dbPTM

MYBB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MYBB_HUMAN
UniProt AC	P10244
Protein Name	Myb-related protein B
Gene Name	MYBL2
Organism	Homo sapiens (Human).
Sequence Length	700
Subcellular Localization	Nucleus.
Protein Description	Transcription factor involved in the regulation of cell survival, proliferation, and differentiation. Transactivates the expression of the CLU gene..
Protein Sequence	MSRRTRCEDLDELHYQDTDSDVPEQRDSKCKVKWTHEEDEQLRALVRQFGQQDWKFLASHFPNRTDQQCQYRWLRVLNPDLVKGPWTKEEDQKVIELVKKYGTKQWTLIAKHLKGRLGKQCRERWHNHLNPEVKKSCWTEEEDRIICEAHKVLGNRWAEIAKMLPGRTDNAVKNHWNSTIKRKVDTGGFLSESKDCKPPVYLLLELEDKDGLQSAQPTEGQGSLLTNWPSVPPTIKEEENSEEELAAATTSKEQEPIGTDLDAVRTPEPLEEFPKREDQEGSPPETSLPYKWVVEAANLLIPAVGSSLSEALDLIESDPDAWCDLSKFDLPEEPSAEDSINNSLVQLQASHQQQVLPPRQPSALVPSVTEYRLDGHTISDLSRSSRGELIPISPSTEVGGSGIGTPPSVLKRQRKRRVALSPVTENSTSLSFLDSCNSLTPKSTPVKTLPFSPSQFLNFWNKQDTLELESPSLTSTPVCSQKVVVTTPLHRDKTPLHQKHAAFVTPDQKYSMDNTPHTPTPFKNALEKYGPLKPLPQTPHLEEDLKEVLRSEAGIELIIEDDIRPEKQKRKPGLRRSPIKKVRKSLALDIVDEDVKLMMSTLPKSLSLPTTAPSNSSSLTLSGIKEDNSLLNQGFLQAKPEKAAVAQKPRSHFTTPAPMSSAWKTVACGGTRDQLFMQEKARQLLGRLKPSHTSRTLILS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Phosphorylation	---MSRRTRCEDLDE ---CCCCCCCCCHHH	38.26	28111955
15	Phosphorylation	EDLDELHYQDTDSDV CCHHHHHCCCCCCCC	22.25	30576142
18	Phosphorylation	DELHYQDTDSDVPEQ HHHHCCCCCCCCCCH	23.13	23898821
20	Phosphorylation	LHYQDTDSDVPEQRD HHCCCCCCCCCCHHC	42.47	22617229
28	Phosphorylation	DVPEQRDSKCKVKWT CCCCHHCCCCCCEEC	41.99	21498570
33	Ubiquitination	RDSKCKVKWTHEEDE HCCCCCCEECCCHHH	31.69	29967540
93	Sumoylation	WTKEEDQKVIELVKK CCHHHHHHHHHHHHH	58.46	-
93	Sumoylation	WTKEEDQKVIELVKK CCHHHHHHHHHHHHH	58.46	-
104	Sumoylation	LVKKYGTKQWTLIAK HHHHHCCHHHHHHHH	39.20	-
104	Sumoylation	LVKKYGTKQWTLIAK HHHHHCCHHHHHHHH	39.20	28112733
110	Ubiquitination	TKQWTLIAKHLKGRL CHHHHHHHHHHHHHH	9.05	29967540
127	Ubiquitination	QCRERWHNHLNPEVK HHHHHHHHHCCHHHH	34.09	29967540
134	Sumoylation	NHLNPEVKKSCWTEE HHCCHHHHHHCCCHH	36.99	-
134	Sumoylation	NHLNPEVKKSCWTEE HHCCHHHHHHCCCHH	36.99	-
134	Ubiquitination	NHLNPEVKKSCWTEE HHCCHHHHHHCCCHH	36.99	29967540
135	Ubiquitination	HLNPEVKKSCWTEEE HCCHHHHHHCCCHHH	56.90	-
136	Phosphorylation	LNPEVKKSCWTEEED CCHHHHHHCCCHHHH	14.79	25404012
138	Ubiquitination	PEVKKSCWTEEEDRI HHHHHHCCCHHHHHH	17.59	29967540
149	Ubiquitination	EDRIICEAHKVLGNR HHHHHHHHHHHHHHH	11.91	29967540
151	Ubiquitination	RIICEAHKVLGNRWA HHHHHHHHHHHHHHH	46.32	29967540
157	Ubiquitination	HKVLGNRWAEIAKML HHHHHHHHHHHHHHC	11.40	29967540
159	Ubiquitination	VLGNRWAEIAKMLPG HHHHHHHHHHHHCCC	36.20	29967540
162	Ubiquitination	NRWAEIAKMLPGRTD HHHHHHHHHCCCCCC	46.78	29967540
168	Phosphorylation	AKMLPGRTDNAVKNH HHHCCCCCCHHHHHH	39.25	26074081
173	Ubiquitination	GRTDNAVKNHWNSTI CCCCHHHHHHHHHCH	40.46	29967540
178	Phosphorylation	AVKNHWNSTIKRKVD HHHHHHHHCHHCCCC	26.73	25159151
181	Ubiquitination	NHWNSTIKRKVDTGG HHHHHCHHCCCCCCC	46.37	29967540
183	Ubiquitination	WNSTIKRKVDTGGFL HHHCHHCCCCCCCCC	39.19	29967540
194	Sumoylation	GGFLSESKDCKPPVY CCCCCCCCCCCCCEE	64.19	28112733
197	Sumoylation	LSESKDCKPPVYLLL CCCCCCCCCCEEEEE	63.59	-
197	Sumoylation	LSESKDCKPPVYLLL CCCCCCCCCCEEEEE	63.59	28112733
234	Phosphorylation	NWPSVPPTIKEEENS CCCCCCCCCCCCCCC	38.31	-
236	Sumoylation	PSVPPTIKEEENSEE CCCCCCCCCCCCCHH	62.64	-
241	Phosphorylation	TIKEEENSEEELAAA CCCCCCCCHHHHHHH	50.06	29255136
242	Phosphorylation	IKEEENSEEELAAAT CCCCCCCHHHHHHHH	68.05	32142685
249	Phosphorylation	EEELAAATTSKEQEP HHHHHHHHCCCCCCC	27.20	26074081
250	Phosphorylation	EELAAATTSKEQEPI HHHHHHHCCCCCCCC	32.83	26074081
251	Phosphorylation	ELAAATTSKEQEPIG HHHHHHCCCCCCCCC	29.82	26074081
259	Phosphorylation	KEQEPIGTDLDAVRT CCCCCCCCCCHHCCC	33.82	22199227
266	Phosphorylation	TDLDAVRTPEPLEEF CCCHHCCCCCCHHHC	25.96	30266825
275	Sumoylation	EPLEEFPKREDQEGS CCHHHCCCCCCCCCC	73.98	28112733
282	Phosphorylation	KREDQEGSPPETSLP CCCCCCCCCCCCCCC	36.21	23401153
286	Phosphorylation	QEGSPPETSLPYKWV CCCCCCCCCCCHHHH	41.14	23663014
287	Phosphorylation	EGSPPETSLPYKWVV CCCCCCCCCCHHHHH	26.19	29255136
290	Phosphorylation	PPETSLPYKWVVEAA CCCCCCCHHHHHHHH	23.83	23186163
362	Phosphorylation	VLPPRQPSALVPSVT CCCCCCCCCCCCCEE	26.37	-
384	Phosphorylation	TISDLSRSSRGELIP CHHHCCCCCCCCEEE	22.47	23090842
385	Phosphorylation	ISDLSRSSRGELIPI HHHCCCCCCCCEEEC	43.10	23090842
387	Ubiquitination	DLSRSSRGELIPISP HCCCCCCCCEEECCC	35.69	-
393	Phosphorylation	RGELIPISPSTEVGG CCCEEECCCCCCCCC	13.88	23401153
395	Phosphorylation	ELIPISPSTEVGGSG CEEECCCCCCCCCCC	30.34	30266825
396	Phosphorylation	LIPISPSTEVGGSGI EEECCCCCCCCCCCC	37.77	30266825
401	Phosphorylation	PSTEVGGSGIGTPPS CCCCCCCCCCCCCHH	22.70	22167270
405	Phosphorylation	VGGSGIGTPPSVLKR CCCCCCCCCHHHHHH	30.06	22167270
408	Phosphorylation	SGIGTPPSVLKRQRK CCCCCCHHHHHHHHH	41.08	22167270
411	Ubiquitination	GTPPSVLKRQRKRRV CCCHHHHHHHHHCCE	44.31	-
411	Sumoylation	GTPPSVLKRQRKRRV CCCHHHHHHHHHCCE	44.31	28112733
421	Phosphorylation	RKRRVALSPVTENST HHCCEEECCCCCCCC	13.95	29255136
424	Phosphorylation	RVALSPVTENSTSLS CEEECCCCCCCCCCH	32.60	29255136
427	Phosphorylation	LSPVTENSTSLSFLD ECCCCCCCCCCHHHH	17.09	25850435
428	Phosphorylation	SPVTENSTSLSFLDS CCCCCCCCCCHHHHH	45.31	25850435
429	Phosphorylation	PVTENSTSLSFLDSC CCCCCCCCCHHHHHC	23.10	28464451
431	Phosphorylation	TENSTSLSFLDSCNS CCCCCCCHHHHHCCC	24.43	26074081
435	Phosphorylation	TSLSFLDSCNSLTPK CCCHHHHHCCCCCCC	19.83	29255136
438	Phosphorylation	SFLDSCNSLTPKSTP HHHHHCCCCCCCCCC	37.64	29255136
440	Phosphorylation	LDSCNSLTPKSTPVK HHHCCCCCCCCCCCC	28.61	29255136
443	Phosphorylation	CNSLTPKSTPVKTLP CCCCCCCCCCCCCCC	38.86	-
444	Phosphorylation	NSLTPKSTPVKTLPF CCCCCCCCCCCCCCC	37.92	10095772
447	Ubiquitination	TPKSTPVKTLPFSPS CCCCCCCCCCCCCHH	45.61	-
447	Sumoylation	TPKSTPVKTLPFSPS CCCCCCCCCCCCCHH	45.61	28112733
448	Phosphorylation	PKSTPVKTLPFSPSQ CCCCCCCCCCCCHHH	39.64	22199227
452	Phosphorylation	PVKTLPFSPSQFLNF CCCCCCCCHHHHHHH	23.00	25159151
454	Phosphorylation	KTLPFSPSQFLNFWN CCCCCCHHHHHHHHC	32.16	28450419
465	Phosphorylation	NFWNKQDTLELESPS HHHCCCCCEEECCCC	21.46	-
470	Phosphorylation	QDTLELESPSLTSTP CCCEEECCCCCCCCC	32.20	29083192
472	Phosphorylation	TLELESPSLTSTPVC CEEECCCCCCCCCCC	54.26	29083192
474	Phosphorylation	ELESPSLTSTPVCSQ EECCCCCCCCCCCCC	34.59	28348404
475	Phosphorylation	LESPSLTSTPVCSQK ECCCCCCCCCCCCCE	35.69	29083192
475	Ubiquitination	LESPSLTSTPVCSQK ECCCCCCCCCCCCCE	35.69	29967540
476	Phosphorylation	ESPSLTSTPVCSQKV CCCCCCCCCCCCCEE	17.95	27050516
480	Phosphorylation	LTSTPVCSQKVVVTT CCCCCCCCCEEEEEC	33.02	29083192
482	Sumoylation	STPVCSQKVVVTTPL CCCCCCCEEEEECCC	22.24	28112733
485	Ubiquitination	VCSQKVVVTTPLHRD CCCCEEEEECCCCCC	5.74	29967540
486	Phosphorylation	CSQKVVVTTPLHRDK CCCEEEEECCCCCCC	15.87	30266825
487	Phosphorylation	SQKVVVTTPLHRDKT CCEEEEECCCCCCCC	16.55	30266825
494	Phosphorylation	TPLHRDKTPLHQKHA CCCCCCCCCCCCCCE	35.06	30576142
499	Ubiquitination	DKTPLHQKHAAFVTP CCCCCCCCCEEEECC	25.18	29967540
499	Sumoylation	DKTPLHQKHAAFVTP CCCCCCCCCEEEECC	25.18	28112733
504	Ubiquitination	HQKHAAFVTPDQKYS CCCCEEEECCCCCCC	6.96	29967540
505	Phosphorylation	QKHAAFVTPDQKYSM CCCEEEECCCCCCCC	18.07	30266825
509	Sumoylation	AFVTPDQKYSMDNTP EEECCCCCCCCCCCC	46.82	-
509	Sumoylation	AFVTPDQKYSMDNTP EEECCCCCCCCCCCC	46.82	28112733
509	Ubiquitination	AFVTPDQKYSMDNTP EEECCCCCCCCCCCC	46.82	29967540
509	Acetylation	AFVTPDQKYSMDNTP EEECCCCCCCCCCCC	46.82	-
509	Ubiquitination	AFVTPDQKYSMDNTP EEECCCCCCCCCCCC	46.82	-
510	Phosphorylation	FVTPDQKYSMDNTPH EECCCCCCCCCCCCC	12.00	26074081
511	Phosphorylation	VTPDQKYSMDNTPHT ECCCCCCCCCCCCCC	27.05	26074081
515	Phosphorylation	QKYSMDNTPHTPTPF CCCCCCCCCCCCCCC	16.51	28450419
518	Phosphorylation	SMDNTPHTPTPFKNA CCCCCCCCCCCCHHH	30.02	25159151
520	Phosphorylation	DNTPHTPTPFKNALE CCCCCCCCCCHHHHH	42.38	22617229
522	Ubiquitination	TPHTPTPFKNALEKY CCCCCCCCHHHHHHH	11.95	29967540
523	Ubiquitination	PHTPTPFKNALEKYG CCCCCCCHHHHHHHC	42.38	29967540
523	Sumoylation	PHTPTPFKNALEKYG CCCCCCCHHHHHHHC	42.38	28112733
528	Ubiquitination	PFKNALEKYGPLKPL CCHHHHHHHCCCCCC	57.25	29967540
529	Phosphorylation	FKNALEKYGPLKPLP CHHHHHHHCCCCCCC	18.01	23312004
533	Acetylation	LEKYGPLKPLPQTPH HHHHCCCCCCCCCCC	47.87	23749302
533	Ubiquitination	LEKYGPLKPLPQTPH HHHHCCCCCCCCCCC	47.87	29967540
533	Sumoylation	LEKYGPLKPLPQTPH HHHHCCCCCCCCCCC	47.87	28112733
538	Phosphorylation	PLKPLPQTPHLEEDL CCCCCCCCCCHHHHH	15.67	25159151
546	Sumoylation	PHLEEDLKEVLRSEA CCHHHHHHHHHHHHH	59.09	-
546	Sumoylation	PHLEEDLKEVLRSEA CCHHHHHHHHHHHHH	59.09	28112733
546	Ubiquitination	PHLEEDLKEVLRSEA CCHHHHHHHHHHHHH	59.09	29967540
560	Ubiquitination	AGIELIIEDDIRPEK HCEEEEECCCCCHHH	42.51	29967540
577	Phosphorylation	RKPGLRRSPIKKVRK CCCCCCCCHHHHHHH	25.25	28112733
584	Ubiquitination	SPIKKVRKSLALDIV CHHHHHHHHHHHHHC	53.46	29967540
584	Sumoylation	SPIKKVRKSLALDIV CHHHHHHHHHHHHHC	53.46	28112733
585	Phosphorylation	PIKKVRKSLALDIVD HHHHHHHHHHHHHCC	14.33	22199227
596	Sumoylation	DIVDEDVKLMMSTLP HHCCHHHHHHHHHCC	42.88	-
596	Sumoylation	DIVDEDVKLMMSTLP HHCCHHHHHHHHHCC	42.88	28112733
600	Phosphorylation	EDVKLMMSTLPKSLS HHHHHHHHHCCCCCC	16.90	20068231
601	Ubiquitination	DVKLMMSTLPKSLSL HHHHHHHHCCCCCCC	29.23	29967540
601	Phosphorylation	DVKLMMSTLPKSLSL HHHHHHHHCCCCCCC	29.23	20068231
615	Ubiquitination	LPTTAPSNSSSLTLS CCCCCCCCCCCEEEE	44.87	29967540
615	Acetylation	LPTTAPSNSSSLTLS CCCCCCCCCCCEEEE	44.87	-
624	Ubiquitination	SSLTLSGIKEDNSLL CCEEEECHHHCCCHH	3.87	29967540
625	Sumoylation	SLTLSGIKEDNSLLN CEEEECHHHCCCHHH	63.64	28112733
625	Ubiquitination	SLTLSGIKEDNSLLN CEEEECHHHCCCHHH	63.64	29967540
629	Phosphorylation	SGIKEDNSLLNQGFL ECHHHCCCHHHCCCC	46.70	25159151
639	Sumoylation	NQGFLQAKPEKAAVA HCCCCCCCHHHHHHC	40.52	-
639	Sumoylation	NQGFLQAKPEKAAVA HCCCCCCCHHHHHHC	40.52	28112733
639	Ubiquitination	NQGFLQAKPEKAAVA HCCCCCCCHHHHHHC	40.52	29967540
639	Acetylation	NQGFLQAKPEKAAVA HCCCCCCCHHHHHHC	40.52	23236377
648	Ubiquitination	EKAAVAQKPRSHFTT HHHHHCCCCHHHCCC	32.43	29967540
648	Acetylation	EKAAVAQKPRSHFTT HHHHHCCCCHHHCCC	32.43	25953088
648	Sumoylation	EKAAVAQKPRSHFTT HHHHHCCCCHHHCCC	32.43	28112733
654	Phosphorylation	QKPRSHFTTPAPMSS CCCHHHCCCCCCCCC	26.84	26074081
655	Phosphorylation	KPRSHFTTPAPMSSA CCHHHCCCCCCCCCC	19.26	26074081
660	Phosphorylation	FTTPAPMSSAWKTVA CCCCCCCCCCCCCHH	18.82	26074081
661	Phosphorylation	TTPAPMSSAWKTVAC CCCCCCCCCCCCHHC	31.71	26074081
693	Phosphorylation	GRLKPSHTSRTLILS CCCCCCCCCCEEECC	25.00	-
695	Methylation	LKPSHTSRTLILS-- CCCCCCCCEEECC--	34.41	-

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
18	T	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
440	T	Phosphorylation	Kinase	CDK2	P24941	Uniprot
444	T	Phosphorylation	Kinase	CDK2	P24941	Uniprot
487	T	Phosphorylation	Kinase	CDK2	P24941	Uniprot
494	T	Phosphorylation	Kinase	CDK2	P24941	Uniprot
520	T	Phosphorylation	Kinase	CDK2	P24941	Uniprot
577	S	Phosphorylation	Kinase	CDK2	P24941	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	SKP2	Q13309	PMID:10871850
-	K	Ubiquitination	E3 ubiquitin ligase	CDC34	P49427	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
520	T	Phosphorylation		10095772
Phosphorylation at Thr-520 is probably involved in transcriptional activity.

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 MYBB_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ZN622_HUMAN	ZNF622	physical	12645566
CDN1C_HUMAN	CDKN1C	physical	12947099
CBP_HUMAN	CREBBP	genetic	11423988
PARP1_HUMAN	PARP1	physical	10744766
CCNA1_HUMAN	CCNA1	physical	11264176
MYBB_HUMAN	MYBL2	physical	10544265
CDK9_HUMAN	CDK9	genetic	10656684
CCNT1_HUMAN	CCNT1	genetic	10656684
CDK9_HUMAN	CDK9	physical	10656684
LZTR1_HUMAN	LZTR1	physical	20211142
TRI15_HUMAN	TRIM15	physical	20211142
ZBTB9_HUMAN	ZBTB9	physical	20211142
LIN54_HUMAN	LIN54	physical	17671431
LIN9_HUMAN	LIN9	physical	17671431
LIN37_HUMAN	LIN37	physical	17671431
RBBP4_HUMAN	RBBP4	physical	17671431
RBL1_HUMAN	RBL1	physical	17671431
LIN9_HUMAN	LIN9	physical	17159899
FLNA_HUMAN	FLNA	physical	18548008
SPTA1_HUMAN	SPTA1	physical	18548008
CLH1_HUMAN	CLTC	physical	18548008
SPTB2_HUMAN	SPTBN1	physical	18548008
CLCA_HUMAN	CLTA	physical	18548008
LIN9_HUMAN	LIN9	physical	18548008
UB2D4_HUMAN	UBE2D4	physical	21988832
CCNF_HUMAN	CCNF	physical	25557911
PA24A_HUMAN	PLA2G4A	physical	14769798
EPAS1_HUMAN	EPAS1	physical	28394947

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 MYBB_HUMAN

Related Literatures of Post-Translational Modification

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-241 AND THR-405, ANDMASS SPECTROMETRY.	19690332 [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-241, AND MASSSPECTROMETRY.	19413330 [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-393, AND MASSSPECTROMETRY.	15302935 [Abstract]
"Identification of cyclin A/Cdk2 phosphorylation sites in B-Myb."; Bartsch O., Horstmann S., Toprak K., Klempnauer K.H., Ferrari S.; Eur. J. Biochem. 260:384-391(1999). Cited for: PHOSPHORYLATION AT THR-440; THR-444; THR-494; THR-520 AND SER-577.	10095772 [Abstract]
"The cell-cycle regulated transcription factor B-Myb is phosphorylatedby cyclin A/Cdk2 at sites that enhance its transactivationproperties."; Saville M.K., Watson R.J.; Oncogene 17:2679-2689(1998). Cited for: PHOSPHORYLATION AT THR-444; THR-487; THR-494 AND SER-577.	9840932 [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 THR-266, AND MASSSPECTROMETRY.	17081983 [Abstract]

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