MN1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MN1_HUMAN
• UniProt AC: Q10571
• Protein Name: Transcriptional activator MN1 {ECO:0000305}
• Gene Name: MN1
• Organism: Homo sapiens (Human).
• Sequence Length: 1320
• Protein Description: Transcriptional activator which specifically regulates expression of TBX22 in the posterior region of the developing palate. Required during later stages of palate development for growth and medial fusion of the palatal shelves. Promotes maturation and normal function of calvarial osteoblasts, including expression of the osteoclastogenic cytokine TNFSF11/RANKL. Necessary for normal development of the membranous bones of the skull (By similarity). May play a role in tumor suppression (Probable)..
• Protein Sequence: MFGLDQFEPQVNSRNAGQGERNFNETGLSMNTHFKAPAFHTGGPPGPVDPAMSALGEPPILGMNMEPYGFHARGHSELHAGGLQAQPVHGFFGGQQPHHGHPGSHHPHQHHPHFGGNFGGPDPGASCLHGGRLLGYGGAAGGLGSQPPFAEGYEHMAESQGPESFGPQRPGNLPDFHSSGASSHAVPAPCLPLDQSPNRAASFHGLPSSSGSDSHSLEPRRVTNQGAVDSLEYNYPGEAPSGHFDMFSPSDSEGQLPHYAAGRQVPGGAFPGASAMPRAAGMVGLSKMHAQPPQQQPQQQQQPQQQQQQHGVFFERFSGARKMPVGLEPSVGSRHPLMQPPQQAPPPPQQQPPQQPPQQQPPPPPGLLVRQNSCPPALPRPQQGEAGTPSGGLQDGGPMLPSQHAQFEYPIHRLENRSMHPYSEPVFSMQHPPPQQAPNQRLQHFDAPPYMNVAKRPRFDFPGSAGVDRCASWNGSMHNGALDNHLSPSAYPGLPGEFTPPVPDSFPSGPPLQHPAPDHQSLQQQQQQQQQQQQQQQQQQQQQQQQQQQQRQNAALMIKQMASRNQQQRLRQPNLAQLGHPGDVGQGGLVHGGPVGGLAQPNFEREGGSTGAGRLGTFEQQAPHLAQESAWFSGPHPPPGDLLPRRMGGSGLPADCGPHDPSLAPPPPPGGSGVLFRGPLQEPMRMPGEGHVPALPSPGLQFGGSLGGLGQLQSPGAGVGLPSAASERRPPPPDFATSALGGQPGFPFGAAGRQSTPHSGPGVNSPPSAGGGGGSSGGGGGGGAYPPQPDFQPSQRTSASKLGALSLGSFNKPSSKDNLFGQSCLAALSTACQNMIASLGAPNLNVTFNKKNPPEGKRKLSQNETDGAAVAGNPGSDYFPGGTAPGAPGPGGPSGTSSSGSKASGPPNPPAQGDGTSLSPNYTLESTSGNDGKPVSGGGGRGRGRRKRDSGHVSPGTFFDKYSAAPDSGGAPGVSPGQQQASGAAVGGSSAGETRGAPTPHEKALTSPSWGKGAELLLGDQPDLIGSLDGGAKSDSSSPNVGEFASDEVSTSYANEDEVSSSSDNPQALVKASRSPLVTGSPKLPPRGVGAGEHGPKAPPPALGLGIMSNSTSTPDSYGGGGGPGHPGTPGLEQVRTPTSSSGAPPPDEIHPLEILQAQIQLQRQQFSISEDQPLGLKGGKKGECAVGASGAQNGDSELGSCCSEAVKSAMSTIDLDSLMAEHSAAWYMPADKALVDSADDDKTLAPWEKAKPQNPNSKEAHDLPANKASASQPGSHLQCLSVHCTDDVGDAKARASVPTWRSLHSDISNRFGTFVAALT

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	-------MFGLDQFE -------CCCCCCCC	28.80	22814378
202	Phosphorylation	QSPNRAASFHGLPSS CCCCCCHHHCCCCCC	19.45	22210691
210	Phosphorylation	FHGLPSSSGSDSHSL HCCCCCCCCCCCCCC	46.80	22210691
259	Phosphorylation	SEGQLPHYAAGRQVP CCCCCCCCCCCCCCC	9.01	-
274	Phosphorylation	GGAFPGASAMPRAAG CCCCCCCCCCHHHHH	30.89	24719451
286	Phosphorylation	AAGMVGLSKMHAQPP HHHHHCHHHHCCCCC	23.23	-
330	Phosphorylation	MPVGLEPSVGSRHPL CCCCCCCCCCCCCCC	29.72	-
333	Phosphorylation	GLEPSVGSRHPLMQP CCCCCCCCCCCCCCC	25.84	29083192
373	Phosphorylation	GLLVRQNSCPPALPR CCEEECCCCCCCCCC	21.47	-
428	O-linked_Glycosylation	PYSEPVFSMQHPPPQ CCCCCCCCCCCCCCC	20.12	29351928
775	Phosphorylation	SAGGGGGSSGGGGGG CCCCCCCCCCCCCCC	29.14	-
776	Phosphorylation	AGGGGGSSGGGGGGG CCCCCCCCCCCCCCC	44.74	22817900
785	Phosphorylation	GGGGGGAYPPQPDFQ CCCCCCCCCCCCCCC	20.79	-
794	Phosphorylation	PQPDFQPSQRTSASK CCCCCCCCCCCCHHH	22.85	-
806	Phosphorylation	ASKLGALSLGSFNKP HHHHCCCHHCCCCCC	30.10	29449344
809	Phosphorylation	LGALSLGSFNKPSSK HCCCHHCCCCCCCCC	30.82	29449344
814	Phosphorylation	LGSFNKPSSKDNLFG HCCCCCCCCCCCCCH	52.18	29449344
815	Phosphorylation	GSFNKPSSKDNLFGQ CCCCCCCCCCCCCHH	53.18	25627689
861	Phosphorylation	PEGKRKLSQNETDGA CCCCCCCCCCCCCCC	33.71	19276368
865	Phosphorylation	RKLSQNETDGAAVAG CCCCCCCCCCCCCCC	47.48	21130716
950	Phosphorylation	RGRRKRDSGHVSPGT CCCCCCCCCCCCCCC	34.53	23663014
954	Phosphorylation	KRDSGHVSPGTFFDK CCCCCCCCCCCCHHH	16.37	23663014
957	Phosphorylation	SGHVSPGTFFDKYSA CCCCCCCCCHHHCCC	25.23	23663014
968	Phosphorylation	KYSAAPDSGGAPGVS HCCCCCCCCCCCCCC	37.76	-
975	Phosphorylation	SGGAPGVSPGQQQAS CCCCCCCCCCCCCCC	29.27	30576142
982	Phosphorylation	SPGQQQASGAAVGGS CCCCCCCCCCCCCCC	25.32	-
994	Phosphorylation	GGSSAGETRGAPTPH CCCCCCCCCCCCCCC	33.22	-
999	Phosphorylation	GETRGAPTPHEKALT CCCCCCCCCCHHHCC	36.42	-
1006	Phosphorylation	TPHEKALTSPSWGKG CCCHHHCCCCCCCCC	43.37	23186163
1007	Phosphorylation	PHEKALTSPSWGKGA CCHHHCCCCCCCCCC	20.14	25159151
1009	Phosphorylation	EKALTSPSWGKGAEL HHHCCCCCCCCCCHH	48.50	23186163
1012	Acetylation	LTSPSWGKGAELLLG CCCCCCCCCCHHHCC	49.00	23954790
1073	Phosphorylation	PQALVKASRSPLVTG HHHHHHHHCCCCCCC	27.81	22167270
1075	Phosphorylation	ALVKASRSPLVTGSP HHHHHHCCCCCCCCC	21.79	23663014
1079	Phosphorylation	ASRSPLVTGSPKLPP HHCCCCCCCCCCCCC	39.36	23663014
1080	Phosphorylation	SRSPLVTGSPKLPPR HCCCCCCCCCCCCCC	34.18	15302935
1081	Phosphorylation	RSPLVTGSPKLPPRG CCCCCCCCCCCCCCC	14.97	30266825
1182	Acetylation	LGLKGGKKGECAVGA CCCCCCCCCCCCCCC	64.32	69079

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

Oops, there are no upstream regulatory protein records of MN1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MN1_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
373	Phosphorylation	382 (9)	Q ⇒ H	rs45589338	Breast cancer	29059683

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EP300_HUMAN	EP300	physical	12569362
NCOA3_HUMAN	NCOA3	physical	12569362

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

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-1081, AND MASSSPECTROMETRY.
PubMed: 15302935