MAP2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MAP2_MOUSE
• UniProt AC: O08663
• Protein Name: Methionine aminopeptidase 2 {ECO:0000255|HAMAP-Rule:MF_03175}
• Gene Name: Metap2
• Organism: Mus musculus (Mouse).
• Sequence Length: 478
• Subcellular Localization: Cytoplasm. About 30% of expressed METAP2 associates with polysomes.
• Protein Description: Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).; Protects eukaryotic initiation factor EIF2S1 from translation-inhibiting phosphorylation by inhibitory kinases such as EIF2AK2/PKR and EIF2AK1/HCR. Plays a critical role in the regulation of protein synthesis..
• Protein Sequence: MAGVEQAASFGGHLNGDLDPDDREEGTSSTAEEAAKKKRRKKKKGKGAVSAVQQELDKESGALVDEVAKQLESQALEEKERDDDDEDGDGDADGATGKKKKKKKKKRGPKVQTDPPSVPICDLYPNGVFPKGQECEYPPTQDGRTAAWRTTSEEKKALDQASEEIWNDFREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLIKENGLNAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYDDICKIDFGTHISGRIIDCAFTVTFNPKYDILLTAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEIDGKTYQVKPIRNLNGHSIGPYRIHAGKTVPIVKGGEATRMEEGEVYAIETFGSTGKGVVHDDMECSHYMKNFDVGHVPIRLPRTKHLLNVINENFGTLAFCRRWLDRLGESKYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVSRGDDY

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
2	Acetylation	------MAGVEQAAS ------CCCHHHHHH	38.38	-
9	Phosphorylation	AGVEQAASFGGHLNG CCHHHHHHCCCCCCC	41.37	26643407
27	Phosphorylation	PDDREEGTSSTAEEA CCCCCCCCCCHHHHH	46.23	25266776
28	Phosphorylation	DDREEGTSSTAEEAA CCCCCCCCCHHHHHH	27.32	26160508
29	Phosphorylation	DREEGTSSTAEEAAK CCCCCCCCHHHHHHH	42.54	25521595
30	Phosphorylation	REEGTSSTAEEAAKK CCCCCCCHHHHHHHH	62.98	26160508
50	Phosphorylation	KKGKGAVSAVQQELD HCCCCHHHHHHHHHH	28.53	28464351
60	O-linked_Glycosylation	QQELDKESGALVDEV HHHHHHCCCHHHHHH	29.67	-
60	Phosphorylation	QQELDKESGALVDEV HHHHHHCCCHHHHHH	29.67	29514104
73	Phosphorylation	EVAKQLESQALEEKE HHHHHHHHHHHHHHH	59.19	29514104
96	Phosphorylation	DGDADGATGKKKKKK CCCCCCCCCCCCCCC	22.92	29514104
99	Ubiquitination	ADGATGKKKKKKKKK CCCCCCCCCCCCCCC	21.66	-
135	S-nitrosocysteine	VFPKGQECEYPPTQD CCCCCCCCCCCCCCC	63.74	-
140	Phosphorylation	QECEYPPTQDGRTAA CCCCCCCCCCCCCCC	38.58	18388127
281	Ubiquitination	DILLTAVKDATNTGI CEEEEEECHHCCCCC	23.22	-
289	Ubiquitination	DATNTGIKCAGIDVR HHCCCCCCCCCEEEE	27.76	-
348	Ubiquitination	GKTVPIVKGGEATRM CCEEEEEECCEEEEC	59.51	-
380	S-nitrosocysteine	VVHDDMECSHYMKNF CCCCCCCCCCCCCCC	37.37	-
427	Ubiquitination	LDRLGESKYLMALKN HHHHCHHHHHHHHHH	56.12	-
468	S-nitrosocysteine	TILLRPTCKEVVSRG EEEECCCHHHHHHCC	3.38	-

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

Oops, there are no upstream regulatory protein records of MAP2_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MAP2_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of MAP2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EIF2A_MOUSE	Eif2a	physical	15544353

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1650; THR-1657 ANDSER-1783, AND MASS SPECTROMETRY.
PubMed: 19367708

"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1791, AND MASSSPECTROMETRY.
PubMed: 17242355

"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608; SER-823; SER-1352;THR-1358; THR-1599; THR-1609; SER-1612; THR-1620 AND SER-1783, ANDMASS SPECTROMETRY.
PubMed: 17114649

"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1352; THR-1358;SER-1426; THR-1445; SER-1485; SER-1539; THR-1609 AND THR-1650, ANDMASS SPECTROMETRY.
PubMed: 16452087

"Proteomic analysis of in vivo phosphorylated synaptic proteins.";
Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,Blackstock W.P., Choudhary J.S., Grant S.G.;
J. Biol. Chem. 280:5972-5982(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-746; SER-1161; SER-1352;THR-1358; SER-1539 AND SER-1783, AND MASS SPECTROMETRY.
PubMed: 15572359

"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608; SER-626; SER-655;SER-730; SER-737; SER-823; SER-1352; THR-1358; SER-1595; THR-1598;THR-1606; THR-1609 AND SER-1615, AND MASS SPECTROMETRY.
PubMed: 15345747