MTAP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MTAP_HUMAN
• UniProt AC: Q13126
• Protein Name: S-methyl-5'-thioadenosine phosphorylase {ECO:0000255|HAMAP-Rule:MF_03155}
• Gene Name: MTAP {ECO:0000255|HAMAP-Rule:MF_03155}
• Organism: Homo sapiens (Human).
• Sequence Length: 283
• Subcellular Localization: Cytoplasm. Nucleus .
• Protein Description: Catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates..
• Protein Sequence: MASGTTTTAVKIGIIGGTGLDDPEILEGRTEKYVDTPFGKPSDALILGKIKNVDCVLLARHGRQHTIMPSKVNYQANIWALKEEGCTHVIVTTACGSLREEIQPGDIVIIDQFIDRTTMRPQSFYDGSHSCARGVCHIPMAEPFCPKTREVLIETAKKLGLRCHSKGTMVTIEGPRFSSRAESFMFRTWGADVINMTTVPEVVLAKEAGICYASIAMATDYDCWKEHEEAVSVDRVLKTLKENANKAKSLLLTTIPQIGSTEWSETLHNLKNMAQFSVLLPRH

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	------MASGTTTTA ------CCCCCCCEE	19.37	-
3	Phosphorylation	-----MASGTTTTAV -----CCCCCCCEEE	35.06	20068231
5	Phosphorylation	---MASGTTTTAVKI ---CCCCCCCEEEEE	20.62	20068231
6	Phosphorylation	--MASGTTTTAVKIG --CCCCCCCEEEEEE	26.19	20068231
7	Phosphorylation	-MASGTTTTAVKIGI -CCCCCCCEEEEEEE	16.76	20068231
8	Phosphorylation	MASGTTTTAVKIGII CCCCCCCEEEEEEEE	27.62	20068231
30	Phosphorylation	PEILEGRTEKYVDTP HHHHCCCCEEECCCC	47.92	22210691
32	Acetylation	ILEGRTEKYVDTPFG HHCCCCEEECCCCCC	50.38	26051181
32	Ubiquitination	ILEGRTEKYVDTPFG HHCCCCEEECCCCCC	50.38	21906983
33	Phosphorylation	LEGRTEKYVDTPFGK HCCCCEEECCCCCCC	9.42	22210691
36	Phosphorylation	RTEKYVDTPFGKPSD CCEEECCCCCCCCCC	15.52	22210691
40	Ubiquitination	YVDTPFGKPSDALIL ECCCCCCCCCCEEEE	41.55	21906983
42	Phosphorylation	DTPFGKPSDALILGK CCCCCCCCCEEEEEE	38.71	22210691
49	Acetylation	SDALILGKIKNVDCV CCEEEEEEECCCCEE	47.24	26051181
49	Ubiquitination	SDALILGKIKNVDCV CCEEEEEEECCCCEE	47.24	21906983
51	Acetylation	ALILGKIKNVDCVLL EEEEEEECCCCEEEE	55.17	21339330
60	Methylation	VDCVLLARHGRQHTI CCEEEEECCCCCCEE	32.53	115483981
71	Ubiquitination	QHTIMPSKVNYQANI CCEECCCCCCCCCEE	28.73	21890473
87	Phosphorylation	ALKEEGCTHVIVTTA EECCCCCCEEEEEEC	29.99	27732954
92	Phosphorylation	GCTHVIVTTACGSLR CCCEEEEEECCCHHH	9.50	27732954
93	Phosphorylation	CTHVIVTTACGSLRE CCEEEEEECCCHHHH	14.73	27732954
97	Phosphorylation	IVTTACGSLREEIQP EEEECCCHHHHHCCC	24.92	27732954
119	Sulfoxidation	QFIDRTTMRPQSFYD EECCCCCCCCCCCCC	6.10	30846556
136	Glutathionylation	HSCARGVCHIPMAEP CCCCCCCCCCCCCCC	2.41	22555962
147	Acetylation	MAEPFCPKTREVLIE CCCCCCCCCHHHHHH	62.49	26051181
157	Ubiquitination	EVLIETAKKLGLRCH HHHHHHHHHHCCEEE	56.82	21906983
157	Acetylation	EVLIETAKKLGLRCH HHHHHHHHHHCCEEE	56.82	26051181
166	Ubiquitination	LGLRCHSKGTMVTIE HCCEEECCCCEEEEE	34.43	-
183	Phosphorylation	RFSSRAESFMFRTWG CCCCCHHHHHHHCCC	22.49	22817900
188	Phosphorylation	AESFMFRTWGADVIN HHHHHHHCCCCCEEC	19.58	22817900
235	Methylation	EEAVSVDRVLKTLKE HHHHCHHHHHHHHHH	33.25	115483975
248	Ubiquitination	KENANKAKSLLLTTI HHHHHHHHHHHHHCC	43.15	2190698
277	Phosphorylation	LKNMAQFSVLLPRH- HHHHHHHEEECCCC-	10.36	29514088

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

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

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RELB_HUMAN	RELB	physical	21988832
ANXA6_HUMAN	ANXA6	physical	22863883
VATA_HUMAN	ATP6V1A	physical	22863883
CUTA_HUMAN	CUTA	physical	22863883
MTPN_HUMAN	MTPN	physical	22863883
PDIA3_HUMAN	PDIA3	physical	22863883
RAB1A_HUMAN	RAB1A	physical	22863883
CENPH_HUMAN	CENPH	physical	25416956
ARF4_HUMAN	ARF4	physical	26344197
ASSY_HUMAN	ASS1	physical	26344197
NNRD_HUMAN	CARKD	physical	26344197
XPO2_HUMAN	CSE1L	physical	26344197
EI2BA_HUMAN	EIF2B1	physical	26344197
FA49B_HUMAN	FAM49B	physical	26344197
GLRX1_HUMAN	GLRX	physical	26344197
GNPI2_HUMAN	GNPDA2	physical	26344197
HINT1_HUMAN	HINT1	physical	26344197
LYPA2_HUMAN	LYPLA2	physical	26344197
PIMT_HUMAN	PCMT1	physical	26344197
PPIL3_HUMAN	PPIL3	physical	26344197
RBM12_HUMAN	RBM12	physical	26344197
SNX12_HUMAN	SNX12	physical	26344197
SNX3_HUMAN	SNX3	physical	26344197
SUMO3_HUMAN	SUMO3	physical	26344197
SUMO4_HUMAN	SUMO4	physical	26344197
TAGL2_HUMAN	TAGLN2	physical	26344197
TAGL3_HUMAN	TAGLN3	physical	26344197
TALDO_HUMAN	TALDO1	physical	26344197
UB2D2_HUMAN	UBE2D2	physical	26344197
UFM1_HUMAN	UFM1	physical	26344197

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 112250: Diaphyseal medullary stenosis with malignant fibrous histiocytoma (DMSMFH)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• DB00173: Adenine

Related Literatures of Post-Translational Modification

Acetylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
PubMed: 19413330

Phosphorylation

"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 AND THR-188, ANDMASS SPECTROMETRY.
PubMed: 15302935