dbPTM

NRG1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NRG1_HUMAN	Jmol._Canvas2D (Jmol) "myJmol"[x]
UniProt AC	Q02297
Protein Name	Pro-neuregulin-1, membrane-bound isoform
Gene Name	NRG1
Organism	Homo sapiens (Human).
Sequence Length	640
Subcellular Localization	Pro-neuregulin-1, membrane-bound isoform: Cell membrane Single-pass type I membrane protein. Does not seem to be active. Neuregulin-1: Secreted. Isoform 8: Nucleus. May be nuclear. Isoform 9: Secreted. Has a signal peptide. Isoform 10:
Protein Description	Direct ligand for ERBB3 and ERBB4 tyrosine kinase receptors. Concomitantly recruits ERBB1 and ERBB2 coreceptors, resulting in ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors. The multiple isoforms perform diverse functions such as inducing growth and differentiation of epithelial, glial, neuronal, and skeletal muscle cells; inducing expression of acetylcholine receptor in synaptic vesicles during the formation of the neuromuscular junction; stimulating lobuloalveolar budding and milk production in the mammary gland and inducing differentiation of mammary tumor cells; stimulating Schwann cell proliferation; implication in the development of the myocardium such as trabeculation of the developing heart. Isoform 10 may play a role in motor and sensory neuron development. Binds to ERBB4. [PubMed: 10867024]
Protein Sequence	MSERKEGRGKGKGKKKERGSGKKPESAAGSQSPALPPRLKEMKSQESAAGSKLVLRCETSSEYSSLRFKWFKNGNELNRKNKPQNIKIQKKPGKSELRINKASLADSGEYMCKVISKLGNDSASANITIVESNEIITGMPASTEGAYVSSESPIRISVSTEGANTSSSTSTSTTGTSHLVKCAEKEKTFCVNGGECFMVKDLSNPSRYLCKCQPGFTGARCTENVPMKVQNQEKAEELYQKRVLTITGICIALLVVGIMCVVAYCKTKKQRKKLHDRLRQSLRSERNNMMNIANGPHHPNPPPENVQLVNQYVSKNVISSEHIVEREAETSFSTSHYTSTAHHSTTVTQTPSHSWSNGHTESILSESHSVIVMSSVENSRHSSPTGGPRGRLNGTGGPRECNSFLRHARETPDSYRDSPHSERYVSAMTTPARMSPVDFHTPSSPKSPPSEMSPPVSSMTVSMPSMAVSPFMEEERPLLLVTPPRLREKKFDHHPQQFSSFHHNPAHDSNSLPASPLRIVEDEEYETTQEYEPAQEPVKKLANSRRAKRTKPNGHIANRLEVDSNTSSQSSNSESETEDERVGEDTPFLGIQNPLAASLEATPAFRLADSRTNPAGRFSTQEEIQARLSSVIANQDPIAV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Acetylation	ERKEGRGKGKGKKKE CCCCCCCCCCCCCCC	56.97	70789
11 (in isoform 11)	Phosphorylation	-	46.93	27174698
12	Acetylation	KEGRGKGKGKKKERG CCCCCCCCCCCCCCC	71.67	133343
12 (in isoform 11)	Phosphorylation	-	71.67	27174698
15	Acetylation	RGKGKGKKKERGSGK CCCCCCCCCCCCCCC	69.41	70797
16	Acetylation	GKGKGKKKERGSGKK CCCCCCCCCCCCCCC	57.01	70793
26	Phosphorylation	GSGKKPESAAGSQSP CCCCCCCCCCCCCCC	31.76	28176443
30	Phosphorylation	KPESAAGSQSPALPP CCCCCCCCCCCCCCH	23.82	28176443
32	Phosphorylation	ESAAGSQSPALPPRL CCCCCCCCCCCCHHH	17.53	28176443
43	Acetylation	PPRLKEMKSQESAAG CHHHHHHHCCCCCCC	50.51	20167786
120	N-linked_Glycosylation	KVISKLGNDSASANI HHHHHHCCCCCCCCE	50.96	UniProtKB CARBOHYD
126	N-linked_Glycosylation	GNDSASANITIVESN CCCCCCCCEEEEECC	29.46	UniProtKB CARBOHYD
149	Phosphorylation	STEGAYVSSESPIRI CCCCEEECCCCCEEE	18.73	28348404
150	Phosphorylation	TEGAYVSSESPIRIS CCCEEECCCCCEEEE	31.86	28348404
152	Phosphorylation	GAYVSSESPIRISVS CEEECCCCCEEEEEE	27.81	28348404
157	O-linked_Glycosylation	SESPIRISVSTEGAN CCCCEEEEEECCCCC	10.52	30620550
164	N-linked_Glycosylation	SVSTEGANTSSSTST EEECCCCCCCCCCCC	51.88	UniProtKB CARBOHYD
169	Phosphorylation	GANTSSSTSTSTTGT CCCCCCCCCCCCCCC	37.66	-
170	Phosphorylation	ANTSSSTSTSTTGTS CCCCCCCCCCCCCCC	23.47	-
177	Phosphorylation	STSTTGTSHLVKCAE CCCCCCCCHHEEECC	19.03	-
203 (in isoform 9)	Phosphorylation	-	57.75	-
232 (in isoform 9)	Phosphorylation	-	36.15	22210691
281	Phosphorylation	LHDRLRQSLRSERNN HHHHHHHHHHHHHHC	21.22	29496963
284	Phosphorylation	RLRQSLRSERNNMMN HHHHHHHHHHHCCCC	46.32	29449344
319	Phosphorylation	YVSKNVISSEHIVER HHHCCCCCCCHHHHH	25.95	28348404
320	Phosphorylation	VSKNVISSEHIVERE HHCCCCCCCHHHHHH	23.28	28348404
382	Phosphorylation	SVENSRHSSPTGGPR CCCCCCCCCCCCCCC	36.58	24706070
383	Phosphorylation	VENSRHSSPTGGPRG CCCCCCCCCCCCCCC	21.98	28102081
385	Phosphorylation	NSRHSSPTGGPRGRL CCCCCCCCCCCCCCC	57.63	28102081
395	Phosphorylation	PRGRLNGTGGPRECN CCCCCCCCCCCHHHH	37.58	-
403	Phosphorylation	GGPRECNSFLRHARE CCCHHHHHHHHHHHC	37.00	22617229
414	Phosphorylation	HARETPDSYRDSPHS HHHCCCCHHCCCCCC	24.22	-
415	Phosphorylation	ARETPDSYRDSPHSE HHCCCCHHCCCCCCH	26.31	-
418	Phosphorylation	TPDSYRDSPHSERYV CCCHHCCCCCCHHHH	18.60	28348404
424	Phosphorylation	DSPHSERYVSAMTTP CCCCCHHHHHHCCCC	8.49	23090842
426	Phosphorylation	PHSERYVSAMTTPAR CCCHHHHHHCCCCCC	11.91	27422710
429	Phosphorylation	ERYVSAMTTPARMSP HHHHHHCCCCCCCCC	29.37	27422710
430	Phosphorylation	RYVSAMTTPARMSPV HHHHHCCCCCCCCCC	11.23	23090842
435	Phosphorylation	MTTPARMSPVDFHTP CCCCCCCCCCCCCCC	19.07	30266825
441	Phosphorylation	MSPVDFHTPSSPKSP CCCCCCCCCCCCCCC	25.51	30266825
443	Phosphorylation	PVDFHTPSSPKSPPS CCCCCCCCCCCCCCH	61.50	23090842
444	Phosphorylation	VDFHTPSSPKSPPSE CCCCCCCCCCCCCHH	37.23	27422710
452 (in isoform 3)	Phosphorylation	-	9.52	28348404
453 (in isoform 3)	Phosphorylation	-	23.23	28348404
454 (in isoform 3)	Phosphorylation	-	31.81	28348404
482	Phosphorylation	ERPLLLVTPPRLREK CCCEEEECCCCCCCC	27.78	28348404
511	Phosphorylation	NPAHDSNSLPASPLR CCCCCCCCCCCCCCE	39.42	27422710
525	Phosphorylation	RIVEDEEYETTQEYE EEECCCCCCCCCCCC	19.27	-
528	Phosphorylation	EDEEYETTQEYEPAQ CCCCCCCCCCCCCCH	13.89	18077418
531	Phosphorylation	EYETTQEYEPAQEPV CCCCCCCCCCCHHHH	19.86	-
551	Acetylation	SRRAKRTKPNGHIAN CCCHHCCCCCCCCCC	40.28	7711269
619	Phosphorylation	TNPAGRFSTQEEIQA CCCCCCCCCHHHHHH	28.02	27422710

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 NRG1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NRG1_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 NRG1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ERBB3_HUMAN	ERBB3	physical	11555649
ERBB2_HUMAN	ERBB2	physical	7592681
ERBB3_HUMAN	ERBB3	physical	7592681
ERBB3_HUMAN	ERBB3	physical	9168115
ERBB4_HUMAN	ERBB4	physical	9168115
MBOA7_HUMAN	MBOAT7	physical	26186194
LSR_HUMAN	LSR	physical	26186194
PGAP1_HUMAN	PGAP1	physical	26186194
K2013_HUMAN	KIAA2013	physical	26186194
SRBP2_HUMAN	SREBF2	physical	26186194
MAN1_HUMAN	LEMD3	physical	26186194
TMTC3_HUMAN	TMTC3	physical	26186194
TMTC4_HUMAN	TMTC4	physical	26186194
PMGT2_HUMAN	POMGNT2	physical	26186194
S38AA_HUMAN	SLC38A10	physical	26186194
ATP7B_HUMAN	ATP7B	physical	26186194
S35B2_HUMAN	SLC35B2	physical	26186194
NDUA3_HUMAN	NDUFA3	physical	26186194
ZDH17_HUMAN	ZDHHC17	physical	26186194
TM39B_HUMAN	TMEM39B	physical	26186194
DAAF5_HUMAN	DNAAF5	physical	26186194
B3GN2_HUMAN	B3GNT2	physical	26186194
RHBT3_HUMAN	RHOBTB3	physical	26186194
CISD2_HUMAN	CISD2	physical	26186194
POMT1_HUMAN	POMT1	physical	26186194
SPTC2_HUMAN	SPTLC2	physical	26186194
GDC_HUMAN	SLC25A16	physical	26186194
RDH11_HUMAN	RDH11	physical	26186194
MGAT1_HUMAN	MGAT1	physical	26186194
HMOX1_HUMAN	HMOX1	physical	26186194
F234B_HUMAN	KIAA1467	physical	26186194
EXTL3_HUMAN	EXTL3	physical	26186194
SCMC3_HUMAN	SLC25A23	physical	26186194
NETO2_HUMAN	NETO2	physical	26186194
AGRL1_HUMAN	LPHN1	physical	26186194
CNTP3_HUMAN	CNTNAP3	physical	26186194
DPB1_HUMAN	HLA-DPB1	physical	26186194
QCR8_HUMAN	UQCRQ	physical	26186194
GLMN_HUMAN	GLMN	physical	26186194
DEGS1_HUMAN	DEGS1	physical	26186194
CSCL2_HUMAN	TMEM63B	physical	26186194
ABCBA_HUMAN	ABCB10	physical	26186194
LARG2_HUMAN	GYLTL1B	physical	26186194
B3GL2_HUMAN	B3GALNT2	physical	26186194
TM181_HUMAN	TMEM181	physical	26186194
INT7_HUMAN	INTS7	physical	26186194
MYO19_HUMAN	MYO19	physical	26186194
GLT11_HUMAN	GALNT11	physical	26186194
C1GLC_HUMAN	C1GALT1C1	physical	26186194
S22AI_HUMAN	SLC22A18	physical	26186194
NEK4_HUMAN	NEK4	physical	26186194
ABCA3_HUMAN	ABCA3	physical	26186194
TM164_HUMAN	TMEM164	physical	26186194
MTCH1_HUMAN	MTCH1	physical	26186194
OPA3_HUMAN	OPA3	physical	26186194
H6ST1_HUMAN	HS6ST1	physical	26186194
SFXN3_HUMAN	SFXN3	physical	26186194
TM2D3_HUMAN	TM2D3	physical	26186194
DSE_HUMAN	DSE	physical	26186194
TM205_HUMAN	TMEM205	physical	26186194
GOLI_HUMAN	RNF130	physical	26186194
PIGU_HUMAN	PIGU	physical	26186194
RHBT3_HUMAN	RHOBTB3	physical	28514442
TM39B_HUMAN	TMEM39B	physical	28514442
SFXN3_HUMAN	SFXN3	physical	28514442
SCMC3_HUMAN	SLC25A23	physical	28514442
GDC_HUMAN	SLC25A16	physical	28514442
POMT1_HUMAN	POMT1	physical	28514442
CSCL2_HUMAN	TMEM63B	physical	28514442
B3GN2_HUMAN	B3GNT2	physical	28514442
AGRL1_HUMAN	LPHN1	physical	28514442
H6ST1_HUMAN	HS6ST1	physical	28514442
GLMN_HUMAN	GLMN	physical	28514442
TMTC4_HUMAN	TMTC4	physical	28514442
LARG2_HUMAN	GYLTL1B	physical	28514442
CISD2_HUMAN	CISD2	physical	28514442
TM2D3_HUMAN	TM2D3	physical	28514442
ATP7B_HUMAN	ATP7B	physical	28514442
S22AI_HUMAN	SLC22A18	physical	28514442
S35B2_HUMAN	SLC35B2	physical	28514442
LSR_HUMAN	LSR	physical	28514442
INT7_HUMAN	INTS7	physical	28514442
CNTP3_HUMAN	CNTNAP3	physical	28514442
TM164_HUMAN	TMEM164	physical	28514442
SRBP2_HUMAN	SREBF2	physical	28514442
PGAP1_HUMAN	PGAP1	physical	28514442
MBOA7_HUMAN	MBOAT7	physical	28514442
MAN1_HUMAN	LEMD3	physical	28514442
DPB1_HUMAN	HLA-DPB1	physical	28514442
LGR4_HUMAN	LGR4	physical	28514442
ZDH17_HUMAN	ZDHHC17	physical	28514442
GLT11_HUMAN	GALNT11	physical	28514442
DAAF5_HUMAN	DNAAF5	physical	28514442
TBB3_HUMAN	TUBB3	physical	28514442
DSE_HUMAN	DSE	physical	28514442
ERBB4_MOUSE	Erbb4	physical	17562386

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 NRG1_HUMAN

Related Literatures of Post-Translational Modification