MGRN1_MOUSE - dbPTM
MGRN1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MGRN1_MOUSE
UniProt AC Q9D074
Protein Name E3 ubiquitin-protein ligase MGRN1
Gene Name Mgrn1
Organism Mus musculus (Mouse).
Sequence Length 532
Subcellular Localization Early endosome . The endosomal localization is dependent on the interaction with TSG101..
Isoform 1: Cytoplasm. Cell membrane.
Isoform 5: Cytoplasm. Nucleus. In the cytoplasm, predominantly localized to the perinuclear region and discrete vesi
Protein Description E3 ubiquitin-protein ligase. Mediates TSG101 monoubiquitination at multiple sites. 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 (By similarity). Acts also as a negative regulator of hedgehog signaling. [PubMed: 29290584]
Protein Sequence MGSILSRRIAGVEDIDIQANSAYRYPPKSGNYFASHFFMGGEKFDTPHPEGYLFGENMDLNFLGSRPVQFPYVTPAPHEPVKTLRSLVNIRKDSLRLVRYKEDADSPTEDGEKPRVLYSLEFTFDADARVAITIYCQAVEELVNGVAVYSCKNPSLQSETVHYKRGVSQQFSLPSFKIDFSEWKDDELNFDLDRGVFPVVIQAVVDEGDVVEVTGHAHVLLAAFEKHVDGSFSVKPLKQKQIVDRVSYLLQEIYGIENKNNQETKPSDDENSDNSSECVVCLSDLRDTLILPCRHLCLCTSCADTLRYQANNCPICRLPFRALLQIRAVRKKPGALSPISFSPVLAQSVDHDEHSSSDSIPPGYEPISLLEALNGLRAVSPAIPSAPLYEEITYSGISDGLSQASCPLAGLDRIMESGLQKGKTQSKSPDSTLRSPSFPIHEEDEEKLSEDSDAPLPPSGVELVLRESSSPESFGTEEGDEPSLKQGSRVPSIDDVLQDGSPQHHGCSQPVPPADIYLPALGPESCSVGIEE
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
24.32-
74PhosphorylationPVQFPYVTPAPHEPV
CCCCCCCCCCCCCCH
14.1121930439
100PhosphorylationDSLRLVRYKEDADSP
HHEEEEEEHHCCCCC
15.9630635358
101UbiquitinationSLRLVRYKEDADSPT
HEEEEEEHHCCCCCC
38.2622790023
101 (in isoform 5)Ubiquitination-38.2622790023
102UbiquitinationLRLVRYKEDADSPTE
EEEEEEHHCCCCCCC
49.8827667366
106PhosphorylationRYKEDADSPTEDGEK
EEHHCCCCCCCCCCC
35.1325521595
108PhosphorylationKEDADSPTEDGEKPR
HHCCCCCCCCCCCCE
51.1425521595
164UbiquitinationQSETVHYKRGVSQQF
CCCEEEECCCCCCCC
28.0022790023
164 (in isoform 5)Ubiquitination-28.0022790023
165UbiquitinationSETVHYKRGVSQQFS
CCEEEECCCCCCCCC
43.5127667366
235 (in isoform 5)Ubiquitination-43.3522790023
235UbiquitinationVDGSFSVKPLKQKQI
CCCCCCCCCCCHHHH
43.3522790023
337 (in isoform 4)Phosphorylation-21.4729899451
337 (in isoform 5)Phosphorylation-21.4729899451
363 (in isoform 4)Phosphorylation-33.8025338131
363 (in isoform 5)Phosphorylation-33.8025338131
377 (in isoform 5)Phosphorylation-34.0529899451
377 (in isoform 4)Phosphorylation-34.0529899451
379 (in isoform 5)Phosphorylation-5.9529899451
379 (in isoform 4)Phosphorylation-5.9529899451
380PhosphorylationLNGLRAVSPAIPSAP
HHCHHCCCCCCCCCC
13.9729899451
381 (in isoform 5)Phosphorylation-27.8429899451
381 (in isoform 4)Phosphorylation-27.8429899451
389PhosphorylationAIPSAPLYEEITYSG
CCCCCCCCEECEECC
15.5118563927
394PhosphorylationPLYEEITYSGISDGL
CCCEECEECCCCCCC
15.5715592455
426PhosphorylationLQKGKTQSKSPDSTL
HHCCCCCCCCCCCCC
40.0925777480
428PhosphorylationKGKTQSKSPDSTLRS
CCCCCCCCCCCCCCC
38.9025521595
429 (in isoform 2)Phosphorylation-43.2219144319
431PhosphorylationTQSKSPDSTLRSPSF
CCCCCCCCCCCCCCC
32.5022324799
432PhosphorylationQSKSPDSTLRSPSFP
CCCCCCCCCCCCCCC
33.3026643407
435PhosphorylationSPDSTLRSPSFPIHE
CCCCCCCCCCCCCCH
28.1926643407
437PhosphorylationDSTLRSPSFPIHEED
CCCCCCCCCCCCHHH
44.9225521595
449PhosphorylationEEDEEKLSEDSDAPL
HHHHHHHCCCCCCCC
50.8821183079
452PhosphorylationEEKLSEDSDAPLPPS
HHHHCCCCCCCCCCC
31.4621183079
459PhosphorylationSDAPLPPSGVELVLR
CCCCCCCCCCEEEEE
54.2325293948
468PhosphorylationVELVLRESSSPESFG
CEEEEECCCCCHHCC
29.6723737553
469PhosphorylationELVLRESSSPESFGT
EEEEECCCCCHHCCC
45.2023737553
470PhosphorylationLVLRESSSPESFGTE
EEEECCCCCHHCCCC
41.8025521595
473PhosphorylationRESSSPESFGTEEGD
ECCCCCHHCCCCCCC
32.1523737553
476PhosphorylationSSPESFGTEEGDEPS
CCCHHCCCCCCCCCC
28.9323737553
483PhosphorylationTEEGDEPSLKQGSRV
CCCCCCCCCCCCCCC
46.2630352176
492PhosphorylationKQGSRVPSIDDVLQD
CCCCCCCCHHHHHCC
35.4722807455
501PhosphorylationDDVLQDGSPQHHGCS
HHHHCCCCCCCCCCC
29.6722807455

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_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MGRN1_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TS101_MOUSETsg101physical
19703557
MGRN1_MOUSEMgrn1physical
12560552
AMFR_MOUSEAmfrphysical
26743086
MFN1_MOUSEMfn1physical
27713096

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MGRN1_MOUSE

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Related Literatures of Post-Translational Modification

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