AGM1_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: AGM1_YEAST
• UniProt AC: P38628
• Protein Name: Phosphoacetylglucosamine mutase {ECO:0000305}
• Gene Name: PCM1 {ECO:0000303|PubMed:8119301}
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 557
• Subcellular Localization: Cytoplasm . Nucleus .
• Protein Description: Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during the synthesis of uridine diphosphate/UDP-GlcNAc, which is a biosynthetic precursor of chitin and also supplies the amino sugars for N-linked oligosaccharides of glycoproteins. [PubMed: 8174553 Also has phosphoglucomutase activity]
• Protein Sequence: MKVDYEQLCKLYDDTCRTKNVQFSYGTAGFRTLAKNLDTVMFSTGILAVLRSLKLQGQYVGVMITASHNPYQDNGVKIVEPDGSMLLATWEPYAMQLANAASFATNFEEFRVELAKLIEHEKIDLNTTVVPHIVVGRDSRESSPYLLRCLTSSMASVFHAQVLDLGCVTTPQLHYITDLSNRRKLEGDTAPVATEQDYYSFFIGAFNELFATYQLEKRLSVPKLFIDTANGIGGPQLKKLLASEDWDVPAEQVEVINDRSDVPELLNFECGADYVKTNQRLPKGLSPSSFDSLYCSFDGDADRVVFYYVDSGSKFHLLDGDKISTLFAKFLSKQLELAHLEHSLKIGVVQTAYANGSSTAYIKNTLHCPVSCTKTGVKHLHHEAATQYDIGIYFEANGHGTIIFSEKFHRTIKSELSKSKLNGDTLALRTLKCFSELINQTVGDAISDMLAVLATLAILKMSPMDWDEEYTDLPNKLVKCIVPDRSIFQTTDQERKLLNPVGLQDKIDLVVAKYPMGRSFVRASGTEDAVRVYAECKDSSKLGQFCDEVVEHVKASA

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
59	Phosphorylation	SLKLQGQYVGVMITA HHCCCCCEEEEEEEC	13.14	22369663
65	Phosphorylation	QYVGVMITASHNPYQ CEEEEEEECCCCCCC	12.19	22369663
67	Phosphorylation	VGVMITASHNPYQDN EEEEEECCCCCCCCC	18.36	22369663
71	Phosphorylation	ITASHNPYQDNGVKI EECCCCCCCCCCEEE	33.54	22369663
116	Acetylation	EFRVELAKLIEHEKI HHHHHHHHHHHHCCC	63.72	24489116
276	Ubiquitination	ECGADYVKTNQRLPK CCCCCCCCCCCCCCC	35.21	23749301
329	Acetylation	KISTLFAKFLSKQLE HHHHHHHHHHHHHHH	39.23	24489116
333	Acetylation	LFAKFLSKQLELAHL HHHHHHHHHHHHHHH	62.13	24489116
353	Phosphorylation	IGVVQTAYANGSSTA EEEEEEEECCCCCEE	12.18	23749301
357	Phosphorylation	QTAYANGSSTAYIKN EEEECCCCCEEEEEC	25.07	23749301
420	Acetylation	KSELSKSKLNGDTLA HHHHHHCCCCCCHHH	50.11	24489116
476	Acetylation	EYTDLPNKLVKCIVP HHCCCCCCEEEEECC	53.36	24489116
506	Acetylation	NPVGLQDKIDLVVAK CCCCCHHHHCEEEEE	25.76	24489116
513	Acetylation	KIDLVVAKYPMGRSF HHCEEEEECCCCCCH	37.97	24489116
541	Acetylation	AECKDSSKLGQFCDE EECCCHHHHHHHHHH	61.66	24489116

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

Oops, there are no upstream regulatory protein records of AGM1_YEAST !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of AGM1_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 AGM1_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
WRIP1_YEAST	MGS1	physical	11805826
SWI4_YEAST	SWI4	genetic	9247198

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 THR-65 AND SER-67, AND MASSSPECTROMETRY.
PubMed: 18407956

"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67, AND MASSSPECTROMETRY.
PubMed: 17330950