AAP1_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: AAP1_YEAST
• UniProt AC: P37898
• Protein Name: Alanine/arginine aminopeptidase
• Gene Name: AAP1
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 856
• Protein Description: Positive effector of glycogen accumulation. May be involved in nutrient-sensing..
• Protein Sequence: MSREVLPNNVTPLHYDITLEPNFRAFTFEGSLKIDLQINDHSINSVQINYLEIDFHSARIEGVNAIEVNKNENQQKATLVFPNGTFENLGPSAKLEIIFSGILNDQMAGFYRAKYTDKVTGETKYMATTQMEATDARRAFPCFDEPNLKATFAVTLVSESFLTHLSNMDVRNETIKEGKKYTTFNTTPKMSTYLVAFIVADLRYVESNNFRIPVRVYSTPGDEKFGQFAANLAARTLRFFEDTFNIEYPLPKMDMVAVHEFSAGAMENWGLVTYRVIDLLLDIENSSLDRIQRVAEVIQHELAHQWFGNLVTMDWWEGLWLNEGFATWMSWYSCNKFQPEWKVWEQYVTDNLQRALNLDSLRSSHPIEVPVNNADEINQIFDAISYSKGSSLLRMISKWLGEETFIKGVSQYLNKFKYGNAKTGDLWDALADASGKDVCSVMNIWTKRVGFPVLSVKEHKNKITLTQHRYLSTGDVKEEEDTTIYPILLALKDSTGIDNTLVLNEKSATFELKNEEFFKINGDQSGIFITSYSDERWAKLSKQANLLSVEDRVGLVADAKALSASGYTSTTNFLNLISNWKNEDSFVVWEQIINSLSALKSTWVFEPEDILNALDKFTLDLVLNKLSELGWNIGEDDSFAIQRLKVTLFSAACTSGNEKMQSIAVEMFEEYANGNKQAIPALFKAVVFNTVARLGGENNYEKIFNIYQNPVSSEEKIIALRALGRFEDKELLERTLSYLLDGTVLNQDFYIPMQGIRVHKKGIERLWAWMQEHWDEIAKRLQPGSPVLGGVLTLGLTNFTSFEALEKISAFYSRKVTKGFDQTLAQALDTIRSKAQWVSRDREIVATYLREHEYDQ

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
70	Acetylation	VNAIEVNKNENQQKA CEEEEECCCCCCCEE	71.46	24489116
123	Phosphorylation	TDKVTGETKYMATTQ ECCCCCCEEEEEEEC	28.90	27017623
149	Ubiquitination	CFDEPNLKATFAVTL CCCCCCCEEEEEEEE	52.61	17644757
181	Phosphorylation	TIKEGKKYTTFNTTP CHHCCCCCCCCCCCC	17.94	28889911
182	Phosphorylation	IKEGKKYTTFNTTPK HHCCCCCCCCCCCCC	33.52	28889911
183	Phosphorylation	KEGKKYTTFNTTPKM HCCCCCCCCCCCCCC	16.29	28889911
186	Phosphorylation	KKYTTFNTTPKMSTY CCCCCCCCCCCCHHH	40.04	28889911
187	Phosphorylation	KYTTFNTTPKMSTYL CCCCCCCCCCCHHHH	23.24	28889911
224	Acetylation	YSTPGDEKFGQFAAN EECCCCHHHHHHHHH	60.58	24489116
248	Phosphorylation	EDTFNIEYPLPKMDM HHCCCCCCCCCCCCE	13.28	28889911
398	Ubiquitination	SLLRMISKWLGEETF HHHHHHHHHHCCCHH	35.20	23749301
470	Phosphorylation	ITLTQHRYLSTGDVK EEEEEEEECCCCCCC	11.68	23749301
473	Phosphorylation	TQHRYLSTGDVKEEE EEEEECCCCCCCCCC	34.50	23749301
702	Acetylation	GGENNYEKIFNIYQN CCCCCHHHHHHHHCC	42.09	24489116
716	Acetylation	NPVSSEEKIIALRAL CCCCCHHHHHHHHHH	35.05	24489116
729	Acetylation	ALGRFEDKELLERTL HHCCCCCHHHHHHHH	42.96	24489116

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

Oops, there are no upstream regulatory protein records of AAP1_YEAST !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of AAP1_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 AAP1_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MSH4_YEAST	MSH4	genetic	20093466
SAC1_YEAST	SAC1	genetic	20093466
PTK1_YEAST	PTK1	genetic	20093466
OCA1_YEAST	OCA1	genetic	20093466
MSB4_YEAST	MSB4	genetic	20093466
PTK1_YEAST	PTK1	genetic	22282571
THIK_YEAST	POT1	genetic	27708008
OCA1_YEAST	OCA1	genetic	27708008

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-248, AND MASSSPECTROMETRY.
PubMed: 18407956