LRSM1_HUMAN - dbPTM
LRSM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LRSM1_HUMAN
UniProt AC Q6UWE0
Protein Name E3 ubiquitin-protein ligase LRSAM1 {ECO:0000305}
Gene Name LRSAM1 {ECO:0000303|PubMed:20865121}
Organism Homo sapiens (Human).
Sequence Length 723
Subcellular Localization Cytoplasm . Displays a punctuate distribution and localizes to a submembranal ring (PubMed:15256501). Localizes to intracellular bacterial pathogens (PubMed:23245322).
Protein Description E3 ubiquitin-protein ligase that mediates monoubiquitination of TSG101 at multiple sites, leading to inactivate the ability of TSG101 to sort endocytic (EGF receptors) and exocytic (HIV-1 viral proteins) cargos. [PubMed: 15256501 Bacterial recognition protein that defends the cytoplasm from invasive pathogens]
Protein Sequence MPLFFRKRKPSEEARKRLEYQMCLAKEAGADDILDISKCELSEIPFGAFATCKVLQKKVLIVHTNHLTSLLPKSCSLLSLATIKVLDLHDNQLTALPDDLGQLTALQVLNVERNQLMQLPRSIGNLTQLQTLNVKDNKLKELPDTVGELRSLRTLNISGNEIQRLPQMLAHVRTLEMLSLDASAMVYPPREVCGAGTAAILQFLCKESGLEYYPPSQYLLPILEQDGIENSRDSPDGPTDRFSREELEWQNRFSDYEKRKEQKMLEKLEFERRLELGQREHTQLLQQSSSQKDEILQTVKEEQSRLEQGLSEHQRHLNAERQRLQEQLKQTEQNISSRIQKLLQDNQRQKKSSEILKSLENERIRMEQLMSITQEETESLRRRDVASAMQQMLTESCKNRLIQMAYESQRQNLVQQACSSMAEMDERFQQILSWQQMDQNKAISQILQESAMQKAAFEALQVKKDLMHRQIRSQIKLIETELLQLTQLELKRKSLDTESLQEMISEQRWALSSLLQQLLKEKQQREEELREILTELEAKSETRQENYWLIQYQRLLNQKPLSLKLQEEGMERQLVALLEELSAEHYLPIFAHHRLSLDLLSQMSPGDLAKVGVSEAGLQHEILRRVQELLDAARIQPELKPPMGEVVTPTAPQEPPESVRPSAPPAELEVQASECVVCLEREAQMIFLNCGHVCCCQQCCQPLRTCPLCRQDIAQRLRIYHSS
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
9UbiquitinationPLFFRKRKPSEEARK
CCCCCCCCCCHHHHH		56.80-
38UbiquitinationDDILDISKCELSEIP
CCCEECCCCCCCCCC		31.87-
69PhosphorylationVHTNHLTSLLPKSCS
EECCHHHHHCCHHCH		33.9824719451
71 (in isoform 3)Ubiquitination-5.1321890473
79PhosphorylationPKSCSLLSLATIKVL
CHHCHHHHHHEEEEE		22.6625814448
100 (in isoform 3)Ubiquitination-6.5021890473
122PhosphorylationQLMQLPRSIGNLTQL
HHHCCCCHHCCCHHC		32.6727174698
127PhosphorylationPRSIGNLTQLQTLNV
CCHHCCCHHCEEECC		31.1027174698
131PhosphorylationGNLTQLQTLNVKDNK
CCCHHCEEECCCCCC		28.9727174698
144 (in isoform 3)Ubiquitination-67.6521890473
179PhosphorylationVRTLEMLSLDASAMV
HHHHHHHCCCCCCCC		23.93-
187PhosphorylationLDASAMVYPPREVCG
CCCCCCCCCCHHHCC		8.40-
218PhosphorylationEYYPPSQYLLPILEQ
CCCCHHHCHHHHHHH		17.9727251275
220 (in isoform 3)Ubiquitination-1.79-
231PhosphorylationEQDGIENSRDSPDGP
HHCCCCCCCCCCCCC		25.3626657352
234PhosphorylationGIENSRDSPDGPTDR
CCCCCCCCCCCCCCC		24.6325159151
239PhosphorylationRDSPDGPTDRFSREE
CCCCCCCCCCCCHHH		45.3926074081
243PhosphorylationDGPTDRFSREELEWQ
CCCCCCCCHHHHHHH		39.4124719451
256PhosphorylationWQNRFSDYEKRKEQK
HHHHCCHHHHHHHHH		23.35-
282PhosphorylationELGQREHTQLLQQSS
HHHHHHHHHHHHHCC		19.0320363803
288PhosphorylationHTQLLQQSSSQKDEI
HHHHHHHCCCCHHHH		20.9929978859
289PhosphorylationTQLLQQSSSQKDEIL
HHHHHHCCCCHHHHH		32.2420873877
290PhosphorylationQLLQQSSSQKDEILQ
HHHHHCCCCHHHHHH		46.6329978859
298PhosphorylationQKDEILQTVKEEQSR
CHHHHHHHHHHHHHH		30.0528258704
304PhosphorylationQTVKEEQSRLEQGLS
HHHHHHHHHHHHHHH		41.9529978859
311PhosphorylationSRLEQGLSEHQRHLN
HHHHHHHHHHHHHHH		39.6028857561
329UbiquitinationQRLQEQLKQTEQNIS
HHHHHHHHHHHHHHH		55.67-
337PhosphorylationQTEQNISSRIQKLLQ
HHHHHHHHHHHHHHH		29.6119664995
341UbiquitinationNISSRIQKLLQDNQR
HHHHHHHHHHHHCHH		49.12-
357UbiquitinationKKSSEILKSLENERI
HHHHHHHHHHHHHHH		59.67-
406PhosphorylationNRLIQMAYESQRQNL
HHHHHHHHHHHHHHH		15.6927642862
452SulfoxidationQILQESAMQKAAFEA
HHHHHHHHHHHHHHH		6.1321406390
491UbiquitinationQLTQLELKRKSLDTE
HHHHHHHHHCCCCHH		48.7021890473
491 (in isoform 1)Ubiquitination-48.7021890473
493 (in isoform 2)Ubiquitination-54.5021890473
493UbiquitinationTQLELKRKSLDTESL
HHHHHHHCCCCHHHH		54.50-
494PhosphorylationQLELKRKSLDTESLQ
HHHHHHCCCCHHHHH		35.1928857561
497PhosphorylationLKRKSLDTESLQEMI
HHHCCCCHHHHHHHH		32.5428857561
499PhosphorylationRKSLDTESLQEMISE
HCCCCHHHHHHHHHH		37.1328555341
520UbiquitinationSLLQQLLKEKQQREE
HHHHHHHHHHHHHHH		72.0321906983
520 (in isoform 1)Ubiquitination-72.0321890473
522UbiquitinationLQQLLKEKQQREEEL
HHHHHHHHHHHHHHH		50.58-
534PhosphorylationEELREILTELEAKSE
HHHHHHHHHHHHCCC		44.1523403867
537 (in isoform 2)Ubiquitination-48.0621890473
562PhosphorylationLLNQKPLSLKLQEEG
HHCCCCCCHHHHHHH		31.8027067055
564UbiquitinationNQKPLSLKLQEEGME
CCCCCCHHHHHHHHH		44.7621890473
564 (in isoform 1)Ubiquitination-44.7621890473
596PhosphorylationIFAHHRLSLDLLSQM
HHHHCHHCHHHHHCC		21.5720068231
601PhosphorylationRLSLDLLSQMSPGDL
HHCHHHHHCCCHHHH		31.0020068231
604PhosphorylationLDLLSQMSPGDLAKV
HHHHHCCCHHHHHHH		20.3525159151
640UbiquitinationARIQPELKPPMGEVV
HHCCCCCCCCCCCCC		45.47-
648PhosphorylationPPMGEVVTPTAPQEP
CCCCCCCCCCCCCCC		21.7927251275
650PhosphorylationMGEVVTPTAPQEPPE
CCCCCCCCCCCCCCC		41.4227251275
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 LRSM1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LRSM1_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 LRSM1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TS101_HUMANTSG101physical
15256501
GP108_HUMANGPR108physical
16169070
NINL_HUMANNINLphysical
16169070
KLC1_HUMANKLC1physical
16169070
F178B_HUMANFAM178Bphysical
16169070
YTHD1_HUMANYTHDF1physical
22939629
MKRN3_HUMANMKRN3physical
22493164
MDM4_HUMANMDM4physical
22493164
RN111_HUMANRNF111physical
22493164
VPS11_HUMANVPS11physical
22493164
TRI74_HUMANTRIM74physical
22493164
ANKY2_HUMANANKMY2physical
22863883
NC2B_HUMANDR1physical
22863883
HSF1_HUMANHSF1physical
22863883
HPBP1_HUMANHSPBP1physical
22863883
MTMR2_HUMANMTMR2physical
22863883
PPME1_HUMANPPME1physical
22863883
UBE3A_HUMANUBE3Aphysical
22863883
LRSM1_HUMANLRSAM1physical
15256501
PHF23_HUMANPHF23physical
25484098
TS101_HUMANTSG101physical
26811492
UB2D1_HUMANUBE2D1physical
26811492
LRSM1_HUMANLRSAM1physical
28335037
UBE2N_HUMANUBE2Nphysical
28335037
TS101_HUMANTSG101physical
28335037
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614436Charcot-Marie-Tooth disease 2P (CMT2P)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LRSM1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-234 AND SER-604, ANDMASS SPECTROMETRY.

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