MFHA1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MFHA1_HUMAN
• UniProt AC: Q9Y4C4
• Protein Name: Malignant fibrous histiocytoma-amplified sequence 1
• Gene Name: MFHAS1
• Organism: Homo sapiens (Human).
• Sequence Length: 1052
• Protein Sequence: MAGMDSGNLKTARLWRDAALRARKLRSNLRQLTLTAAGACPGAGADALESPASPQLVLPANLGDIEALNLGNNGLEEVPEGLGSALGSLRVLVLRRNRFARLPPAVAELGHHLTELDVSHNRLTALGAEVVSALRELRKLNLSHNQLPALPAQLGALAHLEELDVSFNRLAHLPDSLSCLSRLRTLDVDHNQLTAFPRQLLQLVALEELDVSSNRLRGLPEDISALRALKILWLSGAELGTLPAGFCELASLESLMLDNNGLQALPAQFSCLQRLKMLNLSSNLFEEFPAALLPLAGLEELYLSRNQLTSVPSLISGLGRLLTLWLDNNRIRYLPDSIVELTGLEELVLQGNQIAVLPDHFGQLSRVGLWKIKDNPLIQPPYEVCMKGIPYIAAYQKELAHSQPAVQPRLKLLLMGHKAAGKTLLRHCLTEERVEGCPGGGDKEKCYPPSPPPVSKGIEVTSWTADASRGLRFIVYDLAGDESYEVIQPFFLSPGALYVLVVNLATYEPRHFPTTVGSFLHRVGARVPHAVVCIVGTHADLCGERELEEKCLDIHRQIALQEKHDAEGLSRLAKVVDEALARDFELRSASPHAAYYGVSDKNLRRRKAHFQYLLNHRLQILSPVLPVSCRDPRHLRRLRDKLLSVAEHREIFPNLHRVLPRSWQVLEELHFQPPQAQRLWLSWWDSARLGLQAGLTEDRLQSALSYLHESGKLLYFEDSPALKEHVFHNLTRLIDILNVFFQRDPSLLLHKLLLGTSGEGKAEGESSPPMARSTPSQELLRATQLHQYVEGFLLHGLLPAHVIRLLLKPHVQAQQDLQLLLELLEKMGLCYCLNKPKGKPLNGSTAWYKFPCYVQNEVPHAEAWINGTNLAGQSFVAEQLQIEYSFPFTFPLGLFARYSVQINSHVVHRSDGKFQIFAYRGKVPVVVSYRPARGVLQPDTLSIASHASLPNIWTAWQAITPLVEELNVLLQEWPGLHYTVHILCSKCLKRGSPNPHAFPGELLSQPRPEGVAEIICPKNGSERVNVALVYPPTPTVISPCSKKNVGEKHRNQ

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	------MAGMDSGNL ------CCCCCCCCH	33.07	22814378
6	Phosphorylation	--MAGMDSGNLKTAR --CCCCCCCCHHHHH	22.23	24719451
10	Methylation	GMDSGNLKTARLWRD CCCCCCHHHHHHHHH	44.10	115972987
10	Ubiquitination	GMDSGNLKTARLWRD CCCCCCHHHHHHHHH	44.10	-
11	Phosphorylation	MDSGNLKTARLWRDA CCCCCHHHHHHHHHH	21.85	24719451
88	Phosphorylation	GLGSALGSLRVLVLR CHHHHHHHHHHHHHC	17.53	24719451
185	Phosphorylation	SCLSRLRTLDVDHNQ HHHHHCCCCCCCHHH	31.72	-
212	Phosphorylation	ALEELDVSSNRLRGL HHHHHCCCCHHHCCC	22.89	29888752
213	Phosphorylation	LEELDVSSNRLRGLP HHHHCCCCHHHCCCC	26.31	29888752
371	Acetylation	LSRVGLWKIKDNPLI CCCCCCEEECCCCCC	44.94	25953088
387	Ubiquitination	PPYEVCMKGIPYIAA CCHHHHHCCHHHHHH	48.86	-
447	Phosphorylation	GGDKEKCYPPSPPPV CCCHHHCCCCCCCCC	29.28	29759185
450	Phosphorylation	KEKCYPPSPPPVSKG HHHCCCCCCCCCCCC	45.60	26657352
455	Phosphorylation	PPSPPPVSKGIEVTS CCCCCCCCCCEEEEE	30.82	17924679
468	Phosphorylation	TSWTADASRGLRFIV EEEECCCCCCEEEEE	27.68	16094384
563	Ubiquitination	RQIALQEKHDAEGLS HHHHHHHHCCHHHHH	33.55	29967540
570	Phosphorylation	KHDAEGLSRLAKVVD HCCHHHHHHHHHHHH	35.78	23879269
601	Acetylation	AYYGVSDKNLRRRKA HHHCCCCHHHHHHHH	50.83	19608861
601	Malonylation	AYYGVSDKNLRRRKA HHHCCCCHHHHHHHH	50.83	26320211
601	Ubiquitination	AYYGVSDKNLRRRKA HHHCCCCHHHHHHHH	50.83	19608861
641	Ubiquitination	HLRRLRDKLLSVAEH HHHHHHHHHHHHHHH	44.91	-
644	Phosphorylation	RLRDKLLSVAEHREI HHHHHHHHHHHHHHH	29.71	22985185
696	O-linked_Glycosylation	LGLQAGLTEDRLQSA HHHHCCCCHHHHHHH	34.62	55832449
766	Phosphorylation	EGKAEGESSPPMARS CCCCCCCCCCCCCCC	60.03	30001349
767	Phosphorylation	GKAEGESSPPMARST CCCCCCCCCCCCCCC	28.81	30001349
848	Phosphorylation	LNGSTAWYKFPCYVQ CCCCCEEEEECEEEC	10.57	-
898	Phosphorylation	PLGLFARYSVQINSH CCEEEEEEEEEECCE	15.12	26074081
899	Phosphorylation	LGLFARYSVQINSHV CEEEEEEEEEECCEE	11.29	26074081
1004	Phosphorylation	AFPGELLSQPRPEGV CCCCHHHCCCCCCCE	51.25	24719451
1030	Phosphorylation	RVNVALVYPPTPTVI CEEEEEECCCCCCEE	12.35	26552605
1033	Phosphorylation	VALVYPPTPTVISPC EEEECCCCCCEECCC	27.38	28464451
1035	Phosphorylation	LVYPPTPTVISPCSK EECCCCCCEECCCCC	32.71	28464451
1038	Phosphorylation	PPTPTVISPCSKKNV CCCCCEECCCCCCCC	18.60	25159151
1041	Phosphorylation	PTVISPCSKKNVGEK CCEECCCCCCCCCHH	50.47	28464451

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

Oops, there are no upstream regulatory protein records of MFHA1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MFHA1_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 MFHA1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PJA2_HUMAN	PJA2	physical	28471450

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

"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-601, AND MASS SPECTROMETRY.
PubMed: 19608861

Phosphorylation

"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-447; SER-450 ANDSER-455, AND MASS SPECTROMETRY.
PubMed: 17924679

"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry.";
Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.;
Nat. Methods 2:591-598(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468, AND MASSSPECTROMETRY.
PubMed: 16094384