MA1A1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MA1A1_HUMAN
• UniProt AC: P33908
• Protein Name: Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA
• Gene Name: MAN1A1
• Organism: Homo sapiens (Human).
• Sequence Length: 653
• Subcellular Localization: Golgi apparatus membrane; Single-pass type II membrane protein.
• Protein Description: Involved in the maturation of Asn-linked oligosaccharides. Progressively trim alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2)..
• Protein Sequence: MPVGGLLPLFSSPAGGVLGGGLGGGGGRKGSGPAALRLTEKFVLLLVFSAFITLCFGAIFFLPDSSKLLSGVLFHSSPALQPAADHKPGPGARAEDAAEGRARRREEGAPGDPEAALEDNLARIRENHERALREAKETLQKLPEEIQRDILLEKKKVAQDQLRDKAPFRGLPPVDFVPPIGVESREPADAAIREKRAKIKEMMKHAWNNYKGYAWGLNELKPISKGGHSSSLFGNIKGATIVDALDTLFIMEMKHEFEEAKSWVEENLDFNVNAEISVFEVNIRFVGGLLSAYYLSGEEIFRKKAVELGVKLLPAFHTPSGIPWALLNMKSGIGRNWPWASGGSSILAEFGTLHLEFMHLSHLSGNPIFAEKVMNIRTVLNKLEKPQGLYPNYLNPSSGQWGQHHVSVGGLGDSFYEYLLKAWLMSDKTDLEAKKMYFDAVQAIETHLIRKSSSGLTYIAEWKGGLLEHKMGHLTCFAGGMFALGADAAPEGMAQHYLELGAEIARTCHESYNRTFMKLGPEAFRFDGGVEAIATRQNEKYYILRPEVMETYMYMWRLTHDPKYRKWAWEAVEALENHCRVNGGYSGLRDVYLLHESYDDVQQSFFLAETLKYLYLIFSDDDLLPLEHWIFNSEAHLLPILPKDKKEVEIREE

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
11	Phosphorylation	GGLLPLFSSPAGGVL CCCCCCCCCCCCCCC	42.99	28450419
12	Phosphorylation	GLLPLFSSPAGGVLG CCCCCCCCCCCCCCC	16.07	21815630
31	Phosphorylation	GGGGRKGSGPAALRL CCCCCCCCCHHHHHH	44.64	22985185
76	O-linked_Glycosylation	LSGVLFHSSPALQPA HHHHHHCCCCCCCCC	30.59	OGP
77	O-linked_Glycosylation	SGVLFHSSPALQPAA HHHHHCCCCCCCCCC	12.96	OGP
138	O-linked_Glycosylation	ALREAKETLQKLPEE HHHHHHHHHHHCCHH	33.51	OGP
184	Phosphorylation	VPPIGVESREPADAA CCCCCCCCCCHHHHH	39.27	26699800
198	Acetylation	AIREKRAKIKEMMKH HHHHHHHHHHHHHHH	59.34	7960439
200	Acetylation	REKRAKIKEMMKHAW HHHHHHHHHHHHHHH	38.56	7960449
224	O-linked_Glycosylation	LNELKPISKGGHSSS CCCCCCCCCCCCCHH	33.50	OGP
231	Phosphorylation	SKGGHSSSLFGNIKG CCCCCCHHHCCCCCC	30.63	29759185
304	Ubiquitination	GEEIFRKKAVELGVK CHHHHHHHHHHHHCE	54.10	29967540
382	Ubiquitination	NIRTVLNKLEKPQGL CHHHHHHHCCCCCCC	54.59	29967540
435	Acetylation	KTDLEAKKMYFDAVQ CCCHHHHHHHHHHHH	45.97	7959763
453	Phosphorylation	THLIRKSSSGLTYIA HHHHHHCCCCCEEEE	31.31	28634120
454	Phosphorylation	HLIRKSSSGLTYIAE HHHHHCCCCCEEEEE	44.93	28634120
457	Phosphorylation	RKSSSGLTYIAEWKG HHCCCCCEEEEEECC	19.19	28634120
513	N-linked_Glycosylation	RTCHESYNRTFMKLG HHHHHHHCCHHHCCC	45.88	UniProtKB CARBOHYD
515	Phosphorylation	CHESYNRTFMKLGPE HHHHHCCHHHCCCCC	25.17	24719451
518	Ubiquitination	SYNRTFMKLGPEAFR HHCCHHHCCCCCCEE	46.21	-
535	Phosphorylation	GGVEAIATRQNEKYY CCEEEEEECCCCCEE	27.03	24719451

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

Oops, there are no upstream regulatory protein records of MA1A1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MA1A1_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 MA1A1_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of MA1A1_HUMAN !!

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

Phosphorylation

"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND MASSSPECTROMETRY.
PubMed: 19413330