MA2B1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MA2B1_HUMAN
• UniProt AC: O00754
• Protein Name: Lysosomal alpha-mannosidase
• Gene Name: MAN2B1
• Organism: Homo sapiens (Human).
• Sequence Length: 1011
• Subcellular Localization: Lysosome.
• Protein Description: Necessary for the catabolism of N-linked carbohydrates released during glycoprotein turnover. Cleaves all known types of alpha-mannosidic linkages..
• Protein Sequence: MGAYARASGVCARGCLDSAGPWTMSRALRPPLPPLCFFLLLLAAAGARAGGYETCPTVQPNMLNVHLLPHTHDDVGWLKTVDQYFYGIKNDIQHAGVQYILDSVISALLADPTRRFIYVEIAFFSRWWHQQTNATQEVVRDLVRQGRLEFANGGWVMNDEAATHYGAIVDQMTLGLRFLEDTFGNDGRPRVAWHIDPFGHSREQASLFAQMGFDGFFFGRLDYQDKWVRMQKLEMEQVWRASTSLKPPTADLFTGVLPNGYNPPRNLCWDVLCVDQPLVEDPRSPEYNAKELVDYFLNVATAQGRYYRTNHTVMTMGSDFQYENANMWFKNLDKLIRLVNAQQAKGSSVHVLYSTPACYLWELNKANLTWSVKHDDFFPYADGPHQFWTGYFSSRPALKRYERLSYNFLQVCNQLEALVGLAANVGPYGSGDSAPLNEAMAVLQHHDAVSGTSRQHVANDYARQLAAGWGPCEVLLSNALARLRGFKDHFTFCQQLNISICPLSQTAARFQVIVYNPLGRKVNWMVRLPVSEGVFVVKDPNGRTVPSDVVIFPSSDSQAHPPELLFSASLPALGFSTYSVAQVPRWKPQARAPQPIPRRSWSPALTIENEHIRATFDPDTGLLMEIMNMNQQLLLPVRQTFFWYNASIGDNESDQASGAYIFRPNQQKPLPVSRWAQIHLVKTPLVQEVHQNFSAWCSQVVRLYPGQRHLELEWSVGPIPVGDTWGKEVISRFDTPLETKGRFYTDSNGREILERRRDYRPTWKLNQTEPVAGNYYPVNTRIYITDGNMQLTVLTDRSQGGSSLRDGSLELMVHRRLLKDDGRGVSEPLMENGSGAWVRGRHLVLLDTAQAAAAGHRLLAEQEVLAPQVVLAPGGGAAYNLGAPPRTQFSGLRRDLPPSVHLLTLASWGPEMVLLRLEHQFAVGEDSGRNLSAPVTLNLRDLFSTFTITRLQETTLVANQLREAASRLKWTTNTGPTPHQTPYQLDPANITLEPMEIRTFLASVQWKEVDG

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
4	Phosphorylation	----MGAYARASGVC ----CCCCHHHCCCC	13.90	29978859
8	Phosphorylation	MGAYARASGVCARGC CCCCHHHCCCCCCCC	26.63	29978859
18	Phosphorylation	CARGCLDSAGPWTMS CCCCCHHCCCCCCHH	23.37	29978859
23	Phosphorylation	LDSAGPWTMSRALRP HHCCCCCCHHHHHCC	14.38	29978859
25	Phosphorylation	SAGPWTMSRALRPPL CCCCCCHHHHHCCCC	13.66	29978859
118	Phosphorylation	DPTRRFIYVEIAFFS CCCCCEEEEEHHHHH	6.85	-
133	N-linked_Glycosylation	RWWHQQTNATQEVVR HHHHHHCCCHHHHHH	36.33	UniProtKB CARBOHYD
226	Acetylation	GRLDYQDKWVRMQKL CCCCCCCCCHHHHHH	31.87	26822725
295	Phosphorylation	NAKELVDYFLNVATA CHHHHHHHHHHHHHH	11.50	-
301	Phosphorylation	DYFLNVATAQGRYYR HHHHHHHHHCCCEEE	18.41	24719451
310	N-linked_Glycosylation	QGRYYRTNHTVMTMG CCCEEECCCEEEECC	21.60	16399764
310	N-linked_Glycosylation	QGRYYRTNHTVMTMG CCCEEECCCEEEECC	21.60	16399764
334	Ubiquitination	MWFKNLDKLIRLVNA HHHHCHHHHHHHHHH	49.32	-
346 (in isoform 2)	Phosphorylation	-	28.33	-
347 (in isoform 2)	Phosphorylation	-	28.60	-
367	N-linked_Glycosylation	LWELNKANLTWSVKH EEECCCCCCEEEECC	39.34	19159218
450	Phosphorylation	LQHHDAVSGTSRQHV HHHCCCCCCCCHHHH	37.77	-
461	Phosphorylation	RQHVANDYARQLAAG HHHHHHHHHHHHHCC	11.95	20068231
497	N-linked_Glycosylation	FTFCQQLNISICPLS CHHHHHCCEEEECHH	22.94	UniProtKB CARBOHYD
645	N-linked_Glycosylation	RQTFFWYNASIGDNE HHEEEEEECCCCCCC	20.15	UniProtKB CARBOHYD
651	N-linked_Glycosylation	YNASIGDNESDQASG EECCCCCCCCCCCCC	45.52	UniProtKB CARBOHYD
692	N-linked_Glycosylation	LVQEVHQNFSAWCSQ HHHHHHHHHHHHHHH	20.26	UniProtKB CARBOHYD
704	Phosphorylation	CSQVVRLYPGQRHLE HHHCHHHCCCCCEEE	8.51	-
715	Phosphorylation	RHLELEWSVGPIPVG CEEEEEEECCCEECC	14.07	-
731	Phosphorylation	TWGKEVISRFDTPLE CCCHHHHHCCCCCCC	31.88	-
766	N-linked_Glycosylation	YRPTWKLNQTEPVAG CCCCCCCCCCCCCCC	42.89	19159218
832	N-linked_Glycosylation	VSEPLMENGSGAWVR CCCCCCCCCCCCEEC	35.65	UniProtKB CARBOHYD
904	Phosphorylation	PPSVHLLTLASWGPE CCCEEEEHHHHHCHH	27.00	19690332
907	Phosphorylation	VHLLTLASWGPEMVL EEEEHHHHHCHHHEE	35.36	-
930	N-linked_Glycosylation	VGEDSGRNLSAPVTL CCCCCCCCCCCCEEE	41.70	12754519
930	N-linked_Glycosylation	VGEDSGRNLSAPVTL CCCCCCCCCCCCEEE	41.70	12754519
936	Phosphorylation	RNLSAPVTLNLRDLF CCCCCCEEEEHHHHH	14.63	-
954	Phosphorylation	TITRLQETTLVANQL CEEEHHHHHHHHHHH	16.69	24719451
955	Phosphorylation	ITRLQETTLVANQLR EEEHHHHHHHHHHHH	20.62	24719451
977	O-linked_Glycosylation	WTTNTGPTPHQTPYQ CCCCCCCCCCCCCCC	34.45	OGP
989	N-linked_Glycosylation	PYQLDPANITLEPME CCCCCCCCCEECCCC	32.92	UniProtKB CARBOHYD

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

Oops, there are no upstream regulatory protein records of MA2B1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MA2B1_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 MA2B1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ATG7_HUMAN	ATG7	physical	22863883
LC7L2_HUMAN	LUC7L2	physical	22863883
SC24A_HUMAN	SEC24A	physical	22863883
GDE_HUMAN	AGL	physical	26344197
DTD1_HUMAN	DTD1	physical	26344197
LRC47_HUMAN	LRRC47	physical	26344197
NAGAB_HUMAN	NAGA	physical	26344197
SNX2_HUMAN	SNX2	physical	26344197

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 248500: Mannosidosis, alpha B, lysosomal (MANSA)
• 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

"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-367 AND ASN-766, AND MASSSPECTROMETRY.
PubMed: 19159218

"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry.";
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
Nat. Biotechnol. 21:660-666(2003).
Cited for: GLYCOSYLATION AT ASN-930.
PubMed: 12754519