MDGA1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MDGA1_HUMAN
• UniProt AC: Q8NFP4
• Protein Name: MAM domain-containing glycosylphosphatidylinositol anchor protein 1
• Gene Name: MDGA1
• Organism: Homo sapiens (Human).
• Sequence Length: 955
• Subcellular Localization: Cell membrane ; Lipid-anchor, GPI-anchor . Associated with lipid rafts.
• Protein Description: Required for radial migration of cortical neurons in the superficial layer of the neocortex (By similarity). Plays a role in the formation or maintenance of inhibitory synapses. May function by inhibiting the activity of NLGN2..
• Protein Sequence: MEVTCLLLLALIPFHCRGQGVYAPAQAQIVHAGQACVVKEDNISERVYTIREGDTLMLQCLVTGHPRPQVRWTKTAGSASDKFQETSVFNETLRIERIARTQGGRYYCKAENGVGVPAIKSIRVDVQYLDEPMLTVHQTVSDVRGNFYQEKTVFLRCTVNSNPPARFIWKRGSDTLSHSQDNGVDIYEPLYTQGETKVLKLKNLRPQDYASYTCQVSVRNVCGIPDKAITFRLTNTTAPPALKLSVNETLVVNPGENVTVQCLLTGGDPLPQLQWSHGPGPLPLGALAQGGTLSIPSVQARDSGYYNCTATNNVGNPAKKTVNLLVRSMKNATFQITPDVIKESENIQLGQDLKLSCHVDAVPQEKVTYQWFKNGKPARMSKRLLVTRNDPELPAVTSSLELIDLHFSDYGTYLCMASFPGAPVPDLSVEVNISSETVPPTISVPKGRAVVTVREGSPAELQCEVRGKPRPPVLWSRVDKEAALLPSGLPLEETPDGKLRLERVSRDMSGTYRCQTARYNGFNVRPREAQVQLNVQFPPEVEPSSQDVRQALGRPVLLRCSLLRGSPQRIASAVWRFKGQLLPPPPVVPAAAEAPDHAELRLDAVTRDSSGSYECSVSNDVGSAACLFQVSAKAYSPEFYFDTPNPTRSHKLSKNYSYVLQWTQREPDAVDPVLNYRLSIRQLNQHNAVVKAIPVRRVEKGQLLEYILTDLRVPHSYEVRLTPYTTFGAGDMASRIIHYTEPINSPNLSDNTCHFEDEKICGYTQDLTDNFDWTRQNALTQNPKRSPNTGPPTDISGTPEGYYMFIETSRPRELGDRARLVSPLYNASAKFYCVSFFYHMYGKHIGSLNLLVRSRNKGALDTHAWSLSGNKGNVWQQAHVPISPSGPFQIIFEGVRGPGYLGDIAIDDVTLKKGECPRKQTDPNKVVVMPGSGAPCQSSPQLWGPMAIFLLALQR

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
42	N-linked_Glycosylation	ACVVKEDNISERVYT EEEEECCCCCCCEEE	40.55	UniProtKB CARBOHYD
49	Phosphorylation	NISERVYTIREGDTL CCCCCEEEEECCCEE	15.65	24719451
90	N-linked_Glycosylation	FQETSVFNETLRIER HCCCHHHCCCEEEEE	38.91	UniProtKB CARBOHYD
158	Phosphorylation	KTVFLRCTVNSNPPA EEEEEEEECCCCCCC	19.11	17929957
161	Phosphorylation	FLRCTVNSNPPARFI EEEEECCCCCCCEEE	46.51	17929957
235	N-linked_Glycosylation	AITFRLTNTTAPPAL EEEEEEECCCCCCCE	39.77	UniProtKB CARBOHYD
247	N-linked_Glycosylation	PALKLSVNETLVVNP CCEEEEECCEEEECC	32.91	16335952
257	N-linked_Glycosylation	LVVNPGENVTVQCLL EEECCCCCEEEEEEE	40.45	UniProtKB CARBOHYD
307	N-linked_Glycosylation	ARDSGYYNCTATNNV CCCCCCEECCCCCCC	14.26	UniProtKB CARBOHYD
331	N-linked_Glycosylation	LLVRSMKNATFQITP HHHHHHCCCEEEECH	35.25	UniProtKB CARBOHYD
432	N-linked_Glycosylation	PDLSVEVNISSETVP CCCEEEEECCCCCCC	18.21	UniProtKB CARBOHYD
443	Phosphorylation	ETVPPTISVPKGRAV CCCCCEEEECCCEEE	34.54	24719451
457	Phosphorylation	VVTVREGSPAELQCE EEEEECCCCCEEEEE	19.04	23401153
635	Phosphorylation	FQVSAKAYSPEFYFD EEEECCCCCCCEECC	24.85	-
636	Phosphorylation	QVSAKAYSPEFYFDT EEECCCCCCCEECCC	23.86	-
640	Phosphorylation	KAYSPEFYFDTPNPT CCCCCCEECCCCCCC	10.01	-
643	Phosphorylation	SPEFYFDTPNPTRSH CCCEECCCCCCCCCC	18.31	-
655	N-linked_Glycosylation	RSHKLSKNYSYVLQW CCCCCCCCEEEEEEE	27.83	UniProtKB CARBOHYD
656	Phosphorylation	SHKLSKNYSYVLQWT CCCCCCCEEEEEEEE	12.71	24043423
657	Phosphorylation	HKLSKNYSYVLQWTQ CCCCCCEEEEEEEEC	20.40	24043423
658	Phosphorylation	KLSKNYSYVLQWTQR CCCCCEEEEEEEECC	8.53	24043423
663	Phosphorylation	YSYVLQWTQREPDAV EEEEEEEECCCCCCC	12.56	24043423
747	N-linked_Glycosylation	TEPINSPNLSDNTCH CCCCCCCCCCCCCCC	52.58	UniProtKB CARBOHYD
786	Phosphorylation	LTQNPKRSPNTGPPT HHCCCCCCCCCCCCC	28.73	24275569
789	Phosphorylation	NPKRSPNTGPPTDIS CCCCCCCCCCCCCCC	55.22	24275569
796	Phosphorylation	TGPPTDISGTPEGYY CCCCCCCCCCCCEEE	39.15	24275569
798	Phosphorylation	PPTDISGTPEGYYMF CCCCCCCCCCEEEEE	16.04	24275569
802	Phosphorylation	ISGTPEGYYMFIETS CCCCCCEEEEEEECC	7.06	24275569
803	Phosphorylation	SGTPEGYYMFIETSR CCCCCEEEEEEECCC	9.08	-
808	Phosphorylation	GYYMFIETSRPRELG EEEEEEECCCCHHHC	25.81	22210691
809	Phosphorylation	YYMFIETSRPRELGD EEEEEECCCCHHHCH	27.74	22210691
822	Phosphorylation	GDRARLVSPLYNASA CHHHHHHHHHCHHCC	17.49	29083192
825	Phosphorylation	ARLVSPLYNASAKFY HHHHHHHCHHCCHHH	16.44	29083192
826	N-linked_Glycosylation	RLVSPLYNASAKFYC HHHHHHCHHCCHHHH	34.79	UniProtKB CARBOHYD
828	Phosphorylation	VSPLYNASAKFYCVS HHHHCHHCCHHHHHH	28.49	29083192
932	GPI-anchor	KVVVMPGSGAPCQSS CEEEECCCCCCCCCC	26.38	-
939	Phosphorylation	SGAPCQSSPQLWGPM CCCCCCCCCCHHHHH	7.26	-
948 (in isoform 2)	Phosphorylation	-	1.71	-

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

Oops, there are no upstream regulatory protein records of MDGA1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MDGA1_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 MDGA1_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of MDGA1_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

N-linked Glycosylation

"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-247, AND MASSSPECTROMETRY.
PubMed: 16335952