dbPTM

ERBB4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ERBB4_HUMAN
UniProt AC	Q15303
Protein Name	Receptor tyrosine-protein kinase erbB-4
Gene Name	ERBB4
Organism	Homo sapiens (Human).
Sequence Length	1308
Subcellular Localization	Cell membrane Single-pass type I membrane protein . In response to NRG1 treatment, the activated receptor is internalized. ERBB4 intracellular domain: Nucleus . Mitochondrion . Following proteolytical processing E4ICD (E4ICD1 or E4ICD2 genera
Protein Description	Tyrosine-protein kinase that plays an essential role as cell surface receptor for neuregulins and EGF family members and regulates development of the heart, the central nervous system and the mammary gland, gene transcription, cell proliferation, differentiation, migration and apoptosis. Required for normal cardiac muscle differentiation during embryonic development, and for postnatal cardiomyocyte proliferation. Required for normal development of the embryonic central nervous system, especially for normal neural crest cell migration and normal axon guidance. Required for mammary gland differentiation, induction of milk proteins and lactation. Acts as cell-surface receptor for the neuregulins NRG1, NRG2, NRG3 and NRG4 and the EGF family members BTC, EREG and HBEGF. Ligand binding triggers receptor dimerization and autophosphorylation at specific tyrosine residues that then serve as binding sites for scaffold proteins and effectors. Ligand specificity and signaling is modulated by alternative splicing, proteolytic processing, and by the formation of heterodimers with other ERBB family members, thereby creating multiple combinations of intracellular phosphotyrosines that trigger ligand- and context-specific cellular responses. Mediates phosphorylation of SHC1 and activation of the MAP kinases MAPK1/ERK2 and MAPK3/ERK1. Isoform JM-A CYT-1 and isoform JM-B CYT-1 phosphorylate PIK3R1, leading to the activation of phosphatidylinositol 3-kinase and AKT1 and protect cells against apoptosis. Isoform JM-A CYT-1 and isoform JM-B CYT-1 mediate reorganization of the actin cytoskeleton and promote cell migration in response to NRG1. Isoform JM-A CYT-2 and isoform JM-B CYT-2 lack the phosphotyrosine that mediates interaction with PIK3R1, and hence do not phosphorylate PIK3R1, do not protect cells against apoptosis, and do not promote reorganization of the actin cytoskeleton and cell migration. Proteolytic processing of isoform JM-A CYT-1 and isoform JM-A CYT-2 gives rise to the corresponding soluble intracellular domains (4ICD) that translocate to the nucleus, promote nuclear import of STAT5A, activation of STAT5A, mammary epithelium differentiation, cell proliferation and activation of gene expression. The ERBB4 soluble intracellular domains (4ICD) colocalize with STAT5A at the CSN2 promoter to regulate transcription of milk proteins during lactation. The ERBB4 soluble intracellular domains can also translocate to mitochondria and promote apoptosis..
Protein Sequence	MKPATGLWVWVSLLVAAGTVQPSDSQSVCAGTENKLSSLSDLEQQYRALRKYYENCEVVMGNLEITSIEHNRDLSFLRSVREVTGYVLVALNQFRYLPLENLRIIRGTKLYEDRYALAIFLNYRKDGNFGLQELGLKNLTEILNGGVYVDQNKFLCYADTIHWQDIVRNPWPSNLTLVSTNGSSGCGRCHKSCTGRCWGPTENHCQTLTRTVCAEQCDGRCYGPYVSDCCHRECAGGCSGPKDTDCFACMNFNDSGACVTQCPQTFVYNPTTFQLEHNFNAKYTYGAFCVKKCPHNFVVDSSSCVRACPSSKMEVEENGIKMCKPCTDICPKACDGIGTGSLMSAQTVDSSNIDKFINCTKINGNLIFLVTGIHGDPYNAIEAIDPEKLNVFRTVREITGFLNIQSWPPNMTDFSVFSNLVTIGGRVLYSGLSLLILKQQGITSLQFQSLKEISAGNIYITDNSNLCYYHTINWTTLFSTINQRIVIRDNRKAENCTAEGMVCNHLCSSDGCWGPGPDQCLSCRRFSRGRICIESCNLYDGEFREFENGSICVECDPQCEKMEDGLLTCHGPGPDNCTKCSHFKDGPNCVEKCPDGLQGANSFIFKYADPDRECHPCHPNCTQGCNGPTSHDCIYYPWTGHSTLPQHARTPLIAAGVIGGLFILVIVGLTFAVYVRRKSIKKKRALRRFLETELVEPLTPSGTAPNQAQLRILKETELKRVKVLGSGAFGTVYKGIWVPEGETVKIPVAIKILNETTGPKANVEFMDEALIMASMDHPHLVRLLGVCLSPTIQLVTQLMPHGCLLEYVHEHKDNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLARLLEGDEKEYNADGGKMPIKWMALECIHYRKFTHQSDVWSYGVTIWELMTFGGKPYDGIPTREIPDLLEKGERLPQPPICTIDVYMVMVKCWMIDADSRPKFKELAAEFSRMARDPQRYLVIQGDDRMKLPSPNDSKFFQNLLDEEDLEDMMDAEEYLVPQAFNIPPPIYTSRARIDSNRSEIGHSPPPAYTPMSGNQFVYRDGGFAAEQGVSVPYRAPTSTIPEAPVAQGATAEIFDDSCCNGTLRKPVAPHVQEDSSTQRYSADPTVFAPERSPRGELDEEGYMTPMRDKPKQEYLNPVEENPFVSRRKNGDLQALDNPEYHNASNGPPKAEDEYVNEPLYLNTFANTLGKAEYLKNNILSMPEKAKKAFDNPDYWNHSLPPRSTLQHPDYLQEYSTKYFYKQNGRIRPIVAENPEYLSEFSLKPGTVLPPPPYRHRNTVV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
138	N-linked_Glycosylation	LQELGLKNLTEILNG CHHHCCCCHHHHHCC	58.18	16203964
157	Phosphorylation	DQNKFLCYADTIHWQ CCCCEEEEECEECHH	15.06	18452278
173	Phosphorylation	IVRNPWPSNLTLVST HHCCCCCCCEEEEEE	40.37	18452278
174	N-linked_Glycosylation	VRNPWPSNLTLVSTN HCCCCCCCEEEEEEC	32.72	16203964
181	N-linked_Glycosylation	NLTLVSTNGSSGCGR CEEEEEECCCCCCCC	40.62	UniProtKB CARBOHYD
183	Phosphorylation	TLVSTNGSSGCGRCH EEEEECCCCCCCCCC	26.15	18452278
253	N-linked_Glycosylation	CFACMNFNDSGACVT CEEECCCCCCCCEEE	37.22	16203964
358	N-linked_Glycosylation	SNIDKFINCTKINGN CCCHHHEEEEEECCE	30.45	16203964
410	N-linked_Glycosylation	NIQSWPPNMTDFSVF CCCCCCCCCCCCCHH	41.74	16203964
443	Phosphorylation	ILKQQGITSLQFQSL HHHHCCCCEEEECCC	30.15	24043423
444	Phosphorylation	LKQQGITSLQFQSLK HHHCCCCEEEECCCC	20.46	24043423
449	Phosphorylation	ITSLQFQSLKEISAG CCEEEECCCCEECCC	42.57	24719451
473	N-linked_Glycosylation	LCYYHTINWTTLFST EEEEEECCHHHHHCC	31.06	16203964
495	N-linked_Glycosylation	RDNRKAENCTAEGMV CCCCCCCCCCCCCCC	33.04	16203964
530	Ubiquitination	CRRFSRGRICIESCN CCCCCCCCEEEEECC	21.35	21890473
548	N-linked_Glycosylation	GEFREFENGSICVEC CCCEEECCCCEEEEE	55.63	UniProtKB CARBOHYD
553	Ubiquitination	FENGSICVECDPQCE ECCCCEEEEECCCCC	8.59	21890473
576	N-linked_Glycosylation	CHGPGPDNCTKCSHF ECCCCCCCCCCCCCC	38.19	16203964
602	Phosphorylation	DGLQGANSFIFKYAD CCCCCCCCEEEEECC	21.13	24719451
620	N-linked_Glycosylation	ECHPCHPNCTQGCNG CCCCCCCCCCCCCCC	20.15	UniProtKB CARBOHYD
666	Ubiquitination	GGLFILVIVGLTFAV HHHHHHHHHHHHHHH	1.50	21890473
699	Phosphorylation	TELVEPLTPSGTAPN HHEECCCCCCCCCCC	26.56	28355574
701	Phosphorylation	LVEPLTPSGTAPNQA EECCCCCCCCCCCHH	43.47	24076635
703	Phosphorylation	EPLTPSGTAPNQAQL CCCCCCCCCCCHHHH	43.19	25002506
712	Ubiquitination	PNQAQLRILKETELK CCHHHHHHHHHHCCC	9.78	21890473
712	Ubiquitination	PNQAQLRILKETELK CCHHHHHHHHHHCCC	9.78	21890473
712 (in isoform 2)	Ubiquitination	-	9.78	21890473
714	Ubiquitination	QAQLRILKETELKRV HHHHHHHHHHCCCEE	61.28	29967540
722	Ubiquitination	ETELKRVKVLGSGAF HHCCCEEEEECCCCC	35.46	21890473
722 (in isoform 1)	Ubiquitination	-	35.46	21890473
722 (in isoform 3)	Ubiquitination	-	35.46	21890473
726	Phosphorylation	KRVKVLGSGAFGTVY CEEEEECCCCCCCEE	23.84	21945579
731	Phosphorylation	LGSGAFGTVYKGIWV ECCCCCCCEECEEEE	17.76	21945579
733	Phosphorylation	SGAFGTVYKGIWVPE CCCCCCEECEEEECC	11.88	16729043
735	Ubiquitination	AFGTVYKGIWVPEGE CCCCEECEEEECCCC	10.99	21890473
735	Ubiquitination	AFGTVYKGIWVPEGE CCCCEECEEEECCCC	10.99	21890473
735 (in isoform 2)	Ubiquitination	-	10.99	21890473
737	Ubiquitination	GTVYKGIWVPEGETV CCEECEEEECCCCEE	14.31	21890473
738	Ubiquitination	TVYKGIWVPEGETVK CEECEEEECCCCEEE	2.67	21890473
743	Ubiquitination	IWVPEGETVKIPVAI EEECCCCEEECEEEE	37.65	27667366
745	Ubiquitination	VPEGETVKIPVAIKI ECCCCEEECEEEEEE	49.03	22817900
745 (in isoform 1)	Ubiquitination	-	49.03	21890473
745 (in isoform 3)	Ubiquitination	-	49.03	21890473
748	Ubiquitination	GETVKIPVAIKILNE CCEEECEEEEEEHHC	11.08	21890473
760	Ubiquitination	LNETTGPKANVEFMD HHCCCCCCCCCEECC	54.67	21890473
761	Ubiquitination	NETTGPKANVEFMDE HCCCCCCCCCEECCH	28.56	21890473
763	Ubiquitination	TTGPKANVEFMDEAL CCCCCCCCEECCHHH	7.78	21890473
771	Ubiquitination	EFMDEALIMASMDHP EECCHHHHHHCCCCH	2.53	21890473
786	Ubiquitination	HLVRLLGVCLSPTIQ HHHHHHHHHHCHHHH	2.75	21890473
848	Ubiquitination	HRDLAARNVLVKSPN CHHHHHCCCEECCCC	27.09	21890473
848	Ubiquitination	HRDLAARNVLVKSPN CHHHHHCCCEECCCC	27.09	21890473
848 (in isoform 2)	Ubiquitination	-	27.09	21890473
852	Ubiquitination	AARNVLVKSPNHVKI HHCCCEECCCCCEEE	56.91	29901268
858	Ubiquitination	VKSPNHVKITDFGLA ECCCCCEEECCCHHH	32.13	21890473
858 (in isoform 1)	Ubiquitination	-	32.13	21890473
858 (in isoform 3)	Ubiquitination	-	32.13	21890473
873	Acetylation	RLLEGDEKEYNADGG HHHCCCCCEECCCCC	70.95	20167786
873	Ubiquitination	RLLEGDEKEYNADGG HHHCCCCCEECCCCC	70.95	21890473
874	Ubiquitination	LLEGDEKEYNADGGK HHCCCCCEECCCCCC	41.81	21890473
875	Phosphorylation	LEGDEKEYNADGGKM HCCCCCEECCCCCCC	27.07	18721752
881	Acetylation	EYNADGGKMPIKWMA EECCCCCCCCCEEHH	47.21	20167786
884	Ubiquitination	ADGGKMPIKWMALEC CCCCCCCCEEHHHHH	4.95	21890473
899	Ubiquitination	IHYRKFTHQSDVWSY HEECCCCCHHHCHHC	28.42	21890473
925	Ubiquitination	GKPYDGIPTREIPDL CCCCCCCCHHCCHHH	30.82	27667366
935	Ubiquitination	EIPDLLEKGERLPQP CCHHHHHCCCCCCCC	67.07	27667366
946	Phosphorylation	LPQPPICTIDVYMVM CCCCCCCEEEEEEEE	22.41	25262027
950	Phosphorylation	PICTIDVYMVMVKCW CCCEEEEEEEEEEHH	4.73	25262027
950	Ubiquitination	PICTIDVYMVMVKCW CCCEEEEEEEEEEHH	4.73	27667366
951	Ubiquitination	ICTIDVYMVMVKCWM CCEEEEEEEEEEHHE	1.25	27667366
961	Ubiquitination	VKCWMIDADSRPKFK EEHHEECCCCCHHHH	13.02	27667366
976	Ubiquitination	ELAAEFSRMARDPQR HHHHHHHHHCCCCCC	28.27	27667366
984	Phosphorylation	MARDPQRYLVIQGDD HCCCCCCEEEEECCC	10.48	16729043
997	Phosphorylation	DDRMKLPSPNDSKFF CCCCCCCCCCCHHHH	46.93	24076635
1001	Phosphorylation	KLPSPNDSKFFQNLL CCCCCCCHHHHHHHC	37.69	24173317
1022	Phosphorylation	DMMDAEEYLVPQAFN HHCCHHHHHCCHHHC	12.42	16729043
1033 (in isoform 4)	Phosphorylation	-	27.19	28348404
1035	Phosphorylation	FNIPPPIYTSRARID HCCCCCCCCCCEEEC	12.39	18721752
1043 (in isoform 3)	Phosphorylation	-	31.60	28348404
1056	Phosphorylation	GHSPPPAYTPMSGNQ CCCCCCCCCCCCCCE	19.70	16729043
1057	Phosphorylation	HSPPPAYTPMSGNQF CCCCCCCCCCCCCEE	18.02	22210691
1066	Phosphorylation	MSGNQFVYRDGGFAA CCCCEEEEECCCEEC	12.32	18721752
1073	Ubiquitination	YRDGGFAAEQGVSVP EECCCEECCCCCCCC	13.84	21890473
1077	Ubiquitination	GFAAEQGVSVPYRAP CEECCCCCCCCCCCC	5.35	22817900
1081	Phosphorylation	EQGVSVPYRAPTSTI CCCCCCCCCCCCCCC	19.77	18721752
1128	Phosphorylation	EDSSTQRYSADPTVF CCCCCCCCCCCCCEE	9.82	18721752
1140	Phosphorylation	TVFAPERSPRGELDE CEECCCCCCCCCCCC	19.79	17081983
1150	Phosphorylation	GELDEEGYMTPMRDK CCCCCCCCCCCCCCC	10.90	25884760
1162	Phosphorylation	RDKPKQEYLNPVEEN CCCCCHHHCCCCCCC	14.86	16729043
1188	Phosphorylation	QALDNPEYHNASNGP CCCCCCCCCCCCCCC	11.13	16729043
1202	Phosphorylation	PPKAEDEYVNEPLYL CCCCCHHCCCCCCHH	22.39	16729043
1208	Phosphorylation	EYVNEPLYLNTFANT HCCCCCCHHHHHHHH	14.50	16729043
1221	Phosphorylation	NTLGKAEYLKNNILS HHHCCHHHHHHCCCC	28.03	16729043
1239	Ubiquitination	KAKKAFDNPDYWNHS HHHHHHCCCCCCCCC	25.53	21890473
1242	Phosphorylation	KAFDNPDYWNHSLPP HHHCCCCCCCCCCCC	14.90	16729043
1243	Ubiquitination	AFDNPDYWNHSLPPR HHCCCCCCCCCCCCC	11.93	22817900
1246	Phosphorylation	NPDYWNHSLPPRSTL CCCCCCCCCCCCCCC	39.08	24719451
1249	Ubiquitination	YWNHSLPPRSTLQHP CCCCCCCCCCCCCCC	48.42	21890473
1249 (in isoform 3)	Ubiquitination	-	48.42	21890473
1253	Ubiquitination	SLPPRSTLQHPDYLQ CCCCCCCCCCCHHHH	4.67	22817900
1255	Ubiquitination	PPRSTLQHPDYLQEY CCCCCCCCCHHHHHH	21.95	21890473
1255	Ubiquitination	PPRSTLQHPDYLQEY CCCCCCCCCHHHHHH	21.95	21890473
1255 (in isoform 2)	Ubiquitination	-	21.95	21890473
1258	Phosphorylation	STLQHPDYLQEYSTK CCCCCCHHHHHHHHH	18.09	16729043
1259	Ubiquitination	TLQHPDYLQEYSTKY CCCCCHHHHHHHHHH	3.98	22817900
1262	Phosphorylation	HPDYLQEYSTKYFYK CCHHHHHHHHHHHHH	14.53	18721752
1265	Ubiquitination	YLQEYSTKYFYKQNG HHHHHHHHHHHHCCC	27.67	22817900
1265 (in isoform 1)	Ubiquitination	-	27.67	21890473
1266	Phosphorylation	LQEYSTKYFYKQNGR HHHHHHHHHHHCCCE	16.54	18721752
1268	Phosphorylation	EYSTKYFYKQNGRIR HHHHHHHHHCCCEEE	14.47	16729043
1269	Ubiquitination	YSTKYFYKQNGRIRP HHHHHHHHCCCEEEE	27.64	22817900
1275	Ubiquitination	YKQNGRIRPIVAENP HHCCCEEEEEEECCH	17.33	21890473
1279	Ubiquitination	GRIRPIVAENPEYLS CEEEEEEECCHHHHH	16.15	22817900
1280	Ubiquitination	RIRPIVAENPEYLSE EEEEEEECCHHHHHC	63.52	21890473
1281	Ubiquitination	IRPIVAENPEYLSEF EEEEEECCHHHHHCC	25.60	21890473
1284	Phosphorylation	IVAENPEYLSEFSLK EEECCHHHHHCCCCC	19.45	16729043
1284	Ubiquitination	IVAENPEYLSEFSLK EEECCHHHHHCCCCC	19.45	22817900
1285	Ubiquitination	VAENPEYLSEFSLKP EECCHHHHHCCCCCC	3.64	22817900
1289	Phosphorylation	PEYLSEFSLKPGTVL HHHHHCCCCCCCCCC	31.28	24719451
1290	Ubiquitination	EYLSEFSLKPGTVLP HHHHCCCCCCCCCCC	10.61	21890473
1291	Ubiquitination	YLSEFSLKPGTVLPP HHHCCCCCCCCCCCC	39.96	21890473
1294	Ubiquitination	EFSLKPGTVLPPPPY CCCCCCCCCCCCCCC	27.65	22817900
1295	Ubiquitination	FSLKPGTVLPPPPYR CCCCCCCCCCCCCCC	10.54	22817900
1301	Phosphorylation	TVLPPPPYRHRNTVV CCCCCCCCCCCCCCC	25.48	18721752
1306	Ubiquitination	PPYRHRNTVV----- CCCCCCCCCC-----	23.70	21890473
1310	Ubiquitination	HRNTVV--------- CCCCCC---------		22817900

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
699	T	Phosphorylation	Kinase	ERK1	P27361	PSP
875	Y	Phosphorylation	Kinase	ERBB4	Q15303	GPS
1035	Y	Phosphorylation	Kinase	ERBB4	Q15303	GPS
1051	S	Phosphorylation	Kinase	ERK1	P27361	PSP
1056	Y	Phosphorylation	Kinase	ERBB4	Q15303	GPS
1150	Y	Phosphorylation	Kinase	ERBB4	Q15303	GPS
1162	Y	Phosphorylation	Kinase	ERBB4	Q15303	GPS
1188	Y	Phosphorylation	Kinase	ERBB4	Q15303	GPS
1202	Y	Phosphorylation	Kinase	ERBB4	Q15303	GPS
1242	Y	Phosphorylation	Kinase	ERBB4	Q15303	GPS
1258	Y	Phosphorylation	Kinase	ERBB4	Q15303	GPS
1284	Y	Phosphorylation	Kinase	ERBB4	Q15303	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	NEDD4	P46934	PMID:19193720
-	K	Ubiquitination	E3 ubiquitin ligase	WWP1	Q9H0M0	PMID:19047365
-	K	Ubiquitination	E3 ubiquitin ligase	ITCH	Q96J02	PMID:18334649
-	K	Ubiquitination	E3 ubiquitin ligase	RNF41	Q9H4P4	PMID:15314180
-	K	Ubiquitination	E3 ubiquitin ligase	PRKN	O60260	PMID:15632191

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ERBB4_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 ERBB4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DLG3_HUMAN	DLG3	physical	10725395
SNTB2_HUMAN	SNTB2	physical	10725395
DLG4_HUMAN	DLG4	physical	10725395
YAP1_HUMAN	YAP1	physical	15023535
DLG2_HUMAN	DLG2	physical	10725395
STA5A_HUMAN	STAT5A	physical	15534001
SHC1_HUMAN	SHC1	physical	16729043
STA5A_HUMAN	STAT5A	physical	16729043
CRK_HUMAN	CRK	physical	16729043
GRB2_HUMAN	GRB2	physical	16729043
PTN11_HUMAN	PTPN11	physical	16729043
P85B_HUMAN	PIK3R2	physical	16729043
NCK1_HUMAN	NCK1	physical	16729043
DLG4_HUMAN	DLG4	physical	10839362
ERBB2_HUMAN	ERBB2	physical	10839362
DLG1_HUMAN	DLG1	physical	12175853
ITCH_HUMAN	ITCH	physical	18334649
NEDD4_HUMAN	NEDD4	physical	19193720
YAP1_HUMAN	YAP1	physical	12807903
TAB2_HUMAN	TAB2	physical	17018285
DLG4_HUMAN	DLG4	physical	17018285
NCOR1_HUMAN	NCOR1	physical	17018285
PIAS3_HUMAN	PIAS3	physical	22584572
PIAS4_HUMAN	PIAS4	physical	22584572
STA5A_HUMAN	STAT5A	physical	22584572
WWOX_HUMAN	WWOX	physical	22584572
WWP1_HUMAN	WWP1	physical	19047365
TIF1B_HUMAN	TRIM28	physical	20858735
MDM2_HUMAN	MDM2	physical	20858735
P53_HUMAN	TP53	physical	20858735
BYST_HUMAN	BYSL	physical	17360433
TROP_HUMAN	TRO	physical	17360433
ANS1B_HUMAN	ANKS1B	physical	16273093
ANS1A_HUMAN	ANKS1A	physical	16273093
GRB2_HUMAN	GRB2	physical	25140053
CBL_HUMAN	CBL	physical	25140053
ERBB4_HUMAN	ERBB4	physical	20943952
AP2C_HUMAN	TFAP2C	physical	20943952
WWOX_HUMAN	WWOX	physical	20943952
DLG4_HUMAN	DLG4	physical	16767099
PTN6_HUMAN	PTPN6	physical	28065597
PTN7_HUMAN	PTPN7	physical	28065597
PTN11_HUMAN	PTPN11	physical	28065597
PTN12_HUMAN	PTPN12	physical	28065597
PTPRR_HUMAN	PTPRR	physical	28065597
PTPRT_HUMAN	PTPRT	physical	28065597
PPM1A_HUMAN	PPM1A	physical	28065597
PPM1B_HUMAN	PPM1B	physical	28065597
PPM1F_HUMAN	PPM1F	physical	28065597
ILKAP_HUMAN	ILKAP	physical	28065597
TAB1_HUMAN	TAB1	physical	28065597
PTN20_HUMAN	PTPN20B	physical	28065597
DUS6_HUMAN	DUSP6	physical	28065597
DUS10_HUMAN	DUSP10	physical	28065597
DUS16_HUMAN	DUSP16	physical	28065597
DUS14_HUMAN	DUSP14	physical	28065597
DUS18_HUMAN	DUSP18	physical	28065597
DUS19_HUMAN	DUSP19	physical	28065597
DUS21_HUMAN	DUSP21	physical	28065597
STYX_HUMAN	STYX	physical	28065597
PTPC1_HUMAN	PTPDC1	physical	28065597
MTMR2_HUMAN	MTMR2	physical	28065597
MTMR6_HUMAN	MTMR6	physical	28065597
MTMR9_HUMAN	MTMR9	physical	28065597
MPIP3_HUMAN	CDC25C	physical	28065597
NRG2_HUMAN	NRG2	physical	15358134
ESR1_HUMAN	ESR1	physical	19439407
VANG1_HUMAN	VANGL1	physical	27648936
RNF41_HUMAN	RNF41	physical	27648936

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615515	Amyotrophic lateral sclerosis 19 (ALS19)
Kegg Drug
D03350	Canertinib dihydrochloride (USAN)
D09689	Varlitinib (USAN/INN)
D09690	Varlitinib tosylate (USAN)
D09883	Dacomitinib (USAN/INN)
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ERBB4_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"The extracellular region of ErbB4 adopts a tethered conformation inthe absence of ligand."; Bouyain S., Longo P.A., Li S., Ferguson K.M., Leahy D.J.; Proc. Natl. Acad. Sci. U.S.A. 102:15024-15029(2005). Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 26-641, DISULFIDE BONDS, ANDGLYCOSYLATION AT ASN-138; ASN-174; ASN-253; ASN-358; ASN-410; ASN-473;ASN-495 AND ASN-576.	16203964 [Abstract]
Phosphorylation
Reference	PubMed
"System-wide investigation of ErbB4 reveals 19 sites of Tyrphosphorylation that are unusually selective in their recruitmentproperties."; Kaushansky A., Gordus A., Budnik B.A., Lane W.S., Rush J.,MacBeath G.; Chem. Biol. 15:808-817(2008). Cited for: PHOSPHORYLATION AT TYR-875; TYR-1035; TYR-1056; TYR-1150; TYR-1162;TYR-1188; TYR-1202; TYR-1242; TYR-1258 AND TYR-1284, INTERACTION WITHPIK3R1 AND STAT1, AND MASS SPECTROMETRY.	18721752 [Abstract]
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