dbPTM

MBB1A_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MBB1A_MOUSE
UniProt AC	Q7TPV4
Protein Name	Myb-binding protein 1A
Gene Name	Mybbp1a
Organism	Mus musculus (Mouse).
Sequence Length	1344
Subcellular Localization	Nucleus . Nucleus, nucleolus . Cytoplasm . Predominantly nucleolar. Also shuttles between the nucleus and cytoplasm. Nuclear import may be mediated by KPNA2, while export appears to depend partially on XPO1/CRM1.
Protein Description	May activate or repress transcription via interactions with sequence specific DNA-binding proteins. Repression may be mediated at least in part by histone deacetylase activity (HDAC activity). Acts as a corepressor and in concert with CRY1, represses the transcription of the core circadian clock component PER2. Preferentially binds to dimethylated histone H3 'Lys-9' (H3K9me2) on the PER2 promoter. [PubMed: 19129230]
Protein Sequence	MAEMKSPTKAEPATPAEAAQSDRHSLLEHSREFLDFFWDIAKPDQETRLRATEKLLEYLRTRPNDSEMKYALKRLITGLGVGREAARPCYSLALAQLLQSFEDIPLCDILDQIQEKYSLQAMNKAMMRPSLFANLFGVLALFQSGRLVKDKEALMKSVQLLKILSQHPNHLQGQPIKALVDILSEVPESMFQEILPKVLKGNMKVILRSPKYLELFLLAKQRVPTKLESLMGSVDLFSEDNIPSLVNILKVAANSVKKEHKLPNVALDLLRLALKESRFELFWKKVLEEGLLKNPSWTSSYMCFRLLGASLPLLSEEQLQLVMRGDLIRHFGENMVISKPQNLFKIIPEISTYVGTFLEGCQDDPKRQLTMMVAFTTITNQGLPVMPTFWRVTRFLNAEALQSYVAWLRDMFLQPDLNSLVDFSTANQKRAQDASLNVPERAVFRLRKWIIHRLVSLVDHLHLEKDEAVVEQIARFCLFHAFFKTKKATPQIPETKQHFSFPLDDRNRGVFVSAFFSLLQTLSVKFRQTPDLAENGKPWTYRLVQLADMLLNHNRNVTSVTSLTTQQRQAWDQMMSTLKELEARSSETRAIAFQHLLLLVGLHIFKSPAESCDVLGDIQTCIKKSMEQNPRRSRSRAKASQEPVWVEVMVEILLSLLAQPSNLMRQVVRSVFGHICPHLTPRCLQLILAVLSPVTNEDEDDNVVVTDDADEKQLQHGEDEDSDNEDNKNSESDMDSEDGEESEEEDRDKDVDPGFRQQLMEVLKAGNALGGVDNEEEEELGDEAMMALDQNLASLFKEQKMRIQARNEEKNKLQKEKKLRRDFQIRALDLIEVLVTKQPEHPLILELLEPLLNVIQHSMRSKGSTKQEQDLLHKTARIFMHHLCRARRYCHEVGPCAEALHAQVERLVQQAGSQADASVALYYFNASLYLLRVLKGNTNKRHQDGHKLHGADTEDSEDQAANCLDLDFVTRVYSASLESLLTKRNSSLTVPMFLSLFSRYPVICKNLLPVLAQHVAGPSRPRHQAQACLMLQKTLSARELRVCFEDPEWEQLITQLLGKATQTLQTLGEAQSKGEHQKELSILELLNTLLRTVNHEKLSVDLTAPLGVLQSKQQKLQQSLQQGNHSSGSNRLYDLYWQAMRMLGVQRPKSEKKNAKDIPSDTQSPVSTKRKKKGFLPETKKRKKLKSEGTTPEKNAASQQDAVTEGAMPAATGKDQPPSTGKKKRKRVKASTPSQVNGITGAKSPAPSNPTLSPSTPAKTPKLQKKKEKLSQVNGATPVSPIEPESKKHHQEALSTKEVIRKSPHPQSALPKKRARLSLVSRSPSLLQSGVKKRRVASRRVQTP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAEMKSPTK ------CCCCCCCCC	36.57	19131326
6	Phosphorylation	--MAEMKSPTKAEPA --CCCCCCCCCCCCC	36.17	26824392
8	Phosphorylation	MAEMKSPTKAEPATP CCCCCCCCCCCCCCH	50.40	22942356
9	Succinylation	AEMKSPTKAEPATPA CCCCCCCCCCCCCHH	54.88	23806337
9	Acetylation	AEMKSPTKAEPATPA CCCCCCCCCCCCCHH	54.88	23806337
14	Phosphorylation	PTKAEPATPAEAAQS CCCCCCCCHHHHHHC	33.47	25521595
21	Phosphorylation	TPAEAAQSDRHSLLE CHHHHHHCCHHHHHH	31.70	25619855
25	Phosphorylation	AAQSDRHSLLEHSRE HHHCCHHHHHHHHHH	35.23	25159016
30	Phosphorylation	RHSLLEHSREFLDFF HHHHHHHHHHHHHHH	24.91	25159016
54	Acetylation	TRLRATEKLLEYLRT HHHHHHHHHHHHHHH	54.76	22826441
69	Acetylation	RPNDSEMKYALKRLI CCCCHHHHHHHHHHH	24.26	-
156	Acetylation	KDKEALMKSVQLLKI CCHHHHHHHHHHHHH	48.61	23806337
162	Acetylation	MKSVQLLKILSQHPN HHHHHHHHHHHHCCC	50.63	23806337
361	S-nitrosocysteine	VGTFLEGCQDDPKRQ HHHHHHHCCCCHHHH	2.68	-
361	S-nitrosylation	VGTFLEGCQDDPKRQ HHHHHHHCCCCHHHH	2.68	20925432
435	Phosphorylation	QKRAQDASLNVPERA HHHHHHCCCCCCHHH	28.85	27566939
456	Phosphorylation	WIIHRLVSLVDHLHL HHHHHHHHHHHHHCC	27.54	18779572
500	Phosphorylation	PETKQHFSFPLDDRN CCCCCEEECCCCCCC	24.67	26370283
559	Phosphorylation	NHNRNVTSVTSLTTQ HCCCCCCCCCCCHHH	21.08	29514104
561	Phosphorylation	NRNVTSVTSLTTQQR CCCCCCCCCCHHHHH	20.13	19854140
562	Phosphorylation	RNVTSVTSLTTQQRQ CCCCCCCCCHHHHHH	22.89	22006019
564	Phosphorylation	VTSVTSLTTQQRQAW CCCCCCCHHHHHHHH	23.48	29176673
620	Phosphorylation	DVLGDIQTCIKKSME CHHHHHHHHHHHHHH	19.28	18779572
676	S-nitrosocysteine	RSVFGHICPHLTPRC HHHHHHCCCCCCHHH	1.12	-
676	S-nitrosylation	RSVFGHICPHLTPRC HHHHHHCCCCCCHHH	1.12	20925432
706	Phosphorylation	EDDNVVVTDDADEKQ CCCCEEECCCCCHHH	19.29	21659604
722	Phosphorylation	QHGEDEDSDNEDNKN HCCCCCCCCCCCCCC	40.04	25521595
730	Phosphorylation	DNEDNKNSESDMDSE CCCCCCCCCCCCCCC	39.84	21149613
732	Phosphorylation	EDNKNSESDMDSEDG CCCCCCCCCCCCCCC	37.75	25521595
736	Phosphorylation	NSESDMDSEDGEESE CCCCCCCCCCCCCCH	30.83	25521595
742	Phosphorylation	DSEDGEESEEEDRDK CCCCCCCCHHHHHHC	46.11	25521595
890	S-nitrosylation	LCRARRYCHEVGPCA HHHHHHHHHHHHHHH	1.78	20925432
890	S-nitrosocysteine	LCRARRYCHEVGPCA HHHHHHHHHHHHHHH	1.78	-
896	S-nitrosocysteine	YCHEVGPCAEALHAQ HHHHHHHHHHHHHHH	4.37	-
896	S-nitrosylation	YCHEVGPCAEALHAQ HHHHHHHHHHHHHHH	4.37	20925432
953	Phosphorylation	HKLHGADTEDSEDQA CCCCCCCCCCCHHHH	40.95	25619855
956	Phosphorylation	HGADTEDSEDQAANC CCCCCCCCHHHHHHC	36.52	27087446
976	Phosphorylation	VTRVYSASLESLLTK HHHHHHHHHHHHHHH	27.08	22817900
979	Phosphorylation	VYSASLESLLTKRNS HHHHHHHHHHHHCCC	33.69	22817900
987	Phosphorylation	LLTKRNSSLTVPMFL HHHHCCCCCCHHHHH	31.44	19854140
989	Phosphorylation	TKRNSSLTVPMFLSL HHCCCCCCHHHHHHH	25.22	22817900
998	Phosphorylation	PMFLSLFSRYPVICK HHHHHHHHCCCHHHH	35.88	25890499
1000	Phosphorylation	FLSLFSRYPVICKNL HHHHHHCCCHHHHCH	10.72	-
1028	S-nitrosylation	PRHQAQACLMLQKTL HHHHHHHHHHHHHHC	1.20	20925432
1028	S-nitrosocysteine	PRHQAQACLMLQKTL HHHHHHHHHHHHHHC	1.20	-
1043	S-nitrosocysteine	SARELRVCFEDPEWE CHHHHHHHCCCHHHH	2.21	-
1043	S-nitrosylation	SARELRVCFEDPEWE CHHHHHHHCCCHHHH	2.21	20925432
1043	Glutathionylation	SARELRVCFEDPEWE CHHHHHHHCCCHHHH	2.21	24333276
1097	Acetylation	LRTVNHEKLSVDLTA HHHCCCCCCCCCCCC	38.21	23236377
1126	Phosphorylation	SLQQGNHSSGSNRLY HHHCCCCCCHHHHHH	40.15	25338131
1127	Phosphorylation	LQQGNHSSGSNRLYD HHCCCCCCHHHHHHH	38.39	29514104
1129	Phosphorylation	QGNHSSGSNRLYDLY CCCCCCHHHHHHHHH	22.26	25338131
1150	Phosphorylation	LGVQRPKSEKKNAKD HCCCCCCCCCCCCCC	58.28	29176673
1156	Acetylation	KSEKKNAKDIPSDTQ CCCCCCCCCCCCCCC	66.63	23806337
1160	Phosphorylation	KNAKDIPSDTQSPVS CCCCCCCCCCCCCCC	54.33	25521595
1162	Phosphorylation	AKDIPSDTQSPVSTK CCCCCCCCCCCCCCC	34.97	23684622
1164	Phosphorylation	DIPSDTQSPVSTKRK CCCCCCCCCCCCCHH	29.39	27087446
1167	Phosphorylation	SDTQSPVSTKRKKKG CCCCCCCCCCHHHCC	31.43	23375375
1168	Phosphorylation	DTQSPVSTKRKKKGF CCCCCCCCCHHHCCC	34.79	27566939
1187	Phosphorylation	KKRKKLKSEGTTPEK HHHHHHHCCCCCCCC	52.25	26824392
1190	Phosphorylation	KKLKSEGTTPEKNAA HHHHCCCCCCCCCCC	34.82	22942356
1191	Phosphorylation	KLKSEGTTPEKNAAS HHHCCCCCCCCCCCH	40.06	26824392
1198	Phosphorylation	TPEKNAASQQDAVTE CCCCCCCHHHHHHHC	26.43	23684622
1204	Phosphorylation	ASQQDAVTEGAMPAA CHHHHHHHCCCCCCC	30.35	25619855
1212	Phosphorylation	EGAMPAATGKDQPPS CCCCCCCCCCCCCCC	47.04	25619855
1219	Phosphorylation	TGKDQPPSTGKKKRK CCCCCCCCCCCCCCC	57.38	27087446
1220	Phosphorylation	GKDQPPSTGKKKRKR CCCCCCCCCCCCCCC	59.81	27087446
1231	Phosphorylation	KRKRVKASTPSQVNG CCCCCCCCCHHHHCC	34.82	25168779
1232	Phosphorylation	RKRVKASTPSQVNGI CCCCCCCCHHHHCCC	31.64	22942356
1234	Phosphorylation	RVKASTPSQVNGITG CCCCCCHHHHCCCCC	47.01	25168779
1240	Phosphorylation	PSQVNGITGAKSPAP HHHHCCCCCCCCCCC	32.27	25619855
1244	Phosphorylation	NGITGAKSPAPSNPT CCCCCCCCCCCCCCC	26.26	25521595
1248	Phosphorylation	GAKSPAPSNPTLSPS CCCCCCCCCCCCCCC	58.51	27149854
1251	Phosphorylation	SPAPSNPTLSPSTPA CCCCCCCCCCCCCCC	44.08	27087446
1253	Phosphorylation	APSNPTLSPSTPAKT CCCCCCCCCCCCCCC	21.20	27087446
1255	Phosphorylation	SNPTLSPSTPAKTPK CCCCCCCCCCCCCHH	43.58	27087446
1256	Phosphorylation	NPTLSPSTPAKTPKL CCCCCCCCCCCCHHH	30.56	27087446
1260	Phosphorylation	SPSTPAKTPKLQKKK CCCCCCCCHHHHHHH	27.97	22942356
1271	Phosphorylation	QKKKEKLSQVNGATP HHHHHHHHCCCCCCC	43.05	25619855
1277	Phosphorylation	LSQVNGATPVSPIEP HHCCCCCCCCCCCCC	26.14	27087446
1280	Phosphorylation	VNGATPVSPIEPESK CCCCCCCCCCCCCHH	22.74	27087446
1286	Phosphorylation	VSPIEPESKKHHQEA CCCCCCCHHHHHHHH	58.69	22942356
1288	Ubiquitination	PIEPESKKHHQEALS CCCCCHHHHHHHHHC	56.45	-
1295	Phosphorylation	KHHQEALSTKEVIRK HHHHHHHCCHHHHHH	44.47	19854140
1297	Acetylation	HQEALSTKEVIRKSP HHHHHCCHHHHHHCC	46.75	22826441
1303	Phosphorylation	TKEVIRKSPHPQSAL CHHHHHHCCCCCCCC	20.70	26824392
1308	Phosphorylation	RKSPHPQSALPKKRA HHCCCCCCCCCHHHH	35.90	25159016
1318	Phosphorylation	PKKRARLSLVSRSPS CHHHHHHHHHHCCHH	22.60	28725479
1321	Phosphorylation	RARLSLVSRSPSLLQ HHHHHHHHCCHHHHH	32.13	25619855
1322	Citrullination	ARLSLVSRSPSLLQS HHHHHHHCCHHHHHH	45.14	24463520
1322	Citrullination	ARLSLVSRSPSLLQS HHHHHHHCCHHHHHH	45.14	-
1323	Phosphorylation	RLSLVSRSPSLLQSG HHHHHHCCHHHHHHC	16.01	27087446
1325	Phosphorylation	SLVSRSPSLLQSGVK HHHHCCHHHHHHCCC	42.85	27087446
1329	Phosphorylation	RSPSLLQSGVKKRRV CCHHHHHHCCCCCCH	45.59	27087446

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
1280	S	Phosphorylation	Kinase	MAPK1	P63085	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MBB1A_MOUSE !!

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
Oops, there are no SNP-PTM records of MBB1A_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MYOD1_MOUSE	Myod1	physical	22333916
HDAC1_MOUSE	Hdac1	physical	22333916
HDAC2_MOUSE	Hdac2	physical	22333916
ZN746_MOUSE	Zfp746	physical	25315684

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of MBB1A_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1253, AND MASSSPECTROMETRY.	19131326 [Abstract]
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-722, AND MASSSPECTROMETRY.	19367708 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-1164; SER-1198;SER-1253; THR-1277 AND SER-1280, AND MASS SPECTROMETRY.	17242355 [Abstract]
"Phosphoproteomic analysis of the developing mouse brain."; Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; Mol. Cell. Proteomics 3:1093-1101(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1253, AND MASSSPECTROMETRY.	15345747 [Abstract]