MON1B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MON1B_HUMAN
• UniProt AC: Q7L1V2
• Protein Name: Vacuolar fusion protein MON1 homolog B
• Gene Name: MON1B
• Organism: Homo sapiens (Human).
• Sequence Length: 547
• Protein Sequence: MEVGGDTAAPAPGGAEDLEDTQFPSEEAREGGGVHAVPPDPEDEGLEETGSKDKDQPPSPSPPPQSEALSSTSRLWSPAAPENSPTCSPESSSGGQGGDPSDEEWRSQRKHVFVLSEAGKPIYSRYGSVEALSATMGVMTALVSFVQSAGDAIRAIYAEDHKLVFLQQGPLLLVAMSRTSQSAAQLRGELLAVHAQIVSTLTRASVARIFAHKQNYDLRRLLAGSERTLDRLLDSMEQDPGALLLGAVRCVPLARPLRDALGALLRRCTAPGLALSVLAVGGRLITAAQERNVLAECRLDPADLQLLLDWVGAPAFAAGEAWAPVCLPRFNPDGFFYAYVARLDAMPVCLLLLGTQREAFHAMAACRRLVEDGMHALGAMRALGEAASFSNASSASAPAYSVQAVGAPGLRHFLYKPLDIPDHHRQLPQFTSPELEAPYSREEERQRLSDLYHRLHARLHSTSRPLRLIYHVAEKETLLAWVTSKFELYTCLSPLVTKAGAILVVTKLLRWVKKEEDRLFIRYPPKYSTPPATSTDQAAHNGLFTGL

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	-------MEVGGDTA -------CCCCCCCC	9.45	22814378
49	Phosphorylation	EDEGLEETGSKDKDQ HCCCCCCCCCCCCCC	37.06	28111955
51	Phosphorylation	EGLEETGSKDKDQPP CCCCCCCCCCCCCCC	45.13	23312004
59	Phosphorylation	KDKDQPPSPSPPPQS CCCCCCCCCCCCCHH	44.70	29255136
61	Phosphorylation	KDQPPSPSPPPQSEA CCCCCCCCCCCHHHH	55.14	29255136
66	Phosphorylation	SPSPPPQSEALSSTS CCCCCCHHHHCCCCC	30.52	23927012
67	Ubiquitination	PSPPPQSEALSSTSR CCCCCHHHHCCCCCC	48.67	-
70	Phosphorylation	PPQSEALSSTSRLWS CCHHHHCCCCCCCCC	38.32	23927012
71	Phosphorylation	PQSEALSSTSRLWSP CHHHHCCCCCCCCCC	31.11	23927012
72	Phosphorylation	QSEALSSTSRLWSPA HHHHCCCCCCCCCCC	17.94	23927012
73	Phosphorylation	SEALSSTSRLWSPAA HHHCCCCCCCCCCCC	27.59	23927012
84	Phosphorylation	SPAAPENSPTCSPES CCCCCCCCCCCCCCC	21.66	26074081
86	Phosphorylation	AAPENSPTCSPESSS CCCCCCCCCCCCCCC	25.99	26074081
88	Phosphorylation	PENSPTCSPESSSGG CCCCCCCCCCCCCCC	33.89	26074081
91	Phosphorylation	SPTCSPESSSGGQGG CCCCCCCCCCCCCCC	32.94	27251275
92	Phosphorylation	PTCSPESSSGGQGGD CCCCCCCCCCCCCCC	31.19	28348404
93	Phosphorylation	TCSPESSSGGQGGDP CCCCCCCCCCCCCCC	57.11	-
110	Ubiquitination	EEWRSQRKHVFVLSE HHHHHHCCEEEEECC	36.16	-
124	Phosphorylation	EAGKPIYSRYGSVEA CCCCCHHHCCCCHHH	21.53	24719451
213	Ubiquitination	VARIFAHKQNYDLRR HHHHHHHHCCCCHHH	36.49	-
225	Phosphorylation	LRRLLAGSERTLDRL HHHHHHCCHHHHHHH	20.49	22210691
270	Ubiquitination	ALLRRCTAPGLALSV HHHHHCCCCCHHHHH	10.37	-
416	Ubiquitination	GLRHFLYKPLDIPDH CHHHHHCCCCCCCHH	41.05	-
528	Phosphorylation	IRYPPKYSTPPATST EECCCCCCCCCCCCC	40.33	25627689
529	Phosphorylation	RYPPKYSTPPATSTD ECCCCCCCCCCCCCC	30.15	25159151

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

Oops, there are no upstream regulatory protein records of MON1B_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MON1B_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 MON1B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RABX5_HUMAN	RABGEF1	physical	20434987
VPS18_HUMAN	VPS18	physical	20434987
VPS11_HUMAN	VPS11	physical	20434987
VPS16_HUMAN	VPS16	physical	20434987
VP33A_HUMAN	VPS33A	physical	20434987
VPS41_HUMAN	VPS41	physical	20434987

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