dbPTM

ERBB2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ERBB2_HUMAN
UniProt AC	P04626
Protein Name	Receptor tyrosine-protein kinase erbB-2
Gene Name	ERBB2
Organism	Homo sapiens (Human).
Sequence Length	1255
Subcellular Localization	Isoform 1: Cell membrane Single-pass type I membrane protein. Cytoplasm, perinuclear region. Nucleus. Translocation to the nucleus requires endocytosis, probably endosomal sorting and is mediated by importin beta-1/KPNB1. Isoform 2: Cytoplasm. Nucl
Protein Description	Protein tyrosine kinase that is part of several cell surface receptor complexes, but that apparently needs a coreceptor for ligand binding. Essential component of a neuregulin-receptor complex, although neuregulins do not interact with it alone. GP30 is a potential ligand for this receptor. Regulates outgrowth and stabilization of peripheral microtubules (MTs). Upon ERBB2 activation, the MEMO1-RHOA-DIAPH1 signaling pathway elicits the phosphorylation and thus the inhibition of GSK3B at cell membrane. This prevents the phosphorylation of APC and CLASP2, allowing its association with the cell membrane. In turn, membrane-bound APC allows the localization of MACF1 to the cell membrane, which is required for microtubule capture and stabilization.; In the nucleus is involved in transcriptional regulation. Associates with the 5'-TCAAATTC-3' sequence in the PTGS2/COX-2 promoter and activates its transcription. Implicated in transcriptional activation of CDKN1A; the function involves STAT3 and SRC. Involved in the transcription of rRNA genes by RNA Pol I and enhances protein synthesis and cell growth..
Protein Sequence	MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNGDPLNNTTPVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQLALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQCAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTACPYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSANIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSLPDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHTVPWDQLFRNPHQALLHTANRPEDECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVARCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAVVGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKETELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLVDAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPSEGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPEYVNQPDVRPQPPSPREGPLPAARPAGATLERPKTLSPGKNGVVKDVFAFGGAVENPEYLTPQGGAAPQPHPPPAFSPAFDNLYYWDQDPPERGAPPSTFKGTPTAENPEYLGLDVPV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
15 (in isoform 3)	Phosphorylation	-	8.12	29116813
68	N-linked_Glycosylation	ELTYLPTNASLSFLQ EEEEECCCCCCHHHH	26.12	20696930
124	N-linked_Glycosylation	LDNGDPLNNTTPVTG ECCCCCCCCCCCCCC	49.54	UniProtKB CARBOHYD
126 (in isoform 2)	Ubiquitination	-	31.25	-
127	O-linked_Glycosylation	GDPLNNTTPVTGASP CCCCCCCCCCCCCCC	20.20	OGP
137 (in isoform 2)	Ubiquitination	-	4.82	-
150	Ubiquitination	RSLTEILKGGVLIQR HHHHHHHHCCEEEEC	60.32	21906983
175	Methylation	LWKDIFHKNNQLALT EHHHHHHHCCEEEEE	47.01	412433599
175	Ubiquitination	LWKDIFHKNNQLALT EHHHHHHHCCEEEEE	47.01	21890473
182	Phosphorylation	KNNQLALTLIDTNRS HCCEEEEEEEECCCC	18.96	23403867
187	N-linked_Glycosylation	ALTLIDTNRSRACHP EEEEEECCCCCCCCC	35.86	UniProtKB CARBOHYD
196	Phosphorylation	SRACHPCSPMCKGSR CCCCCCCCCCCCCCC	21.81	27251275
259	N-linked_Glycosylation	CLACLHFNHSGICEL CEEECCCCCCCCEEE	20.05	15093539
530	N-linked_Glycosylation	PGPTQCVNCSQFLRG CCCCCCCCHHHHHCC	27.61	19299620
571	N-linked_Glycosylation	HPECQPQNGSVTCFG CCCCCCCCCCEEEEC	51.93	20696930
629	N-linked_Glycosylation	ACQPCPINCTHSCVD CCCCCCCCCCCCCEE	15.13	UniProtKB CARBOHYD
686	Phosphorylation	QQKIRKYTMRRLLQE HHHHHHHHHHHHHHH	13.77	8702975
694	Phosphorylation	MRRLLQETELVEPLT HHHHHHHHCCCCCCC	22.97	23403867
701	Phosphorylation	TELVEPLTPSGAMPN HCCCCCCCCCCCCCC	26.56	27273156
703	Phosphorylation	LVEPLTPSGAMPNQA CCCCCCCCCCCCCHH	33.67	28102081
716	Ubiquitination	QAQMRILKETELRKV HHHHHHHHHHHCCEE	61.28	-
724	Ubiquitination	ETELRKVKVLGSGAF HHHCCEEEEECCCCC	34.47	-
728	Phosphorylation	RKVKVLGSGAFGTVY CEEEEECCCCCCCEE	23.84	21945579
733	Phosphorylation	LGSGAFGTVYKGIWI ECCCCCCCEEEEEEC	17.76	21945579
735	Phosphorylation	SGAFGTVYKGIWIPD CCCCCCEEEEEECCC	11.88	16729043
736	Ubiquitination	GAFGTVYKGIWIPDG CCCCCEEEEEECCCC	39.31	21890473
736	Ubiquitination	GAFGTVYKGIWIPDG CCCCCEEEEEECCCC	39.31	21890473
747	Ubiquitination	IPDGENVKIPVAIKV CCCCCCEEEEEEHHH	53.53	21890473
747	Ubiquitination	IPDGENVKIPVAIKV CCCCCCEEEEEEHHH	53.53	21890473
753	Ubiquitination	VKIPVAIKVLRENTS EEEEEEHHHHHCCCC	26.02	21890473
753	Ubiquitination	VKIPVAIKVLRENTS EEEEEEHHHHHCCCC	26.02	21890473
759	Phosphorylation	IKVLRENTSPKANKE HHHHHCCCCCHHCHH	41.47	28102081
760	Phosphorylation	KVLRENTSPKANKEI HHHHCCCCCHHCHHH	35.66	28102081
772	Phosphorylation	KEILDEAYVMAGVGS HHHHHHHHHHHCCCC	6.68	28102081
779	Phosphorylation	YVMAGVGSPYVSRLL HHHHCCCCHHHHHHH	15.62	28102081
781	Phosphorylation	MAGVGSPYVSRLLGI HHCCCCHHHHHHHHH	16.86	28102081
783	Phosphorylation	GVGSPYVSRLLGICL CCCCHHHHHHHHHHH	16.03	28102081
819	Phosphorylation	ENRGRLGSQDLLNWC HHCCCCCHHHHHHHH	25.72	28102081
854	Ubiquitination	AARNVLVKSPNHVKI HHCCCEECCCCCEEE	56.91	-
860	Ubiquitination	VKSPNHVKITDFGLA ECCCCCEEECCCCEE	32.13	21890473
860	Ubiquitination	VKSPNHVKITDFGLA ECCCCCEEECCCCEE	32.13	21890473
875	Phosphorylation	RLLDIDETEYHADGG EECCCCCCEEECCCC	37.79	28152594
876	Phosphorylation	LLDIDETEYHADGGK ECCCCCCEEECCCCC	33.02	17016520
877	Phosphorylation	LDIDETEYHADGGKV CCCCCCEEECCCCCC	15.10	27273156
883	Ubiquitination	EYHADGGKVPIKWMA EEECCCCCCCCCHHH	50.82	-
887	Ubiquitination	DGGKVPIKWMALESI CCCCCCCCHHHHHHH	25.50	21890473
900	Phosphorylation	SILRRRFTHQSDVWS HHHHHCCCCHHHCHH	19.73	-
923	Phosphorylation	MTFGAKPYDGIPARE HHCCCCCCCCCCHHH	26.54	16729043
937	Ubiquitination	EIPDLLEKGERLPQP HCHHHHHCCCCCCCC	67.07	-
948	Phosphorylation	LPQPPICTIDVYMIM CCCCCCEEEEEEEEE	22.41	-
952	Phosphorylation	PICTIDVYMIMVKCW CCEEEEEEEEEHHHH	4.16	16729043
974	Phosphorylation	PRFRELVSEFSRMAR HHHHHHHHHHHHHCC	45.61	27251275
977	Phosphorylation	RELVSEFSRMARDPQ HHHHHHHHHHCCCCC	19.66	27251275
998	Phosphorylation	NEDLGPASPLDSTFY CCCCCCCCCCCCHHH	29.18	28355574
1002	Phosphorylation	GPASPLDSTFYRSLL CCCCCCCCHHHHHHC	28.26	26356563
1003	Phosphorylation	PASPLDSTFYRSLLE CCCCCCCHHHHHHCC	25.09	26356563
1004	Phosphorylation	ASPLDSTFYRSLLED CCCCCCHHHHHHCCC	5.74	17016520
1005	Phosphorylation	SPLDSTFYRSLLEDD CCCCCHHHHHHCCCC	10.20	16729043
1007	Phosphorylation	LDSTFYRSLLEDDDM CCCHHHHHHCCCCCC	26.40	26356563
1023	Phosphorylation	DLVDAEEYLVPQQGF CCCCHHHHCCCCCCC	12.42	16729043
1049	Phosphorylation	MVHHRHRSSSTRSGG CCEEECCCCCCCCCC	23.63	25219547
1050	Phosphorylation	VHHRHRSSSTRSGGG CEEECCCCCCCCCCC	35.37	21955146
1051	Phosphorylation	HHRHRSSSTRSGGGD EEECCCCCCCCCCCC	29.14	21955146
1052	Phosphorylation	HRHRSSSTRSGGGDL EECCCCCCCCCCCCC	30.70	25219547
1054	Phosphorylation	HRSSSTRSGGGDLTL CCCCCCCCCCCCCEE	41.71	19664994
1060	Phosphorylation	RSGGGDLTLGLEPSE CCCCCCCEECCCCCC	24.42	30266825
1066	Phosphorylation	LTLGLEPSEEEAPRS CEECCCCCCCCCCCC	48.54	30266825
1073	Phosphorylation	SEEEAPRSPLAPSEG CCCCCCCCCCCCCCC	24.17	30266825
1078	Phosphorylation	PRSPLAPSEGAGSDV CCCCCCCCCCCCCCC	42.95	30266825
1083	Phosphorylation	APSEGAGSDVFDGDL CCCCCCCCCCCCCCC	30.02	30266825
1100	Phosphorylation	GAAKGLQSLPTHDPS CCCCCHHHCCCCCCC	41.16	30243723
1103	Phosphorylation	KGLQSLPTHDPSPLQ CCHHHCCCCCCCCCH	44.17	30266825
1107	Phosphorylation	SLPTHDPSPLQRYSE HCCCCCCCCCHHCCC	44.28	30266825
1112	Phosphorylation	DPSPLQRYSEDPTVP CCCCCHHCCCCCCCC	11.94	20498373
1113	Phosphorylation	PSPLQRYSEDPTVPL CCCCHHCCCCCCCCC	37.40	20639409
1117	Phosphorylation	QRYSEDPTVPLPSET HHCCCCCCCCCCCCC	47.26	20639409
1122	Phosphorylation	DPTVPLPSETDGYVA CCCCCCCCCCCCCEE	61.89	26356563
1124	Phosphorylation	TVPLPSETDGYVAPL CCCCCCCCCCCEECC	38.78	26356563
1126	Phosphorylation	PLPSETDGYVAPLTC CCCCCCCCCEECCEE	26.66	17016520
1127	Phosphorylation	LPSETDGYVAPLTCS CCCCCCCCEECCEEC	9.03	27259358
1132	Phosphorylation	DGYVAPLTCSPQPEY CCCEECCEECCCCHH	15.18	26356563
1134	Phosphorylation	YVAPLTCSPQPEYVN CEECCEECCCCHHCC	22.72	26356563
1139	Phosphorylation	TCSPQPEYVNQPDVR EECCCCHHCCCCCCC	16.04	16729043
1151	Phosphorylation	DVRPQPPSPREGPLP CCCCCCCCCCCCCCC	43.18	27362937
1166	Phosphorylation	AARPAGATLERPKTL CCCCCCCCCCCCCCC	28.38	30266825
1172	Phosphorylation	ATLERPKTLSPGKNG CCCCCCCCCCCCCCC	34.84	26699800
1174	Phosphorylation	LERPKTLSPGKNGVV CCCCCCCCCCCCCCC	36.52	28188228
1196	Phosphorylation	GAVENPEYLTPQGGA CCCCCCCCCCCCCCC	19.68	16729043
1198	Phosphorylation	VENPEYLTPQGGAAP CCCCCCCCCCCCCCC	16.80	27251275
1214	Phosphorylation	PHPPPAFSPAFDNLY CCCCCCCCCCCCCCE	19.88	-
1221	Phosphorylation	SPAFDNLYYWDQDPP CCCCCCCEECCCCCC	14.57	15695410
1222	Phosphorylation	PAFDNLYYWDQDPPE CCCCCCEECCCCCCC	12.99	16729043
1235	Phosphorylation	PERGAPPSTFKGTPT CCCCCCCCCCCCCCC	45.47	26356563
1236	Phosphorylation	ERGAPPSTFKGTPTA CCCCCCCCCCCCCCC	34.83	26356563
1240	Phosphorylation	PPSTFKGTPTAENPE CCCCCCCCCCCCCCC	20.32	26356563
1242	Phosphorylation	STFKGTPTAENPEYL CCCCCCCCCCCCCCC	46.58	26356563
1247	Phosphorylation	TPTAENPEYLGLDVP CCCCCCCCCCCCCCC	66.04	17016520
1248	Phosphorylation	PTAENPEYLGLDVPV CCCCCCCCCCCCCCC	13.81	16794579
1248	Dephosphorylation	PTAENPEYLGLDVPV CCCCCCCCCCCCCCC	13.81	11067847

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
686	T	Phosphorylation	Kinase	PRKACA	P17612	GPS
686	T	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
686	T	Phosphorylation	Kinase	PKCA	P05696	PSP
686	T	Phosphorylation	Kinase	PRKCA	P17252	GPS
686	T	Phosphorylation	Kinase	PRKG2	Q13237	GPS
701	T	Phosphorylation	Kinase	MAPK1	P28482	GPS
701	T	Phosphorylation	Kinase	MAPK3	P27361	GPS
877	Y	Phosphorylation	Kinase	ERBB2	P04626	GPS
877	Y	Phosphorylation	Kinase	FYN	P06241	PSP
877	Y	Phosphorylation	Kinase	SRC	P12931	PSP
877	Y	Phosphorylation	Kinase	YES	P07947	PSP
900	T	Phosphorylation	Kinase	PRKAA1	Q13131	GPS
1023	Y	Phosphorylation	Kinase	ERBB2	P04626	GPS
1112	Y	Phosphorylation	Kinase	ERBB2	P04626	GPS
1139	Y	Phosphorylation	Kinase	ERBB2	P04626	PhosphoELM
1172	T	Phosphorylation	Kinase	KCC2A	Q9UQM7	PhosphoELM
1172	T	Phosphorylation	Kinase	CAMK2A	P11275	PSP
1196	Y	Phosphorylation	Kinase	ERBB2	P04626	PhosphoELM
1221	Y	Phosphorylation	Kinase	ERBB2	P04626	PhosphoELM
1222	Y	Phosphorylation	Kinase	ERBB2	P04626	PhosphoELM
1248	Y	Phosphorylation	Kinase	ERBB2	P04626	PhosphoELM
-	K	Ubiquitination	E3 ubiquitin ligase	STUB1	Q9UNE7	PMID:12239347
-	K	Ubiquitination	E3 ubiquitin ligase	CBL	P22681	PMID:10910043

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ERBB2_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 ERBB2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SHC1_HUMAN	SHC1	physical	16729043
SH3L1_HUMAN	SH3BGRL	physical	16729043
PTN11_HUMAN	PTPN11	physical	16729043
GRB2_HUMAN	GRB2	physical	16729043
CTNB1_HUMAN	CTNNB1	physical	11950845
CTNB1_HUMAN	CTNNB1	physical	11245482
ERBB2_HUMAN	ERBB2	physical	14576349
PICK1_HUMAN	PICK1	physical	11278603
ERBIN_HUMAN	ERBB2IP	physical	11278603
P85B_HUMAN	PIK3R2	physical	1334406
DLG4_HUMAN	DLG4	physical	10839362
ERRFI_MOUSE	Errfi1	physical	11003669
STAT3_HUMAN	STAT3	physical	11940572
JAK2_HUMAN	JAK2	physical	11940572
SHC1_HUMAN	SHC1	physical	9710588
GRB2_HUMAN	GRB2	physical	9710588
IL6RB_HUMAN	IL6ST	physical	11821958
ERBIN_HUMAN	ERBB2IP	physical	12379659
EGFR_HUMAN	EGFR	physical	19060928
ERBB2_HUMAN	ERBB2	physical	19060928
ERBB3_HUMAN	ERBB3	physical	19060928
HS90A_HUMAN	HSP90AA1	physical	18655187
EGFR_HUMAN	EGFR	physical	17486068
CHIP_HUMAN	STUB1	physical	12239347
HS90A_HUMAN	HSP90AA1	physical	12006493
HSP74_HUMAN	HSPA4	physical	12006493
CUL5_HUMAN	CUL5	physical	19933325
CHIP_HUMAN	STUB1	physical	17239458
HS90A_HUMAN	HSP90AA1	physical	17239458
HSP74_HUMAN	HSPA4	physical	17239458
HSP74_HUMAN	HSPA4	physical	21503962
HS90A_HUMAN	HSP90AA1	physical	21503962
CHIP_HUMAN	STUB1	physical	12574167
H2AY_HUMAN	H2AFY	physical	22589551
P85A_HUMAN	PIK3R1	physical	9756944
PTN11_HUMAN	PTPN11	physical	9756944
SHC1_HUMAN	SHC1	physical	9756944
GRB2_HUMAN	GRB2	physical	9756944
ERBB2_HUMAN	ERBB2	physical	19077306
PIN1_HUMAN	PIN1	physical	19077306
ERBB3_HUMAN	ERBB3	physical	15504738
PTK6_HUMAN	PTK6	physical	18719096
ACTB_HUMAN	ACTB	physical	21555369
RPA2_HUMAN	POLR1B	physical	21555369
IMB1_HUMAN	KPNB1	physical	16314522
XPO1_HUMAN	XPO1	physical	16314522
CLH1_HUMAN	CLTC	physical	16314522
AP2B1_HUMAN	AP2B1	physical	16314522
EEA1_HUMAN	EEA1	physical	16314522
FGR_HUMAN	FGR	physical	16273093
CHIN_HUMAN	CHN1	physical	16273093
FER_HUMAN	FER	physical	16273093
PLCG2_HUMAN	PLCG2	physical	16273093
PLCG1_HUMAN	PLCG1	physical	16273093
RASA1_HUMAN	RASA1	physical	16273093
JAK1_HUMAN	JAK1	physical	16273093
P85A_HUMAN	PIK3R1	physical	16273093
SHC1_HUMAN	SHC1	physical	16273093
IRS1_HUMAN	IRS1	physical	16273093
STAT3_HUMAN	STAT3	physical	16273093
STAT1_HUMAN	STAT1	physical	16273093
MATK_HUMAN	MATK	physical	16273093
TEC_HUMAN	TEC	physical	16273093
TXK_HUMAN	TXK	physical	16273093
ABL2_HUMAN	ABL2	physical	16273093
KSYK_HUMAN	SYK	physical	16273093
CRK_HUMAN	CRK	physical	16273093
CRKL_HUMAN	CRKL	physical	16273093
BLK_HUMAN	BLK	physical	16273093
BMX_HUMAN	BMX	physical	16273093
VAV2_HUMAN	VAV2	physical	16273093
GRB2_HUMAN	GRB2	physical	16273093
3BP2_HUMAN	SH3BP2	physical	16273093
SHC2_HUMAN	SHC2	physical	16273093
PTN11_HUMAN	PTPN11	physical	16273093
ITK_HUMAN	ITK	physical	16273093
SLAP1_HUMAN	SLA	physical	16273093
JIP2_HUMAN	MAPK8IP2	physical	16273093
RIN1_HUMAN	RIN1	physical	16273093
GRB7_HUMAN	GRB7	physical	16273093
BCAR3_HUMAN	BCAR3	physical	16273093
TNS2_HUMAN	TENC1	physical	16273093
TENS3_HUMAN	TNS3	physical	16273093
DOK6_HUMAN	DOK6	physical	16273093
SH2D5_HUMAN	SH2D5	physical	16273093
SPT6H_HUMAN	SUPT6H	physical	16273093
ANS1B_HUMAN	ANKS1B	physical	16273093
CLNK_HUMAN	CLNK	physical	16273093
DOK4_HUMAN	DOK4	physical	16273093
BLNK_HUMAN	BLNK	physical	16273093
RIN2_HUMAN	RIN2	physical	16273093
SHC3_HUMAN	SHC3	physical	16273093
P55G_HUMAN	PIK3R3	physical	16273093
ANS1A_HUMAN	ANKS1A	physical	16273093
VAV_HUMAN	VAV1	physical	16273093
DOK1_HUMAN	DOK1	physical	16273093
SH23A_HUMAN	SH2D3A	physical	16273093
SLAP2_HUMAN	SLA2	physical	16273093
SH22A_HUMAN	SH2D2A	physical	16273093
CISH_HUMAN	CISH	physical	16273093
VAV3_HUMAN	VAV3	physical	16273093
JIP1_HUMAN	MAPK8IP1	physical	16273093
SH2B3_HUMAN	SH2B3	physical	16273093
TLN1_HUMAN	TLN1	physical	16273093
SRC_HUMAN	SRC	physical	21075308
CP17A_HUMAN	CYP17A1	physical	25640309
ERRFI_HUMAN	ERRFI1	physical	25640309
GLCE_HUMAN	GLCE	physical	25640309
I13R2_HUMAN	IL13RA2	physical	25640309
KLK5_HUMAN	KLK5	physical	25640309
LYPD3_HUMAN	LYPD3	physical	25640309
ARY2_HUMAN	NAT2	physical	25640309
PRD14_HUMAN	PRDM14	physical	25640309
HOP2_HUMAN	PSMC3IP	physical	25640309
RHBT2_HUMAN	RHOBTB2	physical	25640309
THRSP_HUMAN	THRSP	physical	25640309
ANXA6_HUMAN	ANXA6	physical	25640309
AGRB1_HUMAN	BAI1	physical	25640309
CLCN6_HUMAN	CLCN6	physical	25640309
GMPR2_HUMAN	GMPR2	physical	25640309
VIGLN_HUMAN	HDLBP	physical	25640309
SYIC_HUMAN	IARS	physical	25640309
MTCH1_HUMAN	MTCH1	physical	25640309
MUCL1_HUMAN	MUCL1	physical	25640309
PHF23_HUMAN	PHF23	physical	25640309
DPOD2_HUMAN	POLD2	physical	25640309
SAP_HUMAN	PSAP	physical	25640309
STK24_HUMAN	STK24	physical	25640309
TCAL2_HUMAN	TCEAL2	physical	25640309
VAS1_HUMAN	ATP6AP1	physical	25640309
TTC9B_HUMAN	TTC9B	physical	25640309
UTP18_HUMAN	UTP18	physical	25640309
AT1A1_HUMAN	ATP1A1	physical	26496610
EF1G_HUMAN	EEF1G	physical	26496610
TNPO1_HUMAN	TNPO1	physical	26496610
PYC_HUMAN	PC	physical	26496610
SURF4_HUMAN	SURF4	physical	26496610
TFR1_HUMAN	TFRC	physical	26496610
VAPB_HUMAN	VAPB	physical	26496610
PTSS1_HUMAN	PTDSS1	physical	26496610
HPSE_HUMAN	HPSE	physical	26496610
Z280C_HUMAN	ZNF280C	physical	26496610
GRDN_HUMAN	CCDC88A	physical	26496610
RPA2_HUMAN	POLR1B	physical	26496610
ZN622_HUMAN	ZNF622	physical	26496610
CHIP_HUMAN	STUB1	physical	26716506
CBL_HUMAN	CBL	physical	26716506
EGFR_HUMAN	EGFR	physical	20211985
HS90A_HUMAN	HSP90AA1	physical	16144943
EGFR_HUMAN	EGFR	physical	18803307
ITAV_HUMAN	ITGAV	physical	26222911
ITB1_HUMAN	ITGB1	physical	12600989
FAK1_HUMAN	PTK2	physical	12600989
TOP1_HUMAN	TOP1	genetic	28319113
RIR2_HUMAN	RRM2	genetic	28319113
SRC_HUMAN	SRC	genetic	28319113
CADH2_HUMAN	CDH2	physical	19033391
SHC1_HUMAN	SHC1	physical	28065597
PTN6_HUMAN	PTPN6	physical	28065597
PTPRR_HUMAN	PTPRR	physical	28065597
PTN11_HUMAN	PTPN11	physical	28065597
PTPRT_HUMAN	PTPRT	physical	28065597
PTPRU_HUMAN	PTPRU	physical	28065597
PTPRA_HUMAN	PTPRA	physical	28065597
MPZL2_HUMAN	MPZL2	physical	28065597
SSH1_HUMAN	SSH1	physical	28065597
PPM1A_HUMAN	PPM1A	physical	28065597
PPM1F_HUMAN	PPM1F	physical	28065597
ILKAP_HUMAN	ILKAP	physical	28065597
DUS14_HUMAN	DUSP14	physical	28065597
DUS18_HUMAN	DUSP18	physical	28065597
DUS19_HUMAN	DUSP19	physical	28065597
STYX_HUMAN	STYX	physical	28065597
GAB1_HUMAN	GAB1	physical	23612964

Drug and Disease Associations

Kegg Disease
H00018	Gastric cancer
H00019	Pancreatic cancer
H00022	Bladder cancer
H00026	Endometrial Cancer
H00027	Ovarian cancer
H00028	Choriocarcinoma
H00030	Cervical cancer
H00031	Breast cancer
H00046	Cholangiocarcinoma
OMIM Disease
137215	Hereditary diffuse gastric cancer (HDGC)
137800	Glioma (GLM)
167000	Ovarian cancer (OC)
211980	Lung cancer (LNCR)
613659	Gastric cancer (GASC)
Kegg Drug
D02714	Everolimus (JAN/USAN/INN); Afinitor (TN); Votubia (TN); Zortress (TN)
D03257	Trastuzumab (genetical recombination) (JAN); Trastuzumab (INN); Herceptin (TN)
D03350	Canertinib dihydrochloride (USAN)
D04024	Lapatinib tosilate hydrate (JAN); Lapatinib ditosylate (USAN); Tykerb (TN)
D04025	Mubritinib (USAN/INN)
D05446	Pertuzumab (genetical recombination) (JAN); Pertuzumab (USAN/INN); Perjeta (TN)
D08108	Lapatinib (INN)
D08950	Neratinib (INN/USAN)
D09689	Varlitinib (USAN/INN)
D09690	Varlitinib tosylate (USAN)
D09724	Afatinib (USAN/INN)
D09733	Afatinib maleate (JAN); Afatinib dimaleate (USAN)
D09883	Dacomitinib (USAN/INN)
D09980	Trastuzumab emtansine (genetical recombination) (JAN); Trastuzumab emtansine (USAN/INN); Kadcyla (TN
D10344	Nelipepimut-S (USAN); Neuvax
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ERBB2_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Structural basis for high-affinity HER2 receptor binding by anengineered protein."; Eigenbrot C., Ultsch M., Dubnovitsky A., Abrahmsen L., Hard T.; Proc. Natl. Acad. Sci. U.S.A. 107:15039-15044(2010). Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 23-646 IN COMPLEX WITHENGINEERED ANTIBODY ZHER2, DISULFIDE BONDS, AND GLYCOSYLATION ATASN-68; ASN-259 AND ASN-571.	20696930 [Abstract]
"Variants of the antibody herceptin that interact with HER2 and VEGFat the antigen binding site."; Bostrom J., Yu S.F., Kan D., Appleton B.A., Lee C.V., Billeci K.,Man W., Peale F., Ross S., Wiesmann C., Fuh G.; Science 323:1610-1614(2009). Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 23-646 IN COMPLEX WITH THEANTIBODY HERCEPTIN, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-259 ANDASN-530.	19299620 [Abstract]
"Insights into ErbB signaling from the structure of the ErbB2-pertuzumab complex."; Franklin M.C., Carey K.D., Vajdos F.F., Leahy D.J., de Vos A.M.,Sliwkowski M.X.; Cancer Cell 5:317-328(2004). Cited for: X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 23-646 IN COMPLEX WITH THEANTIBODY PERTUZUMAB, INTERACTION WITH ERBB3, MUTAGENESIS OF317-LEU-HIS-318, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-187;ASN-259 AND ASN-530.	15093539 [Abstract]
Phosphorylation
Reference	PubMed
"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-1054, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1054, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks."; Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.; Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1248, AND MASSSPECTROMETRY.	17389395 [Abstract]
"Plexin-B2, but not Plexin-B1, critically modulates neuronal migrationand patterning of the developing nervous system in vivo."; Deng S., Hirschberg A., Worzfeld T., Penachioni J.Y., Korostylev A.,Swiercz J.M., Vodrazka P., Mauti O., Stoeckli E.T., Tamagnone L.,Offermanns S., Kuner R.; J. Neurosci. 27:6333-6347(2007). Cited for: PHOSPHORYLATION AT TYR-1248.	17554007 [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-735, AND MASSSPECTROMETRY.	18083107 [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 TYR-1248, AND MASSSPECTROMETRY.	17081983 [Abstract]