MAP1_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MAP1_YEAST
• UniProt AC: Q01662
• Protein Name: Methionine aminopeptidase 1 {ECO:0000255|HAMAP-Rule:MF_03174}
• Gene Name: MAP1
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 387
• Subcellular Localization: Cytoplasm.
• 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). Plays the major role in N-terminal methionine removal. Less efficient when the second residue is Val..
• Protein Sequence: MSTATTTVTTSDQASHPTKIYCSGLQCGRETSSQMKCPVCLKQGIVSIFCDTSCYENNYKAHKALHNAKDGLEGAYDPFPKFKYSGKVKASYPLTPRRYVPEDIPKPDWAANGLPVSEQRNDRLNNIPIYKKDQIKKIRKACMLGREVLDIAAAHVRPGITTDELDEIVHNETIKRGAYPSPLNYYNFPKSLCTSVNEVICHGVPDKTVLKEGDIVNLDVSLYYQGYHADLNETYYVGENISKEALNTTETSRECLKLAIKMCKPGTTFQELGDHIEKHATENKCSVVRTYCGHGVGEFFHCSPNIPHYAKNRTPGVMKPGMVFTIEPMINEGTWKDMTWPDDWTSTTQDGKLSAQFEHTLLVTEHGVEILTARNKKSPGGPRQRIK

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	------MSTATTTVT ------CCCCEEEEE		22814378
2	Phosphorylation	------MSTATTTVT ------CCCCEEEEE		22369663
3	Phosphorylation	-----MSTATTTVTT -----CCCCEEEEEC		22369663
5	Phosphorylation	---MSTATTTVTTSD ---CCCCEEEEECCC		22369663
6	Phosphorylation	--MSTATTTVTTSDQ --CCCCEEEEECCCC		22369663
7	Phosphorylation	-MSTATTTVTTSDQA -CCCCEEEEECCCCC		22369663
9	Phosphorylation	STATTTVTTSDQASH CCCEEEEECCCCCCC		22369663
10	Phosphorylation	TATTTVTTSDQASHP CCEEEEECCCCCCCC		22369663
11	Phosphorylation	ATTTVTTSDQASHPT CEEEEECCCCCCCCC		22369663
15	Phosphorylation	VTTSDQASHPTKIYC EECCCCCCCCCEEEE		22369663
18	Phosphorylation	SDQASHPTKIYCSGL CCCCCCCCEEEECCC		22369663
21	Phosphorylation	ASHPTKIYCSGLQCG CCCCCEEEECCCCCC		19779198
36	Ubiquitination	RETSSQMKCPVCLKQ CCCCCCCCCCEEECC		23749301
69	Acetylation	HKALHNAKDGLEGAY HHHHHHHCCCCCCCC		24489116
81	Acetylation	GAYDPFPKFKYSGKV CCCCCCCCCEECCEE		24489116
91	Phosphorylation	YSGKVKASYPLTPRR ECCEEEECCCCCCCC		22369663
92	Phosphorylation	SGKVKASYPLTPRRY CCEEEECCCCCCCCC		22369663
95	Phosphorylation	VKASYPLTPRRYVPE EEECCCCCCCCCCCC		22369663
106	Acetylation	YVPEDIPKPDWAANG CCCCCCCCCCHHHCC		24489116
131	Acetylation	LNNIPIYKKDQIKKI HHCCCCCCHHHHHHH		22865919
131	Succinylation	LNNIPIYKKDQIKKI HHCCCCCCHHHHHHH		23954790
175	Ubiquitination	IVHNETIKRGAYPSP HHCCCCCCCCCCCCC		22817900
195	Phosphorylation	FPKSLCTSVNEVICH CCHHHCCCCHHHHCC		30377154
207	Ubiquitination	ICHGVPDKTVLKEGD HCCCCCCCCEEEECC		22817900
211	Ubiquitination	VPDKTVLKEGDIVNL CCCCCEEEECCEEEE		22817900
242	Phosphorylation	YYVGENISKEALNTT EEECCCCCHHHHCCC		28889911
278	Acetylation	ELGDHIEKHATENKC HHHHHHHHHHCCCCC		22865919
311	Ubiquitination	PNIPHYAKNRTPGVM CCCCHHHCCCCCCCC		22817900
319	Acetylation	NRTPGVMKPGMVFTI CCCCCCCCCCEEEEE		24489116

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

Oops, there are no upstream regulatory protein records of MAP1_YEAST !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MAP1_YEAST !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of MAP1_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MAP2_YEAST	MAP2	genetic	8618900
MAP2_YEAST	MAP2	genetic	9367524
YN8H_YEAST	YNR029C	physical	18719252
RKM3_YEAST	RKM3	physical	18719252
SSB1_YEAST	SSB1	physical	19536198
COG4_YEAST	COG4	genetic	21288874
UBP8_YEAST	UBP8	genetic	21288874
SWR1_YEAST	SWR1	genetic	21288874
VPS72_YEAST	VPS72	genetic	21288874
RL35A_YEAST	RPL35A	physical	26195668
RL35B_YEAST	RPL35A	physical	26195668

Drug and Disease Associations

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