MGRN1_HUMAN - dbPTM
MGRN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MGRN1_HUMAN
UniProt AC O60291
Protein Name E3 ubiquitin-protein ligase MGRN1
Gene Name MGRN1
Organism Homo sapiens (Human).
Sequence Length 552
Subcellular Localization Early endosome . The endosomal localization is dependent on the interaction with TSG101.
Isoform 1: Cytoplasm, cytosol. Nucleus. Translocation from the cytosol to the nucleus is seen only in the presence of MC1R and MC4R, but not TBXA2R. Exclud
Protein Description E3 ubiquitin-protein ligase. Mediates monoubiquitination at multiple sites of TSG101 in the presence of UBE2D1, but not of UBE2G1, nor UBE2H. Plays a role in the regulation of endosome-to-lysosome trafficking. Impairs MC1R- and MC4R-signaling by competing with GNAS-binding to MCRs and inhibiting agonist-induced cAMP production. Does not inhibit ADRB2-signaling. Does not promote MC1R ubiquitination. Acts also as a negative regulator of hedgehog signaling (By similarity)..
Protein Sequence MGSILSRRIAGVEDIDIQANSAYRYPPKSGNYFASHFFMGGEKFDTPHPEGYLFGENMDLNFLGSRPVQFPYVTPAPHEPVKTLRSLVNIRKDSLRLVRYKDDADSPTEDGDKPRVLYSLEFTFDADARVAITIYCQASEEFLNGRAVYSPKSPSLQSETVHYKRGVSQQFSLPSFKIDFSEWKDDELNFDLDRGVFPVVIQAVVDEGDVVEVTGHAHVLLAAFEKHMDGSFSVKPLKQKQIVDRVSYLLQEIYGIENKNNQETKPSDDENSDNSNECVVCLSDLRDTLILPCRHLCLCTSCADTLRYQANNCPICRLPFRALLQIRAVRKKPGALSPVSFSPVLAQSLEHDEHSCPFKKSKPHPASLASKKPKRETNSDSVPPGYEPISLLEALNGLRAVSPAIPSAPLYEEITYSGISDGLSQASCPLAAIDHILDSSRQKGRPQSKAPDSTLRSPSSPIHEEDEEKLSEDVDAPPPLGGAELALRESSSPESFITEEVDESSSPQQGTRAASIENVLQDSSPEHCGRGPPADIYLPALGPDSCSVGIDE
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
2Myristoylation------MGSILSRRI
------CCCHHHHCC		24.3220213681
2N-myristoyl glycine------MGSILSRRI
------CCCHHHHCC		24.32-
3Phosphorylation-----MGSILSRRIA
-----CCCHHHHCCC		21.0324719451
6Phosphorylation--MGSILSRRIAGVE
--CCCHHHHCCCCCE		20.1724719451
44UbiquitinationFFMGGEKFDTPHPEG
EECCCCCCCCCCCCC		12.6021890473
63UbiquitinationENMDLNFLGSRPVQF
CCCCCCCCCCCCCCC		6.2322053931
82 (in isoform 4)Ubiquitination-53.1921890473
82 (in isoform 2)Ubiquitination-53.1921890473
82 (in isoform 1)Ubiquitination-53.1921890473
82 (in isoform 3)Ubiquitination-53.1921890473
82UbiquitinationPAPHEPVKTLRSLVN
CCCCCCHHHHHHHHH		53.1922817900
100PhosphorylationDSLRLVRYKDDADSP
HCEEEEEECCCCCCC		15.9923312004
101 (in isoform 3)Ubiquitination-38.2721890473
101 (in isoform 4)Ubiquitination-38.2721890473
101 (in isoform 2)Ubiquitination-38.2721890473
101 (in isoform 1)Ubiquitination-38.2721890473
101UbiquitinationSLRLVRYKDDADSPT
CEEEEEECCCCCCCC		38.2722053931
101AcetylationSLRLVRYKDDADSPT
CEEEEEECCCCCCCC		38.27133063
106PhosphorylationRYKDDADSPTEDGDK
EECCCCCCCCCCCCC		35.1328985074
108PhosphorylationKDDADSPTEDGDKPR
CCCCCCCCCCCCCCE		51.1427732954
126UbiquitinationSLEFTFDADARVAIT
EEEEEECCCCEEEEE		14.2623000965
153PhosphorylationRAVYSPKSPSLQSET
CEEECCCCCCCCCCE		24.0925159151
155PhosphorylationVYSPKSPSLQSETVH
EECCCCCCCCCCEEE		46.2425159151
158PhosphorylationPKSPSLQSETVHYKR
CCCCCCCCCEEEECC		40.2924114839
160PhosphorylationSPSLQSETVHYKRGV
CCCCCCCEEEECCCC		20.1724114839
164 (in isoform 2)Ubiquitination-28.0021890473
1642-HydroxyisobutyrylationQSETVHYKRGVSQQF
CCCEEEECCCCCCCC		28.00-
164 (in isoform 1)Ubiquitination-28.0021890473
164 (in isoform 3)Ubiquitination-28.0021890473
164 (in isoform 4)Ubiquitination-28.0021890473
164UbiquitinationQSETVHYKRGVSQQF
CCCEEEECCCCCCCC		28.0023000965
175PhosphorylationSQQFSLPSFKIDFSE
CCCCCCCEEEECHHH		44.4524719451
227UbiquitinationLLAAFEKHMDGSFSV
HHHHHHHHCCCCCCC		16.6221963094
228UbiquitinationLAAFEKHMDGSFSVK
HHHHHHHCCCCCCCC		10.3921963094
235UbiquitinationMDGSFSVKPLKQKQI
CCCCCCCCCCCHHHH		43.3533845483
247PhosphorylationKQIVDRVSYLLQEIY
HHHHHHHHHHHHHHH		15.7921955146
248PhosphorylationQIVDRVSYLLQEIYG
HHHHHHHHHHHHHHC		14.4721955146
254PhosphorylationSYLLQEIYGIENKNN
HHHHHHHHCCCCCCC		15.9921955146
259AcetylationEIYGIENKNNQETKP
HHHCCCCCCCCCCCC		44.4820167786
265UbiquitinationNKNNQETKPSDDENS
CCCCCCCCCCCCCCC		41.6021963094
266UbiquitinationKNNQETKPSDDENSD
CCCCCCCCCCCCCCC		50.8721963094
283PhosphorylationNECVVCLSDLRDTLI
CEEEEEEHHHHCCEE		29.4924719451
332UbiquitinationQIRAVRKKPGALSPV
HHHHHHCCCCCCCCC		37.8129967540
337PhosphorylationRKKPGALSPVSFSPV
HCCCCCCCCCCCCHH		23.7929255136
340PhosphorylationPGALSPVSFSPVLAQ
CCCCCCCCCCHHHHH		24.3229255136
342PhosphorylationALSPVSFSPVLAQSL
CCCCCCCCHHHHHHC		13.4429255136
348PhosphorylationFSPVLAQSLEHDEHS
CCHHHHHHCCCCCCC		30.0723312004
355PhosphorylationSLEHDEHSCPFKKSK
HCCCCCCCCCCCCCC		22.8023312004
360UbiquitinationEHSCPFKKSKPHPAS
CCCCCCCCCCCCCHH		65.1829967540
361PhosphorylationHSCPFKKSKPHPASL
CCCCCCCCCCCCHHH		52.5929457462
362UbiquitinationSCPFKKSKPHPASLA
CCCCCCCCCCCHHHC		57.1129967540
367PhosphorylationKSKPHPASLASKKPK
CCCCCCHHHCCCCCC		28.9922210691
402PhosphorylationLNGLRAVSPAIPSAP
HHHHHCCCCCCCCCC		13.9726356563
407PhosphorylationAVSPAIPSAPLYEEI
CCCCCCCCCCCCEEC		36.0826356563
411PhosphorylationAIPSAPLYEEITYSG
CCCCCCCCEECCCCC		15.5126356563
415PhosphorylationAPLYEEITYSGISDG
CCCCEECCCCCCCCC		18.21-
416PhosphorylationPLYEEITYSGISDGL
CCCEECCCCCCCCCC		15.5726356563
417PhosphorylationLYEEITYSGISDGLS
CCEECCCCCCCCCCC		22.47-
424PhosphorylationSGISDGLSQASCPLA
CCCCCCCCCCCCHHH		29.2725332170
427UbiquitinationSDGLSQASCPLAAID
CCCCCCCCCHHHHHH		14.5029967540
427PhosphorylationSDGLSQASCPLAAID
CCCCCCCCCHHHHHH		14.5025332170
437PhosphorylationLAAIDHILDSSRQKG
HHHHHHHHHHHHHCC		4.7232142685
439PhosphorylationAIDHILDSSRQKGRP
HHHHHHHHHHHCCCC		24.7925332170
449UbiquitinationQKGRPQSKAPDSTLR
HCCCCCCCCCCCCCC		59.7029967540
453PhosphorylationPQSKAPDSTLRSPSS
CCCCCCCCCCCCCCC		28.4325849741
454PhosphorylationQSKAPDSTLRSPSSP
CCCCCCCCCCCCCCC		33.3028450419
457PhosphorylationAPDSTLRSPSSPIHE
CCCCCCCCCCCCCCH		32.0425159151
459PhosphorylationDSTLRSPSSPIHEED
CCCCCCCCCCCCHHH		50.4129255136
460PhosphorylationSTLRSPSSPIHEEDE
CCCCCCCCCCCHHHH		31.1229255136
471PhosphorylationEEDEEKLSEDVDAPP
HHHHHHHCCCCCCCC		42.7028122231
490PhosphorylationAELALRESSSPESFI
HHEEEECCCCCCHHC		29.6729978859
491PhosphorylationELALRESSSPESFIT
HEEEECCCCCCHHCC		45.2029978859
492PhosphorylationLALRESSSPESFITE
EEEECCCCCCHHCCE		41.8029978859
493PhosphorylationALRESSSPESFITEE
EEECCCCCCHHCCEE		43.1032142685
495PhosphorylationRESSSPESFITEEVD
ECCCCCCHHCCEECC		25.9029978859
498PhosphorylationSSPESFITEEVDESS
CCCCHHCCEECCCCC		24.8827251275
502PhosphorylationSFITEEVDESSSPQQ
HHCCEECCCCCCCCC		54.0332142685
504PhosphorylationITEEVDESSSPQQGT
CCEECCCCCCCCCCC		31.4928450419
505PhosphorylationTEEVDESSSPQQGTR
CEECCCCCCCCCCCC		43.9528450419
506PhosphorylationEEVDESSSPQQGTRA
EECCCCCCCCCCCCH		35.6930278072
511PhosphorylationSSSPQQGTRAASIEN
CCCCCCCCCHHHHHH		16.8828450419
515 (in isoform 3)Phosphorylation-29.4725884760
515PhosphorylationQQGTRAASIENVLQD
CCCCCHHHHHHHHHC		29.4723927012
521 (in isoform 3)Phosphorylation-44.2328348404
522 (in isoform 3)Phosphorylation-47.0928348404
523PhosphorylationIENVLQDSSPEHCGR
HHHHHHCCCHHHCCC		34.5323401153
524PhosphorylationENVLQDSSPEHCGRG
HHHHHCCCHHHCCCC		42.4722167270
525 (in isoform 3)Phosphorylation-39.0228348404
531 (in isoform 3)Phosphorylation-20.1628348404
537 (in isoform 2)Phosphorylation-13.7425884760
543 (in isoform 2)Phosphorylation-31.0628348404
544 (in isoform 2)Phosphorylation-61.5528348404
547 (in isoform 2)Phosphorylation-27.5928348404
553 (in isoform 2)Phosphorylation-28348404
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 MGRN1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MGRN1_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 MGRN1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MSHR_HUMANMC1Rphysical
19737927
MC4R_HUMANMC4Rphysical
19737927
TS101_HUMANTSG101physical
17229889
MRAP_HUMANMRAPphysical
21862608
TS101_HUMANTSG101physical
19703557
UB2D1_HUMANUBE2D1physical
17229889
ITCH_HUMANITCHphysical
23253940
NEDD4_HUMANNEDD4physical
23253940
HSP74_HUMANHSPA4physical
23756845
TRI74_HUMANTRIM74physical
22493164
GDU1_ARATHGDU1physical
24036454
GDU2_ARATHGDU2physical
24036454
GDU3_ARATHGDU3physical
24036454
GDU5_ARATHGDU5physical
24036454
GDU7_ARATHGDU7physical
24036454
TBA4A_HUMANTUBA4Aphysical
24556679
ATX3_HUMANATXN3physical
24769000
HD_HUMANHTTphysical
24769000
APBB1_HUMANAPBB1physical
25342469
AMFR_HUMANAMFRphysical
26743086
ANR46_HUMANANKRD46physical
28514442
ATRN_HUMANATRNphysical
28514442
CI040_HUMANC9orf40physical
28514442
PDCD2_HUMANPDCD2physical
28514442
INT7_HUMANINTS7physical
28514442
TIM29_HUMANC19orf52physical
28514442
HSDL1_HUMANHSDL1physical
28514442
MEGF8_HUMANMEGF8physical
28514442
MFN1_HUMANMFN1physical
27713096
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 MGRN1_HUMAN

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Related Literatures of Post-Translational Modification
Myristoylation
ReferencePubMed
"Strategy for comprehensive identification of human N-myristoylatedproteins using an insect cell-free protein synthesis system.";
Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E.,Tsunasawa S., Utsumi T.;
Proteomics 10:1780-1793(2010).
Cited for: MYRISTOYLATION AT GLY-2.
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-524, AND MASSSPECTROMETRY.

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