dbPTM

MAP2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MAP2_HUMAN
UniProt AC	P50579
Protein Name	Methionine aminopeptidase 2 {ECO:0000255\|HAMAP-Rule:MF_03175}
Gene Name	METAP2 {ECO:0000255\|HAMAP-Rule:MF_03175}
Organism	Homo sapiens (Human).
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). The catalytic activity of human METAP2 toward Met-Val peptides is consistently two orders of magnitude higher than that of METAP1, suggesting that it is responsible for processing proteins containing N-terminal Met-Val and Met-Thr sequences in vivo.; 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	MAGVEEVAASGSHLNGDLDPDDREEGAASTAEEAAKKKRRKKKKSKGPSAAGEQEPDKESGASVDEVARQLERSALEDKERDEDDEDGDGDGDGATGKKKKKKKKKRGPKVQTDPPSVPICDLYPNGVFPKGQECEYPPTQDGRTAAWRTTSEEKKALDQASEEIWNDFREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLIKENGLNAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYDDICKIDFGTHISGRIIDCAFTVTFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEIDGKTYQVKPIRNLNGHSIGQYRIHAGKTVPIVKGGEATRMEEGEVYAIETFGSTGKGVVHDDMECSHYMKNFDVGHVPIRLPRTKHLLNVINENFGTLAFCRRWLDRLGESKYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVSRGDDY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAGVEEVAA ------CCCHHCHHC	38.38	19413330
10	Phosphorylation	GVEEVAASGSHLNGD CHHCHHCCCCCCCCC	61.47	25159151
12	Phosphorylation	EEVAASGSHLNGDLD HCHHCCCCCCCCCCC	23.89	28464451
23	Methylation	GDLDPDDREEGAAST CCCCHHHHHHHHHHH	21.93	115483157
29	Phosphorylation	DREEGAASTAEEAAK HHHHHHHHHHHHHHH	50.99	29255136
30	Phosphorylation	REEGAASTAEEAAKK HHHHHHHHHHHHHHH	68.10	29255136
45	Phosphorylation	KRRKKKKSKGPSAAG HHHHHHHCCCCCCCC	15.03	23401153
45 (in isoform 2)	Phosphorylation	-	15.03	28985074
46	Acetylation	RRKKKKSKGPSAAGE HHHHHHCCCCCCCCC	54.61	26051181
49	Phosphorylation	KKKSKGPSAAGEQEP HHHCCCCCCCCCCCC	28.77	25159151
49 (in isoform 2)	Phosphorylation	-	28.77	21815630
58	Ubiquitination	AGEQEPDKESGASVD CCCCCCCCCCCCCHH	20.31	21906983
58	Acetylation	AGEQEPDKESGASVD CCCCCCCCCCCCCHH	20.31	26051181
58	Ubiquitination	AGEQEPDKESGASVD CCCCCCCCCCCCCHH	20.31	-
59 (in isoform 2)	Phosphorylation	-	26.00	25627689
60	Phosphorylation	EQEPDKESGASVDEV CCCCCCCCCCCHHHH	38.33	25159151
60	O-linked_Glycosylation	EQEPDKESGASVDEV CCCCCCCCCCCHHHH	38.33	UniProtKB CARBOHYD
62 (in isoform 2)	Phosphorylation	-	19.84	25159151
63	Phosphorylation	PDKESGASVDEVARQ CCCCCCCCHHHHHHH	27.61	23927012
63	O-linked_Glycosylation	PDKESGASVDEVARQ CCCCCCCCHHHHHHH	27.61	UniProtKB CARBOHYD
74	Phosphorylation	VARQLERSALEDKER HHHHHHHHHHHHHHC	18.81	23401153
79	Acetylation	ERSALEDKERDEDDE HHHHHHHHHCCCCCC	4.93	26051181
79	Ubiquitination	ERSALEDKERDEDDE HHHHHHHHHCCCCCC	4.93	-
79	Ubiquitination	ERSALEDKERDEDDE HHHHHHHHHCCCCCC	4.93	21890473
96	Phosphorylation	DGDGDGATGKKKKKK CCCCCCCCCCCCCCC	22.92	25159151
98	Ubiquitination	DGDGATGKKKKKKKK CCCCCCCCCCCCCCC	2.04	-
98	Acetylation	DGDGATGKKKKKKKK CCCCCCCCCCCCCCC	2.04	26051181
98	Ubiquitination	DGDGATGKKKKKKKK CCCCCCCCCCCCCCC	2.04	983
99	Ubiquitination	GDGATGKKKKKKKKK CCCCCCCCCCCCCCC	21.66	-
113	Phosphorylation	KRGPKVQTDPPSVPI CCCCCCCCCCCCCCC	53.46	25367160
117	Phosphorylation	KVQTDPPSVPICDLY CCCCCCCCCCCCCCC	39.18	29214152
137	Phosphorylation	PKGQECEYPPTQDGR CCCCCCCCCCCCCCC	51.07	-
145	Phosphorylation	PPTQDGRTAAWRTTS CCCCCCCCCCCCCCH	38.48	-
150	Phosphorylation	GRTAAWRTTSEEKKA CCCCCCCCCHHHHHH	36.11	29449344
151	Phosphorylation	RTAAWRTTSEEKKAL CCCCCCCCHHHHHHH	50.01	29449344
152	Phosphorylation	TAAWRTTSEEKKALD CCCCCCCHHHHHHHH	33.21	29449344
156	Ubiquitination	RTTSEEKKALDQASE CCCHHHHHHHHHHHH	13.71	-
182	Phosphorylation	AHRQVRKYVMSWIKP HHHHHHHHHHHHHCC	62.25	-
186	Ubiquitination	VRKYVMSWIKPGMTM HHHHHHHHHCCCCCH	52.46	-
209	Ubiquitination	DCSRKLIKENGLNAG HHHHHHHHHCCCCCC	61.29	-
249	Ubiquitination	LQYDDICKIDFGTHI EEECCEEEEECCCCC	17.90	-
255	Ubiquitination	CKIDFGTHISGRIID EEEECCCCCCCCEEE	55.35	-
258	Ubiquitination	DFGTHISGRIIDCAF ECCCCCCCCEEEEEE	58.68	-
266	Ubiquitination	RIIDCAFTVTFNPKY CEEEEEEEEEECCCH	4.93	-
272	Ubiquitination	FTVTFNPKYDTLLKA EEEEECCCHHHHHHH	53.25	-
278	Ubiquitination	PKYDTLLKAVKDATN CCHHHHHHHHHHHHC	18.63	-
281	Ubiquitination	DTLLKAVKDATNTGI HHHHHHHHHHHCCCC	5.40	21890473
289	Ubiquitination	DATNTGIKCAGIDVR HHHCCCCCCCCEEEE	11.85	-
289	Acetylation	DATNTGIKCAGIDVR HHHCCCCCCCCEEEE	11.85	26051181
300	Ubiquitination	IDVRLCDVGEAIQEV EEEEECCHHHHHHHH	47.85	-
319	Phosphorylation	EVEIDGKTYQVKPIR EEEECCEEEEEEECC	33.81	28152594
319	Ubiquitination	EVEIDGKTYQVKPIR EEEECCEEEEEEECC	33.81	-
320	Phosphorylation	VEIDGKTYQVKPIRN EEECCEEEEEEECCC	14.59	28152594
323	Acetylation	DGKTYQVKPIRNLNG CCEEEEEEECCCCCC	29.21	26051181
323	Ubiquitination	DGKTYQVKPIRNLNG CCEEEEEEECCCCCC	29.21	-
325	Ubiquitination	KTYQVKPIRNLNGHS EEEEEEECCCCCCCE	24.37	-
336	Nitration	NGHSIGQYRIHAGKT CCCEEEEEEEECCCE	36.07	-
342	Ubiquitination	QYRIHAGKTVPIVKG EEEEECCCEEEEEEC	24.75	-
348	Ubiquitination	GKTVPIVKGGEATRM CCEEEEEECCEEEEC	68.36	-
365	Phosphorylation	GEVYAIETFGSTGKG CCEEEEEECCCCCCC	27.94	-
369	Phosphorylation	AIETFGSTGKGVVHD EEEECCCCCCCCCCC	67.09	-
378	Sulfoxidation	KGVVHDDMECSHYMK CCCCCCCCCCCCCCC	48.84	30846556
384	Sulfoxidation	DMECSHYMKNFDVGH CCCCCCCCCCCCCCC	52.42	30846556
385	Acetylation	MECSHYMKNFDVGHV CCCCCCCCCCCCCCC	36.61	26051181
385	Ubiquitination	MECSHYMKNFDVGHV CCCCCCCCCCCCCCC	36.61	-
404	Acetylation	PRTKHLLNVINENFG CCHHHHHHHHHHCCH	4.66	19608861
404	Ubiquitination	PRTKHLLNVINENFG CCHHHHHHHHHHCCH	4.66	19608861
404	Ubiquitination	PRTKHLLNVINENFG CCHHHHHHHHHHCCH	4.66	21890473
404	Ubiquitination	PRTKHLLNVINENFG CCHHHHHHHHHHCCH	4.66	21890473
426	Phosphorylation	WLDRLGESKYLMALK HHHHHCHHHHHHHHH	12.69	20068231
427	2-Hydroxyisobutyrylation	LDRLGESKYLMALKN HHHHCHHHHHHHHHH	20.73	-
427	Malonylation	LDRLGESKYLMALKN HHHHCHHHHHHHHHH	20.73	26320211
427	Acetylation	LDRLGESKYLMALKN HHHHCHHHHHHHHHH	20.73	19608861
427	Ubiquitination	LDRLGESKYLMALKN HHHHCHHHHHHHHHH	20.73	21890473
436	S-nitrosocysteine	LMALKNLCDLGIVDP HHHHHHHHHCCCCCC	45.81	-
448	S-nitrosocysteine	VDPYPPLCDIKGSYT CCCCCCCCCCCCCEE	32.42	-
453	Phosphorylation	PLCDIKGSYTAQFEH CCCCCCCCEEEEEEE	40.56	28152594
454	Phosphorylation	LCDIKGSYTAQFEHT CCCCCCCEEEEEEEE	60.95	28152594
455	Phosphorylation	CDIKGSYTAQFEHTI CCCCCCEEEEEEEEE	28.75	28152594
461	Phosphorylation	YTAQFEHTILLRPTC EEEEEEEEEEECCCH	67.44	29052541
467	Phosphorylation	HTILLRPTCKEVVSR EEEEECCCHHHHHHC	63.69	29052541

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
-	K	Ubiquitination	E3 ubiquitin ligase	BTRC	Q9Y297	PMID:11438690

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MAP2_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 MAP2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
E2AK2_HUMAN	EIF2AK2	physical	11123929
A4_HUMAN	APP	physical	21832049
MTOR_HUMAN	MTOR	physical	19446321
HMGA1_HUMAN	HMGA1	physical	18850631
TKFC_HUMAN	DAK	physical	22863883
G3P_HUMAN	GAPDH	physical	22863883
GBP1_HUMAN	GBP1	physical	22863883
PSA_HUMAN	NPEPPS	physical	22863883

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
DB00134	L-Methionine
DB01422	Nitroxoline

Regulatory Network of MAP2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1782, AND MASSSPECTROMETRY.	18220336 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND MASSSPECTROMETRY.	17525332 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1798; SER-1799; SER-1800AND SER-1802, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Phosphoproteomic analysis of synaptosomes from human cerebralcortex."; DeGiorgis J.A., Jaffe H., Moreira J.E., Carlotti C.G. Jr., Leite J.P.,Pant H.C., Dosemeci A.; J. Proteome Res. 4:306-315(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-833, AND MASSSPECTROMETRY.	15822905 [Abstract]