dbPTM

BCR_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BCR_HUMAN
UniProt AC	P11274
Protein Name	Breakpoint cluster region protein
Gene Name	BCR
Organism	Homo sapiens (Human).
Sequence Length	1271
Subcellular Localization	Cell junction, synapse, postsynaptic cell membrane, postsynaptic density .
Protein Description	GTPase-activating protein for RAC1 and CDC42. Promotes the exchange of RAC or CDC42-bound GDP by GTP, thereby activating them. Displays serine/threonine kinase activity..
Protein Sequence	MVDPVGFAEAWKAQFPDSEPPRMELRSVGDIEQELERCKASIRRLEQEVNQERFRMIYLQTLLAKEKKSYDRQRWGFRRAAQAPDGASEPRASASRPQPAPADGADPPPAEEPEARPDGEGSPGKARPGTARRPGAAASGERDDRGPPASVAALRSNFERIRKGHGQPGADAEKPFYVNVEFHHERGLVKVNDKEVSDRISSLGSQAMQMERKKSQHGAGSSVGDASRPPYRGRSSESSCGVDGDYEDAELNPRFLKDNLIDANGGSRPPWPPLEYQPYQSIYVGGMMEGEGKGPLLRSQSTSEQEKRLTWPRRSYSPRSFEDCGGGYTPDCSSNENLTSSEEDFSSGQSSRVSPSPTTYRMFRDKSRSPSQNSQQSFDSSSPPTPQCHKRHRHCPVVVSEATIVGVRKTGQIWPNDGEGAFHGDADGSFGTPPGYGCAADRAEEQRRHQDGLPYIDDSPSSSPHLSSKGRGSRDALVSGALESTKASELDLEKGLEMRKWVLSGILASEETYLSHLEALLLPMKPLKAAATTSQPVLTSQQIETIFFKVPELYEIHKEFYDGLFPRVQQWSHQQRVGDLFQKLASQLGVYRAFVDNYGVAMEMAEKCCQANAQFAEISENLRARSNKDAKDPTTKNSLETLLYKPVDRVTRSTLVLHDLLKHTPASHPDHPLLQDALRISQNFLSSINEEITPRRQSMTVKKGEHRQLLKDSFMVELVEGARKLRHVFLFTDLLLCTKLKKQSGGKTQQYDCKWYIPLTDLSFQMVDELEAVPNIPLVPDEELDALKIKISQIKNDIQREKRANKGSKATERLKKKLSEQESLLLLMSPSMAFRVHSRNGKSYTFLISSDYERAEWRENIREQQKKCFRSFSLTSVELQMLTNSCVKLQTVHSIPLTINKEDDESPGLYGFLNVIVHSATGFKQSSNLYCTLEVDSFGYFVNKAKTRVYRDTAEPNWNEEFEIELEGSQTLRILCYEKCYNKTKIPKEDGESTDRLMGKGQVQLDPQALQDRDWQRTVIAMNGIEVKLSVKFNSREFSLKRMPSRKQTGVFGVKIAVVTKRERSKVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDVNNKDVSVMMSEMDVNAIAGTLKLYFRELPEPLFTDEFYPNFAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFGPTLLRPSEKESKLPANPSQPITMTDSWSLEVMSQVQVLLYFLQLEAIPAPDSKRQSILFSTEV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MVDPVGFA -------CCCCCCHH	35.59	22223895
18	Phosphorylation	WKAQFPDSEPPRMEL HHHHCCCCCCCCEEE	52.84	21406692
58	Phosphorylation	QERFRMIYLQTLLAK HHHHHHHHHHHHHHH	5.39	22817900
88	Phosphorylation	AQAPDGASEPRASAS HCCCCCCCCCCCCCC	54.38	21815630
93	Phosphorylation	GASEPRASASRPQPA CCCCCCCCCCCCCCC	28.23	23403867
95	Phosphorylation	SEPRASASRPQPAPA CCCCCCCCCCCCCCC	41.83	23403867
122	Phosphorylation	ARPDGEGSPGKARPG CCCCCCCCCCCCCCC	26.61	19664994
122 (in isoform 1)	Phosphorylation	-	26.61	-
130	Phosphorylation	PGKARPGTARRPGAA CCCCCCCCCCCCCCC	21.48	26074081
139	Phosphorylation	RRPGAAASGERDDRG CCCCCCCCCCCCCCC	36.14	26074081
150	Phosphorylation	DDRGPPASVAALRSN CCCCCCHHHHHHHHH	20.33	26074081
156	Phosphorylation	ASVAALRSNFERIRK HHHHHHHHHHHHHHC	46.88	26074081
177	Phosphorylation	ADAEKPFYVNVEFHH CCCCCCEEEEEEEEC	10.31	21945579
177 (in isoform 1)	Phosphorylation	-	10.31	-
177	Dephosphorylation	ADAEKPFYVNVEFHH CCCCCCEEEEEEEEC	10.31	9566916
194	Acetylation	GLVKVNDKEVSDRIS CCEECCCHHHHHHHH	55.61	7709545
194	Ubiquitination	GLVKVNDKEVSDRIS CCEECCCHHHHHHHH	55.61	24816145
201	Phosphorylation	KEVSDRISSLGSQAM HHHHHHHHHHHHHHH	22.02	29978859
202	Phosphorylation	EVSDRISSLGSQAMQ HHHHHHHHHHHHHHH	34.09	29978859
205	Phosphorylation	DRISSLGSQAMQMER HHHHHHHHHHHHHHH	21.76	23917254
208	Sulfoxidation	SSLGSQAMQMERKKS HHHHHHHHHHHHHHH	2.78	21406390
213	Acetylation	QAMQMERKKSQHGAG HHHHHHHHHHHCCCC	43.39	7709557
214	Ubiquitination	AMQMERKKSQHGAGS HHHHHHHHHHCCCCC	62.66	-
215	Phosphorylation	MQMERKKSQHGAGSS HHHHHHHHHCCCCCC	30.37	23401153
221	Phosphorylation	KSQHGAGSSVGDASR HHHCCCCCCCCCCCC	22.71	25159151
222	Phosphorylation	SQHGAGSSVGDASRP HHCCCCCCCCCCCCC	29.24	23927012
227	Phosphorylation	GSSVGDASRPPYRGR CCCCCCCCCCCCCCC	50.49	30576142
231	Phosphorylation	GDASRPPYRGRSSES CCCCCCCCCCCCCCC	28.51	30576142
235	Phosphorylation	RPPYRGRSSESSCGV CCCCCCCCCCCCCCC	41.08	23401153
236	Phosphorylation	PPYRGRSSESSCGVD CCCCCCCCCCCCCCC	39.89	25159151
238	Phosphorylation	YRGRSSESSCGVDGD CCCCCCCCCCCCCCC	32.64	25159151
239	Phosphorylation	RGRSSESSCGVDGDY CCCCCCCCCCCCCCH	15.73	25159151
246	Phosphorylation	SCGVDGDYEDAELNP CCCCCCCHHHCCCCH	22.65	8955135
246 (in isoform 1)	Phosphorylation	-	22.65	-
267	Phosphorylation	LIDANGGSRPPWPPL EECCCCCCCCCCCCC	42.91	-
276	Phosphorylation	PPWPPLEYQPYQSIY CCCCCCCCCCCCEEE	23.59	8955135
276 (in isoform 1)	Phosphorylation	-	23.59	-
279	Phosphorylation	PPLEYQPYQSIYVGG CCCCCCCCCEEEECC	10.20	8955135
279 (in isoform 1)	Phosphorylation	-	10.20	-
281	Phosphorylation	LEYQPYQSIYVGGMM CCCCCCCEEEECCCC	15.28	27642862
283	Phosphorylation	YQPYQSIYVGGMMEG CCCCCEEEECCCCCC	9.78	8622703
283 (in isoform 1)	Phosphorylation	-	9.78	-
299	Phosphorylation	GKGPLLRSQSTSEQE CCCCCCCCCCCCHHH	28.58	26552605
301	Phosphorylation	GPLLRSQSTSEQEKR CCCCCCCCCCHHHHC	34.84	27273156
302	Phosphorylation	PLLRSQSTSEQEKRL CCCCCCCCCHHHHCC	28.75	26552605
303	Phosphorylation	LLRSQSTSEQEKRLT CCCCCCCCHHHHCCC	42.39	28985074
310	Phosphorylation	SEQEKRLTWPRRSYS CHHHHCCCCCCCCCC	37.14	12522270
310 (in isoform 1)	Phosphorylation	-	37.14	-
315	Phosphorylation	RLTWPRRSYSPRSFE CCCCCCCCCCCCCCC	31.10	30576142
315 (in isoform 1)	Phosphorylation	-	31.10	-
316	Phosphorylation	LTWPRRSYSPRSFED CCCCCCCCCCCCCCC	22.38	20068231
317	Phosphorylation	TWPRRSYSPRSFEDC CCCCCCCCCCCCCCC	18.32	21955146
317 (in isoform 1)	Phosphorylation	-	18.32	-
320	Phosphorylation	RRSYSPRSFEDCGGG CCCCCCCCCCCCCCC	36.05	26074081
328	Phosphorylation	FEDCGGGYTPDCSSN CCCCCCCCCCCCCCC	20.55	22817900
328 (in isoform 1)	Phosphorylation	-	20.55	-
329	Phosphorylation	EDCGGGYTPDCSSNE CCCCCCCCCCCCCCC	18.87	30576142
333	Phosphorylation	GGYTPDCSSNENLTS CCCCCCCCCCCCCCC	43.51	28348404
334	Phosphorylation	GYTPDCSSNENLTSS CCCCCCCCCCCCCCC	55.27	28348404
340	Phosphorylation	SSNENLTSSEEDFSS CCCCCCCCCHHHHCC	38.63	-
346	Phosphorylation	TSSEEDFSSGQSSRV CCCHHHHCCCCCCCC	45.97	30576142
350	Phosphorylation	EDFSSGQSSRVSPSP HHHCCCCCCCCCCCC	24.52	30576142
351	Phosphorylation	DFSSGQSSRVSPSPT HHCCCCCCCCCCCCC	28.90	-
354	Phosphorylation	SGQSSRVSPSPTTYR CCCCCCCCCCCCHHH	20.67	23401153
354 (in isoform 1)	Phosphorylation	-	20.67	-
356	Phosphorylation	QSSRVSPSPTTYRMF CCCCCCCCCCHHHHH	27.63	25159151
356 (in isoform 1)	Phosphorylation	-	27.63	-
358	Phosphorylation	SRVSPSPTTYRMFRD CCCCCCCCHHHHHCC	40.57	23927012
359	Phosphorylation	RVSPSPTTYRMFRDK CCCCCCCHHHHHCCC	16.71	23927012
360	Phosphorylation	VSPSPTTYRMFRDKS CCCCCCHHHHHCCCC	11.54	23927012
360 (in isoform 1)	Phosphorylation	-	11.54	-
367	Phosphorylation	YRMFRDKSRSPSQNS HHHHCCCCCCCCCCC	42.13	23403867
369	Phosphorylation	MFRDKSRSPSQNSQQ HHCCCCCCCCCCCCC	35.67	23403867
371	Phosphorylation	RDKSRSPSQNSQQSF CCCCCCCCCCCCCCC	43.15	23403867
374	Phosphorylation	SRSPSQNSQQSFDSS CCCCCCCCCCCCCCC	23.20	23403867
377	Phosphorylation	PSQNSQQSFDSSSPP CCCCCCCCCCCCCCC	24.31	23403867
380	Phosphorylation	NSQQSFDSSSPPTPQ CCCCCCCCCCCCCCH	30.61	26657352
381	Phosphorylation	SQQSFDSSSPPTPQC CCCCCCCCCCCCCHH	49.02	26657352
382	Phosphorylation	QQSFDSSSPPTPQCH CCCCCCCCCCCCHHC	38.56	23403867
385	Phosphorylation	FDSSSPPTPQCHKRH CCCCCCCCCHHCCCC	29.40	23403867
400	O-linked_Glycosylation	RHCPVVVSEATIVGV CCCCEEEEECEEEEE	15.20	28657654
410	Phosphorylation	TIVGVRKTGQIWPND EEEEEEECCCCCCCC	24.61	28122231
429	Phosphorylation	FHGDADGSFGTPPGY CCCCCCCCCCCCCCC	22.50	23401153
432	Phosphorylation	DADGSFGTPPGYGCA CCCCCCCCCCCCCCH	25.05	28985074
436	Phosphorylation	SFGTPPGYGCAADRA CCCCCCCCCCHHHHH	18.14	16464493
436 (in isoform 1)	Phosphorylation	-	18.14	-
455	Phosphorylation	RHQDGLPYIDDSPSS HHCCCCCCCCCCCCC	23.25	22167270
459	Phosphorylation	GLPYIDDSPSSSPHL CCCCCCCCCCCCCCC	23.96	22167270
459 (in isoform 1)	Phosphorylation	-	23.96	-
461	Phosphorylation	PYIDDSPSSSPHLSS CCCCCCCCCCCCCCC	47.61	22167270
462	Phosphorylation	YIDDSPSSSPHLSSK CCCCCCCCCCCCCCC	51.80	22167270
463	Phosphorylation	IDDSPSSSPHLSSKG CCCCCCCCCCCCCCC	22.22	22167270
463 (in isoform 1)	Phosphorylation	-	22.22	-
467	Phosphorylation	PSSSPHLSSKGRGSR CCCCCCCCCCCCCCH	27.28	22167270
467 (in isoform 1)	Phosphorylation	-	27.28	-
468	Phosphorylation	SSSPHLSSKGRGSRD CCCCCCCCCCCCCHH	45.55	23927012
471	Methylation	PHLSSKGRGSRDALV CCCCCCCCCCHHHHH	43.58	-
473	Phosphorylation	LSSKGRGSRDALVSG CCCCCCCCHHHHHHH	26.15	23401153
479	Phosphorylation	GSRDALVSGALESTK CCHHHHHHHHHHCCC	21.14	23403867
484	Phosphorylation	LVSGALESTKASELD HHHHHHHCCCHHHCC	35.74	23403867
485	Phosphorylation	VSGALESTKASELDL HHHHHHCCCHHHCCH	22.66	23403867
486	Ubiquitination	SGALESTKASELDLE HHHHHCCCHHHCCHH	60.23	29967540
488	Phosphorylation	ALESTKASELDLEKG HHHCCCHHHCCHHHH	40.00	23917254
494	Ubiquitination	ASELDLEKGLEMRKW HHHCCHHHHHHHHHH	75.89	29967540
513	Phosphorylation	ILASEETYLSHLEAL HHCCCCHHHHHHHHH	14.97	-
515	Phosphorylation	ASEETYLSHLEALLL CCCCHHHHHHHHHHC	18.66	-
540	Phosphorylation	TSQPVLTSQQIETIF CCCCCCCHHHHHHEE	18.87	-
549	Ubiquitination	QIETIFFKVPELYEI HHHHEEEECHHHHHH	46.24	29967540
554	Phosphorylation	FFKVPELYEIHKEFY EEECHHHHHHHHHHH	15.92	22817900
558	Ubiquitination	PELYEIHKEFYDGLF HHHHHHHHHHHHCCH	56.00	29967540
561	Phosphorylation	YEIHKEFYDGLFPRV HHHHHHHHHCCHHHH	15.36	23917254
572	Phosphorylation	FPRVQQWSHQQRVGD HHHHHHHCHHHHHHH	13.69	-
583	Ubiquitination	RVGDLFQKLASQLGV HHHHHHHHHHHHHCH	38.39	22817900
583 (in isoform 1)	Ubiquitination	-	38.39	21906983
583 (in isoform 2)	Ubiquitination	-	38.39	21906983
586	Phosphorylation	DLFQKLASQLGVYRA HHHHHHHHHHCHHHH	36.05	23186163
591	Phosphorylation	LASQLGVYRAFVDNY HHHHHCHHHHHHCCH	8.40	12522270
591 (in isoform 1)	Phosphorylation	-	8.40	-
598	Phosphorylation	YRAFVDNYGVAMEMA HHHHHCCHHHHHHHH	14.44	21447384
598 (in isoform 1)	Phosphorylation	-	14.44	-
626	Phosphorylation	SENLRARSNKDAKDP HHHHHHHCCCCCCCC	47.44	-
634	Phosphorylation	NKDAKDPTTKNSLET CCCCCCCCCHHHHHH	61.61	27251275
635	Phosphorylation	KDAKDPTTKNSLETL CCCCCCCCHHHHHHH	33.35	27251275
636	Ubiquitination	DAKDPTTKNSLETLL CCCCCCCHHHHHHHH	47.20	29967540
638	Phosphorylation	KDPTTKNSLETLLYK CCCCCHHHHHHHHCC	29.19	21945579
641	Phosphorylation	TTKNSLETLLYKPVD CCHHHHHHHHCCCCC	27.62	21945579
644	Phosphorylation	NSLETLLYKPVDRVT HHHHHHHCCCCCHHH	19.16	21945579
644 (in isoform 1)	Phosphorylation	-	19.16	-
645	Ubiquitination	SLETLLYKPVDRVTR HHHHHHCCCCCHHHH	38.24	29967540
651	Phosphorylation	YKPVDRVTRSTLVLH CCCCCHHHHHHHHHH	21.57	26434776
653	Phosphorylation	PVDRVTRSTLVLHDL CCCHHHHHHHHHHHH	19.41	20873877
654	Phosphorylation	VDRVTRSTLVLHDLL CCHHHHHHHHHHHHH	20.00	30087585
662	Ubiquitination	LVLHDLLKHTPASHP HHHHHHHHCCCCCCC	53.37	-
681	Phosphorylation	LQDALRISQNFLSSI HHHHHHHCHHHHHHC	16.79	22210691
686	Phosphorylation	RISQNFLSSINEEIT HHCHHHHHHCCCCCC	25.65	24076635
687	Phosphorylation	ISQNFLSSINEEITP HCHHHHHHCCCCCCC	31.42	22210691
693	Phosphorylation	SSINEEITPRRQSMT HHCCCCCCCCCCCCC	17.64	21815630
698	Phosphorylation	EITPRRQSMTVKKGE CCCCCCCCCCCCCCC	18.01	30576142
700	Phosphorylation	TPRRQSMTVKKGEHR CCCCCCCCCCCCCHH	34.13	29396449
747	Acetylation	LKKQSGGKTQQYDCK HHHHCCCCCEEEEEE	46.84	25953088
751	Phosphorylation	SGGKTQQYDCKWYIP CCCCCEEEEEEEEEE	17.31	-
756	Phosphorylation	QQYDCKWYIPLTDLS EEEEEEEEEECCCCE	4.34	-
792	Phosphorylation	DALKIKISQIKNDIQ HHHHHHHHHHHHHHH	22.35	24719451
795	Ubiquitination	KIKISQIKNDIQREK HHHHHHHHHHHHHHH	40.71	29967540
819	Phosphorylation	ERLKKKLSEQESLLL HHHHHHCCHHHHHHH	46.22	26552605
823	Phosphorylation	KKLSEQESLLLLMSP HHCCHHHHHHHHHCH	24.82	26552605
829	Phosphorylation	ESLLLLMSPSMAFRV HHHHHHHCHHHEEEE	17.50	26552605
831	Phosphorylation	LLLLMSPSMAFRVHS HHHHHCHHHEEEEEC	18.55	24719451
843	Phosphorylation	VHSRNGKSYTFLISS EECCCCCEEEEEEEC	30.70	-
844	Phosphorylation	HSRNGKSYTFLISSD ECCCCCEEEEEEECC	12.66	22817900
845	Phosphorylation	SRNGKSYTFLISSDY CCCCCEEEEEEECCH	21.03	-
852	Phosphorylation	TFLISSDYERAEWRE EEEEECCHHHHHHHH	14.84	22817900
871	Phosphorylation	QQKKCFRSFSLTSVE HHHHHHHHCCCCHHH	10.03	20873877
873	Phosphorylation	KKCFRSFSLTSVELQ HHHHHHCCCCHHHHH	31.80	20873877
875	Phosphorylation	CFRSFSLTSVELQML HHHHCCCCHHHHHHH	29.54	20873877
876	Phosphorylation	FRSFSLTSVELQMLT HHHCCCCHHHHHHHH	20.91	28122231
894	Phosphorylation	VKLQTVHSIPLTINK EEEEEEEECEEEECC	22.89	23186163
898	Phosphorylation	TVHSIPLTINKEDDE EEEECEEEECCCCCC	19.70	26434776
906	Phosphorylation	INKEDDESPGLYGFL ECCCCCCCCCHHHHH	31.12	26434776
910	Phosphorylation	DDESPGLYGFLNVIV CCCCCCHHHHHHHHE	16.25	26434776
919	Phosphorylation	FLNVIVHSATGFKQS HHHHHEECCCCCCCC	19.34	-
921	Phosphorylation	NVIVHSATGFKQSSN HHHEECCCCCCCCCC	46.28	-
953	Phosphorylation	KTRVYRDTAEPNWNE HCCEEECCCCCCCCC	24.75	22468782
993	Phosphorylation	IPKEDGESTDRLMGK CCCCCCCCCCCCCCC	40.93	25627689
1000	Ubiquitination	STDRLMGKGQVQLDP CCCCCCCCCEEECCH	32.00	29967540
1003	Ubiquitination	RLMGKGQVQLDPQAL CCCCCCEEECCHHHH	9.22	29967540
1017	Ubiquitination	LQDRDWQRTVIAMNG HHCCCHHHEEEEECC	27.06	22817900
1018	Phosphorylation	QDRDWQRTVIAMNGI HCCCHHHEEEEECCE	10.93	-
1022	Ubiquitination	WQRTVIAMNGIEVKL HHHEEEEECCEEEEE	3.03	21963094
1030	Phosphorylation	NGIEVKLSVKFNSRE CCEEEEEEEEECCCC	19.97	21406692
1035	Phosphorylation	KLSVKFNSREFSLKR EEEEEECCCCEEEEE	36.00	28355574
1039	Phosphorylation	KFNSREFSLKRMPSR EECCCCEEEEECCCC	28.38	28355574
1047	Ubiquitination	LKRMPSRKQTGVFGV EEECCCCCCCCCCCE	57.45	29967540
1047	Malonylation	LKRMPSRKQTGVFGV EEECCCCCCCCCCCE	57.45	26320211
1049	Phosphorylation	RMPSRKQTGVFGVKI ECCCCCCCCCCCEEE	38.05	25159151
1058	Ubiquitination	VFGVKIAVVTKRERS CCCEEEEEEECCHHH	6.82	29967540
1061	Ubiquitination	VKIAVVTKRERSKVP EEEEEEECCHHHCCC	40.42	22817900
1066	Ubiquitination	VTKRERSKVPYIVRQ EECCHHHCCCHHHHH	54.15	21963094
1066	Malonylation	VTKRERSKVPYIVRQ EECCHHHCCCHHHHH	54.15	26320211
1069	Phosphorylation	RERSKVPYIVRQCVE CHHHCCCHHHHHHHH	18.29	28064214
1089	Phosphorylation	GMEEVGIYRVSGVAT CCHHCEEEEEECCHH	10.07	23917254
1102	Ubiquitination	ATDIQALKAAFDVNN HHHHHHHHHHHCCCC	40.46	29967540
1153	Ubiquitination	PNFAEGIALSDPVAK CCCCCCCCCCCHHHH	16.33	29967540
1197	Ubiquitination	AEKEAVNKMSLHNLA HHHHHHHHCCHHHHH	24.22	29967540
1220 (in isoform 1)	Phosphorylation	-	60.63	-
1220	Phosphorylation	RPSEKESKLPANPSQ CCCCCCCCCCCCCCC	60.63	32142685
1264	Phosphorylation	APDSKRQSILFSTEV CCCCCCCEEEEEECC	25.87	19664994
1268	Phosphorylation	KRQSILFSTEV---- CCCEEEEEECC----	21.88	23403867
1269	Phosphorylation	RQSILFSTEV----- CCEEEEEECC-----	33.17	22210691

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
177	Y	Phosphorylation	Kinase	FES	P07332	PhosphoELM
177	Y	Phosphorylation	Kinase	ABL-FAMILY	-	GPS
177	Y	Phosphorylation	Kinase	LYN	P07948	PSP
177	Y	Phosphorylation	Kinase	JAK2	O60674	GPS
177	Y	Phosphorylation	Kinase	HCK	P08631	Uniprot
177	Y	Phosphorylation	Kinase	FYN	P06241	PSP
177	Y	Phosphorylation	Kinase	BCR-ABL1	A9UF07	PSP
177	Y	Phosphorylation	Kinase	ABL1	P00519	PhosphoELM
246	Y	Phosphorylation	Kinase	FES	P07332	Uniprot
276	Y	Phosphorylation	Kinase	FES	P07332	PhosphoELM
279	Y	Phosphorylation	Kinase	FES	P07332	PhosphoELM
283	Y	Phosphorylation	Kinase	FES	P07332	PhosphoELM
283	Y	Phosphorylation	Kinase	BCR-ABL1	A9UF07	PSP
283	Y	Phosphorylation	Kinase	ABL-FAMILY	-	GPS
328	Y	Phosphorylation	Kinase	BCR-ABL1	A9UF07	PSP
360	Y	Phosphorylation	Kinase	ABL1	P00519	PhosphoELM
360	Y	Phosphorylation	Kinase	ABL-FAMILY	-	GPS
360	Y	Phosphorylation	Kinase	BCR-ABL1	A9UF07	PSP
1264	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	CBL	P22681	PMID:20675402

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HCK_HUMAN	HCK	physical	12592324
PTN6_HUMAN	PTPN6	physical	9788431
FES_HUMAN	FES	physical	10706130
RB_HUMAN	RB1	physical	9071815
ERCC3_HUMAN	ERCC3	physical	9874796
GRB2_HUMAN	GRB2	physical	10887132
ABL1_HUMAN	ABL1	physical	12543778
GAB2_HUMAN	GAB2	physical	15143164
HCK_HUMAN	HCK	physical	10849448
HXA9_HUMAN	HOXA9	genetic	12393433
CRKL_HUMAN	CRKL	physical	8978305
CRKL_HUMAN	CRKL	physical	10194128
GRB2_HUMAN	GRB2	physical	15143164
CRKL_HUMAN	CRKL	physical	15143164
KIT_HUMAN	KIT	physical	8757502
PK3CG_HUMAN	PIK3CG	physical	7606002
AFAD_HUMAN	MLLT4	physical	12808105
IGS21_HUMAN	IGSF21	physical	16169070
P53_HUMAN	TP53	physical	16169070
U119A_HUMAN	UNC119	physical	16169070
GRB2_HUMAN	GRB2	physical	9178913
RAC1_HUMAN	RAC1	physical	9535855
CDC42_HUMAN	CDC42	physical	9535855
RHOA_HUMAN	RHOA	physical	9535855
GRB2_HUMAN	GRB2	physical	7529874
IL3_HUMAN	IL3	physical	9209414
TS101_HUMAN	TSG101	physical	16778200
GRB2_HUMAN	GRB2	physical	14725908
CBL_HUMAN	CBL	physical	8621719
ERBIN_HUMAN	ERBB2IP	physical	15123239
DOK1_HUMAN	DOK1	physical	9822717
HS90A_HUMAN	HSP90AA1	physical	16723087
TEBP_HUMAN	PTGES3	physical	16723087
HSP74_HUMAN	HSPA4	physical	16723087
CH60_HUMAN	HSPD1	physical	16723087
PK3CG_HUMAN	PIK3CG	physical	25241761
P85A_HUMAN	PIK3R1	physical	18346204
UBP15_HUMAN	USP15	physical	27173435
JIP4_HUMAN	SPAG9	physical	27173435
MCM2_HUMAN	MCM2	physical	27173435
MCM4_HUMAN	MCM4	physical	27173435
WEE1_HUMAN	WEE1	physical	27173435
KC1A_HUMAN	CSNK1A1	physical	27173435
MCM6_HUMAN	MCM6	physical	27173435
ABL1_HUMAN	ABL1	physical	21653319

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
608232	Leukemia, chronic myeloid (CML)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB06616	Bosutinib
DB08901	Ponatinib

Regulatory Network of BCR_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 TYR-177; SER-459 ANDSER-1264, AND MASS SPECTROMETRY.	19690332 [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-459 AND SER-463, ANDMASS SPECTROMETRY.	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-122, AND MASSSPECTROMETRY.	18220336 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-459, AND MASSSPECTROMETRY.	18088087 [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-459, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry."; Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.; Anal. Chem. 76:2763-2772(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1264, AND MASSSPECTROMETRY.	15144186 [Abstract]
"Profiling of tyrosine phosphorylation pathways in human cells usingmass spectrometry."; Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T.,Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.; Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-177; THR-310; SER-459;SER-463; TYR-591 AND TYR-644, AND MASS SPECTROMETRY.	12522270 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-177, AND MASSSPECTROMETRY.	18083107 [Abstract]
"The c-Fes tyrosine kinase cooperates with the breakpoint clusterregion protein (Bcr) to induce neurite extension in a Rac- and Cdc42-dependent manner."; Laurent C.E., Smithgall T.E.; Exp. Cell Res. 299:188-198(2004). Cited for: INTERACTION WITH FES/FPS; ABL1; PIK3R1 AND GRB2, MUTAGENESIS OFTYR-177, AND PHOSPHORYLATION AT TYR-246.	15302586 [Abstract]
"The Src family kinase Hck interacts with Bcr-Abl by a kinase-independent mechanism and phosphorylates the Grb2-binding site ofBcr."; Warmuth M., Bergmann M., Priess A., Hauslmann K., Emmerich B.,Hallek M.; J. Biol. Chem. 272:33260-33270(1997). Cited for: PHOSPHORYLATION AT TYR-177 BY HCK, MUTAGENESIS OF TYR-177, ANDINTERACTION WITH HCK AND GRB2.	9407116 [Abstract]