dbPTM

BACH1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BACH1_HUMAN	Jmol._Canvas2D (Jmol) "myJmol"[x]
UniProt AC	O14867
Protein Name	Transcription regulator protein BACH1
Gene Name	BACH1
Organism	Homo sapiens (Human).
Sequence Length	736
Subcellular Localization	Nucleus .
Protein Description	Transcriptional regulator that acts as repressor or activator. Binds, in vitro, to NF-E2 binding sites. Play important roles in coordinating transcription activation and repression by MAFK..
Protein Sequence	MSLSENSVFAYESSVHSTNVLLSLNDQRKKDVLCDVTIFVEGQRFRAHRSVLAACSSYFHSRIVGQADGELNITLPEEVTVKGFEPLIQFAYTAKLILSKENVDEVCKCVEFLSVHNIEESCFQFLKFKFLDSTADQQECPRKKCFSSHCQKTDLKLSLLDQRDLETDEVEEFLENKNVQTPQCKLRRYQGNAKASPPLQDSASQTYESMCLEKDAALALPSLCPKYRKFQKAFGTDRVRTGESSVKDIHASVQPNERSENECLGGVPECRDLQVMLKCDESKLAMEPEETKKDPASQCPTEKSEVTPFPHNSSIDPHGLYSLSLLHTYDQYGDLNFAGMQNTTVLTEKPLSGTDVQEKTFGESQDLPLKSDLGTREDSSVASSDRSSVEREVAEHLAKGFWSDICSTDTPCQMQLSPAVAKDGSEQISQKRSECPWLGIRISESPEPGQRTFTTLSSVNCPFISTLSTEGCSSNLEIGNDDYVSEPQQEPCPYACVISLGDDSETDTEGDSESCSAREQECEVKLPFNAQRIISLSRNDFQSLLKMHKLTPEQLDCIHDIRRRSKNRIAAQRCRKRKLDCIQNLESEIEKLQSEKESLLKERDHILSTLGETKQNLTGLCQKVCKEAALSQEQIQILAKYSAADCPLSFLISEKDKSTPDGELALPSIFSLSDRPPAVLPPCARGNSEPGYARGQESQQMSTATSEQAGPAEQCRQSGGISDFCQQMTDKCTTDE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSLSENSVF ------CCCCCCCEE	40.37	24043423
4	Phosphorylation	----MSLSENSVFAY ----CCCCCCCEEEE	27.68	24043423
7	Phosphorylation	-MSLSENSVFAYESS -CCCCCCCEEEEECC	17.98	24043423
11	Phosphorylation	SENSVFAYESSVHST CCCCEEEEECCCCCC	12.60	24043423
13	Phosphorylation	NSVFAYESSVHSTNV CCEEEEECCCCCCEE	25.61	24043423
14	Phosphorylation	SVFAYESSVHSTNVL CEEEEECCCCCCEEE	16.35	24043423
17	Phosphorylation	AYESSVHSTNVLLSL EEECCCCCCEEEEEC	21.37	24043423
18	Phosphorylation	YESSVHSTNVLLSLN EECCCCCCEEEEECC	17.92	24043423
23	Phosphorylation	HSTNVLLSLNDQRKK CCCEEEEECCCHHHC	22.44	24043423
100	Ubiquitination	TAKLILSKENVDEVC HHHHHHCCCCHHHHH	50.27	29967540
129	Ubiquitination	CFQFLKFKFLDSTAD HHHHHHHHCCCCCCC	43.35	29967540
133	Phosphorylation	LKFKFLDSTADQQEC HHHHCCCCCCCHHHC	27.87	27251275
134	Phosphorylation	KFKFLDSTADQQECP HHHCCCCCCCHHHCC	33.64	27251275
156	Ubiquitination	HCQKTDLKLSLLDQR HHHHHHHCHHHHHHH	38.55	29967540
158	Phosphorylation	QKTDLKLSLLDQRDL HHHHHCHHHHHHHCC	25.87	21815630
177	Ubiquitination	VEEFLENKNVQTPQC HHHHHHCCCCCCCCH	49.47	29967540
181	Phosphorylation	LENKNVQTPQCKLRR HHCCCCCCCCHHHHH	15.85	28985074
185	Ubiquitination	NVQTPQCKLRRYQGN CCCCCCHHHHHHCCC	39.52	29967540
196	Phosphorylation	YQGNAKASPPLQDSA HCCCCCCCCCCCCCC	26.75	30266825
202	Phosphorylation	ASPPLQDSASQTYES CCCCCCCCCCHHHHH	19.50	29978859
204	Phosphorylation	PPLQDSASQTYESMC CCCCCCCCHHHHHHH	27.32	29978859
206	Phosphorylation	LQDSASQTYESMCLE CCCCCCHHHHHHHCH	27.11	29449344
207	Phosphorylation	QDSASQTYESMCLEK CCCCCHHHHHHHCHH	9.81	29449344
232	Ubiquitination	PKYRKFQKAFGTDRV HHHHHHHHHHCCCCC	49.14	29967540
236	Phosphorylation	KFQKAFGTDRVRTGE HHHHHHCCCCCCCCC	17.74	-
241	Phosphorylation	FGTDRVRTGESSVKD HCCCCCCCCCCCHHH	42.30	23312004
244	Phosphorylation	DRVRTGESSVKDIHA CCCCCCCCCHHHHHH	41.60	23312004
245	Phosphorylation	RVRTGESSVKDIHAS CCCCCCCCHHHHHHC	28.96	28857561
247	Acetylation	RTGESSVKDIHASVQ CCCCCCHHHHHHCCC	53.57	25953088
247	Ubiquitination	RTGESSVKDIHASVQ CCCCCCHHHHHHCCC	53.57	29967540
297	Phosphorylation	ETKKDPASQCPTEKS HHCCCCHHHCCCCCC	37.39	22985185
321	Phosphorylation	SIDPHGLYSLSLLHT CCCCCCCEEHEEEEE	16.50	19369195
322	Phosphorylation	IDPHGLYSLSLLHTY CCCCCCEEHEEEEEE	19.27	19369195
328	Phosphorylation	YSLSLLHTYDQYGDL EEHEEEEEECCCCCC	28.85	19369195
359	Ubiquitination	SGTDVQEKTFGESQD CCCCCCCCCCCCCCC	31.87	29967540
360	Phosphorylation	GTDVQEKTFGESQDL CCCCCCCCCCCCCCC	35.80	25159151
364	Phosphorylation	QEKTFGESQDLPLKS CCCCCCCCCCCCCCC	29.40	21815630
370	Ubiquitination	ESQDLPLKSDLGTRE CCCCCCCCCCCCCCC	39.73	29967540
379	Phosphorylation	DLGTREDSSVASSDR CCCCCCCCCCCCCCC	23.20	30242111
380	Phosphorylation	LGTREDSSVASSDRS CCCCCCCCCCCCCCH	33.74	25002506
383	Phosphorylation	REDSSVASSDRSSVE CCCCCCCCCCCHHHH	30.53	25002506
384	Phosphorylation	EDSSVASSDRSSVER CCCCCCCCCCHHHHH	27.57	30576142
387	Phosphorylation	SVASSDRSSVEREVA CCCCCCCHHHHHHHH	43.66	25159151
388	Phosphorylation	VASSDRSSVEREVAE CCCCCCHHHHHHHHH	28.97	29496963
408	Phosphorylation	FWSDICSTDTPCQMQ CHHHHCCCCCCCCCC	39.21	28102081
410	Phosphorylation	SDICSTDTPCQMQLS HHHCCCCCCCCCCCC	26.50	28102081
417	Phosphorylation	TPCQMQLSPAVAKDG CCCCCCCCHHHCCCC	8.23	30576142
443	Phosphorylation	PWLGIRISESPEPGQ CCEEEEECCCCCCCC	23.36	23927012
445	Phosphorylation	LGIRISESPEPGQRT EEEEECCCCCCCCCC	27.98	29255136
504	Phosphorylation	VISLGDDSETDTEGD EEEECCCCCCCCCCC	47.32	-
506	Phosphorylation	SLGDDSETDTEGDSE EECCCCCCCCCCCCC	52.77	-
535	Phosphorylation	FNAQRIISLSRNDFQ CCHHHHHEECHHHHH	20.23	24719451
543	Phosphorylation	LSRNDFQSLLKMHKL ECHHHHHHHHHHCCC	35.35	23186163
549	Ubiquitination	QSLLKMHKLTPEQLD HHHHHHCCCCHHHHH	51.02	29967540
551	Phosphorylation	LLKMHKLTPEQLDCI HHHHCCCCHHHHHHH	29.59	-
578	Ubiquitination	AQRCRKRKLDCIQNL HHHHHHHHHHHHHHH	52.27	29967540
596	Ubiquitination	IEKLQSEKESLLKER HHHHHHHHHHHHHHH	58.83	29967540
598	Phosphorylation	KLQSEKESLLKERDH HHHHHHHHHHHHHHH	50.50	24719451
614	Ubiquitination	LSTLGETKQNLTGLC HHHHHHHHHHHHHHH	32.65	29967540
626	Ubiquitination	GLCQKVCKEAALSQE HHHHHHHHHHCCCHH	54.07	29967540
631	Phosphorylation	VCKEAALSQEQIQIL HHHHHCCCHHHHHHH	27.26	25693802
653	Phosphorylation	CPLSFLISEKDKSTP CCHHHEEECCCCCCC	40.52	24719451
655	Ubiquitination	LSFLISEKDKSTPDG HHHEEECCCCCCCCC	64.76	29967540
658	Phosphorylation	LISEKDKSTPDGELA EEECCCCCCCCCCCC	56.13	27251275
659	Phosphorylation	ISEKDKSTPDGELAL EECCCCCCCCCCCCC	31.01	27251275
688	Phosphorylation	PPCARGNSEPGYARG CCCCCCCCCCCCCCC	48.25	25627689
692	Phosphorylation	RGNSEPGYARGQESQ CCCCCCCCCCCHHHH	12.11	27486199
718	Phosphorylation	PAEQCRQSGGISDFC HHHHHHHCCCHHHHH	21.45	21815630
722	Phosphorylation	CRQSGGISDFCQQMT HHHCCCHHHHHHHHH	28.10	25850435

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
-	K	Ubiquitination	E3 ubiquitin ligase	RBCK1	Q9BYM8	PMID:17682061

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of BACH1_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 BACH1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BACH1_HUMAN	BACH1	physical	8887638
PATZ1_HUMAN	PATZ1	physical	10669750
HOIL1_HUMAN	RBCK1	physical	17682061
HMMR_HUMAN	HMMR	physical	19011633
MAFG_HUMAN	MAFG	physical	19011633
MAFK_HUMAN	MAFK	physical	19011633
P53_HUMAN	TP53	physical	19011633
HDAC1_HUMAN	HDAC1	physical	19011633
NCOR1_HUMAN	NCOR1	physical	19011633
XPO1_HUMAN	XPO1	physical	15175654
BRCA1_HUMAN	BRCA1	physical	17664283
BRCA2_HUMAN	BRCA2	physical	17664283
BARD1_HUMAN	BARD1	physical	17664283
HMMR_HUMAN	HMMR	physical	15809329
NF2L2_HUMAN	NFE2L2	physical	15734732
BACH1_HUMAN	BACH1	physical	11069897
BRCA1_HUMAN	BRCA1	physical	16391231
NBN_HUMAN	NBN	physical	16391231
MRE11_HUMAN	MRE11A	physical	16391231
MLH1_HUMAN	MLH1	physical	16391231
TOPB1_HUMAN	TOPBP1	physical	16391231
BARD1_HUMAN	BARD1	physical	16391231
BRCA1_HUMAN	BRCA1	physical	17525340
MAFG_HUMAN	MAFG	physical	23661758
MAFF_HUMAN	MAFF	physical	23661758
HMMR_HUMAN	HMMR	physical	26496610
MAFG_HUMAN	MAFG	physical	26496610
PLRG1_HUMAN	PLRG1	physical	26496610
TAF4B_HUMAN	TAF4B	physical	26496610
DX39B_HUMAN	DDX39B	physical	26496610
MAFK_HUMAN	MAFK	physical	26496610
PABP2_HUMAN	PABPN1	physical	26496610
MAFF_HUMAN	MAFF	physical	26496610
VIR_HUMAN	KIAA1429	physical	26496610
TM208_HUMAN	TMEM208	physical	26496610
PPHLN_HUMAN	PPHLN1	physical	26496610
FA83D_HUMAN	FAM83D	physical	26496610
TB10A_HUMAN	TBC1D10A	physical	26496610
MAFF_HUMAN	MAFF	physical	28514442
HMMR_HUMAN	HMMR	physical	28514442
FA83D_HUMAN	FAM83D	physical	28514442
ATP23_HUMAN	XRCC6BP1	physical	28514442
ZHANG_HUMAN	CREBZF	physical	28514442
FXL17_HUMAN	FBXL17	physical	28514442
ZN131_HUMAN	ZNF131	physical	28514442
MAFG_HUMAN	MAFG	physical	28514442
ATF7_HUMAN	ATF7	physical	28514442
FBX22_HUMAN	FBXO22	physical	28514442
K1468_HUMAN	KIAA1468	physical	28514442
MAFK_HUMAN	MAFK	physical	28514442
ASAP3_HUMAN	ASAP3	physical	28514442
TXND3_HUMAN	NME8	physical	27173435
TRIPB_HUMAN	TRIP11	physical	27173435
XPO1_HUMAN	XPO1	physical	27393035

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 BACH1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 TYR-321; SER-322 ANDTHR-328, AND MASS SPECTROMETRY.	19369195 [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-445, AND MASSSPECTROMETRY.	18669648 [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-445, AND MASSSPECTROMETRY.	16964243 [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-196 AND SER-445, ANDMASS SPECTROMETRY.	15302935 [Abstract]