LSG1_HUMAN - dbPTM
LSG1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LSG1_HUMAN
UniProt AC Q9H089
Protein Name Large subunit GTPase 1 homolog
Gene Name LSG1
Organism Homo sapiens (Human).
Sequence Length 658
Subcellular Localization Cytoplasm . Endoplasmic reticulum . Nucleus, Cajal body . Shuttles between the Cajal bodies in the nucleus and the endoplasmic reticulum.
Protein Description GTPase required for the XPO1/CRM1-mediated nuclear export of the 60S ribosomal subunit. Probably acts by mediating the release of NMD3 from the 60S ribosomal subunit after export into the cytoplasm (Probable)..
Protein Sequence MGRRRAPAGGSLGRALMRHQTQRSRSHRHTDSWLHTSELNDGYDWGRLNLQSVTEQSSLDDFLATAELAGTEFVAEKLNIKFVPAEARTGLLSFEESQRIKKLHEENKQFLCIPRRPNWNQNTTPEELKQAEKDNFLEWRRQLVRLEEEQKLILTPFERNLDFWRQLWRVIERSDIVVQIVDARNPLLFRCEDLECYVKEMDANKENVILINKADLLTAEQRSAWAMYFEKEDVKVIFWSALAGAIPLNGDSEEEANRDDRQSNTTKFGHSSFDQAEISHSESEHLPARDSPSLSENPTTDEDDSEYEDCPEEEEDDWQTCSEEDGPKEEDCSQDWKESSTADSEARSRKTPQKRQIHNFSHLVSKQELLELFKELHTGRKVKDGQLTVGLVGYPNVGKSSTINTIMGNKKVSVSATPGHTKHFQTLYVEPGLCLCDCPGLVMPSFVSTKAEMTCSGILPIDQMRDHVPPVSLVCQNIPRHVLEATYGINIITPREDEDPHRPPTSEELLTAYGYMRGFMTAHGQPDQPRSARYILKDYVSGKLLYCHPPPGRDPVTFQHQHQRLLENKMNSDEIKMQLGRNKKAKQIENIVDKTFFHQENVRALTKGVQAVMGYKPGSGVVTASTASSENGAGKPWKKHGNRNKKEKSRRLYKHLDM
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
5Dimethylation---MGRRRAPAGGSL
---CCCCCCCCCCHH		43.49-
5Methylation---MGRRRAPAGGSL
---CCCCCCCCCCHH		43.4924391531
11PhosphorylationRRAPAGGSLGRALMR
CCCCCCCHHHHHHHH		27.0828555341
14DimethylationPAGGSLGRALMRHQT
CCCCHHHHHHHHHHH		29.82-
14MethylationPAGGSLGRALMRHQT
CCCCHHHHHHHHHHH		29.8224391329
30PhosphorylationRSRSHRHTDSWLHTS
HHHHHCCCCCEEEHH		31.5229449344
32PhosphorylationRSHRHTDSWLHTSEL
HHHCCCCCEEEHHHC		32.4628857561
36PhosphorylationHTDSWLHTSELNDGY
CCCCEEEHHHCCCCC		23.0229449344
37PhosphorylationTDSWLHTSELNDGYD
CCCEEEHHHCCCCCC		29.3729449344
43PhosphorylationTSELNDGYDWGRLNL
HHHCCCCCCCCCCCH		16.0427642862
52PhosphorylationWGRLNLQSVTEQSSL
CCCCCHHHHHCCCCH		33.8930624053
54PhosphorylationRLNLQSVTEQSSLDD
CCCHHHHHCCCCHHH		33.2923663014
55UbiquitinationLNLQSVTEQSSLDDF
CCHHHHHCCCCHHHH		46.4322817900
57PhosphorylationLQSVTEQSSLDDFLA
HHHHHCCCCHHHHHH		27.0023663014
58PhosphorylationQSVTEQSSLDDFLAT
HHHHCCCCHHHHHHH		35.2023663014
65PhosphorylationSLDDFLATAELAGTE
CHHHHHHHHHHCCCH		23.8628348404
77UbiquitinationGTEFVAEKLNIKFVP
CCHHHHHHCCCEEEE		36.7823000965
81UbiquitinationVAEKLNIKFVPAEAR
HHHHCCCEEEECHHH		38.9623000965
93PhosphorylationEARTGLLSFEESQRI
HHHCCCCCHHHHHHH		35.3430108239
97PhosphorylationGLLSFEESQRIKKLH
CCCCHHHHHHHHHHH		19.9830108239
102UbiquitinationEESQRIKKLHEENKQ
HHHHHHHHHHHHHCC		53.3429967540
108UbiquitinationKKLHEENKQFLCIPR
HHHHHHHCCEEEEEC		45.7829967540
108AcetylationKKLHEENKQFLCIPR
HHHHHHHCCEEEEEC		45.7826051181
123PhosphorylationRPNWNQNTTPEELKQ
CCCCCCCCCHHHHHH		33.6825627689
124PhosphorylationPNWNQNTTPEELKQA
CCCCCCCCHHHHHHH		35.9325159151
129UbiquitinationNTTPEELKQAEKDNF
CCCHHHHHHHHHHCH		51.2229967540
133UbiquitinationEELKQAEKDNFLEWR
HHHHHHHHHCHHHHH		62.0729967540
151UbiquitinationVRLEEEQKLILTPFE
HHHHHHHHEEECCHH		40.5524816145
155PhosphorylationEEQKLILTPFERNLD
HHHHEEECCHHHCHH		20.95-
199UbiquitinationEDLECYVKEMDANKE
CCCEEEEEECCCCCC		22.3529967540
2052-HydroxyisobutyrylationVKEMDANKENVILIN
EEECCCCCCCEEEEE		53.00-
2132-HydroxyisobutyrylationENVILINKADLLTAE
CCEEEEEHHHHCCHH		35.96-
213UbiquitinationENVILINKADLLTAE
CCEEEEEHHHHCCHH		35.9621906983
240PhosphorylationDVKVIFWSALAGAIP
HHHHHEHHHHHCCCC		11.5826074081
252PhosphorylationAIPLNGDSEEEANRD
CCCCCCCCHHHHCCC		48.5925159151
263PhosphorylationANRDDRQSNTTKFGH
HCCCCCCCCCCCCCC		36.7226074081
265PhosphorylationRDDRQSNTTKFGHSS
CCCCCCCCCCCCCCC		36.2929514088
266PhosphorylationDDRQSNTTKFGHSSF
CCCCCCCCCCCCCCC		28.7326074081
271PhosphorylationNTTKFGHSSFDQAEI
CCCCCCCCCCCHHHC		32.8326074081
272PhosphorylationTTKFGHSSFDQAEIS
CCCCCCCCCCHHHCC		27.4525849741
279PhosphorylationSFDQAEISHSESEHL
CCCHHHCCCCCCCCC		16.6826074081
281PhosphorylationDQAEISHSESEHLPA
CHHHCCCCCCCCCCC		35.7126074081
283PhosphorylationAEISHSESEHLPARD
HHCCCCCCCCCCCCC		33.0726074081
320PhosphorylationEEEDDWQTCSEEDGP
CCCCCCCCCCCCCCC		17.47-
322PhosphorylationEDDWQTCSEEDGPKE
CCCCCCCCCCCCCCC		47.62-
333PhosphorylationGPKEEDCSQDWKESS
CCCCCCCCHHHHHHH		43.4221815630
383AcetylationLHTGRKVKDGQLTVG
HHCCCCCCCCCEEEE		60.217370285
383UbiquitinationLHTGRKVKDGQLTVG
HHCCCCCCCCCEEEE		60.21-
394PhosphorylationLTVGLVGYPNVGKSS
EEEEEECCCCCCCCC		5.5520068231
411UbiquitinationNTIMGNKKVSVSATP
CHHCCCCEEEEECCC		43.6822817900
413PhosphorylationIMGNKKVSVSATPGH
HCCCCEEEEECCCCC		21.1625159151
413O-linked_GlycosylationIMGNKKVSVSATPGH
HCCCCEEEEECCCCC		21.1630379171
415PhosphorylationGNKKVSVSATPGHTK
CCCEEEEECCCCCCC		20.9320068231
417PhosphorylationKKVSVSATPGHTKHF
CEEEEECCCCCCCCC		23.4625159151
418UbiquitinationKVSVSATPGHTKHFQ
EEEEECCCCCCCCCE		32.0824816145
421PhosphorylationVSATPGHTKHFQTLY
EECCCCCCCCCEEEE		31.9329496963
486PhosphorylationPRHVLEATYGINIIT
CHHHHHHHCCEEEEC		16.9529759185
487PhosphorylationRHVLEATYGINIITP
HHHHHHHCCEEEECC		24.0529759185
493PhosphorylationTYGINIITPREDEDP
HCCEEEECCCCCCCC		16.7029759185
569UbiquitinationHQRLLENKMNSDEIK
HHHHHHHCCCHHHHH		30.0422817900
572PhosphorylationLLENKMNSDEIKMQL
HHHHCCCHHHHHHHH		32.8728985074
576UbiquitinationKMNSDEIKMQLGRNK
CCCHHHHHHHHCCCH		20.6724816145
586UbiquitinationLGRNKKAKQIENIVD
HCCCHHHHHHHHHHH		61.7729967540
595PhosphorylationIENIVDKTFFHQENV
HHHHHHHHHHCHHHH		27.3728555341
606PhosphorylationQENVRALTKGVQAVM
HHHHHHHHHHHHHHC		25.43-
615PhosphorylationGVQAVMGYKPGSGVV
HHHHHCCCCCCCCEE		8.91-
616AcetylationVQAVMGYKPGSGVVT
HHHHCCCCCCCCEEE		36.8526051181
625PhosphorylationGSGVVTASTASSENG
CCCEEEEECCCCCCC		18.3625627689
626PhosphorylationSGVVTASTASSENGA
CCEEEEECCCCCCCC		28.2625627689
628PhosphorylationVVTASTASSENGAGK
EEEEECCCCCCCCCC		37.9724719451
629PhosphorylationVTASTASSENGAGKP
EEEECCCCCCCCCCC		32.3925627689
635AcetylationSSENGAGKPWKKHGN
CCCCCCCCCCHHCCC		47.3626051181
653PhosphorylationKEKSRRLYKHLDM--
HHHHHHHHHHHCC--		8.4427642862
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 LSG1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LSG1_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 LSG1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZN622_HUMANZNF622physical
24778252
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 LSG1_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-252, 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-252, AND MASSSPECTROMETRY.

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