dbPTM

N4BP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	N4BP1_HUMAN
UniProt AC	O75113
Protein Name	NEDD4-binding protein 1
Gene Name	N4BP1
Organism	Homo sapiens (Human).
Sequence Length	896
Subcellular Localization	Nucleus, nucleolus. Nucleus, PML body. Primarily localizes to the nucleolus. Also localizes to the PML nuclear bodies, when desumoylated (By similarity)..
Protein Description	Inhibitor of the E3 ubiquitin-protein ligase ITCH. Acts by interacting with the second WW domain of ITCH, leading to compete with ITCH's substrates and impairing ubiquitination of substrates (By similarity)..
Protein Sequence	MAARAVLDEFTAPAEKAELLEQSRGRIEGLFGVSLAVLGALGAEEPLPARIWLQLCGAQEAVHSAKEYIKGICEPELEERECYPKDMHCIFVGAESLFLKSLIQDTCADLCILDIGLLGIRGSAEAVVMARSHIQQFVKLFENKENLPSSQKESEVKREFKQFVEAHADNYTMDLLILPTSLKKELLTLTQGEENLFETGDDEVIEMRDSQQTEFTQNAATGLNISRDETVLQEEARNKAGTPVSELTKQMDTVLSSSPDVLFDPINGLTPDEEALSNERICQKRRFSDSEERHTKKQFSLENVQEGEILHDAKTLAGNVIADLSDSSADSENLSPDIKETTEEMEYNILVNFFKTMGYSQEIVEKVIKVYGPSTEPLLLLEEIEKENKRFQEDREFSAGTVYPETNKTKNKGVYSSTNELTTDSTPKKTQAHTQQNMVEKFSQLPFKVEAKPCTSNCRINTFRTVPIEQKHEVWGSNQNYICNTDPETDGLSPSVASPSPKEVNFVSRGASSHQPRVPLFPENGLHQQPEPLLPNNMKSACEKRLGCCSSPHSKPNCSTLSPPMPLPQLLPSVTDARSAGPSDHIDSSVTGVQRFRDTLKIPYKLELKNEPGRTDLKHIVIDGSNVAITHGLKKFFSCRGIAIAVEYFWKLGNRNITVFVPQWRTRRDPNVTEQHFLTQLQELGILSLTPARMVFGERIASHDDRFLLHLADKTGGIIVTNDNFREFVNESVSWREIITKRLLQYTFVGDIFMVPDDPLGRSGPRLEEFLQKEVCLRDMQPLLSALPNVGMFDPSFRVPGTQAASTSHQPPTRIQGAPSSHWLPQQPHFPLLPALPSLQQNLPMPAQRSSAETNELREALLKIFPDSEQRLKIDQILVAHPYMKDLNALSAMVLD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
16	Ubiquitination	EFTAPAEKAELLEQS HHCCHHHHHHHHHHH	49.63	29967540
70	Ubiquitination	HSAKEYIKGICEPEL HHHHHHHCCCCCHHH	41.12	29967540
129	Sulfoxidation	GSAEAVVMARSHIQQ CCHHHHHHHHHHHHH	1.74	21406390
144	Ubiquitination	FVKLFENKENLPSSQ HHHHHHCCCCCCCHH	40.56	27667366
149	Phosphorylation	ENKENLPSSQKESEV HCCCCCCCHHHHHHH	48.87	23312004
150	Phosphorylation	NKENLPSSQKESEVK CCCCCCCHHHHHHHH	43.25	17525332
152	Ubiquitination	ENLPSSQKESEVKRE CCCCCHHHHHHHHHH	66.22	33845483
172	O-linked_Glycosylation	EAHADNYTMDLLILP HHHHHCCCEEEEEEC	15.51	30059200
180	O-linked_Glycosylation	MDLLILPTSLKKELL EEEEEECCCHHHHHH	43.15	30059200
180	Phosphorylation	MDLLILPTSLKKELL EEEEEECCCHHHHHH	43.15	29396449
181	Phosphorylation	DLLILPTSLKKELLT EEEEECCCHHHHHHH	35.93	29396449
213	Phosphorylation	EMRDSQQTEFTQNAA EECCCCCCEEEHHHH	25.98	28122231
216	Phosphorylation	DSQQTEFTQNAATGL CCCCCEEEHHHHCCC	18.06	28450419
221	Phosphorylation	EFTQNAATGLNISRD EEEHHHHCCCCCCCC	39.53	30576142
226	Phosphorylation	AATGLNISRDETVLQ HHCCCCCCCCHHHHH	32.38	26055452
230	Phosphorylation	LNISRDETVLQEEAR CCCCCCHHHHHHHHH	30.70	30576142
239	Ubiquitination	LQEEARNKAGTPVSE HHHHHHHCCCCCHHH	42.51	27667366
242	Phosphorylation	EARNKAGTPVSELTK HHHHCCCCCHHHHHH	25.94	19664994
245	Phosphorylation	NKAGTPVSELTKQMD HCCCCCHHHHHHHHH	28.26	30266825
248	Phosphorylation	GTPVSELTKQMDTVL CCCHHHHHHHHHHHH	18.38	23927012
253	Phosphorylation	ELTKQMDTVLSSSPD HHHHHHHHHHHCCCC	20.29	28464451
256	Phosphorylation	KQMDTVLSSSPDVLF HHHHHHHHCCCCEEC	25.16	28464451
257	Phosphorylation	QMDTVLSSSPDVLFD HHHHHHHCCCCEECC	41.55	26657352
258	Phosphorylation	MDTVLSSSPDVLFDP HHHHHHCCCCEECCC	23.03	22115753
270	Phosphorylation	FDPINGLTPDEEALS CCCCCCCCCCHHHHC	30.05	25850435
288	Phosphorylation	ICQKRRFSDSEERHT HHHHCCCCCHHHHHH	38.11	23401153
290	Phosphorylation	QKRRFSDSEERHTKK HHCCCCCHHHHHHHH	39.91	29255136
295	Phosphorylation	SDSEERHTKKQFSLE CCHHHHHHHHCCCCC	46.27	23312004
297	Ubiquitination	SEERHTKKQFSLENV HHHHHHHHCCCCCCC	58.70	21890473
300	Phosphorylation	RHTKKQFSLENVQEG HHHHHCCCCCCCCCC	32.07	29255136
325	Phosphorylation	GNVIADLSDSSADSE CCHHHHCCCCCCCCC	35.67	25159151
327	Phosphorylation	VIADLSDSSADSENL HHHHCCCCCCCCCCC	24.85	30576142
328	Phosphorylation	IADLSDSSADSENLS HHHCCCCCCCCCCCC	40.88	27732954
331	Phosphorylation	LSDSSADSENLSPDI CCCCCCCCCCCCCCH	28.27	29116813
335	Phosphorylation	SADSENLSPDIKETT CCCCCCCCCCHHHHH	31.91	29507054
366	Ubiquitination	YSQEIVEKVIKVYGP CCHHHHHHHHHHHCC	38.06	23000965
369	Ubiquitination	EIVEKVIKVYGPSTE HHHHHHHHHHCCCCH	32.18	23000965
386	Ubiquitination	LLLEEIEKENKRFQE HHHHHHHHHCHHHHH	72.71	29967540
398	Phosphorylation	FQEDREFSAGTVYPE HHHCCCCCCCCCCCC	22.49	26657352
401	Phosphorylation	DREFSAGTVYPETNK CCCCCCCCCCCCCCC	19.31	28857561
403	Phosphorylation	EFSAGTVYPETNKTK CCCCCCCCCCCCCCC	8.66	25690035
406	Phosphorylation	AGTVYPETNKTKNKG CCCCCCCCCCCCCCC	37.19	-
408	Ubiquitination	TVYPETNKTKNKGVY CCCCCCCCCCCCCCC	69.19	33845483
412	Ubiquitination	ETNKTKNKGVYSSTN CCCCCCCCCCCCCCC	51.84	21906983
415	Phosphorylation	KTKNKGVYSSTNELT CCCCCCCCCCCCCCC	12.94	28796482
416	O-linked_Glycosylation	TKNKGVYSSTNELTT CCCCCCCCCCCCCCC	28.42	30059200
416	Phosphorylation	TKNKGVYSSTNELTT CCCCCCCCCCCCCCC	28.42	28152594
417	Phosphorylation	KNKGVYSSTNELTTD CCCCCCCCCCCCCCC	19.98	28152594
418	Phosphorylation	NKGVYSSTNELTTDS CCCCCCCCCCCCCCC	27.11	29396449
422	Phosphorylation	YSSTNELTTDSTPKK CCCCCCCCCCCCCCC	23.52	30576142
423	Phosphorylation	SSTNELTTDSTPKKT CCCCCCCCCCCCCCC	40.34	29978859
425	Phosphorylation	TNELTTDSTPKKTQA CCCCCCCCCCCCCHH	44.51	25159151
426	Phosphorylation	NELTTDSTPKKTQAH CCCCCCCCCCCCHHH	41.77	25159151
428	Ubiquitination	LTTDSTPKKTQAHTQ CCCCCCCCCCHHHHH	69.42	29967540
429	Ubiquitination	TTDSTPKKTQAHTQQ CCCCCCCCCHHHHHH	47.26	29967540
441	Ubiquitination	TQQNMVEKFSQLPFK HHHHHHHHHHCCCCE	38.62	21890473
448	Sumoylation	KFSQLPFKVEAKPCT HHHCCCCEEECCCCC	36.91	-
448	Sumoylation	KFSQLPFKVEAKPCT HHHCCCCEEECCCCC	36.91	-
448	Ubiquitination	KFSQLPFKVEAKPCT HHHCCCCEEECCCCC	36.91	29967540
452	Ubiquitination	LPFKVEAKPCTSNCR CCCEEECCCCCCCCE	27.41	29967540
471	Ubiquitination	RTVPIEQKHEVWGSN EEEECCCCCCCCCCC	29.01	29967540
477	Phosphorylation	QKHEVWGSNQNYICN CCCCCCCCCCCEECC	21.38	28111955
481	Phosphorylation	VWGSNQNYICNTDPE CCCCCCCEECCCCCC	9.33	27642862
485	Phosphorylation	NQNYICNTDPETDGL CCCEECCCCCCCCCC	48.82	28111955
489	Phosphorylation	ICNTDPETDGLSPSV ECCCCCCCCCCCCCC	40.53	29978859
493	Phosphorylation	DPETDGLSPSVASPS CCCCCCCCCCCCCCC	22.21	29978859
495	Phosphorylation	ETDGLSPSVASPSPK CCCCCCCCCCCCCHH	27.26	29978859
498	Phosphorylation	GLSPSVASPSPKEVN CCCCCCCCCCHHHCC	24.61	25159151
500	Phosphorylation	SPSVASPSPKEVNFV CCCCCCCCHHHCCEE	46.22	29978859
502	Ubiquitination	SVASPSPKEVNFVSR CCCCCCHHHCCEECC	77.84	29967540
508	Phosphorylation	PKEVNFVSRGASSHQ HHHCCEECCCCCCCC	22.36	24719451
509	Methylation	KEVNFVSRGASSHQP HHCCEECCCCCCCCC	39.12	81450715
517	Methylation	GASSHQPRVPLFPEN CCCCCCCCCCCCCCC	35.79	115484381
539	Ubiquitination	PLLPNNMKSACEKRL CCCCCCHHHHHHHHH	36.70	29967540
550	Phosphorylation	EKRLGCCSSPHSKPN HHHHCCCCCCCCCCC	51.48	28348404
551	Phosphorylation	KRLGCCSSPHSKPNC HHHCCCCCCCCCCCC	16.84	28348404
554	Phosphorylation	GCCSSPHSKPNCSTL CCCCCCCCCCCCCCC	53.87	21712546
559	Phosphorylation	PHSKPNCSTLSPPMP CCCCCCCCCCCCCCC	38.74	26074081
560	Phosphorylation	HSKPNCSTLSPPMPL CCCCCCCCCCCCCCH	33.19	26074081
562	Phosphorylation	KPNCSTLSPPMPLPQ CCCCCCCCCCCCHHH	27.35	27050516
573	Phosphorylation	PLPQLLPSVTDARSA CHHHHCCCCCCHHHC	37.30	26074081
575	Phosphorylation	PQLLPSVTDARSAGP HHHCCCCCCHHHCCC	28.42	26074081
579	Phosphorylation	PSVTDARSAGPSDHI CCCCCHHHCCCCCCC	39.02	22210691
583	Phosphorylation	DARSAGPSDHIDSSV CHHHCCCCCCCCCCC	40.69	22210691
589	Phosphorylation	PSDHIDSSVTGVQRF CCCCCCCCCCCHHHH	21.68	22210691
591	Phosphorylation	DHIDSSVTGVQRFRD CCCCCCCCCHHHHHH	33.32	22210691
601	Ubiquitination	QRFRDTLKIPYKLEL HHHHHHCCCCEEEEE	43.67	21906983
605	Ubiquitination	DTLKIPYKLELKNEP HHCCCCEEEEECCCC	30.08	27667366
609	Ubiquitination	IPYKLELKNEPGRTD CCEEEEECCCCCCCC	50.30	29967540
618	Ubiquitination	EPGRTDLKHIVIDGS CCCCCCCCEEEEECC	33.81	29967540
634	Ubiquitination	VAITHGLKKFFSCRG EEECCCHHHHHCCCH	52.72	29967540
666	Phosphorylation	VFVPQWRTRRDPNVT EEEECCCCCCCCCCC	27.39	24719451
734	Phosphorylation	EFVNESVSWREIITK HHHCCCCCHHHHHHH	29.69	-
773	Ubiquitination	RLEEFLQKEVCLRDM HHHHHHHHHHHHHHH	55.02	22505724
802	O-linked_Glycosylation	PSFRVPGTQAASTSH CCCCCCCCCCCCCCC	14.68	30059200
807	O-linked_Glycosylation	PGTQAASTSHQPPTR CCCCCCCCCCCCCCC	26.04	30059200
813	O-linked_Glycosylation	STSHQPPTRIQGAPS CCCCCCCCCCCCCCC	47.27	30059200
820	Phosphorylation	TRIQGAPSSHWLPQQ CCCCCCCCCCCCCCC	34.01	27251275
821	Phosphorylation	RIQGAPSSHWLPQQP CCCCCCCCCCCCCCC	20.02	27251275
838	Phosphorylation	PLLPALPSLQQNLPM CCCCCCHHHHHCCCC	39.39	27251275
863	Ubiquitination	ELREALLKIFPDSEQ HHHHHHHHHCCCHHH	43.05	-

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
-	K	Ubiquitination	E3 ubiquitin ligase	NEDD4	P46934	PMID:17114934

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of N4BP1_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 N4BP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of N4BP1_HUMAN !!

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 N4BP1_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 SER-258, AND MASSSPECTROMETRY.	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-226 AND SER-258, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150, AND MASSSPECTROMETRY.	17525332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-242, AND MASSSPECTROMETRY.	19413330 [Abstract]