLYNIGNVYHAKGKQL
HEEECCEEECCCCEE		10.48-
161UbiquitinationNVYHAKGKQLSWNAA
CEEECCCCEEECCCC		47.57-
187UbiquitinationDVRETLCKASEFYER
HHHHHHHHHHHHHHH		59.05-
192PhosphorylationLCKASEFYERNLSLV
HHHHHHHHHHHHHHH		15.2129496907
197PhosphorylationEFYERNLSLVKELGD
HHHHHHHHHHHHHHH		34.3724719451
200UbiquitinationERNLSLVKELGDRAA
HHHHHHHHHHHHHHH		53.14-
212PhosphorylationRAAQGRAYGNLGNTH
HHHHCHHCCCCCCCC		12.7526425664
218PhosphorylationAYGNLGNTHYLLGNF
HCCCCCCCCEEECCC		15.3129496907
230PhosphorylationGNFTEATTFHKERLA
CCCCCCCHHHHHHHH		30.6926425664
233UbiquitinationTEATTFHKERLAIAK
CCCCHHHHHHHHHHH		40.10-
240UbiquitinationKERLAIAKEFGDKAA
HHHHHHHHHHCHHHH		47.68-
245UbiquitinationIAKEFGDKAAERRAY
HHHHHCHHHHHHHHH		50.29-
252PhosphorylationKAAERRAYSNLGNAH
HHHHHHHHCCCCCCH		9.0429496907
271PhosphorylationRFDVAAEYYKKTLQL
CHHHHHHHHHHHHHH		18.8318083107
272PhosphorylationFDVAAEYYKKTLQLS
HHHHHHHHHHHHHHH		9.4918083107
274MalonylationVAAEYYKKTLQLSRQ
HHHHHHHHHHHHHHH		38.0426320211
274UbiquitinationVAAEYYKKTLQLSRQ
HHHHHHHHHHHHHHH		38.04-
311PhosphorylationDYERAAEYHLRHLLI
HHHHHHHHHHHHHHH		11.0421552520
325MethylationIAQELADRVGEGRAC
HHHHHHHHHCCCHHH		32.50-
354UbiquitinationQALTFAKKHLQISQE
HHHHHHHHHHHHHHH		46.23-
386PhosphorylationQLVLGRLTSPAASEK
HHHHHHCCCCHHHCC		31.1625850435
387PhosphorylationLVLGRLTSPAASEKP
HHHHHCCCCHHHCCC		19.6823401153
391PhosphorylationRLTSPAASEKPDLAG
HCCCCHHHCCCCCCC		48.5423186163
393 (in isoform 1)Ubiquitination-41.1421890473
393UbiquitinationTSPAASEKPDLAGYE
CCCHHHCCCCCCCHH		41.142190698
399PhosphorylationEKPDLAGYEAQGARP
CCCCCCCHHCCCCCC		11.5027642862
409PhosphorylationQGARPKRTQRLSAET
CCCCCCCCHHCCHHH		24.9423312004
413PhosphorylationPKRTQRLSAETWDLL
CCCCHHCCHHHHHHH		26.6722617229
416PhosphorylationTQRLSAETWDLLRLP
CHHCCHHHHHHHHCC		24.8029083192
421MethylationAETWDLLRLPLEREQ
HHHHHHHHCCCCHHH		41.37-
442PhosphorylationSGDWRGPSRDSLPLP
CCCCCCCCCCCCCCC		52.0925159151
445PhosphorylationWRGPSRDSLPLPVRS
CCCCCCCCCCCCCCC		30.6725159151
448PhosphorylationPSRDSLPLPVRSRKY
CCCCCCCCCCCCCCC		8.1018669648
462PhosphorylationYQEGPDAERRPREGS
CCCCCCCCCCCCCCC		57.5118669648
469PhosphorylationERRPREGSHSPLDSA
CCCCCCCCCCCCCCC		18.9529255136
470PhosphorylationRRPREGSHSPLDSAD
CCCCCCCCCCCCCCC		44.2718669648
471PhosphorylationRPREGSHSPLDSADV
CCCCCCCCCCCCCCC		28.9323401153
475PhosphorylationGSHSPLDSADVRVHV
CCCCCCCCCCCEEEC		33.7723403867
479MethylationPLDSADVRVHVPRTS
CCCCCCCEEECCCCC		17.24-
485PhosphorylationVRVHVPRTSIPRAPS
CEEECCCCCCCCCCC		25.5728464451
486PhosphorylationRVHVPRTSIPRAPSS
EEECCCCCCCCCCCC		31.6922199227
492PhosphorylationTSIPRAPSSDEECFF
CCCCCCCCCCHHHHH		49.8125159151
493PhosphorylationSIPRAPSSDEECFFD
CCCCCCCCCHHHHHH		48.2430278072
497GlutathionylationAPSSDEECFFDLLTK
CCCCCHHHHHHHHHH		3.7622555962
503PhosphorylationECFFDLLTKFQSSRM
HHHHHHHHHHHHCCC		36.7927251275
504UbiquitinationCFFDLLTKFQSSRMD
HHHHHHHHHHHCCCC		41.18-
520PhosphorylationQRCPLDDGQAGAAEA
CCCCCCCCCCCCHHH		20.9218669648
541PhosphorylationEDRIAQPSMTASPQT
HHHCCCCCCCCCCCH		19.3829255136
543PhosphorylationRIAQPSMTASPQTEE
HCCCCCCCCCCCHHH		28.4629255136
545PhosphorylationAQPSMTASPQTEEFF
CCCCCCCCCCHHHHH		14.3629255136
548PhosphorylationSMTASPQTEEFFDLI
CCCCCCCHHHHHHHH		40.6528464451
557PhosphorylationEFFDLIASSQSRRLD
HHHHHHHHHCCCCHH		23.1627732954
569PhosphorylationRLDDQRASVGSLPGL
CHHHCCCCCCCCCCE		29.2423403867
572PhosphorylationDQRASVGSLPGLRIT
HCCCCCCCCCCEEEE		29.2720873877
581PhosphorylationPGLRITHSNAGHLRG
CCEEEECCCCCCCCC		21.5227732954
628SulfoxidationVLPRGPTMPDEDFFS
CCCCCCCCCCHHHHH		4.4230846556
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of GPSM1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GPSM1_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of GPSM1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CD158_HUMANCCDC158physical
16189514
USBP1_HUMANUSHBP1physical
16189514
USP9X_HUMANUSP9Xphysical
20305814
PP6R3_HUMANPPP6R3physical
23718855
RBP1_HUMANRALBP1physical
23718855
GPSM1_HUMANGPSM1physical
25416956
GNAI3_HUMANGNAI3physical
21209316
MLP3A_HUMANMAP1LC3Aphysical
21209316
NUMA1_HUMANNUMA1physical
26186194
UGPA_HUMANUGP2physical
26186194
BRD4_HUMANBRD4physical
26186194
PP6R3_HUMANPPP6R3physical
26186194
SAPC2_HUMANSAPCD2physical
26186194
KLH18_HUMANKLHL18physical
26186194
UGPA_HUMANUGP2physical
28514442
BRD4_HUMANBRD4physical
28514442
SAPC2_HUMANSAPCD2physical
28514442
NUMA1_HUMANNUMA1physical
28514442
KLH18_HUMANKLHL18physical
28514442
DACH1_HUMANDACH1physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GPSM1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492, AND MASSSPECTROMETRY.
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-471; SER-492 ANDSER-493, AND MASS SPECTROMETRY.

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