MMTA2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MMTA2_HUMAN
• UniProt AC: Q9BU76
• Protein Name: Multiple myeloma tumor-associated protein 2
• Gene Name: MMTAG2
• Organism: Homo sapiens (Human).
• Sequence Length: 263
• Protein Sequence: MFGSSRGGVRGGQDQFNWEDVKTDKQRENYLGNSLMAPVGRWQKGRDLTWYAKGRAPCAGPSREEELAAVREAEREALLAALGYKNVKKQPTGLSKEDFAEVCKREGGDPEEKGVDRLLGLGSASGSVGRVAMSREDKEAAKLGLSVFTHHRVESGGPGTSAASARRKPRAEDQTESSCESHRKSKKEKKKKKKRKHKKEKKKKDKEHRRPAEATSSPTSPERPRHHHHDSDSNSPCCKRRKRGHSGDRRSPSRRWHDRGSEA

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
1	Acetylation	-------MFGSSRGG -------CCCCCCCC	8.50	-
6	Methylation	--MFGSSRGGVRGGQ --CCCCCCCCCCCCC	47.81	115368585
10	Methylation	GSSRGGVRGGQDQFN CCCCCCCCCCCCCCC	46.96	115388421
22	Sumoylation	QFNWEDVKTDKQREN CCCHHHHCCHHHHHH	64.43	28112733
22	Ubiquitination	QFNWEDVKTDKQREN CCCHHHHCCHHHHHH	64.43	32015554
34	Phosphorylation	RENYLGNSLMAPVGR HHHHCCCCCCCCCCC	20.09	24532841
53	Acetylation	RDLTWYAKGRAPCAG CCCEEEECCCCCCCC	32.98	19608861
53	Ubiquitination	RDLTWYAKGRAPCAG CCCEEEECCCCCCCC	32.98	32015554
85	Ubiquitination	LLAALGYKNVKKQPT HHHHHCCCCCCCCCC	54.16	32015554
92	Phosphorylation	KNVKKQPTGLSKEDF CCCCCCCCCCCHHHH	48.54	22798277
96	Ubiquitination	KQPTGLSKEDFAEVC CCCCCCCHHHHHHHH	67.36	32015554
104	Ubiquitination	EDFAEVCKREGGDPE HHHHHHHHHHCCCHH	59.67	32015554
104	Sumoylation	EDFAEVCKREGGDPE HHHHHHHHHHCCCHH	59.67	-
104	Sumoylation	EDFAEVCKREGGDPE HHHHHHHHHHCCCHH	59.67	28112733
113	Sumoylation	EGGDPEEKGVDRLLG HCCCHHHHCHHHHHC	63.67	28112733
123	Phosphorylation	DRLLGLGSASGSVGR HHHHCCCCCCCCHHH	25.05	25159151
125	Phosphorylation	LLGLGSASGSVGRVA HHCCCCCCCCHHHHC	33.04	25159151
127	Phosphorylation	GLGSASGSVGRVAMS CCCCCCCCHHHHCCC	20.92	25159151
146	Phosphorylation	EAAKLGLSVFTHHRV HHHHHCCEEEECCCC	17.24	28555341
149	Phosphorylation	KLGLSVFTHHRVESG HHCCEEEECCCCCCC	18.02	28555341
155	Phosphorylation	FTHHRVESGGPGTSA EECCCCCCCCCCCCH	46.31	25159151
160	Phosphorylation	VESGGPGTSAASARR CCCCCCCCCHHHHCC	20.51	29255136
161	Phosphorylation	ESGGPGTSAASARRK CCCCCCCCHHHHCCC	27.96	29255136
164	Phosphorylation	GPGTSAASARRKPRA CCCCCHHHHCCCCCC	23.25	23401153
175	Phosphorylation	KPRAEDQTESSCESH CCCCHHCCHHHHHHH	50.59	29255136
177	Phosphorylation	RAEDQTESSCESHRK CCHHCCHHHHHHHHH	43.61	23401153
177 (in isoform 4)	Phosphorylation	-	43.61	22468782
178	Phosphorylation	AEDQTESSCESHRKS CHHCCHHHHHHHHHH	18.70	29255136
181 (in isoform 4)	Phosphorylation	-	32.68	22468782
181	Phosphorylation	QTESSCESHRKSKKE CCHHHHHHHHHHHHH	32.68	29255136
215	Phosphorylation	HRRPAEATSSPTSPE HCCCCHHCCCCCCCC	22.65	29255136
216	Phosphorylation	RRPAEATSSPTSPER CCCCHHCCCCCCCCC	41.17	29255136
217	Phosphorylation	RPAEATSSPTSPERP CCCHHCCCCCCCCCC	28.04	29255136
219	Phosphorylation	AEATSSPTSPERPRH CHHCCCCCCCCCCCC	59.88	29255136
220	Phosphorylation	EATSSPTSPERPRHH HHCCCCCCCCCCCCC	28.31	29255136
231	Phosphorylation	PRHHHHDSDSNSPCC CCCCCCCCCCCCCCH	38.28	28102081
233	Phosphorylation	HHHHDSDSNSPCCKR CCCCCCCCCCCCHHH	43.06	23663014
235	Phosphorylation	HHDSDSNSPCCKRRK CCCCCCCCCCHHHCC	24.22	28102081
246	Phosphorylation	KRRKRGHSGDRRSPS HHCCCCCCCCCCCCC	45.25	30177828
251	Phosphorylation	GHSGDRRSPSRRWHD CCCCCCCCCCCCCCC	28.28	30177828
253	Phosphorylation	SGDRRSPSRRWHDRG CCCCCCCCCCCCCCC	35.41	30177828
261	Phosphorylation	RRWHDRGSEA----- CCCCCCCCCC-----	31.11	30576142

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

Oops, there are no upstream regulatory protein records of MMTA2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MMTA2_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 MMTA2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
CEP70_HUMAN	CEP70	physical	19060904

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
• There are no disease associations of PTM sites.

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 MET-1, AND MASS SPECTROMETRY.
PubMed: 19413330

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53, AND MASS SPECTROMETRY.
PubMed: 19608861

Phosphorylation

"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127 AND SER-164, ANDMASS SPECTROMETRY.
PubMed: 18669648

"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164, AND MASSSPECTROMETRY.
PubMed: 19007248