dbPTM

MA2A1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MA2A1_HUMAN
UniProt AC	Q16706
Protein Name	Alpha-mannosidase 2
Gene Name	MAN2A1
Organism	Homo sapiens (Human).
Sequence Length	1144
Subcellular Localization	Golgi apparatus membrane Single-pass type II membrane protein .
Protein Description	Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans; the final hydrolytic step in the N-glycan maturation pathway..
Protein Sequence	MKLSRQFTVFGSAIFCVVIFSLYLMLDRGHLDYPRNPRREGSFPQGQLSMLQEKIDHLERLLAENNEIISNIRDSVINLSESVEDGPKSSQSNFSQGAGSHLLPSQLSLSVDTADCLFASQSGSHNSDVQMLDVYSLISFDNPDGGVWKQGFDITYESNEWDTEPLQVFVVPHSHNDPGWLKTFNDYFRDKTQYIFNNMVLKLKEDSRRKFIWSEISYLSKWWDIIDIQKKDAVKSLIENGQLEIVTGGWVMPDEATPHYFALIDQLIEGHQWLENNIGVKPRSGWAIDPFGHSPTMAYLLNRAGLSHMLIQRVHYAVKKHFALHKTLEFFWRQNWDLGSVTDILCHMMPFYSYDIPHTCGPDPKICCQFDFKRLPGGRFGCPWGVPPETIHPGNVQSRARMLLDQYRKKSKLFRTKVLLAPLGDDFRYCEYTEWDLQFKNYQQLFDYMNSQSKFKVKIQFGTLSDFFDALDKADETQRDKGQSMFPVLSGDFFTYADRDDHYWSGYFTSRPFYKRMDRIMESHLRAAEILYYFALRQAHKYKINKFLSSSLYTALTEARRNLGLFQHHDAITGTAKDWVVVDYGTRLFHSLMVLEKIIGNSAFLLILKDKLTYDSYSPDTFLEMDLKQKSQDSLPQKNIIRLSAEPRYLVVYNPLEQDRISLVSVYVSSPTVQVFSASGKPVEVQVSAVWDTANTISETAYEISFRAHIPPLGLKVYKILESASSNSHLADYVLYKNKVEDSGIFTIKNMINTEEGITLENSFVLLRFDQTGLMKQMMTKEDGKHHEVNVQFSWYGTTIKRDKSGAYLFLPDGNAKPYVYTTPPFVRVTHGRIYSEVTCFFDHVTHRVRLYHIQGIEGQSVEVSNIVDIRKVYNREIAMKISSDIKSQNRFYTDLNGYQIQPRMTLSKLPLQANVYPMTTMAYIQDAKHRLTLLSAQSLGVSSLNSGQIEVIMDRRLMQDDNRGLEQGIQDNKITANLFRILLEKRSAVNTEEEKKSVSYPSLLSHITSSLMNHPVIPMANKFSSPTLELQGEFSPLQSSLPCDIHLVNLRTIQSKVGNGHSNEAALILHRKGFDCRFSSKGTGLFCSTTQGKILVQKLLNKFIVESLTPSSLSLMHSPPGTQNISEINLSPMEISTFRIQLR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
33	Phosphorylation	LDRGHLDYPRNPRRE HHCCCCCCCCCCCCC	15.51	-
42	O-linked_Glycosylation	RNPRREGSFPQGQLS CCCCCCCCCCHHHHH	29.06	OGP
70	Phosphorylation	AENNEIISNIRDSVI HHCCHHHHHHHHHHH	31.68	24719451
75	Phosphorylation	IISNIRDSVINLSES HHHHHHHHHHCCCCC	18.30	24275569
78	N-linked_Glycosylation	NIRDSVINLSESVED HHHHHHHCCCCCCCC	35.05	16335952
80	Phosphorylation	RDSVINLSESVEDGP HHHHHCCCCCCCCCC	24.28	23911959
82	Phosphorylation	SVINLSESVEDGPKS HHHCCCCCCCCCCCC	27.68	21082442
93	N-linked_Glycosylation	GPKSSQSNFSQGAGS CCCCCCCCCCCCCCC	32.71	UniProtKB CARBOHYD
105	O-linked_Glycosylation	AGSHLLPSQLSLSVD CCCCCCCCCEECEEE	43.66	55823709
192	Phosphorylation	NDYFRDKTQYIFNNM HHHHCCHHHHHHHCE	30.78	24719451
194	Phosphorylation	YFRDKTQYIFNNMVL HHCCHHHHHHHCEEE	16.83	24719451
207	Phosphorylation	VLKLKEDSRRKFIWS EEEECHHHHCHHHHH	34.77	30576142
218	Phosphorylation	FIWSEISYLSKWWDI HHHHHHHHHHHHHHH	22.21	-
307	Phosphorylation	LLNRAGLSHMLIQRV HHHHCCHHHHHHHHH	13.11	24719451
373	Ubiquitination	ICCQFDFKRLPGGRF EEEEEECCCCCCCCC	55.67	-
407	Phosphorylation	ARMLLDQYRKKSKLF HHHHHHHHHHHCHHC	24.86	19845377
417	2-Hydroxyisobutyrylation	KSKLFRTKVLLAPLG HCHHCCCEEEEEECC	26.99	-
442	Phosphorylation	WDLQFKNYQQLFDYM HHHHCCCHHHHHHHH	9.75	-
473	Ubiquitination	DFFDALDKADETQRD HHHHHHHHCCHHHHH	59.60	29967540
484	Phosphorylation	TQRDKGQSMFPVLSG HHHHHCCCCCCEECC	30.93	29759185
490	Phosphorylation	QSMFPVLSGDFFTYA CCCCCEECCCEEEEC	36.23	29759185
509	Phosphorylation	HYWSGYFTSRPFYKR CCCCCCCCCCHHHHH	18.49	-
514	Phosphorylation	YFTSRPFYKRMDRIM CCCCCHHHHHHHHHH	10.60	-
523	Phosphorylation	RMDRIMESHLRAAEI HHHHHHHHHHHHHHH	15.50	26074081
532	Phosphorylation	LRAAEILYYFALRQA HHHHHHHHHHHHHHH	11.38	-
533	Phosphorylation	RAAEILYYFALRQAH HHHHHHHHHHHHHHH	4.48	-
614	Phosphorylation	ILKDKLTYDSYSPDT EECCCCCCCCCCCCC	17.21	30576142
618	Phosphorylation	KLTYDSYSPDTFLEM CCCCCCCCCCCCHHH	21.91	30576142
621	Phosphorylation	YDSYSPDTFLEMDLK CCCCCCCCCHHHCCC	33.24	30576142
716	Ubiquitination	HIPPLGLKVYKILES CCCCCCHHHHHHHHH	41.54	-
723	Phosphorylation	KVYKILESASSNSHL HHHHHHHHHCCCCCH	29.97	21712546
733	Phosphorylation	SNSHLADYVLYKNKV CCCCHHCEEEECCCC	6.17	21712546
737	Ubiquitination	LADYVLYKNKVEDSG HHCEEEECCCCCCCC	46.24	29967540
739	2-Hydroxyisobutyrylation	DYVLYKNKVEDSGIF CEEEECCCCCCCCCE	42.73	-
739	Ubiquitination	DYVLYKNKVEDSGIF CEEEECCCCCCCCCE	42.73	29967540
743	Phosphorylation	YKNKVEDSGIFTIKN ECCCCCCCCCEEEEC	21.93	-
747	Phosphorylation	VEDSGIFTIKNMINT CCCCCCEEEECCCCC	29.17	-
801	Ubiquitination	SWYGTTIKRDKSGAY EEEEEEEEECCCCCE	53.07	-
852	Phosphorylation	VTHRVRLYHIQGIEG CCCEEEEEEEECCCC	6.06	-
865	Phosphorylation	EGQSVEVSNIVDIRK CCCEEEEEEEEEHHH	13.82	-
887	Ubiquitination	MKISSDIKSQNRFYT HHHCCCHHHCCCEEE	51.48	29967540
933	Phosphorylation	QDAKHRLTLLSAQSL HHHHHHHHHHHHHHH	26.13	24275569
939	Phosphorylation	LTLLSAQSLGVSSLN HHHHHHHHHCCCCCC	27.14	24275569
944	Phosphorylation	AQSLGVSSLNSGQIE HHHHCCCCCCCCCEE	29.21	24275569
998	Phosphorylation	NTEEEKKSVSYPSLL CCHHHHHCCCHHHHH	27.62	-
1125	N-linked_Glycosylation	HSPPGTQNISEINLS CCCCCCCCCEEEECC	39.32	16335952

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of MA2A1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MA2A1_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of MA2A1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
CAN1_HUMAN	CAPN1	physical	26344197

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.

Regulatory Network of MA2A1_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"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-78 AND ASN-1125, AND MASSSPECTROMETRY.	16335952 [Abstract]