dbPTM

ERRFI_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ERRFI_HUMAN
UniProt AC	Q9UJM3
Protein Name	ERBB receptor feedback inhibitor 1
Gene Name	ERRFI1
Organism	Homo sapiens (Human).
Sequence Length	462
Subcellular Localization	Cytoplasm . Cell membrane Peripheral membrane protein Cytoplasmic side. Nucleus. Associated with the plasma membrane of basal skin keratinocytes. Translocates into the nucleus of differentiating suprabasal keratinocytes (By similarity)..
Protein Description	Negative regulator of EGFR signaling in skin morphogenesis. Acts as a negative regulator for several EGFR family members, including ERBB2, ERBB3 and ERBB4. Inhibits EGFR catalytic activity by interfering with its dimerization. Inhibits autophosphorylation of EGFR, ERBB2 and ERBB4. Important for normal keratinocyte proliferation and differentiation. Plays a role in modulating the response to steroid hormones in the uterus. Required for normal response to progesterone in the uterus and for fertility. Mediates epithelial estrogen responses in the uterus by regulating ESR1 levels and activation. Important for regulation of endometrium cell proliferation. Important for normal prenatal and perinatal lung development (By similarity)..
Protein Sequence	MSIAGVAAQEIRVPLKTGFLHNGRAMGNMRKTYWSSRSEFKNNFLNIDPITMAYSLNSSAQERLIPLGHASKSAPMNGHCFAENGPSQKSSLPPLLIPPSENLGPHEEDQVVCGFKKLTVNGVCASTPPLTPIKNSPSLFPCAPLCERGSRPLPPLPISEALSLDDTDCEVEFLTSSDTDFLLEDSTLSDFKYDVPGRRSFRGCGQINYAYFDTPAVSAADLSYVSDQNGGVPDPNPPPPQTHRRLRRSHSGPAGSFNKPAIRISNCCIHRASPNSDEDKPEVPPRVPIPPRPVKPDYRRWSAEVTSSTYSDEDRPPKVPPREPLSPSNSRTPSPKSLPSYLNGVMPPTQSFAPDPKYVSSKALQRQNSEGSASKVPCILPIIENGKKVSSTHYYLLPERPPYLDKYEKFFREAEETNGGAQIQPLPADCGISSATEKPDSKTKMDLGGHVKRKHLSYVVSP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSIAGVAAQ ------CCCCCCEEE	22.58	22814378
33	Phosphorylation	MGNMRKTYWSSRSEF CCCCHHHHCCCHHHH	13.31	-
54	Phosphorylation	IDPITMAYSLNSSAQ CCHHHEEEECCCCHH	11.67	25159151
71	Phosphorylation	LIPLGHASKSAPMNG EEECCCCCCCCCCCC	22.82	23312004
73	Phosphorylation	PLGHASKSAPMNGHC ECCCCCCCCCCCCCC	34.80	28985074
116	Acetylation	DQVVCGFKKLTVNGV CCEEECCEEEEECCE	31.96	24468295
119	Phosphorylation	VCGFKKLTVNGVCAS EECCEEEEECCEECC	22.32	23403867
126	Phosphorylation	TVNGVCASTPPLTPI EECCEECCCCCCCCC	36.00	27273156
127	Phosphorylation	VNGVCASTPPLTPIK ECCEECCCCCCCCCC	15.48	27273156
131	Phosphorylation	CASTPPLTPIKNSPS ECCCCCCCCCCCCCC	28.83	27273156
136	Phosphorylation	PLTPIKNSPSLFPCA CCCCCCCCCCCCCCH	15.74	21815630
138	Phosphorylation	TPIKNSPSLFPCAPL CCCCCCCCCCCCHHH	42.32	22199227
176	Phosphorylation	CEVEFLTSSDTDFLL CEEEEECCCCCCEEE	28.50	-
193	Phosphorylation	STLSDFKYDVPGRRS CCCCCCCCCCCCCCC	23.36	-
224	Phosphorylation	VSAADLSYVSDQNGG CCHHHHHHCCCCCCC	15.98	-
249	Phosphorylation	THRRLRRSHSGPAGS HHHHHHHHCCCCCCC	18.64	23927012
251	Phosphorylation	RRLRRSHSGPAGSFN HHHHHHCCCCCCCCC	47.95	20201521
256	Phosphorylation	SHSGPAGSFNKPAIR HCCCCCCCCCCCEEE	27.96	23927012
265	Phosphorylation	NKPAIRISNCCIHRA CCCEEEEECCEEEEC	17.61	28985074
273	Phosphorylation	NCCIHRASPNSDEDK CCEEEECCCCCCCCC	25.27	29255136
276	Phosphorylation	IHRASPNSDEDKPEV EEECCCCCCCCCCCC	45.84	29255136
302	Phosphorylation	KPDYRRWSAEVTSST CCCHHCCEEEECCCC	16.85	22617229
306	Phosphorylation	RRWSAEVTSSTYSDE HCCEEEECCCCCCCC	14.41	29978859
307	Phosphorylation	RWSAEVTSSTYSDED CCEEEECCCCCCCCC	26.34	29978859
308	Phosphorylation	WSAEVTSSTYSDEDR CEEEECCCCCCCCCC	23.23	29978859
309	Phosphorylation	SAEVTSSTYSDEDRP EEEECCCCCCCCCCC	27.15	29978859
310	Phosphorylation	AEVTSSTYSDEDRPP EEECCCCCCCCCCCC	18.97	23312004
311	Phosphorylation	EVTSSTYSDEDRPPK EECCCCCCCCCCCCC	34.31	23312004
326	Phosphorylation	VPPREPLSPSNSRTP CCCCCCCCCCCCCCC	36.68	29255136
328	Phosphorylation	PREPLSPSNSRTPSP CCCCCCCCCCCCCCC	44.02	29116813
330	Phosphorylation	EPLSPSNSRTPSPKS CCCCCCCCCCCCCCC	41.70	29116813
332	Phosphorylation	LSPSNSRTPSPKSLP CCCCCCCCCCCCCCH	28.12	29116813
334	Phosphorylation	PSNSRTPSPKSLPSY CCCCCCCCCCCCHHH	44.33	29116813
337	Phosphorylation	SRTPSPKSLPSYLNG CCCCCCCCCHHHHCC	49.23	28188228
340	Phosphorylation	PSPKSLPSYLNGVMP CCCCCCHHHHCCCCC	47.77	22199227
341	Phosphorylation	SPKSLPSYLNGVMPP CCCCCHHHHCCCCCC	11.40	27259358
358	Phosphorylation	SFAPDPKYVSSKALQ CCCCCHHHCCHHHHH	15.79	-
361	Phosphorylation	PDPKYVSSKALQRQN CCHHHCCHHHHHHCC	16.35	-
362	Ubiquitination	DPKYVSSKALQRQNS CHHHCCHHHHHHCCC	45.68	-
369	Phosphorylation	KALQRQNSEGSASKV HHHHHCCCCCCHHCC	34.69	23927012
372	Phosphorylation	QRQNSEGSASKVPCI HHCCCCCCHHCCCEE	25.89	22777824
374	Phosphorylation	QNSEGSASKVPCILP CCCCCCHHCCCEEEE	35.56	22777824
390	Phosphorylation	IENGKKVSSTHYYLL EECCEEEEECEEEEC	38.10	28152594
391	Phosphorylation	ENGKKVSSTHYYLLP ECCEEEEECEEEECC	23.38	28152594
392	Phosphorylation	NGKKVSSTHYYLLPE CCEEEEECEEEECCC	13.34	28152594
394	Phosphorylation	KKVSSTHYYLLPERP EEEEECEEEECCCCC	8.90	27273156
395	Phosphorylation	KVSSTHYYLLPERPP EEEECEEEECCCCCC	8.31	25159151
403	Phosphorylation	LLPERPPYLDKYEKF ECCCCCCCHHHHHHH	30.16	27259358
407	Phosphorylation	RPPYLDKYEKFFREA CCCCHHHHHHHHHHH	24.82	27642862
457	Phosphorylation	HVKRKHLSYVVSP-- CEECEEEEEEECC--	18.66	28442448
458	Phosphorylation	VKRKHLSYVVSP--- EECEEEEEEECC---	15.95	25159151
461	Phosphorylation	KHLSYVVSP------ EEEEEEECC------	18.17	28355574

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
251	S	Phosphorylation	Kinase	CHEK1	O14757	GPS
302	S	Phosphorylation	Kinase	CHEK1	O14757	GPS
394	Y	Phosphorylation	Kinase	ABL	P00519	PSP
395	Y	Phosphorylation	Kinase	ABL	P00519	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	NEDD4	P46934	PMID:27557663

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EGFR_HUMAN	EGFR	physical	19815557
PGFRB_HUMAN	PDGFRB	physical	19815557
UFO_HUMAN	AXL	physical	19815557
ALK_HUMAN	ALK	physical	19815557
LTK_HUMAN	LTK	physical	19815557
GRB2_HUMAN	GRB2	physical	21988832
1433T_HUMAN	YWHAQ	physical	24189400
ACTA_HUMAN	ACTA2	physical	24189400
ACTB_HUMAN	ACTB	physical	24189400
ACTBL_HUMAN	ACTBL2	physical	24189400
ACTC_HUMAN	ACTC1	physical	24189400
ACTG_HUMAN	ACTG1	physical	24189400
ACTH_HUMAN	ACTG2	physical	24189400
ACTS_HUMAN	ACTA1	physical	24189400
EGFR_HUMAN	EGFR	physical	24189400
ERBB2_HUMAN	ERBB2	physical	24189400
ERRFI_HUMAN	ERRFI1	physical	24189400
GFAP_HUMAN	GFAP	physical	24189400
GRB2_HUMAN	GRB2	physical	24189400
HSP7C_HUMAN	HSPA8	physical	24189400
MASP1_HUMAN	MASP1	physical	24189400
POTEE_HUMAN	POTEE	physical	24189400
POTEF_HUMAN	POTEF	physical	24189400
RS27A_HUMAN	RPS27A	physical	24189400
SHC1_HUMAN	SHC1	physical	24189400
SHC2_HUMAN	SHC2	physical	24189400
TBA1A_HUMAN	TUBA1A	physical	24189400
TBA1B_HUMAN	TUBA1B	physical	24189400
TBA1C_HUMAN	TUBA1C	physical	24189400
UBS3B_HUMAN	UBASH3B	physical	24189400
1433E_HUMAN	YWHAE	physical	24189400
1433Z_HUMAN	YWHAZ	physical	24189400
ANXA2_HUMAN	ANXA2	physical	24189400
TBB5_HUMAN	TUBB	physical	24189400
TCPG_HUMAN	CCT3	physical	24189400
EGFR_HUMAN	EGFR	physical	26280531
GCP60_HUMAN	ACBD3	physical	20351267
AOXA_HUMAN	AOX1	physical	20351267
ARRD5_HUMAN	ARRDC5	physical	20351267
RUBCL_HUMAN	KIAA0226L	physical	20351267
CRHBP_HUMAN	CRHBP	physical	20351267
DCTN6_HUMAN	DCTN6	physical	20351267
FBLN3_HUMAN	EFEMP1	physical	20351267
MIP18_HUMAN	FAM96B	physical	20351267
GAS1_HUMAN	GAS1	physical	20351267
GNPI2_HUMAN	GNPDA2	physical	20351267
GRB2_HUMAN	GRB2	physical	20351267
TF2H2_HUMAN	GTF2H2	physical	20351267
HYDIN_HUMAN	HYDIN	physical	20351267
IL2RG_HUMAN	IL2RG	physical	20351267
CSN5_HUMAN	COPS5	physical	20351267
MFSD5_HUMAN	MFSD5	physical	20351267
MMP26_HUMAN	MMP26	physical	20351267
NEUR1_HUMAN	NEU1	physical	20351267
NPC2_HUMAN	NPC2	physical	20351267
OSTF1_HUMAN	OSTF1	physical	20351267
PAPS1_HUMAN	PAPSS1	physical	20351267
PCCA_HUMAN	PCCA	physical	20351267
PCNA_HUMAN	PCNA	physical	20351267
PDCD2_HUMAN	PDCD2	physical	20351267
PHIPL_HUMAN	PHYHIPL	physical	20351267
PKHA3_HUMAN	PLEKHA3	physical	20351267
PPIA_HUMAN	PPIA	physical	20351267
PSA7_HUMAN	PSMA7	physical	20351267
PSB6_HUMAN	PSMB6	physical	20351267
RAB18_HUMAN	RAB18	physical	20351267
SH3Y1_HUMAN	SH3YL1	physical	20351267
S7A13_HUMAN	SLC7A13	physical	20351267
STX8_HUMAN	STX8	physical	20351267
TAC2N_HUMAN	TC2N	physical	20351267
TIMP4_HUMAN	TIMP4	physical	20351267
TM2D3_HUMAN	TM2D3	physical	20351267
TM165_HUMAN	TMEM165	physical	20351267
TMM59_HUMAN	TMEM59	physical	20351267
WDR61_HUMAN	WDR61	physical	20351267
1433B_HUMAN	YWHAB	physical	20351267
ZPBP1_HUMAN	ZPBP	physical	20351267
NEDD4_HUMAN	NEDD4	physical	27557663

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 ERRFI_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251, AND MASSSPECTROMETRY.	19369195 [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-461, AND MASSSPECTROMETRY.	18691976 [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-461, AND MASSSPECTROMETRY.	18669648 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-394 AND TYR-395, ANDMASS SPECTROMETRY.	19534553 [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-394 AND TYR-395, ANDMASS SPECTROMETRY.	18083107 [Abstract]