dbPTM

BCL9L_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BCL9L_HUMAN
UniProt AC	Q86UU0
Protein Name	B-cell CLL/lymphoma 9-like protein
Gene Name	BCL9L
Organism	Homo sapiens (Human).
Sequence Length	1499
Subcellular Localization	Nucleus .
Protein Description	Transcriptional regulator that acts as an activator. Promotes beta-catenin transcriptional activity. Plays a role in tumorigenesis. Enhances the neoplastic transforming activity of CTNNB1 (By similarity)..
Protein Sequence	MRILANKTRLPHPRRREAPGSPPLSPRGHCPPAPAKPMHPENKLTNHGKTGNGGAQSQHQNVNQGPTCNVGSKGVGAGNHGAKANQISPSNSSLKNPQAGVPPFSSLKGKVKRDRSVSVDSGEQREAGTPSLDSEAKEVAPRSKRRCVLERKQPYSGDEWCSGPDSEEDDKPIGATHNCNVADPAMAAPQLGPGQTTQLPLSESSVPGAPHGPPPGLRPDAPGGGGGGGGVPGKPPSQFVYVFTTHLANTAAEAVLQGRADSILAYHQQNVPRAKLDQAPKVPPTPEPLPLSTPSAGTPQSQPPPLPPPPPPAPGSAPPALPPEGPPEDSSQDLAPNSVGAASTGGGTGGTHPNTPTATTANNPLPPGGDPSSAPGPALLGEAAAPGNGQRSLVGSEGLSKEQLEHRERSLQTLRDIERLLLRSGETEPFLKGPPGGAGEGGPPAQAPPPPQQPPTAPPSGLKKYEEPLQSMISQTQSLGGPPLEHEVPGHPPGGDMGQQMNMMIQRLGQDSLTPEQVAWRKLQEEYYEEKRRKEEQIGLHGSRPLQDMMGMGGMMVRGPPPPYHSKPGDQWPPGMGAQLRGPMDVQDPMQLRGGPPFPGPRFPGNQIQRVPGFGGMQSMPMEVPMNAMQRPVRPGMGWTEDLPPMGGPSNFAQNTMPYPGGQGEAERFMTPRVREELLRHQLLEKRSMGMQRPLGMAGSGMGQSMEMERMMQAHRQMDPAMFPGQMAGGEGLAGTPMGMEFGGGRGLLSPPMGQSGLREVDPPMGPGNLNMNMNVNMNMNMNLNVQMTPQQQMLMSQKMRGPGDLMGPQGLSPEEMARVRAQNSSGVMGGPQKMLMPSQFPNQGQQGFSGGQGPYQAMSQDMGNTQDMFSPDQSSMPMSNVGTTRLSHMPLPPASNPPGTVHSAPNRGLGRRPSDLTISINQMGSPGMGHLKSPTLSQVHSPLVTSPSANLKSPQTPSQMVPLPSANPPGPLKSPQVLGSSLSVRSPTGSPSRLKSPSMAVPSPGWVASPKTAMPSPGVSQNKQPPLNMNSSTTLSNMEQGTLPPSGPRSSSSAPPANPPSGLMNPSLPFTSSPDPTPSQNPLSLMMTQMSKYAMPSSTPLYHNAIKTIATSDDELLPDRPLLPPPPPPQGSGPGISNSQPSQMHLNSAAAQSPMGMNLPGQQPLSHEPPPAMLPSPTPLGSNIPLHPNAQGTGGPPQNSMMMAPGGPDSLNAPCGPVPSSSQMMPFPPRLQQPHGAMAPTGGGGGGPGLQQHYPSGMALPPEDLPNQPPGPMPPQQHLMGKAMAGRMGDAYPPGVLPGVASVLNDPELSEVIRPTPTGIPEFDLSRIIPSEKPSSTLQYFPKSENQPPKAQPPNLHLMNLQNMMAEQTPSRPPNLPGQQGVQRGLNMSMCHPGQMSLLGRTGVPPQQGMVPHGLHQGVMSPPQGLMTQQNFMLMKQRGVGGEVYSQPPHMLSPQGSLMGPPPQQNLMVSHPLRQRSVSLDSQMGYLPAPGGMANLPF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Acetylation	-MRILANKTRLPHPR -CCCCCCCCCCCCCC	29.43	25953088
21	Phosphorylation	RRREAPGSPPLSPRG CCCCCCCCCCCCCCC	23.45	29255136
25	Phosphorylation	APGSPPLSPRGHCPP CCCCCCCCCCCCCCC	20.51	29255136
36	Acetylation	HCPPAPAKPMHPENK CCCCCCCCCCCCCCC	41.64	19608861
43	Acetylation	KPMHPENKLTNHGKT CCCCCCCCCCCCCCC	55.84	21466224
49	Acetylation	NKLTNHGKTGNGGAQ CCCCCCCCCCCCCCC	45.79	23954790
73	Acetylation	PTCNVGSKGVGAGNH CCCCCCCCCCCCCCC	52.25	23954790
83	Acetylation	GAGNHGAKANQISPS CCCCCCCCCCCCCCC	53.08	26051181
88	Phosphorylation	GAKANQISPSNSSLK CCCCCCCCCCCCCCC	16.71	22167270
90	Phosphorylation	KANQISPSNSSLKNP CCCCCCCCCCCCCCC	42.42	30266825
92	Phosphorylation	NQISPSNSSLKNPQA CCCCCCCCCCCCCCC	41.19	30266825
93	Phosphorylation	QISPSNSSLKNPQAG CCCCCCCCCCCCCCC	47.84	30266825
105	Phosphorylation	QAGVPPFSSLKGKVK CCCCCCHHHCCCCCC	40.30	23927012
106	Phosphorylation	AGVPPFSSLKGKVKR CCCCCHHHCCCCCCC	34.18	25159151
108	Acetylation	VPPFSSLKGKVKRDR CCCHHHCCCCCCCCC	59.64	19608861
110	Acetylation	PFSSLKGKVKRDRSV CHHHCCCCCCCCCCE	42.89	23954790
116	Phosphorylation	GKVKRDRSVSVDSGE CCCCCCCCEECCCCC	24.04	29255136
118	Phosphorylation	VKRDRSVSVDSGEQR CCCCCCEECCCCCCC	22.81	29255136
121	Phosphorylation	DRSVSVDSGEQREAG CCCEECCCCCCCCCC	41.91	25159151
129	Phosphorylation	GEQREAGTPSLDSEA CCCCCCCCCCCCHHH	19.42	29255136
131	Phosphorylation	QREAGTPSLDSEAKE CCCCCCCCCCHHHHH	44.65	21815630
134	Phosphorylation	AGTPSLDSEAKEVAP CCCCCCCHHHHHHCC	44.76	23403867
137	Acetylation	PSLDSEAKEVAPRSK CCCCHHHHHHCCHHH	48.98	19608861
275	Ubiquitination	QQNVPRAKLDQAPKV HHCCCHHHHCCCCCC	54.60	-
401	Ubiquitination	VGSEGLSKEQLEHRE CCCCCCCHHHHHHHH	55.30	-
410	Phosphorylation	QLEHRERSLQTLRDI HHHHHHHHHHHHHHH	21.78	20068231
424	Phosphorylation	IERLLLRSGETEPFL HHHHHHHCCCCCCCC	40.73	25159151
432	Acetylation	GETEPFLKGPPGGAG CCCCCCCCCCCCCCC	70.52	26051181
460	Phosphorylation	QPPTAPPSGLKKYEE CCCCCCCCHHHHCHH	56.55	28555341
465	Phosphorylation	PPSGLKKYEEPLQSM CCCHHHHCHHHHHHH	24.76	28985074
476	Phosphorylation	LQSMISQTQSLGGPP HHHHHHHHHHCCCCC	17.21	28985074
512	Phosphorylation	IQRLGQDSLTPEQVA HHHHCCCCCCHHHHH	26.67	22199227
514	Phosphorylation	RLGQDSLTPEQVAWR HHCCCCCCHHHHHHH	28.82	21815630
522	Sumoylation	PEQVAWRKLQEEYYE HHHHHHHHHHHHHHH	43.77	-
522	Sumoylation	PEQVAWRKLQEEYYE HHHHHHHHHHHHHHH	43.77	-
527	Phosphorylation	WRKLQEEYYEEKRRK HHHHHHHHHHHHHHH	18.54	-
531	Ubiquitination	QEEYYEEKRRKEEQI HHHHHHHHHHHHHHH	45.63	-
534	Acetylation	YYEEKRRKEEQIGLH HHHHHHHHHHHHCCC	70.41	12656583
564	Phosphorylation	VRGPPPPYHSKPGDQ ECCCCCCCCCCCCCC	25.21	28634298
566	Phosphorylation	GPPPPYHSKPGDQWP CCCCCCCCCCCCCCC	34.40	20068231
593	Methylation	VQDPMQLRGGPPFPG CCCCCHHCCCCCCCC	31.00	-
602	Dimethylation	GPPFPGPRFPGNQIQ CCCCCCCCCCCCCCE	57.20	-
602	Methylation	GPPFPGPRFPGNQIQ CCCCCCCCCCCCCCE	57.20	-
610	Methylation	FPGNQIQRVPGFGGM CCCCCCEECCCCCCC	37.92	-
668	Methylation	GGQGEAERFMTPRVR CCCCHHHHHCCHHHH	33.41	-
675	Methylation	RFMTPRVREELLRHQ HHCCHHHHHHHHHHH	32.71	-
680	Asymmetric dimethylarginine	RVREELLRHQLLEKR HHHHHHHHHHHHHHH	28.29	-
680	Methylation	RVREELLRHQLLEKR HHHHHHHHHHHHHHH	28.29	-
705	Phosphorylation	AGSGMGQSMEMERMM CCCCHHHHHHHHHHH	15.81	28348404
750	Phosphorylation	GGGRGLLSPPMGQSG CCCCCCCCCCCCCCC	31.81	29255136
756	Phosphorylation	LSPPMGQSGLREVDP CCCCCCCCCCCCCCC	33.78	30266825
813	Phosphorylation	LMGPQGLSPEEMARV CCCCCCCCHHHHHHH	36.77	28355574
821	Methylation	PEEMARVRAQNSSGV HHHHHHHHHHCCCCC	25.54	-
888	O-linked_Glycosylation	NVGTTRLSHMPLPPA CCCCCCCCCCCCCCC	17.91	30059200
896	O-linked_Glycosylation	HMPLPPASNPPGTVH CCCCCCCCCCCCCCC	56.49	30059200
896	Phosphorylation	HMPLPPASNPPGTVH CCCCCCCCCCCCCCC	56.49	22210691
915	Phosphorylation	RGLGRRPSDLTISIN CCCCCCCHHCEEEEE	43.36	27273156
918	Phosphorylation	GRRPSDLTISINQMG CCCCHHCEEEEECCC	20.05	23927012
920	Phosphorylation	RPSDLTISINQMGSP CCHHCEEEEECCCCC	15.39	23927012
926	Phosphorylation	ISINQMGSPGMGHLK EEEECCCCCCCCCCC	16.97	25159151
934	Phosphorylation	PGMGHLKSPTLSQVH CCCCCCCCCCHHHCC	29.49	30266825
936	Phosphorylation	MGHLKSPTLSQVHSP CCCCCCCCHHHCCCC	46.24	30266825
938	Phosphorylation	HLKSPTLSQVHSPLV CCCCCCHHHCCCCCC	32.41	30266825
942	Phosphorylation	PTLSQVHSPLVTSPS CCHHHCCCCCCCCCC	22.52	19664994
946	O-linked_Glycosylation	QVHSPLVTSPSANLK HCCCCCCCCCCCCCC	42.47	30059200
946	Phosphorylation	QVHSPLVTSPSANLK HCCCCCCCCCCCCCC	42.47	23401153
947	O-linked_Glycosylation	VHSPLVTSPSANLKS CCCCCCCCCCCCCCC	14.91	30059200
947	Phosphorylation	VHSPLVTSPSANLKS CCCCCCCCCCCCCCC	14.91	19664994
949	O-linked_Glycosylation	SPLVTSPSANLKSPQ CCCCCCCCCCCCCCC	29.56	30059200
949	Phosphorylation	SPLVTSPSANLKSPQ CCCCCCCCCCCCCCC	29.56	30266825
954	Phosphorylation	SPSANLKSPQTPSQM CCCCCCCCCCCHHHC	25.96	28355574
957	Phosphorylation	ANLKSPQTPSQMVPL CCCCCCCCHHHCCCC	28.43	28355574
959	Phosphorylation	LKSPQTPSQMVPLPS CCCCCCHHHCCCCCC	34.00	25159151
966	Phosphorylation	SQMVPLPSANPPGPL HHCCCCCCCCCCCCC	48.65	27251275
975	Phosphorylation	NPPGPLKSPQVLGSS CCCCCCCCCCCCCCC	28.40	19664994
981	Phosphorylation	KSPQVLGSSLSVRSP CCCCCCCCCCEEECC	24.76	23401153
982	Phosphorylation	SPQVLGSSLSVRSPT CCCCCCCCCEEECCC	23.90	30278072
984	Phosphorylation	QVLGSSLSVRSPTGS CCCCCCCEEECCCCC	19.89	30278072
987	Phosphorylation	GSSLSVRSPTGSPSR CCCCEEECCCCCHHH	25.34	23401153
989	Phosphorylation	SLSVRSPTGSPSRLK CCEEECCCCCHHHCC	52.09	23401153
991	Phosphorylation	SVRSPTGSPSRLKSP EEECCCCCHHHCCCC	23.37	28355574
993	Phosphorylation	RSPTGSPSRLKSPSM ECCCCCHHHCCCCCC	52.52	23927012
997	Phosphorylation	GSPSRLKSPSMAVPS CCHHHCCCCCCCCCC	27.14	25159151
999	Phosphorylation	PSRLKSPSMAVPSPG HHHCCCCCCCCCCCC	26.85	28355574
1004	Phosphorylation	SPSMAVPSPGWVASP CCCCCCCCCCCCCCC	29.46	28355574
1010	O-linked_Glycosylation	PSPGWVASPKTAMPS CCCCCCCCCCCCCCC	19.81	30059200
1010	Phosphorylation	PSPGWVASPKTAMPS CCCCCCCCCCCCCCC	19.81	28355574
1013	Phosphorylation	GWVASPKTAMPSPGV CCCCCCCCCCCCCCC	31.41	26657352
1017	Phosphorylation	SPKTAMPSPGVSQNK CCCCCCCCCCCCCCC	22.62	19664994
1021	O-linked_Glycosylation	AMPSPGVSQNKQPPL CCCCCCCCCCCCCCC	33.67	30059200
1021	Phosphorylation	AMPSPGVSQNKQPPL CCCCCCCCCCCCCCC	33.67	30266825
1051	Phosphorylation	LPPSGPRSSSSAPPA CCCCCCCCCCCCCCC	37.39	28348404
1052	Phosphorylation	PPSGPRSSSSAPPAN CCCCCCCCCCCCCCC	29.59	28348404
1053	Phosphorylation	PSGPRSSSSAPPANP CCCCCCCCCCCCCCC	31.59	28348404
1054	Phosphorylation	SGPRSSSSAPPANPP CCCCCCCCCCCCCCC	46.90	28348404
1072	Phosphorylation	MNPSLPFTSSPDPTP CCCCCCCCCCCCCCC	26.76	22199227
1073	O-linked_Glycosylation	NPSLPFTSSPDPTPS CCCCCCCCCCCCCCC	40.01	30059200
1073	Phosphorylation	NPSLPFTSSPDPTPS CCCCCCCCCCCCCCC	40.01	22199227
1074	Phosphorylation	PSLPFTSSPDPTPSQ CCCCCCCCCCCCCCC	30.20	22199227
1078	Phosphorylation	FTSSPDPTPSQNPLS CCCCCCCCCCCCHHH	42.84	22199227
1080	Phosphorylation	SSPDPTPSQNPLSLM CCCCCCCCCCHHHHH	45.10	22199227
1085	Phosphorylation	TPSQNPLSLMMTQMS CCCCCHHHHHHHHHH	18.57	22199227
1094	Phosphorylation	MMTQMSKYAMPSSTP HHHHHHHHCCCCCCC	10.79	29759185
1098	Phosphorylation	MSKYAMPSSTPLYHN HHHHCCCCCCCCCCC	33.49	29759185
1100	Phosphorylation	KYAMPSSTPLYHNAI HHCCCCCCCCCCCHH	22.96	24719451
1177	Phosphorylation	PPPAMLPSPTPLGSN CCCCCCCCCCCCCCC	37.13	26074081
1179	Phosphorylation	PAMLPSPTPLGSNIP CCCCCCCCCCCCCCC	35.17	26074081
1334	Acetylation	SRIIPSEKPSSTLQY HHCCCCCCCCCCCCC	55.31	23954790
1344	Sumoylation	STLQYFPKSENQPPK CCCCCCCCCCCCCCC	61.58	-
1344	Sumoylation	STLQYFPKSENQPPK CCCCCCCCCCCCCCC	61.58	28112733
1390	Phosphorylation	VQRGLNMSMCHPGQM HHHCCCHHHCCCCCH	19.72	27732954
1398	Phosphorylation	MCHPGQMSLLGRTGV HCCCCCHHHHCCCCC	16.74	27732954
1422	Phosphorylation	GLHQGVMSPPQGLMT CCCCCCCCCCCCCCH	30.90	23403867
1429	Phosphorylation	SPPQGLMTQQNFMLM CCCCCCCHHHCEECH	31.85	23403867
1439	Methylation	NFMLMKQRGVGGEVY CEECHHHHCCCCCCC	35.92	-
1446	Phosphorylation	RGVGGEVYSQPPHML HCCCCCCCCCCCCCC	9.40	27642862
1447	Phosphorylation	GVGGEVYSQPPHMLS CCCCCCCCCCCCCCC	41.19	29523821
1454	Phosphorylation	SQPPHMLSPQGSLMG CCCCCCCCCCCCCCC	13.96	25159151
1458	Phosphorylation	HMLSPQGSLMGPPPQ CCCCCCCCCCCCCCC	15.22	25159151
1478	Phosphorylation	SHPLRQRSVSLDSQM CCCCCCCCCCCCCCC	14.02	25159151
1480	Phosphorylation	PLRQRSVSLDSQMGY CCCCCCCCCCCCCCC	27.92	28355574
1483	Phosphorylation	QRSVSLDSQMGYLPA CCCCCCCCCCCCCCC	27.62	23663014
1487	Phosphorylation	SLDSQMGYLPAPGGM CCCCCCCCCCCCCCC	12.27	18669648

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
Oops, there are no upstream regulatory protein records of BCL9L_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of BCL9L_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 BCL9L_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
CTNB1_HUMAN	CTNNB1	physical	24360964

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 BCL9L_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-36; LYS-108 AND LYS-137, ANDMASS SPECTROMETRY.	19608861 [Abstract]
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-36, AND MASS SPECTROMETRY.	16916647 [Abstract]
Phosphorylation
Reference	PubMed
"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-88 AND SER-1017, 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-21; SER-25; SER-118;SER-813; SER-999; SER-1004; SER-1010 AND SER-1017, AND MASSSPECTROMETRY.	18669648 [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-750; SER-813; SER-987AND SER-991, AND MASS SPECTROMETRY.	18220336 [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-88, AND MASSSPECTROMETRY.	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-21; SER-25; SER-915;SER-954 AND THR-957, AND MASS SPECTROMETRY.	17081983 [Abstract]