GNL1_HUMAN - dbPTM
GNL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GNL1_HUMAN
UniProt AC P36915
Protein Name Guanine nucleotide-binding protein-like 1
Gene Name GNL1
Organism Homo sapiens (Human).
Sequence Length 607
Subcellular Localization
Protein Description Possible regulatory or functional link with the histocompatibility cluster..
Protein Sequence MPRKKPFSVKQKKKQLQDKRERKRGLQDGLRSSSNSRSGSRERREEQTDTSDGESVTHHIRRLNQQPSQGLGPRGYDPNRYRLHFERDSREEVERRKRAAREQVLQPVSAELLELDIREVYQPGSVLDFPRRPPWSYEMSKEQLMSQEERSFQDYLGKIHGAYSSEKLSYFEHNLETWRQLWRVLEMSDIVLLITDIRHPVVNFPPALYEYVTGELGLALVLVLNKVDLAPPALVVAWKHYFHQHYPQLHVVLFTSFPRDPRTPQDPSSVLKKSRRRGRGWTRALGPEQLLRACEAITVGKVDLSSWREKIARDVAGATWGNGSGEEEEEEDGPAVLVEQQTDSAMEPTGPTQERYKDGVVTIGCVGFPNVGKSSLINGLVGRKVVSVSRTPGHTRYFQTYFLTPSVKLCDCPGLIFPSLLPRQLQVLAGIYPIAQIQEPYTAVGYLASRIPVQALLHLRHPEAEDPSAEHPWCAWDICEAWAEKRGYKTAKAARNDVYRAANSLLRLAVDGRLSLCFHPPGYSEQKGTWESHPETTELVVLQGRVGPAGDEEEEEEEELSSSCEEEGEEDRDADEEGEGDEETPTSAPGSSLAGRNPYALLGEDEC
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
8PhosphorylationMPRKKPFSVKQKKKQ
CCCCCCCCHHHHHHH		36.6130576142
20 (in isoform 2)Ubiquitination-58.1921890473
32PhosphorylationGLQDGLRSSSNSRSG
HHHHHHHCCCCCCCC		43.0628176443
33PhosphorylationLQDGLRSSSNSRSGS
HHHHHHCCCCCCCCC		27.4028176443
34PhosphorylationQDGLRSSSNSRSGSR
HHHHHCCCCCCCCCH		39.8228176443
36PhosphorylationGLRSSSNSRSGSRER
HHHCCCCCCCCCHHH		29.7628176443
38PhosphorylationRSSSNSRSGSRERRE
HCCCCCCCCCHHHHH		40.7225332170
40PhosphorylationSSNSRSGSRERREEQ
CCCCCCCCHHHHHHH		32.0123828894
48PhosphorylationRERREEQTDTSDGES
HHHHHHHCCCCCCHH		44.5229255136
50PhosphorylationRREEQTDTSDGESVT
HHHHHCCCCCCHHHH		31.9129255136
51PhosphorylationREEQTDTSDGESVTH
HHHHCCCCCCHHHHH		46.5629255136
55PhosphorylationTDTSDGESVTHHIRR
CCCCCCHHHHHHHHH		37.5329255136
57PhosphorylationTSDGESVTHHIRRLN
CCCCHHHHHHHHHHH		19.6030266825
68PhosphorylationRRLNQQPSQGLGPRG
HHHHCCCCCCCCCCC		32.3217525332
74MethylationPSQGLGPRGYDPNRY
CCCCCCCCCCCCCCC		55.28-
76PhosphorylationQGLGPRGYDPNRYRL
CCCCCCCCCCCCCEE		29.5226074081
81PhosphorylationRGYDPNRYRLHFERD
CCCCCCCCEEEECCC		24.94-
82MethylationGYDPNRYRLHFERDS
CCCCCCCEEEECCCC		20.60-
89PhosphorylationRLHFERDSREEVERR
EEEECCCCHHHHHHH		48.0627251275
136PhosphorylationFPRRPPWSYEMSKEQ
CCCCCCCCHHCCHHH		19.59-
137PhosphorylationPRRPPWSYEMSKEQL
CCCCCCCHHCCHHHH		16.28-
141UbiquitinationPWSYEMSKEQLMSQE
CCCHHCCHHHHHCHH		48.44-
155PhosphorylationEERSFQDYLGKIHGA
HHHHHHHHHHHHHCC		13.43-
158 (in isoform 1)Ubiquitination-29.0021890473
158UbiquitinationSFQDYLGKIHGAYSS
HHHHHHHHHHCCCCC		29.0021890473
158UbiquitinationSFQDYLGKIHGAYSS
HHHHHHHHHHCCCCC		29.0021890473
263PhosphorylationSFPRDPRTPQDPSSV
CCCCCCCCCCCHHHH		30.5921815630
269PhosphorylationRTPQDPSSVLKKSRR
CCCCCHHHHHHHHHH		36.5428555341
282PhosphorylationRRRGRGWTRALGPEQ
HHCCCCHHHHCCHHH		14.64-
301UbiquitinationCEAITVGKVDLSSWR
HHHEEECCCCHHHHH		28.39-
319PhosphorylationARDVAGATWGNGSGE
HHHHCCCCCCCCCCC		32.7528122231
324PhosphorylationGATWGNGSGEEEEEE
CCCCCCCCCCHHHCC		47.2128355574
342PhosphorylationAVLVEQQTDSAMEPT
EEEEEEECCCCCCCC		31.4528464451
344PhosphorylationLVEQQTDSAMEPTGP
EEEEECCCCCCCCCC		32.6622199227
349PhosphorylationTDSAMEPTGPTQERY
CCCCCCCCCCCHHHH		42.3522199227
352PhosphorylationAMEPTGPTQERYKDG
CCCCCCCCHHHHCCC		44.3922199227
357UbiquitinationGPTQERYKDGVVTIG
CCCHHHHCCCEEEEE		54.98-
374PhosphorylationGFPNVGKSSLINGLV
CCCCCCHHHHHHCCC		25.1721406692
375PhosphorylationFPNVGKSSLINGLVG
CCCCCHHHHHHCCCC		36.4328857561
387PhosphorylationLVGRKVVSVSRTPGH
CCCCCEEEEECCCCC		19.8428555341
389PhosphorylationGRKVVSVSRTPGHTR
CCCEEEEECCCCCCE		23.9528555341
400PhosphorylationGHTRYFQTYFLTPSV
CCCEEEEEEEECCCC		13.3228152594
401PhosphorylationHTRYFQTYFLTPSVK
CCEEEEEEEECCCCE		5.9428152594
404PhosphorylationYFQTYFLTPSVKLCD
EEEEEEECCCCEECC		12.0128152594
432PhosphorylationLQVLAGIYPIAQIQE
HHHHHCCCCHHHCCC		6.4124043423
441PhosphorylationIAQIQEPYTAVGYLA
HHHCCCCCHHHHHHH		13.4324043423
442PhosphorylationAQIQEPYTAVGYLAS
HHCCCCCHHHHHHHH		26.1124043423
446PhosphorylationEPYTAVGYLASRIPV
CCCHHHHHHHHHCCH		7.7824043423
449PhosphorylationTAVGYLASRIPVQAL
HHHHHHHHHCCHHHH		28.3124043423
561PhosphorylationEEEEEELSSSCEEEG
HHHHHHHHHHCHHCC		24.4025850435
562PhosphorylationEEEEELSSSCEEEGE
HHHHHHHHHCHHCCC		52.1925850435
563PhosphorylationEEEELSSSCEEEGEE
HHHHHHHHCHHCCCC		23.3625850435
584PhosphorylationEGEGDEETPTSAPGS
CCCCCCCCCCCCCCC		29.8021815630
586PhosphorylationEGDEETPTSAPGSSL
CCCCCCCCCCCCCCC		44.9629978859
587PhosphorylationGDEETPTSAPGSSLA
CCCCCCCCCCCCCCC		33.4029978859
591PhosphorylationTPTSAPGSSLAGRNP
CCCCCCCCCCCCCCC		22.5629978859
592PhosphorylationPTSAPGSSLAGRNPY
CCCCCCCCCCCCCCC		28.3129978859
599PhosphorylationSLAGRNPYALLGEDE
CCCCCCCCHHCCCCC		17.2728796482
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 GNL1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GNL1_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 GNL1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RL5_HUMANRPL5physical
22939629
RS15A_HUMANRPS15Aphysical
22939629
GDIA_HUMANGDI1physical
18255255
TP4A1_HUMANPTP4A1physical
18255255
HINT1_HUMANHINT1physical
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 GNL1_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 THR-48; THR-50 AND SER-51,AND MASS SPECTROMETRY.
"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-32; SER-33; SER-34;THR-48; THR-50; SER-51; SER-324; SER-561; SER-562 AND SER-563, 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-51, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND MASSSPECTROMETRY.

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