GNL3_HUMAN - dbPTM
GNL3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GNL3_HUMAN
UniProt AC Q9BVP2
Protein Name Guanine nucleotide-binding protein-like 3
Gene Name GNL3
Organism Homo sapiens (Human).
Sequence Length 549
Subcellular Localization Nucleus . Nucleus, nucleolus . Shuttles between the nucleus and nucleolus.
Protein Description May be required to maintain the proliferative capacity of stem cells. Stabilizes MDM2 by preventing its ubiquitination, and hence proteasomal degradation (By similarity)..
Protein Sequence MKRPKLKKASKRMTCHKRYKIQKKVREHHRKLRKEAKKRGHKKPRKDPGVPNSAPFKEALLREAELRKQRLEELKQQQKLDRQKELEKKRKLETNPDIKPSNVEPMEKEFGLCKTENKAKSGKQNSKKLYCQELKKVIEASDVVLEVLDARDPLGCRCPQVEEAIVQSGQKKLVLILNKSDLVPKENLESWLNYLKKELPTVVFRASTKPKDKGKITKRVKAKKNAAPFRSEVCFGKEGLWKLLGGFQETCSKAIRVGVIGFPNVGKSSIINSLKQEQMCNVGVSMGLTRSMQVVPLDKQITIIDSPSFIVSPLNSSSALALRSPASIEVVKPMEAASAILSQADARQVVLKYTVPGYRNSLEFFTVLAQRRGMHQKGGIPNVEGAAKLLWSEWTGASLAYYCHPPTSWTPPPYFNESIVVDMKSGFNLEELEKNNAQSIRAIKGPHLANSILFQSSGLTNGIIEEKDIHEELPKRKERKQEEREDDKDSDQETVDEEVDENSSGMFAAEETGEALSEETTAGEQSTRSFILDKIIEEDDAYDFSTDYV
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
5Acetylation---MKRPKLKKASKR
---CCCHHHHHHHHH		76.5819810321
12UbiquitinationKLKKASKRMTCHKRY
HHHHHHHHCCHHHHH		24.1324816145
17AcetylationSKRMTCHKRYKIQKK
HHHCCHHHHHHHHHH		60.6230588993
24UbiquitinationKRYKIQKKVREHHRK
HHHHHHHHHHHHHHH		30.1024816145
34UbiquitinationEHHRKLRKEAKKRGH
HHHHHHHHHHHHCCC		72.9033845483
45UbiquitinationKRGHKKPRKDPGVPN
HCCCCCCCCCCCCCC		65.9623000965
46AcetylationRGHKKPRKDPGVPNS
CCCCCCCCCCCCCCC		76.4526051181
46UbiquitinationRGHKKPRKDPGVPNS
CCCCCCCCCCCCCCC		76.4533845483
53PhosphorylationKDPGVPNSAPFKEAL
CCCCCCCCHHHHHHH		31.1121815630
57AcetylationVPNSAPFKEALLREA
CCCCHHHHHHHHHHH		40.8125953088
57UbiquitinationVPNSAPFKEALLREA
CCCCHHHHHHHHHHH		40.8123000965
63UbiquitinationFKEALLREAELRKQR
HHHHHHHHHHHHHHH		46.6033845483
67AcetylationLLREAELRKQRLEEL
HHHHHHHHHHHHHHH		25.2719608861
75UbiquitinationKQRLEELKQQQKLDR
HHHHHHHHHHHHHHH		49.7133845483
77UbiquitinationRLEELKQQQKLDRQK
HHHHHHHHHHHHHHH		40.5724816145
79AcetylationEELKQQQKLDRQKEL
HHHHHHHHHHHHHHH		48.2819608861
87UbiquitinationLDRQKELEKKRKLET
HHHHHHHHHHHHHCC		58.5933845483
89UbiquitinationRQKELEKKRKLETNP
HHHHHHHHHHHCCCC		45.4424816145
91SumoylationKELEKKRKLETNPDI
HHHHHHHHHCCCCCC		60.6028112733
94PhosphorylationEKKRKLETNPDIKPS
HHHHHHCCCCCCCCC		63.5928555341
99SumoylationLETNPDIKPSNVEPM
HCCCCCCCCCCCCCC		50.18-
99AcetylationLETNPDIKPSNVEPM
HCCCCCCCCCCCCCC		50.1826051181
99SumoylationLETNPDIKPSNVEPM
HCCCCCCCCCCCCCC		50.1828112733
99UbiquitinationLETNPDIKPSNVEPM
HCCCCCCCCCCCCCC		50.1833845483
101PhosphorylationTNPDIKPSNVEPMEK
CCCCCCCCCCCCCHH		48.80-
102UbiquitinationNPDIKPSNVEPMEKE
CCCCCCCCCCCCHHH		51.1829967540
108AcetylationSNVEPMEKEFGLCKT
CCCCCCHHHHCCCCC		52.6826051181
114SumoylationEKEFGLCKTENKAKS
HHHHCCCCCCCCCCC		65.01-
114AcetylationEKEFGLCKTENKAKS
HHHHCCCCCCCCCCC		65.0125953088
114SumoylationEKEFGLCKTENKAKS
HHHHCCCCCCCCCCC		65.0128112733
114UbiquitinationEKEFGLCKTENKAKS
HHHHCCCCCCCCCCC		65.0129967540
123UbiquitinationENKAKSGKQNSKKLY
CCCCCCCCCCCCHHH		54.0929967540
124UbiquitinationNKAKSGKQNSKKLYC
CCCCCCCCCCCHHHH		64.0529967540
128AcetylationSGKQNSKKLYCQELK
CCCCCCCHHHHHHHH		44.5026051181
130PhosphorylationKQNSKKLYCQELKKV
CCCCCHHHHHHHHHH		10.8528152594
1352-HydroxyisobutyrylationKLYCQELKKVIEASD
HHHHHHHHHHHHHHH		44.21-
135AcetylationKLYCQELKKVIEASD
HHHHHHHHHHHHHHH		44.2125953088
135UbiquitinationKLYCQELKKVIEASD
HHHHHHHHHHHHHHH		44.2129967540
136UbiquitinationLYCQELKKVIEASDV
HHHHHHHHHHHHHHH		62.1629967540
141PhosphorylationLKKVIEASDVVLEVL
HHHHHHHHHHHHHHH		20.39-
159UbiquitinationDPLGCRCPQVEEAIV
CCCCCCCCHHHHHHH		23.1522505724
171UbiquitinationAIVQSGQKKLVLILN
HHHHCCCCEEEEEEC		52.1522505724
173UbiquitinationVQSGQKKLVLILNKS
HHCCCCEEEEEECHH		4.9629967540
179AcetylationKLVLILNKSDLVPKE
EEEEEECHHHCCCHH		41.7321339330
179SumoylationKLVLILNKSDLVPKE
EEEEEECHHHCCCHH		41.7328112733
179UbiquitinationKLVLILNKSDLVPKE
EEEEEECHHHCCCHH		41.73-
184UbiquitinationLNKSDLVPKENLESW
ECHHHCCCHHHHHHH		45.6129967540
184 (in isoform 2)Ubiquitination-45.6121906983
185UbiquitinationNKSDLVPKENLESWL
CHHHCCCHHHHHHHH		52.3229967540
194PhosphorylationNLESWLNYLKKELPT
HHHHHHHHHHHHCCE		20.0919702290
1962-HydroxyisobutyrylationESWLNYLKKELPTVV
HHHHHHHHHHCCEEE		33.56-
196AcetylationESWLNYLKKELPTVV
HHHHHHHHHHCCEEE		33.5626051181
196SumoylationESWLNYLKKELPTVV
HHHHHHHHHHCCEEE		33.5628112733
196UbiquitinationESWLNYLKKELPTVV
HHHHHHHHHHCCEEE		33.5621906983
196 (in isoform 1)Ubiquitination-33.5621906983
197UbiquitinationSWLNYLKKELPTVVF
HHHHHHHHHCCEEEE		62.9924816145
209UbiquitinationVVFRASTKPKDKGKI
EEEECCCCCCCCCCC		47.8024816145
212UbiquitinationRASTKPKDKGKITKR
ECCCCCCCCCCCCHH		73.7524816145
224MethylationTKRVKAKKNAAPFRS
CHHHHHCCCCCCCCC		57.59-
224UbiquitinationTKRVKAKKNAAPFRS
CHHHHHCCCCCCCCC		57.5924816145
225UbiquitinationKRVKAKKNAAPFRSE
HHHHHCCCCCCCCCC		40.4029967540
225 (in isoform 2)Ubiquitination-40.4021906983
230MethylationKKNAAPFRSEVCFGK
CCCCCCCCCCCCCCC		30.74-
2372-HydroxyisobutyrylationRSEVCFGKEGLWKLL
CCCCCCCCHHHHHHH		28.49-
237AcetylationRSEVCFGKEGLWKLL
CCCCCCCCHHHHHHH		28.4925825284
237UbiquitinationRSEVCFGKEGLWKLL
CCCCCCCCHHHHHHH		28.4921906983
237 (in isoform 1)Ubiquitination-28.4921906983
241UbiquitinationCFGKEGLWKLLGGFQ
CCCCHHHHHHHHHHH		10.5029967540
242AcetylationFGKEGLWKLLGGFQE
CCCHHHHHHHHHHHH		38.5926051181
242UbiquitinationFGKEGLWKLLGGFQE
CCCHHHHHHHHHHHH		38.59-
250PhosphorylationLLGGFQETCSKAIRV
HHHHHHHHHHHCCEE		15.9920068231
252PhosphorylationGGFQETCSKAIRVGV
HHHHHHHHHCCEEEC		32.3220068231
253AcetylationGFQETCSKAIRVGVI
HHHHHHHHCCEEECC		50.4025953088
253SumoylationGFQETCSKAIRVGVI
HHHHHHHHCCEEECC		50.4028112733
253UbiquitinationGFQETCSKAIRVGVI
HHHHHHHHCCEEECC		50.4029967540
255UbiquitinationQETCSKAIRVGVIGF
HHHHHHCCEEECCCC		4.1629967540
263UbiquitinationRVGVIGFPNVGKSSI
EEECCCCCCCCHHHH		29.4129967540
267SumoylationIGFPNVGKSSIINSL
CCCCCCCHHHHHHHH		36.4328112733
267UbiquitinationIGFPNVGKSSIINSL
CCCCCCCHHHHHHHH		36.4329967540
268PhosphorylationGFPNVGKSSIINSLK
CCCCCCHHHHHHHHC		22.3520068231
269PhosphorylationFPNVGKSSIINSLKQ
CCCCCHHHHHHHHCH		30.8520068231
273PhosphorylationGKSSIINSLKQEQMC
CHHHHHHHHCHHHCC		26.9120068231
275SumoylationSSIINSLKQEQMCNV
HHHHHHHCHHHCCCC		52.16-
275AcetylationSSIINSLKQEQMCNV
HHHHHHHCHHHCCCC		52.1626051181
275SumoylationSSIINSLKQEQMCNV
HHHHHHHCHHHCCCC		52.1628112733
275UbiquitinationSSIINSLKQEQMCNV
HHHHHHHCHHHCCCC		52.1629967540
289PhosphorylationVGVSMGLTRSMQVVP
CCCCCCCCCCEEEEE		18.24-
291PhosphorylationVSMGLTRSMQVVPLD
CCCCCCCCEEEEECC		14.3425159151
292SulfoxidationSMGLTRSMQVVPLDK
CCCCCCCEEEEECCC		2.9421406390
299UbiquitinationMQVVPLDKQITIIDS
EEEEECCCCEEEECC		51.81-
302PhosphorylationVPLDKQITIIDSPSF
EECCCCEEEECCCCE		14.9124043423
306PhosphorylationKQITIIDSPSFIVSP
CCEEEECCCCEEEEC		16.4324043423
308PhosphorylationITIIDSPSFIVSPLN
EEEECCCCEEEECCC		31.4024043423
312PhosphorylationDSPSFIVSPLNSSSA
CCCCEEEECCCCCCC		20.8924043423
316PhosphorylationFIVSPLNSSSALALR
EEEECCCCCCCHHHC		33.0924043423
317PhosphorylationIVSPLNSSSALALRS
EEECCCCCCCHHHCC		20.6824043423
318PhosphorylationVSPLNSSSALALRSP
EECCCCCCCHHHCCC		27.4223403867
320UbiquitinationPLNSSSALALRSPAS
CCCCCCCHHHCCCCC		5.0829967540
320 (in isoform 2)Ubiquitination-5.0821906983
324PhosphorylationSSALALRSPASIEVV
CCCHHHCCCCCEEEE		26.1825159151
332AcetylationPASIEVVKPMEAASA
CCCEEEECHHHHHHH		43.7726051181
332UbiquitinationPASIEVVKPMEAASA
CCCEEEECHHHHHHH		43.772190698
332 (in isoform 1)Ubiquitination-43.7721906983
338PhosphorylationVKPMEAASAILSQAD
ECHHHHHHHHHCHHH		23.9223607784
342PhosphorylationEAASAILSQADARQV
HHHHHHHCHHHHHHH		19.7420068231
352AcetylationDARQVVLKYTVPGYR
HHHHHHHEEECCCCH		27.5426051181
352UbiquitinationDARQVVLKYTVPGYR
HHHHHHHEEECCCCH		27.54-
361PhosphorylationTVPGYRNSLEFFTVL
ECCCCHHHHHHHHHH		21.9330108239
365UbiquitinationYRNSLEFFTVLAQRR
CHHHHHHHHHHHHHC		3.1827667366
366PhosphorylationRNSLEFFTVLAQRRG
HHHHHHHHHHHHHCC		21.67-
377AcetylationQRRGMHQKGGIPNVE
HHCCCHHCCCCCCHH		44.4125953088
377UbiquitinationQRRGMHQKGGIPNVE
HHCCCHHCCCCCCHH		44.4127667366
388SumoylationPNVEGAAKLLWSEWT
CCHHHHHHHHHHCCC		43.51-
422UbiquitinationFNESIVVDMKSGFNL
CCCCEEEECCCCCCH		28.0929967540
434AcetylationFNLEELEKNNAQSIR
CCHHHHHHCCHHHHH		69.0326051181
434UbiquitinationFNLEELEKNNAQSIR
CCHHHHHHCCHHHHH		69.0329967540
444SumoylationAQSIRAIKGPHLANS
HHHHHHHCCHHHHHH		66.46-
444SumoylationAQSIRAIKGPHLANS
HHHHHHHCCHHHHHH		66.46-
444UbiquitinationAQSIRAIKGPHLANS
HHHHHHHCCHHHHHH		66.46-
467AcetylationTNGIIEEKDIHEELP
CCCCCCHHHHHHHCC		49.5526051181
4752-HydroxyisobutyrylationDIHEELPKRKERKQE
HHHHHCCHHHHHHHH		84.47-
490PhosphorylationEREDDKDSDQETVDE
HHCCCCCCCCHHHHH		47.1124275569
494PhosphorylationDKDSDQETVDEEVDE
CCCCCCHHHHHHHHC		27.8522210691
503PhosphorylationDEEVDENSSGMFAAE
HHHHHCCCCCCCCHH		26.6526471730
504PhosphorylationEEVDENSSGMFAAEE
HHHHCCCCCCCCHHH		45.9526126808
512PhosphorylationGMFAAEETGEALSEE
CCCCHHHHHCCCCCC		31.6524275569
517PhosphorylationEETGEALSEETTAGE
HHHHCCCCCCCCCCC		40.2020068231
520PhosphorylationGEALSEETTAGEQST
HCCCCCCCCCCCHHH		20.2124144214
521PhosphorylationEALSEETTAGEQSTR
CCCCCCCCCCCHHHH		35.6324144214
526PhosphorylationETTAGEQSTRSFILD
CCCCCCHHHHHHHHH		22.8324144214
527PhosphorylationTTAGEQSTRSFILDK
CCCCCHHHHHHHHHH		29.9924144214
529PhosphorylationAGEQSTRSFILDKII
CCCHHHHHHHHHHHH		19.4125218447
534SumoylationTRSFILDKIIEEDDA
HHHHHHHHHHCCCCC		41.98-
542PhosphorylationIIEEDDAYDFSTDYV
HHCCCCCCCCCCCCC		25.2328796482
545PhosphorylationEDDAYDFSTDYV---
CCCCCCCCCCCC---		19.9228796482
546PhosphorylationDDAYDFSTDYV----
CCCCCCCCCCC----		31.2028796482
548PhosphorylationAYDFSTDYV------
CCCCCCCCC------		14.2428796482
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
-KUbiquitinationE3 ubiquitin ligaseMDM2Q00987
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GNL3_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 GNL3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
P53_HUMANTP53physical
12464630
MDM2_HUMANMDM2physical
18426907
MDM2_HUMANMDM2physical
21132010
TERF1_HUMANTERF1physical
19487455
MDM2_HUMANMDM2physical
19033382
P53_HUMANTP53physical
19033382
RL11_HUMANRPL11physical
22939629
RL6_HUMANRPL6physical
22939629
NOP56_HUMANNOP56physical
22939629
RS7_HUMANRPS7physical
22939629
RL18A_HUMANRPL18Aphysical
22939629
RL7_HUMANRPL7physical
22939629
RL15_HUMANRPL15physical
22939629
RL23_HUMANRPL23physical
22939629
RS15A_HUMANRPS15Aphysical
22939629
RL37A_HUMANRPL37Aphysical
22939629
RS6_HUMANRPS6physical
22939629
RL19_HUMANRPL19physical
22939629
RL4_HUMANRPL4physical
22939629
RS4X_HUMANRPS4Xphysical
22939629
RS5_HUMANRPS5physical
22939629
RS3_HUMANRPS3physical
22939629
RL5_HUMANRPL5physical
22939629
NH2L1_HUMANNHP2L1physical
22939629
RS8_HUMANRPS8physical
22939629
RS24_HUMANRPS24physical
22939629
NOP58_HUMANNOP58physical
22939629
RS14_HUMANRPS14physical
22939629
IF6_HUMANEIF6physical
22939629
IF4A3_HUMANEIF4A3physical
22939629
RNPS1_HUMANRNPS1physical
22939629
RRP7A_HUMANRRP7Aphysical
22939629
NOP2_HUMANNOP2physical
22939629
RRS1_HUMANRRS1physical
22939629
MK67I_HUMANNIFKphysical
22939629
SPB1_HUMANFTSJ3physical
22939629
STAT3_HUMANSTAT3physical
21988832
CDN2A_HUMANCDKN2Aphysical
24769896
ARF_HUMANCDKN2Aphysical
24769896
RL14_HUMANRPL14physical
26344197
RS4X_HUMANRPS4Xphysical
26344197
CDN1B_HUMANCDKN1Bphysical
27998760
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 GNL3_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-79, AND MASS SPECTROMETRY.
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-529, AND MASSSPECTROMETRY.

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