dbPTM

MBB1A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MBB1A_HUMAN
UniProt AC	Q9BQG0
Protein Name	Myb-binding protein 1A
Gene Name	MYBBP1A
Organism	Homo sapiens (Human).
Sequence Length	1328
Subcellular Localization	Cytoplasm . Nucleus . Nucleus, nucleolus . Shuttles between the nucleus and cytoplasm. Nuclear import may be mediated by KPNA2, while export appears to depend partially on XPO1/CRM1 (By similarity). Predominantly nucleolar.
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..
Protein Sequence	MESRDPAQPMSPGEATQSGARPADRYGLLKHSREFLDFFWDIAKPEQETRLAATEKLLEYLRGRPKGSEMKYALKRLITGLGVGRETARPCYSLALAQLLQSFEDLPLCSILQQIQEKYDLHQVKKAMLRPALFANLFGVLALFQSGRLVKDQEALMKSVKLLQALAQYQNHLQEQPRKALVDILSEVSKATLQEILPEVLKADLNIILSSPEQLELFLLAQQKVPSKLKKLVGSVNLFSDENVPRLVNVLKMAASSVKKDRKLPAIALDLLRLALKEDKFPRFWKEVVEQGLLKMQFWPASYLCFRLLGAALPLLTKEQLHLVMQGDVIRHYGEHVCTAKLPKQFKFAPEMDDYVGTFLEGCQDDPERQLAVLVAFSSVTNQGLPVTPTFWRVVRFLSPPALQGYVAWLRAMFLQPDLDSLVDFSTNNQKKAQDSSLHMPERAVFRLRKWIIFRLVSIVDSLHLEMEEALTEQVARFCLFHSFFVTKKPTSQIPETKHPFSFPLENQAREAVSSAFFSLLQTLSTQFKQAPGQTQGGQPWTYHLVQFADLLLNHSHNVTTVTPFTAQQRQAWDRMLQTLKELEAHSAEARAAAFQHLLLLVGIHLLKSPAESCDLLGDIQTCIRKSLGEKPRRSRTKTIDPQEPPWVEVLVEILLALLAQPSHLMRQVARSVFGHICSHLTPRALQLILDVLNPETSEDENDRVVVTDDSDERRLKGAEDKSEEGEDNRSSESEEESEGEESEEEERDGDVDQGFREQLMTVLQAGKALGGEDSENEEELGDEAMMALDQSLASLFAEQKLRIQARRDEKNKLQKEKALRRDFQIRVLDLVEVLVTKQPENALVLELLEPLLSIIRRSLRSSSSKQEQDLLHKTARIFTHHLCRARRYCHDLGERAGALHAQVERLVQQAGRQPDSPTALYHFNASLYLLRVLKGNTAEGCVHETQEKQKAGTDPSHMPTGPQAASCLDLNLVTRVYSTALSSFLTKRNSPLTVPMFLSLFSRHPVLCQSLLPILVQHITGPVRPRHQACLLLQKTLSMREVRSCFEDPEWKQLMGQVLAKVTENLRVLGEAQTKAQHQQALSSLELLNVLFRTCKHEKLTLDLTVLLGVLQGQQQSLQQGAHSTGSSRLHDLYWQAMKTLGVQRPKLEKKDAKEIPSATQSPISKKRKKKGFLPETKKRKKRKSEDGTPAEDGTPAATGGSQPPSMGRKKRNRTKAKVPAQANGTPTTKSPAPGAPTRSPSTPAKSPKLQKKNQKPSQVNGAPGSPTEPAGQKQHQKALPKKGVLGKSPLSALARKKARLSLVIRSPSLLQSGAKKKAQVRKAGKP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MESRDPAQ -------CCCCCCCC	44.98	-
3	Phosphorylation	-----MESRDPAQPM -----CCCCCCCCCC	54.57	26074081
10	Sulfoxidation	SRDPAQPMSPGEATQ CCCCCCCCCCCCCCC	5.12	21406390
11	Phosphorylation	RDPAQPMSPGEATQS CCCCCCCCCCCCCCC	36.11	19664994
11 (in isoform 2)	Phosphorylation	-	36.11	24719451
16	Phosphorylation	PMSPGEATQSGARPA CCCCCCCCCCCCCCH	20.97	23927012
16 (in isoform 2)	Phosphorylation	-	20.97	21406692
18	Phosphorylation	SPGEATQSGARPADR CCCCCCCCCCCCHHH	30.02	25159151
18 (in isoform 2)	Phosphorylation	-	30.02	21406692
26	Phosphorylation	GARPADRYGLLKHSR CCCCHHHHHCHHHHH	16.81	24732914
30	Acetylation	ADRYGLLKHSREFLD HHHHHCHHHHHHHHH	44.57	26051181
30	Methylation	ADRYGLLKHSREFLD HHHHHCHHHHHHHHH	44.57	115973417
30	Ubiquitination	ADRYGLLKHSREFLD HHHHHCHHHHHHHHH	44.57	29967540
30 (in isoform 2)	Ubiquitination	-	44.57	-
32	Phosphorylation	RYGLLKHSREFLDFF HHHCHHHHHHHHHHH	31.73	26074081
44	Ubiquitination	DFFWDIAKPEQETRL HHHHHHCCHHHHHHH	49.80	-
49	Phosphorylation	IAKPEQETRLAATEK HCCHHHHHHHHHHHH	30.58	21406692
54	Phosphorylation	QETRLAATEKLLEYL HHHHHHHHHHHHHHH	28.22	21406692
56	Acetylation	TRLAATEKLLEYLRG HHHHHHHHHHHHHCC	54.76	25953088
56	Ubiquitination	TRLAATEKLLEYLRG HHHHHHHHHHHHHCC	54.76	21963094
56 (in isoform 1)	Ubiquitination	-	54.76	21890473
56 (in isoform 2)	Ubiquitination	-	54.76	21890473
60	Phosphorylation	ATEKLLEYLRGRPKG HHHHHHHHHCCCCCC	11.15	17081983
71	Acetylation	RPKGSEMKYALKRLI CCCCHHHHHHHHHHH	24.26	19608861
71	Ubiquitination	RPKGSEMKYALKRLI CCCCHHHHHHHHHHH	24.26	29967540
71 (in isoform 2)	Ubiquitination	-	24.26	-
79	Phosphorylation	YALKRLITGLGVGRE HHHHHHHHHCCCCHH	30.83	-
93	O-linked_Glycosylation	ETARPCYSLALAQLL HHHHHHHHHHHHHHH	17.55	29351928
95	Ubiquitination	ARPCYSLALAQLLQS HHHHHHHHHHHHHHH	8.56	21963094
102	O-linked_Glycosylation	ALAQLLQSFEDLPLC HHHHHHHHCCCCCHH	30.49	29351928
125	Acetylation	KYDLHQVKKAMLRPA HCCHHHHHHHHHHHH	28.39	26051181
125	Ubiquitination	KYDLHQVKKAMLRPA HCCHHHHHHHHHHHH	28.39	33845483
128	Sulfoxidation	LHQVKKAMLRPALFA HHHHHHHHHHHHHHH	4.47	28183972
151	Ubiquitination	FQSGRLVKDQEALMK HHCCCCCCCHHHHHH	59.28	-
151 (in isoform 2)	Ubiquitination	-	59.28	-
157	Sulfoxidation	VKDQEALMKSVKLLQ CCCHHHHHHHHHHHH	3.81	21406390
158	Acetylation	KDQEALMKSVKLLQA CCHHHHHHHHHHHHH	53.61	19608861
158	Malonylation	KDQEALMKSVKLLQA CCHHHHHHHHHHHHH	53.61	26320211
158	Ubiquitination	KDQEALMKSVKLLQA CCHHHHHHHHHHHHH	53.61	22817900
161	Ubiquitination	EALMKSVKLLQALAQ HHHHHHHHHHHHHHH	51.04	21890473
161 (in isoform 1)	Ubiquitination	-	51.04	21890473
161 (in isoform 2)	Ubiquitination	-	51.04	21890473
169	Phosphorylation	LLQALAQYQNHLQEQ HHHHHHHHHHHHHHC	12.99	28152594
179	Acetylation	HLQEQPRKALVDILS HHHHCHHHHHHHHHH	53.40	26051181
179	Ubiquitination	HLQEQPRKALVDILS HHHHCHHHHHHHHHH	53.40	22817900
179 (in isoform 1)	Ubiquitination	-	53.40	21890473
179 (in isoform 2)	Ubiquitination	-	53.40	21890473
186	Phosphorylation	KALVDILSEVSKATL HHHHHHHHHHCHHHH	35.96	-
189	Phosphorylation	VDILSEVSKATLQEI HHHHHHHCHHHHHHH	16.72	20071362
228	Ubiquitination	AQQKVPSKLKKLVGS HHCCCCHHHHHHHCC	59.25	22817900
230	Ubiquitination	QKVPSKLKKLVGSVN CCCCHHHHHHHCCCC	48.04	22817900
231	Malonylation	KVPSKLKKLVGSVNL CCCHHHHHHHCCCCC	59.86	26320211
231	Ubiquitination	KVPSKLKKLVGSVNL CCCHHHHHHHCCCCC	59.86	22817900
231 (in isoform 1)	Ubiquitination	-	59.86	21890473
231 (in isoform 2)	Ubiquitination	-	59.86	21890473
252	Acetylation	PRLVNVLKMAASSVK HHHHHHHHHHHHHCC	23.39	25953088
252	Ubiquitination	PRLVNVLKMAASSVK HHHHHHHHHHHHHCC	23.39	24816145
259	Acetylation	KMAASSVKKDRKLPA HHHHHHCCCCCCCCH	51.40	25953088
277	Ubiquitination	DLLRLALKEDKFPRF HHHHHHHHCCCCHHH	59.25	-
286	Acetylation	DKFPRFWKEVVEQGL CCCHHHHHHHHHHCC	37.61	26051181
302	Phosphorylation	KMQFWPASYLCFRLL HHCCCCHHHHHHHHH	17.98	20068231
303	Phosphorylation	MQFWPASYLCFRLLG HCCCCHHHHHHHHHH	15.03	20068231
329	Ubiquitination	HLVMQGDVIRHYGEH HHHHCCCHHHHHCCC	5.46	24816145
333	Phosphorylation	QGDVIRHYGEHVCTA CCCHHHHHCCCEEEC	17.85	28152594
341	Acetylation	GEHVCTAKLPKQFKF CCCEEECCCCCCCCC	47.36	25953088
341	Ubiquitination	GEHVCTAKLPKQFKF CCCEEECCCCCCCCC	47.36	32015554
341 (in isoform 2)	Ubiquitination	-	47.36	-
347	Ubiquitination	AKLPKQFKFAPEMDD CCCCCCCCCCCCCCC	37.82	21963094
363	Glutathionylation	VGTFLEGCQDDPERQ HHHHHHHCCCCHHHH	2.68	22555962
374	Ubiquitination	PERQLAVLVAFSSVT HHHHHHHHHHHHHHC	1.59	24816145
399	Phosphorylation	WRVVRFLSPPALQGY HHHHHHHCCHHHHHH	26.56	-
413	Sulfoxidation	YVAWLRAMFLQPDLD HHHHHHHHHHCCCHH	2.52	28183972
421	Phosphorylation	FLQPDLDSLVDFSTN HHCCCHHHHCCCCCC	37.27	20873877
426	O-linked_Glycosylation	LDSLVDFSTNNQKKA HHHHCCCCCCCHHHH	26.26	29351928
426	Phosphorylation	LDSLVDFSTNNQKKA HHHHCCCCCCCHHHH	26.26	20873877
427	O-linked_Glycosylation	DSLVDFSTNNQKKAQ HHHCCCCCCCHHHHC	37.88	29351928
432	Ubiquitination	FSTNNQKKAQDSSLH CCCCCHHHHCCCCCC	41.33	-
432 (in isoform 2)	Ubiquitination	-	41.33	-
450	Acetylation	RAVFRLRKWIIFRLV HHHHHHHHHHHHHHH	47.54	26051181
487	Phosphorylation	LFHSFFVTKKPTSQI HHHHHHCCCCCCCCC	28.35	-
488	Acetylation	FHSFFVTKKPTSQIP HHHHHCCCCCCCCCC	51.99	26051181
489	Acetylation	HSFFVTKKPTSQIPE HHHHCCCCCCCCCCC	44.13	26051181
491	Phosphorylation	FFVTKKPTSQIPETK HHCCCCCCCCCCCCC	41.99	25850435
492	Phosphorylation	FVTKKPTSQIPETKH HCCCCCCCCCCCCCC	34.34	25849741
497	Phosphorylation	PTSQIPETKHPFSFP CCCCCCCCCCCCCCC	29.33	25850435
498	Acetylation	TSQIPETKHPFSFPL CCCCCCCCCCCCCCC	47.85	25953088
498	Ubiquitination	TSQIPETKHPFSFPL CCCCCCCCCCCCCCC	47.85	-
502	Phosphorylation	PETKHPFSFPLENQA CCCCCCCCCCCCHHH	30.33	23312004
514	Phosphorylation	NQAREAVSSAFFSLL HHHHHHHHHHHHHHH	24.01	21601212
523	Phosphorylation	AFFSLLQTLSTQFKQ HHHHHHHHHHHHHHC	23.73	21601212
561	Ubiquitination	NHSHNVTTVTPFTAQ HCCCCCCEECCCCHH	20.35	24816145
581	Acetylation	DRMLQTLKELEAHSA HHHHHHHHHHHHCCH	64.74	26051181
581	Ubiquitination	DRMLQTLKELEAHSA HHHHHHHHHHHHCCH	64.74	24816145
581 (in isoform 1)	Ubiquitination	-	64.74	21890473
581 (in isoform 2)	Ubiquitination	-	64.74	21890473
591	Methylation	EAHSAEARAAAFQHL HHCCHHHHHHHHHHH	19.10	115388349
613	Phosphorylation	LLKSPAESCDLLGDI HHCCHHHHCCHHHHH	18.29	25159151
614	Ubiquitination	LKSPAESCDLLGDIQ HCCHHHHCCHHHHHH	3.00	24816145
626	Ubiquitination	DIQTCIRKSLGEKPR HHHHHHHHHCCCCCC	30.07	24816145
631	Acetylation	IRKSLGEKPRRSRTK HHHHCCCCCCCCCCC	41.86	23749302
631	Ubiquitination	IRKSLGEKPRRSRTK HHHHCCCCCCCCCCC	41.86	29967540
635	Phosphorylation	LGEKPRRSRTKTIDP CCCCCCCCCCCCCCC	45.65	17081983
637	Phosphorylation	EKPRRSRTKTIDPQE CCCCCCCCCCCCCCC	33.51	29759185
663	Phosphorylation	LALLAQPSHLMRQVA HHHHCCHHHHHHHHH	19.71	-
672	Phosphorylation	LMRQVARSVFGHICS HHHHHHHHHHHHHHH	16.44	20873877
683	Ubiquitination	HICSHLTPRALQLIL HHHHCCCHHHHHHHH	26.38	21963094
697	Phosphorylation	LDVLNPETSEDENDR HHHHCCCCCCCCCCC	38.38	29116813
698	Phosphorylation	DVLNPETSEDENDRV HHHCCCCCCCCCCCE	41.19	20873877
708	Phosphorylation	ENDRVVVTDDSDERR CCCCEEECCCHHHHH	23.60	21815630
711	Phosphorylation	RVVVTDDSDERRLKG CEEECCCHHHHHHCC	44.15	25849741
723	Phosphorylation	LKGAEDKSEEGEDNR HCCCCCCCCCCCCCC	53.88	25137130
731	Phosphorylation	EEGEDNRSSESEEES CCCCCCCCCCCCCHH	44.72	25137130
732	Phosphorylation	EGEDNRSSESEEESE CCCCCCCCCCCCHHC	41.74	25137130
734	Phosphorylation	EDNRSSESEEESEGE CCCCCCCCCCHHCCC	52.86	25137130
736	Ubiquitination	NRSSESEEESEGEES CCCCCCCCHHCCCCC	75.90	21890473
738	Phosphorylation	SSESEEESEGEESEE CCCCCCHHCCCCCHH	54.93	25137130
743	Phosphorylation	EESEGEESEEEERDG CHHCCCCCHHHHHCC	46.11	25137130
761	Sulfoxidation	QGFREQLMTVLQAGK HHHHHHHHHHHHHHH	2.14	21406390
775	Phosphorylation	KALGGEDSENEEELG HHHCCCCCCCHHHHH	37.71	25159151
775 (in isoform 2)	Phosphorylation	-	37.71	24719451
784	Ubiquitination	NEEELGDEAMMALDQ CHHHHHHHHHHHHHH	36.34	21890473
792	Phosphorylation	AMMALDQSLASLFAE HHHHHHHHHHHHHHH	26.10	25159151
795	Phosphorylation	ALDQSLASLFAEQKL HHHHHHHHHHHHHHH	29.34	30175587
813	Ubiquitination	ARRDEKNKLQKEKAL HHHHHHHHHHHHHHH	64.46	24816145
859	Phosphorylation	LLSIIRRSLRSSSSK HHHHHHHHHHCCCCH	20.48	-
862	Phosphorylation	IIRRSLRSSSSKQEQ HHHHHHHCCCCHHHH	39.61	20873877
863	Phosphorylation	IRRSLRSSSSKQEQD HHHHHHCCCCHHHHH	32.00	20873877
864	Phosphorylation	RRSLRSSSSKQEQDL HHHHHCCCCHHHHHH	42.68	20873877
865	Phosphorylation	RSLRSSSSKQEQDLL HHHHCCCCHHHHHHH	40.06	22210691
866	Ubiquitination	SLRSSSSKQEQDLLH HHHCCCCHHHHHHHH	60.86	24816145
866 (in isoform 2)	Ubiquitination	-	60.86	-
874	Ubiquitination	QEQDLLHKTARIFTH HHHHHHHHHHHHHHH	43.80	-
874 (in isoform 2)	Ubiquitination	-	43.80	-
888	Ubiquitination	HHLCRARRYCHDLGE HHHHHHHHHHHHHHH	37.13	21890473
889	Phosphorylation	HLCRARRYCHDLGER HHHHHHHHHHHHHHH	6.65	28152594
896	Methylation	YCHDLGERAGALHAQ HHHHHHHHHCHHHHH	36.20	115484091
920	Ubiquitination	RQPDSPTALYHFNAS CCCCCCCHHHHHHHH	14.98	24816145
933	Ubiquitination	ASLYLLRVLKGNTAE HHHHHHHHHCCCCCC	6.99	24816145
935	Acetylation	LYLLRVLKGNTAEGC HHHHHHHCCCCCCCC	47.46	26822725
935	Ubiquitination	LYLLRVLKGNTAEGC HHHHHHHCCCCCCCC	47.46	21963094
935 (in isoform 2)	Ubiquitination	-	47.46	-
942	Glutathionylation	KGNTAEGCVHETQEK CCCCCCCCCCCHHHH	1.81	22555962
946	Phosphorylation	AEGCVHETQEKQKAG CCCCCCCHHHHHHCC	27.44	25159151
949	Acetylation	CVHETQEKQKAGTDP CCCCHHHHHHCCCCC	47.48	26051181
949	Ubiquitination	CVHETQEKQKAGTDP CCCCHHHHHHCCCCC	47.48	29967540
967	Ubiquitination	PTGPQAASCLDLNLV CCCHHHHHHHCHHHH	20.44	24816145
968	Glutathionylation	TGPQAASCLDLNLVT CCHHHHHHHCHHHHH	2.69	22555962
978	Phosphorylation	LNLVTRVYSTALSSF HHHHHHHHHHHHHHH	9.30	24719451
978 (in isoform 2)	Phosphorylation	-	9.30	24719451
979	Phosphorylation	NLVTRVYSTALSSFL HHHHHHHHHHHHHHH	12.35	28152594
980	Phosphorylation	LVTRVYSTALSSFLT HHHHHHHHHHHHHHH	17.58	24719451
980 (in isoform 2)	Phosphorylation	-	17.58	24719451
983	Phosphorylation	RVYSTALSSFLTKRN HHHHHHHHHHHHHCC	19.31	20860994
984	Phosphorylation	VYSTALSSFLTKRNS HHHHHHHHHHHHCCC	25.73	21406692
987	Phosphorylation	TALSSFLTKRNSPLT HHHHHHHHHCCCCCH	26.41	20860994
987 (in isoform 2)	Phosphorylation	-	26.41	21406692
988	Acetylation	ALSSFLTKRNSPLTV HHHHHHHHCCCCCHH	52.29	25953088
988	Ubiquitination	ALSSFLTKRNSPLTV HHHHHHHHCCCCCHH	52.29	21890473
988 (in isoform 1)	Ubiquitination	-	52.29	21890473
988 (in isoform 2)	Ubiquitination	-	52.29	21890473
991	Phosphorylation	SFLTKRNSPLTVPMF HHHHHCCCCCHHHHH	25.89	27461979
994	Phosphorylation	TKRNSPLTVPMFLSL HHCCCCCHHHHHHHH	26.41	27461979
994 (in isoform 2)	Phosphorylation	-	26.41	24719451
1000	Phosphorylation	LTVPMFLSLFSRHPV CHHHHHHHHHHCCHH	18.99	27461979
1003	Phosphorylation	PMFLSLFSRHPVLCQ HHHHHHHHCCHHHHH	34.67	27461979
1011	Phosphorylation	RHPVLCQSLLPILVQ CCHHHHHHHHHHHHH	30.77	-
1021	Phosphorylation	PILVQHITGPVRPRH HHHHHHCCCCCCHHH	33.05	-
1031	S-nitrosocysteine	VRPRHQACLLLQKTL CCHHHHHHHHHHHHC	1.90	-
1031	S-nitrosylation	VRPRHQACLLLQKTL CCHHHHHHHHHHHHC	1.90	19483679
1036	Acetylation	QACLLLQKTLSMREV HHHHHHHHHCCHHHH	51.94	26051181
1036	Ubiquitination	QACLLLQKTLSMREV HHHHHHHHHCCHHHH	51.94	21890473
1036 (in isoform 1)	Ubiquitination	-	51.94	21890473
1036 (in isoform 2)	Ubiquitination	-	51.94	21890473
1046	Glutathionylation	SMREVRSCFEDPEWK CHHHHHHHCCCHHHH	2.80	22555962
1053	Acetylation	CFEDPEWKQLMGQVL HCCCHHHHHHHHHHH	31.71	26051181
1053	Ubiquitination	CFEDPEWKQLMGQVL HCCCHHHHHHHHHHH	31.71	29967540
1062	Acetylation	LMGQVLAKVTENLRV HHHHHHHHHHHHHHH	45.59	26051181
1062	Ubiquitination	LMGQVLAKVTENLRV HHHHHHHHHHHHHHH	45.59	-
1062 (in isoform 2)	Ubiquitination	-	45.59	-
1067	Ubiquitination	LAKVTENLRVLGEAQ HHHHHHHHHHHHHHH	3.05	24816145
1139	Sulfoxidation	HDLYWQAMKTLGVQR HHHHHHHHHHHCCCC	1.72	28183972
1140	Acetylation	DLYWQAMKTLGVQRP HHHHHHHHHHCCCCC	43.55	26051181
1140	Ubiquitination	DLYWQAMKTLGVQRP HHHHHHHHHHCCCCC	43.55	22817900
1140 (in isoform 1)	Ubiquitination	-	43.55	21890473
1140 (in isoform 2)	Ubiquitination	-	43.55	21890473
1148	Sumoylation	TLGVQRPKLEKKDAK HHCCCCCCCCCCCHH	72.04	28112733
1148	Ubiquitination	TLGVQRPKLEKKDAK HHCCCCCCCCCCCHH	72.04	29967540
1155	Acetylation	KLEKKDAKEIPSATQ CCCCCCHHHCCCCCC	67.33	26051181
1155	Ubiquitination	KLEKKDAKEIPSATQ CCCCCCHHHCCCCCC	67.33	29967540
1159	Phosphorylation	KDAKEIPSATQSPIS CCHHHCCCCCCCCCC	50.00	29255136
1159 (in isoform 2)	Phosphorylation	-	50.00	24719451
1161	Phosphorylation	AKEIPSATQSPISKK HHHCCCCCCCCCCHH	33.64	29255136
1161 (in isoform 2)	Phosphorylation	-	33.64	21406692
1163	Phosphorylation	EIPSATQSPISKKRK HCCCCCCCCCCHHHH	21.61	19664994
1163 (in isoform 2)	Phosphorylation	-	21.61	24719451
1166	Phosphorylation	SATQSPISKKRKKKG CCCCCCCCHHHHHCC	35.19	29255136
1167	Acetylation	ATQSPISKKRKKKGF CCCCCCCHHHHHCCC	58.27	25953088
1172	Ubiquitination	ISKKRKKKGFLPETK CCHHHHHCCCCCHHH	58.91	24816145
1178	Phosphorylation	KKGFLPETKKRKKRK HCCCCCHHHHCCCCC	39.67	24173317
1179	Acetylation	KGFLPETKKRKKRKS CCCCCHHHHCCCCCC	49.25	25953088
1185	Acetylation	TKKRKKRKSEDGTPA HHHCCCCCCCCCCCC	68.05	26051181
1185	Ubiquitination	TKKRKKRKSEDGTPA HHHCCCCCCCCCCCC	68.05	24816145
1186	Phosphorylation	KKRKKRKSEDGTPAE HHCCCCCCCCCCCCC	44.98	30266825
1186 (in isoform 2)	Phosphorylation	-	44.98	24719451
1190	Phosphorylation	KRKSEDGTPAEDGTP CCCCCCCCCCCCCCC	31.48	30266825
1196	Phosphorylation	GTPAEDGTPAATGGS CCCCCCCCCCCCCCC	23.29	30266825
1196 (in isoform 2)	Phosphorylation	-	23.29	27251275
1200	Phosphorylation	EDGTPAATGGSQPPS CCCCCCCCCCCCCCC	44.15	23927012
1203	Phosphorylation	TPAATGGSQPPSMGR CCCCCCCCCCCCCCC	40.64	23927012
1207	Phosphorylation	TGGSQPPSMGRKKRN CCCCCCCCCCCCCCC	40.32	23927012
1208	Sulfoxidation	GGSQPPSMGRKKRNR CCCCCCCCCCCCCCC	8.10	21406390
1219	Acetylation	KRNRTKAKVPAQANG CCCCCCCCCCCCCCC	50.75	25953088
1219	Ubiquitination	KRNRTKAKVPAQANG CCCCCCCCCCCCCCC	50.75	24816145
1227	Phosphorylation	VPAQANGTPTTKSPA CCCCCCCCCCCCCCC	19.78	30266825
1227 (in isoform 2)	Phosphorylation	-	19.78	27251275
1229	Phosphorylation	AQANGTPTTKSPAPG CCCCCCCCCCCCCCC	46.85	30266825
1230	Phosphorylation	QANGTPTTKSPAPGA CCCCCCCCCCCCCCC	30.63	30266825
1231	Acetylation	ANGTPTTKSPAPGAP CCCCCCCCCCCCCCC	57.85	25953088
1232	Phosphorylation	NGTPTTKSPAPGAPT CCCCCCCCCCCCCCC	24.97	30266825
1232 (in isoform 2)	Phosphorylation	-	24.97	21406692
1239	Phosphorylation	SPAPGAPTRSPSTPA CCCCCCCCCCCCCCC	43.15	23927012
1239 (in isoform 2)	Phosphorylation	-	43.15	21406692
1241	Phosphorylation	APGAPTRSPSTPAKS CCCCCCCCCCCCCCC	26.19	25159151
1241 (in isoform 2)	Phosphorylation	-	26.19	24719451
1243	Phosphorylation	GAPTRSPSTPAKSPK CCCCCCCCCCCCCHH	48.55	30266825
1244	Phosphorylation	APTRSPSTPAKSPKL CCCCCCCCCCCCHHH	30.56	30266825
1244 (in isoform 2)	Phosphorylation	-	30.56	24719451
1247	Acetylation	RSPSTPAKSPKLQKK CCCCCCCCCHHHHHC	69.37	25953088
1248	Phosphorylation	SPSTPAKSPKLQKKN CCCCCCCCHHHHHCC	29.40	25159151
1259	Phosphorylation	QKKNQKPSQVNGAPG HHCCCCCCCCCCCCC	54.52	29255136
1267	Phosphorylation	QVNGAPGSPTEPAGQ CCCCCCCCCCCCCCH	27.82	19664994
1267 (in isoform 2)	Phosphorylation	-	27.82	24719451
1269	Phosphorylation	NGAPGSPTEPAGQKQ CCCCCCCCCCCCHHH	57.19	22167270
1269 (in isoform 2)	Phosphorylation	-	57.19	21406692
1284	Acetylation	HQKALPKKGVLGKSP HHHHCCCCCCCCCCH	52.92	25953088
1289	Acetylation	PKKGVLGKSPLSALA CCCCCCCCCHHHHHH	44.75	25953088
1290	Phosphorylation	KKGVLGKSPLSALAR CCCCCCCCHHHHHHH	29.31	29255136
1290 (in isoform 2)	Phosphorylation	-	29.31	24719451
1293	Phosphorylation	VLGKSPLSALARKKA CCCCCHHHHHHHHHH	25.31	23927012
1293 (in isoform 2)	Phosphorylation	-	25.31	24719451
1303	Phosphorylation	ARKKARLSLVIRSPS HHHHHHHHHHHCCHH	18.29	25159151
1303 (in isoform 2)	Phosphorylation	-	18.29	24719451
1307	Citrullination	ARLSLVIRSPSLLQS HHHHHHHCCHHHHHC	34.73	-
1307	Citrullination	ARLSLVIRSPSLLQS HHHHHHHCCHHHHHC	34.73	-
1308	O-linked_Glycosylation	RLSLVIRSPSLLQSG HHHHHHCCHHHHHCC	14.02	29351928
1308	Phosphorylation	RLSLVIRSPSLLQSG HHHHHHCCHHHHHCC	14.02	29255136
1308 (in isoform 2)	Phosphorylation	-	14.02	29743597
1310	Phosphorylation	SLVIRSPSLLQSGAK HHHHCCHHHHHCCHH	42.85	29255136
1310 (in isoform 2)	Phosphorylation	-	42.85	24719451
1314	Phosphorylation	RSPSLLQSGAKKKAQ CCHHHHHCCHHHHHH	40.46	25159151
1314 (in isoform 2)	Phosphorylation	-	40.46	29743597
1317	Acetylation	SLLQSGAKKKAQVRK HHHHCCHHHHHHHHH	59.33	25953088
1319	Acetylation	LQSGAKKKAQVRKAG HHCCHHHHHHHHHCC	43.26	19824341
1319	Ubiquitination	LQSGAKKKAQVRKAG HHCCHHHHHHHHHCC	43.26	24816145

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
1303	S	Phosphorylation	Kinase	AURKA	O14965	GPS
1303	S	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
1310	S	Phosphorylation	Kinase	CHEK1	O14757	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MBB1A_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
Oops, there are no SNP-PTM records of MBB1A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
AIRE_HUMAN	AIRE	physical	20085707
VHL_HUMAN	VHL	physical	21386990
ELOC_HUMAN	TCEB1	physical	21386990
ELOB_HUMAN	TCEB2	physical	21386990
TAF1D_HUMAN	TAF1D	physical	21386990
NOP2_HUMAN	NOP2	physical	21386990
NUCL_HUMAN	NCL	physical	21386990
LYAR_HUMAN	LYAR	physical	21386990
RIOX2_HUMAN	MINA	physical	21386990
BOP1_HUMAN	BOP1	physical	21386990
SIR7_HUMAN	SIRT7	physical	22147730
UBF1_HUMAN	UBTF	physical	22147730
SMCA5_HUMAN	SMARCA5	physical	22147730
RPA1_HUMAN	POLR1A	physical	22147730
SIR7_HUMAN	SIRT7	physical	22586326
RPA1_HUMAN	POLR1A	physical	22586326
SMCA5_HUMAN	SMARCA5	physical	22586326
UBF1_HUMAN	UBTF	physical	22586326
A4_HUMAN	APP	physical	21832049
RL7_HUMAN	RPL7	physical	22939629
RL4_HUMAN	RPL4	physical	22939629
RL6_HUMAN	RPL6	physical	22939629
RS3_HUMAN	RPS3	physical	22939629
RS13_HUMAN	RPS13	physical	22939629
RL23A_HUMAN	RPL23A	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RL37A_HUMAN	RPL37A	physical	22939629
RL1D1_HUMAN	RSL1D1	physical	22939629
RL18_HUMAN	RPL18	physical	22939629
RS2_HUMAN	RPS2	physical	22939629
RL5_HUMAN	RPL5	physical	22939629
RS11_HUMAN	RPS11	physical	22939629
RS14_HUMAN	RPS14	physical	22939629
RS24_HUMAN	RPS24	physical	22939629
RS23_HUMAN	RPS23	physical	22939629
RS8_HUMAN	RPS8	physical	22939629
RNPS1_HUMAN	RNPS1	physical	22939629
SPB1_HUMAN	FTSJ3	physical	22939629
RED_HUMAN	IK	physical	22939629
RRS1_HUMAN	RRS1	physical	22939629
RRP7A_HUMAN	RRP7A	physical	22939629
CAVN1_HUMAN	PTRF	physical	22939629
NOP16_HUMAN	NOP16	physical	22939629
SND1_HUMAN	SND1	physical	22939629
ROA0_HUMAN	HNRNPA0	physical	22939629
MCM5_HUMAN	MCM5	physical	22939629
NICA_HUMAN	NCSTN	physical	22939629
TF65_HUMAN	RELA	physical	24175631
PRP8_HUMAN	PRPF8	physical	26344197
ZN746_HUMAN	ZNF746	physical	25315684

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.

Regulatory Network of MBB1A_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-11; SER-711; SER-775;SER-1163; THR-1227; SER-1232; SER-1290; SER-1308; SER-1310 ANDSER-1314, ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASSSPECTROMETRY.	19007248 [Abstract]
"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-71 AND LYS-158, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-775; SER-1163; SER-1267AND SER-1310, AND MASS SPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-775, AND MASSSPECTROMETRY.	19369195 [Abstract]
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1159; THR-1161;SER-1163; THR-1196; SER-1207; THR-1227; SER-1267 AND THR-1269, ANDMASS SPECTROMETRY.	19413330 [Abstract]
"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-11; SER-775; SER-1159;SER-1163; SER-1186; THR-1190; THR-1196; SER-1207; SER-1241; THR-1244;SER-1248; SER-1267; SER-1290; SER-1293; SER-1303; SER-1308 ANDSER-1314, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-775; SER-1159;THR-1161; SER-1163; THR-1227; SER-1267 AND SER-1290, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1186 AND THR-1190, ANDMASS SPECTROMETRY.	18220336 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1163 AND SER-1166, ANDMASS SPECTROMETRY.	18187866 [Abstract]
"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-11; SER-711; SER-775;SER-1163; THR-1227; SER-1232; SER-1290; SER-1308; SER-1310 ANDSER-1314, ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASSSPECTROMETRY.	19007248 [Abstract]
"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 SER-1290; SER-1293; SER-1308AND SER-1314, AND MASS SPECTROMETRY.	17924679 [Abstract]
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-775; SER-1163 ANDSER-1267, AND MASS SPECTROMETRY.	16565220 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-1159; SER-1163;SER-1290; SER-1308 AND SER-1314, AND MASS SPECTROMETRY.	16964243 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; TYR-60; SER-775 ANDSER-1267, AND MASS SPECTROMETRY.	17081983 [Abstract]
"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-1163, AND MASSSPECTROMETRY.	15302935 [Abstract]