GPN1_HUMAN - dbPTM
GPN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GPN1_HUMAN
UniProt AC Q9HCN4
Protein Name GPN-loop GTPase 1 {ECO:0000303|PubMed:20855544}
Gene Name GPN1 {ECO:0000303|PubMed:20855544, ECO:0000312|HGNC:HGNC:17030}
Organism Homo sapiens (Human).
Sequence Length 374
Subcellular Localization Cytoplasm . Nucleus . Shuttles between the nucleus and the cytoplasm.
Protein Description Small GTPase required for proper nuclear import of RNA polymerase II (RNAPII). [PubMed: 20855544]
Protein Sequence MAASAAAAELQASGGPRHPVCLLVLGMAGSGKTTFVQRLTGHLHAQGTPPYVINLDPAVHEVPFPANIDIRDTVKYKEVMKQYGLGPNGGIVTSLNLFATRFDQVMKFIEKAQNMSKYVLIDTPGQIEVFTWSASGTIITEALASSFPTVVIYVMDTSRSTNPVTFMSNMLYACSILYKTKLPFIVVMNKTDIIDHSFAVEWMQDFEAFQDALNQETTYVSNLTRSMSLVLDEFYSSLRVVGVSAVLGTGLDELFVQVTSAAEEYEREYRPEYERLKKSLANAESQQQREQLERLRKDMGSVALDAGTAKDSLSPVLHPSDLILTRGTLDEEDEEADSDTDDIDHRVTEESHEEPAFQNFMQESMAQYWKRNNK
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
2Acetylation------MAASAAAAE
------CCHHHHHHH		15.3222223895
4Phosphorylation----MAASAAAAELQ
----CCHHHHHHHHH		14.6518491316
13 (in isoform 4)Phosphorylation-31.18-
13PhosphorylationAAAELQASGGPRHPV
HHHHHHHCCCCCCCE		31.1821406692
18 (in isoform 5)Phosphorylation-23.4418491316
18PhosphorylationQASGGPRHPVCLLVL
HHCCCCCCCEEEEEE		23.4418491316
27PhosphorylationVCLLVLGMAGSGKTT
EEEEEEECCCCCHHH		3.14-
40PhosphorylationTTFVQRLTGHLHAQG
HHHHHHHHCCCCCCC		25.41-
111AcetylationQVMKFIEKAQNMSKY
HHHHHHHHHHCCCCE		50.9225953088
125UbiquitinationYVLIDTPGQIEVFTW
EEEECCCCEEEEEEE		43.10-
125UbiquitinationYVLIDTPGQIEVFTW
EEEECCCCEEEEEEE		43.10-
160PhosphorylationYVMDTSRSTNPVTFM
EEEECCCCCCCCCHH		32.1025072903
161PhosphorylationVMDTSRSTNPVTFMS
EEECCCCCCCCCHHH		42.2925072903
165PhosphorylationSRSTNPVTFMSNMLY
CCCCCCCCHHHHHHH		18.1925072903
168PhosphorylationTNPVTFMSNMLYACS
CCCCCHHHHHHHHHH		18.2025072903
172PhosphorylationTFMSNMLYACSILYK
CHHHHHHHHHHHHHH		8.5225072903
175PhosphorylationSNMLYACSILYKTKL
HHHHHHHHHHHHCCC		13.8825072903
178PhosphorylationLYACSILYKTKLPFI
HHHHHHHHHCCCCEE		18.2325072903
202UbiquitinationDHSFAVEWMQDFEAF
CCCHHHHHHHHHHHH		5.3221890473
218UbiquitinationDALNQETTYVSNLTR
HHHCCCHHHHHHHHH		22.6021890473
277UbiquitinationRPEYERLKKSLANAE
CHHHHHHHHHHHCHH		46.68-
278UbiquitinationPEYERLKKSLANAES
HHHHHHHHHHHCHHH		56.1221890473
285UbiquitinationKSLANAESQQQREQL
HHHHCHHHHHHHHHH		30.7721890473
291UbiquitinationESQQQREQLERLRKD
HHHHHHHHHHHHHHH		51.30-
292UbiquitinationSQQQREQLERLRKDM
HHHHHHHHHHHHHHH		3.3721890473
292UbiquitinationSQQQREQLERLRKDM
HHHHHHHHHHHHHHH		3.37-
297UbiquitinationEQLERLRKDMGSVAL
HHHHHHHHHHCCHHH		57.5721890473
299SulfoxidationLERLRKDMGSVALDA
HHHHHHHHCCHHHCC		4.9021406390
301PhosphorylationRLRKDMGSVALDAGT
HHHHHHCCHHHCCCC		9.5128464451
302PhosphorylationLRKDMGSVALDAGTA
HHHHHCCHHHCCCCC		5.2024719451
308PhosphorylationSVALDAGTAKDSLSP
CHHHCCCCCCCCCCC		32.0526055452
310UbiquitinationALDAGTAKDSLSPVL
HHCCCCCCCCCCCCC		47.92-
311UbiquitinationLDAGTAKDSLSPVLH
HCCCCCCCCCCCCCC		52.96-
312PhosphorylationDAGTAKDSLSPVLHP
CCCCCCCCCCCCCCH		30.0025159151
314PhosphorylationGTAKDSLSPVLHPSD
CCCCCCCCCCCCHHH		19.5329255136
315PhosphorylationTAKDSLSPVLHPSDL
CCCCCCCCCCCHHHE		37.67-
320PhosphorylationLSPVLHPSDLILTRG
CCCCCCHHHEEEEEC		34.0123927012
322PhosphorylationPVLHPSDLILTRGTL
CCCCHHHEEEEECCC		3.9720068231
324UbiquitinationLHPSDLILTRGTLDE
CCHHHEEEEECCCCH		3.29-
324UbiquitinationLHPSDLILTRGTLDE
CCHHHEEEEECCCCH		3.29-
325PhosphorylationHPSDLILTRGTLDEE
CHHHEEEEECCCCHH		21.7623927012
326PhosphorylationPSDLILTRGTLDEED
HHHEEEEECCCCHHC		32.4318691976
328PhosphorylationDLILTRGTLDEEDEE
HEEEEECCCCHHCHH		27.9622167270
334PhosphorylationGTLDEEDEEADSDTD
CCCCHHCHHCCCCCC		59.3620068231
338PhosphorylationEEDEEADSDTDDIDH
HHCHHCCCCCCCCCH		49.8322167270
339PhosphorylationEDEEADSDTDDIDHR
HCHHCCCCCCCCCHH		55.4920068231
340PhosphorylationDEEADSDTDDIDHRV
CHHCCCCCCCCCHHH		39.2522167270
342PhosphorylationEADSDTDDIDHRVTE
HCCCCCCCCCHHHCH		50.7520166139
348PhosphorylationDDIDHRVTEESHEEP
CCCCHHHCHHCCCCH		33.7128348404
351PhosphorylationDHRVTEESHEEPAFQ
CHHHCHHCCCCHHHH		29.9328464451
352PhosphorylationHRVTEESHEEPAFQN
HHHCHHCCCCHHHHH		46.8720166139
354PhosphorylationVTEESHEEPAFQNFM
HCHHCCCCHHHHHHH		36.1817081983
364PhosphorylationFQNFMQESMAQYWKR
HHHHHHHHHHHHHHH		11.5228348404
368PhosphorylationMQESMAQYWKRNNK-
HHHHHHHHHHHHCC-		11.8928796482
370MethylationESMAQYWKRNNK---
HHHHHHHHHHCC---		40.07-
384Methylation-----------------
-----------------		-
384Ubiquitination-----------------
-----------------		-
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 GPN1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GPN1_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 GPN1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RPAP2_HUMANRPAP2physical
17643375
TCPE_HUMANCCT5physical
17643375
RPAP3_HUMANRPAP3physical
17643375
HNRH1_HUMANHNRNPH1physical
17643375
PIHD1_HUMANPIH1D1physical
17643375
RPB2_HUMANPOLR2Bphysical
17643375
RPC1_HUMANPOLR3Aphysical
17643375
RPAP1_HUMANRPAP1physical
17643375
TCPD_HUMANCCT4physical
17643375
HNRPU_HUMANHNRNPUphysical
17643375
TCPA_HUMANTCP1physical
17643375
RPB1_HUMANPOLR2Aphysical
17643375
RMP_HUMANURI1physical
17643375
RPC5_HUMANPOLR3Ephysical
17643375
RPC2_HUMANPOLR3Bphysical
17643375
IMA1_HUMANKPNA2physical
17643375
RUVB1_HUMANRUVBL1physical
17643375
U5S1_HUMANEFTUD2physical
17643375
TCPQ_HUMANCCT8physical
17643375
HSP7C_HUMANHSPA8physical
17643375
TCPZ_HUMANCCT6Aphysical
17643375
HS90B_HUMANHSP90AB1physical
17643375
GPN3_HUMANGPN3physical
17643375
PUF60_HUMANPUF60physical
17643375
HNRH2_HUMANHNRNPH2physical
17643375
TCOF_HUMANTCOF1physical
17643375
MED17_HUMANMED17physical
17643375
HNRPD_HUMANHNRNPDphysical
17643375
ARMX3_HUMANARMCX3physical
17643375
GRP75_HUMANHSPA9physical
17643375
DDB1_HUMANDDB1physical
17643375
HPBP1_HUMANHSPBP1physical
22863883
OGT1_HUMANOGTphysical
22863883
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 GPN1_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-338, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, 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-338, 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-312; SER-314 ANDSER-338, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312 AND THR-340, ANDMASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312 AND SER-314, ANDMASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, AND MASSSPECTROMETRY.

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