MARH1_HUMAN - dbPTM
MARH1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MARH1_HUMAN
UniProt AC Q8TCQ1
Protein Name E3 ubiquitin-protein ligase MARCH1
Gene Name 1-Mar
Organism Homo sapiens (Human).
Sequence Length 289
Subcellular Localization Golgi apparatus, trans-Golgi network membrane
Multi-pass membrane protein . Lysosome membrane
Multi-pass membrane protein . Cytoplasmic vesicle membrane
Multi-pass membrane protein . Late endosome membrane
Multi-pass membrane protein . Early endos
Protein Description E3 ubiquitin-protein ligase that mediates ubiquitination of TFRC, CD86, FAS and MHC class II proteins, such as HLA-DR alpha and beta, and promotes their subsequent endocytosis and sorting to lysosomes via multivesicular bodies. By constitutively ubiquitinating MHC class II proteins in immature dendritic cells, down-regulates their cell surface localization thus sequestering them in the intracellular endosomal system..
Protein Sequence MLGWCEAIARNPHRIPNNTRTPEISGDLADASQTSTLNEKSPGRSASRSSNISKASSPTTGTAPRSQSRLSVCPSTQDICRICHCEGDEESPLITPCRCTGTLRFVHQSCLHQWIKSSDTRCCELCKYDFIMETKLKPLRKWEKLQMTTSERRKIFCSVTFHVIAITCVVWSLYVLIDRTAEEIKQGNDNGVLEWPFWTKLVVVAIGFTGGLVFMYVQCKVYVQLWRRLKAYNRVIFVQNCPDTAKKLEKNFSCNVNTDIKDAVVVPVPQTGANSLPSAEGGPPEVVSV
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
20 (in isoform 2)Phosphorylation-50.8622985185
21 (in isoform 2)Phosphorylation-24.2022985185
45PhosphorylationNEKSPGRSASRSSNI
CCCCCCCCCCCCCCC
36.1920068231
47PhosphorylationKSPGRSASRSSNISK
CCCCCCCCCCCCCCC
33.6620068231
49PhosphorylationPGRSASRSSNISKAS
CCCCCCCCCCCCCCC
25.8220068231
50PhosphorylationGRSASRSSNISKASS
CCCCCCCCCCCCCCC
36.7530576142
53PhosphorylationASRSSNISKASSPTT
CCCCCCCCCCCCCCC
26.8120068231
56PhosphorylationSSNISKASSPTTGTA
CCCCCCCCCCCCCCC
40.3623403867
57PhosphorylationSNISKASSPTTGTAP
CCCCCCCCCCCCCCC
31.0023403867
59PhosphorylationISKASSPTTGTAPRS
CCCCCCCCCCCCCCC
39.5423403867
60PhosphorylationSKASSPTTGTAPRSQ
CCCCCCCCCCCCCCC
35.6020068231
62PhosphorylationASSPTTGTAPRSQSR
CCCCCCCCCCCCCCC
31.2529449344
66PhosphorylationTTGTAPRSQSRLSVC
CCCCCCCCCCCCEEC
31.3030377224
68PhosphorylationGTAPRSQSRLSVCPS
CCCCCCCCCCEECCC
36.1130377224
71PhosphorylationPRSQSRLSVCPSTQD
CCCCCCCEECCCCCC
22.1424719451
158O-linked_GlycosylationERRKIFCSVTFHVIA
HHHHHHHHHHHHHHH
17.2829351928
160PhosphorylationRKIFCSVTFHVIAIT
HHHHHHHHHHHHHHH
7.54-
160O-linked_GlycosylationRKIFCSVTFHVIAIT
HHHHHHHHHHHHHHH
7.5429351928
271PhosphorylationVVVPVPQTGANSLPS
EEEECCCCCCCCCCC
31.9923532336
275PhosphorylationVPQTGANSLPSAEGG
CCCCCCCCCCCCCCC
40.9223532336

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 MARH1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MARH1_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 MARH1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
2B1F_HUMANHLA-DRB1physical
23264739
2B13_HUMANHLA-DRB1physical
23264739
2B1G_HUMANHLA-DRB1physical
23264739
DRA_HUMANHLA-DRAphysical
23264739
TFR1_HUMANTFRCphysical
23606747
UBE2H_HUMANUBE2Hphysical
14722266
UB2R1_HUMANCDC34physical
14722266
UB2D1_HUMANUBE2D1physical
14722266
INSR_HUMANINSRphysical
27577745

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MARH1_HUMAN

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Related Literatures of Post-Translational Modification

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