MARHA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MARHA_HUMAN
• UniProt AC: Q8NA82
• Protein Name: Probable E3 ubiquitin-protein ligase MARCH10
• Gene Name: 10-Mar
• Organism: Homo sapiens (Human).
• Sequence Length: 808
• Protein Description: E3 ubiquitin-protein ligase (Probable). E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates..
• Protein Sequence: MLHDARDRQKFFSDVQYLRDMQHKVDSEYQACLRRQEYRRDPNEKKRDQFWGQETSFERSRFSSRSSSKQSSSEEDALTEPRSSIKISAFKCDSKLPAIDQTSVKQKHKSTMTVRKAEKVDPSEPSPADQAPMVLLRKRKPNLRRFTVSPESHSPRASGDRSRQKQQWPAKVPVPRGADQVVQQEGLMCNTKLKRPNQERRNLVPSSQPMTENAPDRAKKGDPSAPSQSELHPALSQAFQGKNSPQVLSEFSGPPLTPTTVGGPRKASFRFRDEDFYSILSLNSRRESDDTEEETQSEECLWVGVRSPCSPSHHKRSRFGGTSTPQAKNKNFEENAENCRGHSSRRSEPSHGSLRISNAMEPATERPSAGQRLSQDPGLPDRESATEKDRGGSENAKKSPLSWDTKSEPRQEVGVNAENVWSDCISVEHRPGTHDSEGYWKDYLNSSQNSLDYFISGRPISPRSSVNSSYNPPASFMHSALRDDIPVDLSMSSTSVHSSDSEGNSGFHVCQPLSPIRNRTPFASAENHNYFPVNSAHEFAVREAEDTTLTSQPQGAPLYTDLLLNPQGNLSLVDSSSSSPSRMNSEGHLHVSGSLQENTPFTFFAVSHFPNQNDNGSRMAASGFTDEKETSKIKADPEKLKKLQESLLEEDSEEEGDLCRICQIAGGSPSNPLLEPCGCVGSLQFVHQECLKKWLKVKITSGADLGAVKTCEMCKQGLLVDLGDFNMIEFYQKHQQSQAQNELMNSGLYLVLLLHLYEQRFAELMRLNHNQVERERLSRNYPQPRTEENENSELGDGNEGSISQSQVV

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
1	Acetylation	-------MLHDARDR -------CCCCHHHH	7.28	-
27	Phosphorylation	DMQHKVDSEYQACLR HHHHHHCHHHHHHHH	40.99	-
55	Phosphorylation	DQFWGQETSFERSRF HHCCCCCCHHHHHHH	30.72	25693802
56	Phosphorylation	QFWGQETSFERSRFS HCCCCCCHHHHHHHC	25.10	25693802
64	Phosphorylation	FERSRFSSRSSSKQS HHHHHHCCCCCCCCC	33.21	-
69	Acetylation	FSSRSSSKQSSSEED HCCCCCCCCCCCHHH	57.03	22424773
72	Phosphorylation	RSSSKQSSSEEDALT CCCCCCCCCHHHHHC	39.00	-
83	O-linked_Glycosylation	DALTEPRSSIKISAF HHHCCCHHHCEEEEE	47.32	30379171
83	Phosphorylation	DALTEPRSSIKISAF HHHCCCHHHCEEEEE	47.32	30622161
84	Phosphorylation	ALTEPRSSIKISAFK HHCCCHHHCEEEEEE	29.22	30622161
88	O-linked_Glycosylation	PRSSIKISAFKCDSK CHHHCEEEEEECCCC	23.73	30379171
94	Phosphorylation	ISAFKCDSKLPAIDQ EEEEECCCCCCCCCC	45.63	30622161
102	Phosphorylation	KLPAIDQTSVKQKHK CCCCCCCCCCCHHCC	31.57	30622161
103	Phosphorylation	LPAIDQTSVKQKHKS CCCCCCCCCCHHCCC	22.99	30622161
110	Phosphorylation	SVKQKHKSTMTVRKA CCCHHCCCCEEEEEE	24.11	27251275
113	Phosphorylation	QKHKSTMTVRKAEKV HHCCCCEEEEEEEEC	19.76	27251275
206	Phosphorylation	ERRNLVPSSQPMTEN HHCCCCCCCCCCCCC	33.84	22210691
207	Phosphorylation	RRNLVPSSQPMTENA HCCCCCCCCCCCCCC	32.03	22210691
211	Phosphorylation	VPSSQPMTENAPDRA CCCCCCCCCCCCCHH	32.54	22210691
291	Phosphorylation	SRRESDDTEEETQSE CCCCCCCCCHHHHHC	50.73	-
307	Phosphorylation	CLWVGVRSPCSPSHH EEEEECCCCCCCCCC	28.05	-
399	Phosphorylation	GSENAKKSPLSWDTK CCCCCCCCCCCCCCC	30.30	29083192
402	Phosphorylation	NAKKSPLSWDTKSEP CCCCCCCCCCCCCCC	26.70	29083192
405	Phosphorylation	KSPLSWDTKSEPRQE CCCCCCCCCCCCCHH	30.16	29083192
407	Phosphorylation	PLSWDTKSEPRQEVG CCCCCCCCCCCHHCC	55.73	29083192
433	Phosphorylation	SVEHRPGTHDSEGYW EEECCCCCCCCCCHH	25.78	-
436	Phosphorylation	HRPGTHDSEGYWKDY CCCCCCCCCCHHHHH	25.89	-
456	Phosphorylation	NSLDYFISGRPISPR CCCCEEECCCCCCCC	20.89	24719451
778	Phosphorylation	QVERERLSRNYPQPR HHHHHHHHHCCCCCC	25.38	24719451

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of MARHA_HUMAN !!

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of MARHA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049

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.

Related Literatures of Post-Translational Modification

Acetylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
PubMed: 19413330