GNL3L_HUMAN - dbPTM
GNL3L_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GNL3L_HUMAN
UniProt AC Q9NVN8
Protein Name Guanine nucleotide-binding protein-like 3-like protein
Gene Name GNL3L
Organism Homo sapiens (Human).
Sequence Length 582
Subcellular Localization Nucleus, nucleolus .
Protein Description Stabilizes TERF1 telomeric association by preventing TERF1 recruitment by PML. Stabilizes TERF1 protein by preventing its ubiquitination and hence proteasomal degradation. Does so by interfering with TERF1-binding to FBXO4 E3 ubiquitin-protein ligase. Required for cell proliferation. By stabilizing TRF1 protein during mitosis, promotes metaphase-to-anaphase transition. Stabilizes MDM2 protein by preventing its ubiquitination, and hence proteasomal degradation. By acting on MDM2, may affect TP53 activity. Required for normal processing of ribosomal pre-rRNA. Binds GTP..
Protein Sequence MMKLRHKNKKPGEGSKGHKKISWPYPQPAKQNGKKATSKVPSAPHFVHPNDHANREAELKKKWVEEMREKQQAAREQERQKRRTIESYCQDVLRRQEEFEHKEEVLQELNMFPQLDDEATRKAYYKEFRKVVEYSDVILEVLDARDPLGCRCFQMEEAVLRAQGNKKLVLVLNKIDLVPKEVVEKWLDYLRNELPTVAFKASTQHQVKNLNRCSVPVDQASESLLKSKACFGAENLMRVLGNYCRLGEVRTHIRVGVVGLPNVGKSSLINSLKRSRACSVGAVPGITKFMQEVYLDKFIRLLDAPGIVPGPNSEVGTILRNCVHVQKLADPVTPVETILQRCNLEEISNYYGVSGFQTTEHFLTAVAHRLGKKKKGGLYSQEQAAKAVLADWVSGKISFYIPPPATHTLPTHLSAEIVKEMTEVFDIEDTEQANEDTMECLATGESDELLGDTDPLEMEIKLLHSPMTKIADAIENKTTVYKIGDLTGYCTNPNRHQMGWAKRNVDHRPKSNSMVDVCSVDRRSVLQRIMETDPLQQGQALASALKNKKKMQKRADKIASKLSDSMMSALDLSGNADDGVGD
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
20SumoylationEGSKGHKKISWPYPQ
CCCCCCCCCCCCCCC		35.98-
20SumoylationEGSKGHKKISWPYPQ
CCCCCCCCCCCCCCC		35.98-
22PhosphorylationSKGHKKISWPYPQPA
CCCCCCCCCCCCCCC		30.7725159151
39UbiquitinationNGKKATSKVPSAPHF
CCCCCCCCCCCCCCC		54.53-
42PhosphorylationKATSKVPSAPHFVHP
CCCCCCCCCCCCCCC		58.3725159151
60UbiquitinationANREAELKKKWVEEM
CCHHHHHHHHHHHHH		43.76-
61UbiquitinationNREAELKKKWVEEMR
CHHHHHHHHHHHHHH		65.57-
62SumoylationREAELKKKWVEEMRE
HHHHHHHHHHHHHHH		55.68-
62UbiquitinationREAELKKKWVEEMRE
HHHHHHHHHHHHHHH		55.68-
62SumoylationREAELKKKWVEEMRE
HHHHHHHHHHHHHHH		55.68-
70UbiquitinationWVEEMREKQQAAREQ
HHHHHHHHHHHHHHH		37.03-
84PhosphorylationQERQKRRTIESYCQD
HHHHHHHHHHHHHHH		32.8821815630
87PhosphorylationQKRRTIESYCQDVLR
HHHHHHHHHHHHHHH		27.6225159151
88PhosphorylationKRRTIESYCQDVLRR
HHHHHHHHHHHHHHC		4.9526074081
122UbiquitinationLDDEATRKAYYKEFR
CCHHHHHHHHHHHHH		36.06-
124PhosphorylationDEATRKAYYKEFRKV
HHHHHHHHHHHHHHH		20.3629496907
125PhosphorylationEATRKAYYKEFRKVV
HHHHHHHHHHHHHHH		14.6529496907
126UbiquitinationATRKAYYKEFRKVVE
HHHHHHHHHHHHHHH		37.39-
167UbiquitinationLRAQGNKKLVLVLNK
HHHCCCCEEEEEEEC		48.07-
174UbiquitinationKLVLVLNKIDLVPKE
EEEEEEECCCCCCHH		33.17-
180UbiquitinationNKIDLVPKEVVEKWL
ECCCCCCHHHHHHHH		56.51-
185UbiquitinationVPKEVVEKWLDYLRN
CCHHHHHHHHHHHHH		41.25-
200MethylationELPTVAFKASTQHQV
CCCCCEECCCCHHHH		31.52-
200UbiquitinationELPTVAFKASTQHQV
CCCCCEECCCCHHHH		31.52-
208UbiquitinationASTQHQVKNLNRCSV
CCCHHHHCCCCCCCC		49.50-
214PhosphorylationVKNLNRCSVPVDQAS
HCCCCCCCCCHHHHH		26.6421815630
221PhosphorylationSVPVDQASESLLKSK
CCCHHHHHHHHHHCH		23.2927050516
223PhosphorylationPVDQASESLLKSKAC
CHHHHHHHHHHCHHC		36.1825159151
226UbiquitinationQASESLLKSKACFGA
HHHHHHHHCHHCCCH		56.02-
228UbiquitinationSESLLKSKACFGAEN
HHHHHHCHHCCCHHH		47.81-
237SulfoxidationCFGAENLMRVLGNYC
CCCHHHHHHHHCHHH		4.1421406390
265UbiquitinationVGLPNVGKSSLINSL
ECCCCCCHHHHHHHH		32.3721906983
271PhosphorylationGKSSLINSLKRSRAC
CHHHHHHHHHHHCCC		28.4227067055
273UbiquitinationSSLINSLKRSRACSV
HHHHHHHHHHCCCCC		48.42-
275PhosphorylationLINSLKRSRACSVGA
HHHHHHHHCCCCCCC		23.7322985185
279PhosphorylationLKRSRACSVGAVPGI
HHHHCCCCCCCCCCH		23.7022985185
287PhosphorylationVGAVPGITKFMQEVY
CCCCCCHHHHHHHHH		24.9326552605
288UbiquitinationGAVPGITKFMQEVYL
CCCCCHHHHHHHHHH		36.60-
288AcetylationGAVPGITKFMQEVYL
CCCCCHHHHHHHHHH		36.6026051181
294PhosphorylationTKFMQEVYLDKFIRL
HHHHHHHHHHHHHHH		14.3922817900
297UbiquitinationMQEVYLDKFIRLLDA
HHHHHHHHHHHHHCC		39.8421906983
317PhosphorylationGPNSEVGTILRNCVH
CCCCHHHHHHHHCCH		23.2427067055
327AcetylationRNCVHVQKLADPVTP
HHCCHHHHHCCCCCC		44.5526051181
327UbiquitinationRNCVHVQKLADPVTP
HHCCHHHHHCCCCCC		44.55-
333PhosphorylationQKLADPVTPVETILQ
HHHCCCCCCHHHHHH		27.3127050516
348PhosphorylationRCNLEEISNYYGVSG
HCCHHHHHHHHCCCC		23.2729978859
350PhosphorylationNLEEISNYYGVSGFQ
CHHHHHHHHCCCCCH		8.5329978859
351PhosphorylationLEEISNYYGVSGFQT
HHHHHHHHCCCCCHH		18.4629978859
354PhosphorylationISNYYGVSGFQTTEH
HHHHHCCCCCHHHHH		29.5329978859
358PhosphorylationYGVSGFQTTEHFLTA
HCCCCCHHHHHHHHH		31.7129978859
359PhosphorylationGVSGFQTTEHFLTAV
CCCCCHHHHHHHHHH		19.3829978859
364PhosphorylationQTTEHFLTAVAHRLG
HHHHHHHHHHHHHHC		20.3829978859
375SumoylationHRLGKKKKGGLYSQE
HHHCCCCCCCCCCHH		68.07-
375UbiquitinationHRLGKKKKGGLYSQE
HHHCCCCCCCCCCHH		68.07-
375SumoylationHRLGKKKKGGLYSQE
HHHCCCCCCCCCCHH		68.07-
379PhosphorylationKKKKGGLYSQEQAAK
CCCCCCCCCHHHHHH		16.1627642862
386UbiquitinationYSQEQAAKAVLADWV
CCHHHHHHHHHHHHH		41.8821906983
465PhosphorylationMEIKLLHSPMTKIAD
HHHHHHHCCCHHHHH		19.1429255136
468PhosphorylationKLLHSPMTKIADAIE
HHHHCCCHHHHHHHH		23.7630266825
469UbiquitinationLLHSPMTKIADAIEN
HHHCCCHHHHHHHHC		29.64-
477SumoylationIADAIENKTTVYKIG
HHHHHHCCCEEEEEC		32.5525114211
477UbiquitinationIADAIENKTTVYKIG
HHHHHHCCCEEEEEC		32.5521906983
477SumoylationIADAIENKTTVYKIG
HHHHHHCCCEEEEEC		32.55-
478PhosphorylationADAIENKTTVYKIGD
HHHHHCCCEEEEECC		32.8329083192
479PhosphorylationDAIENKTTVYKIGDL
HHHHCCCEEEEECCC		24.3729083192
481PhosphorylationIENKTTVYKIGDLTG
HHCCCEEEEECCCCC		8.5229083192
482SumoylationENKTTVYKIGDLTGY
HCCCEEEEECCCCCC		35.56-
482SumoylationENKTTVYKIGDLTGY
HCCCEEEEECCCCCC		35.56-
482UbiquitinationENKTTVYKIGDLTGY
HCCCEEEEECCCCCC		35.56-
489PhosphorylationKIGDLTGYCTNPNRH
EECCCCCCCCCCCHH		7.2927642862
491PhosphorylationGDLTGYCTNPNRHQM
CCCCCCCCCCCHHHC		45.2728555341
502AcetylationRHQMGWAKRNVDHRP
HHHCCCHHCCCCCCC		37.6919608861
502UbiquitinationRHQMGWAKRNVDHRP
HHHCCCHHCCCCCCC		37.6919608861
511PhosphorylationNVDHRPKSNSMVDVC
CCCCCCCCCCCEEEC		36.5028450419
513PhosphorylationDHRPKSNSMVDVCSV
CCCCCCCCCEEECCC		27.5521815630
519PhosphorylationNSMVDVCSVDRRSVL
CCCEEECCCCHHHHH		27.2221815630
543PhosphorylationQQGQALASALKNKKK
HHHHHHHHHHHCHHH		34.6821815630
546UbiquitinationQALASALKNKKKMQK
HHHHHHHHCHHHHHH		67.45-
548UbiquitinationLASALKNKKKMQKRA
HHHHHHCHHHHHHHH		52.78-
563PhosphorylationDKIASKLSDSMMSAL
HHHHHHHHHHHHHHH		31.2321601212
573PhosphorylationMMSALDLSGNADDGV
HHHHHHHCCCCCCCC		29.6625159151
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 GNL3L_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GNL3L_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 GNL3L_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MDM2_HUMANMDM2physical
21132010
P53_HUMANTP53physical
21132010
TERF1_HUMANTERF1physical
19487455
TERT_HUMANTERTphysical
19487455
ROP1A_HUMANROPN1physical
25416956
LZTS2_HUMANLZTS2physical
25416956
NMD3_HUMANNMD3physical
26344197
NOP58_HUMANNOP58physical
26344197
OLA1_HUMANOLA1physical
26344197
PESC_HUMANPES1physical
26344197
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 GNL3L_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-502, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-465, AND MASSSPECTROMETRY.

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