dbPTM

NOSIP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NOSIP_HUMAN
UniProt AC	Q9Y314
Protein Name	Nitric oxide synthase-interacting protein
Gene Name	NOSIP
Organism	Homo sapiens (Human).
Sequence Length	301
Subcellular Localization	Cytoplasm . Nucleus . Translocates from nucleus to cytoplasm in the G2 phase of the cell cycle (PubMed:16135813).
Protein Description	E3 ubiquitin-protein ligase that is essential for proper development of the forebrain, the eye, and the face. Catalyzes monoubiquitination of serine/threonine-protein phosphatase 2A (PP2A) catalytic subunit PPP2CA/PPP2CB (By similarity). Negatively regulates nitric oxide production by inducing NOS1 and NOS3 translocation to actin cytoskeleton and inhibiting their enzymatic activity. [PubMed: 11149895]
Protein Sequence	MTRHGKNCTAGAVYTYHEKKKDTAASGYGTQNIRLSRDAVKDFDCCCLSLQPCHDPVVTPDGYLYEREAILEYILHQKKEIARQMKAYEKQRGTRREEQKELQRAASQDHVRGFLEKESAIVSRPLNPFTAKALSGTSPDDVQPGPSVGPPSKDKDKVLPSFWIPSLTPEAKATKLEKPSRTVTCPMSGKPLRMSDLTPVHFTPLDSSVDRVGLITRSERYVCAVTRDSLSNATPCAVLRPSGAVVTLECVEKLIRKDMVDPVTGDKLTDRDIIVLQRGGTGFAGSGVKLQAEKSRPVMQA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Ubiquitination	--MTRHGKNCTAGAV --CCCCCCCCCCCCE	42.60	-
6	Sumoylation	--MTRHGKNCTAGAV --CCCCCCCCCCCCE	42.60	-
6	Sumoylation	--MTRHGKNCTAGAV --CCCCCCCCCCCCE	42.60	-
8	S-nitrosylation	MTRHGKNCTAGAVYT CCCCCCCCCCCCEEE	2.92	22178444
9	Phosphorylation	TRHGKNCTAGAVYTY CCCCCCCCCCCEEEE	37.20	21945579
14	Phosphorylation	NCTAGAVYTYHEKKK CCCCCCEEEEECCCC	10.88	21945579
15	Phosphorylation	CTAGAVYTYHEKKKD CCCCCEEEEECCCCC	16.29	21945579
16	Phosphorylation	TAGAVYTYHEKKKDT CCCCEEEEECCCCCC	7.12	21945579
19	2-Hydroxyisobutyrylation	AVYTYHEKKKDTAAS CEEEEECCCCCCCCC	52.38	-
19	Acetylation	AVYTYHEKKKDTAAS CEEEEECCCCCCCCC	52.38	25953088
20	Ubiquitination	VYTYHEKKKDTAASG EEEEECCCCCCCCCC	53.55	-
21	Ubiquitination	YTYHEKKKDTAASGY EEEECCCCCCCCCCC	71.96	-
23	Phosphorylation	YHEKKKDTAASGYGT EECCCCCCCCCCCCC	32.76	29759185
26	Phosphorylation	KKKDTAASGYGTQNI CCCCCCCCCCCCCCE	30.04	28152594
28	Nitration	KDTAASGYGTQNIRL CCCCCCCCCCCCEEE	17.95	-
28	Phosphorylation	KDTAASGYGTQNIRL CCCCCCCCCCCCEEE	17.95	28152594
30	Phosphorylation	TAASGYGTQNIRLSR CCCCCCCCCCEEECC	15.23	17525332
36	Phosphorylation	GTQNIRLSRDAVKDF CCCCEEECCHHHCCC	20.47	25159151
41	Acetylation	RLSRDAVKDFDCCCL EECCHHHCCCCEEEE	55.16	26051181
41	Ubiquitination	RLSRDAVKDFDCCCL EECCHHHCCCCEEEE	55.16	-
73	Phosphorylation	EREAILEYILHQKKE EHHHHHHHHHHHHHH	12.82	27642862
78	Ubiquitination	LEYILHQKKEIARQM HHHHHHHHHHHHHHH	41.44	-
78	Acetylation	LEYILHQKKEIARQM HHHHHHHHHHHHHHH	41.44	25953088
79	Ubiquitination	EYILHQKKEIARQMK HHHHHHHHHHHHHHH	48.02	-
86	Ubiquitination	KEIARQMKAYEKQRG HHHHHHHHHHHHHHC	39.21	-
90	Ubiquitination	RQMKAYEKQRGTRRE HHHHHHHHHHCCCHH	32.40	-
94	Phosphorylation	AYEKQRGTRREEQKE HHHHHHCCCHHHHHH	28.83	-
100	Sumoylation	GTRREEQKELQRAAS CCCHHHHHHHHHHHH	64.77	-
100	Sumoylation	GTRREEQKELQRAAS CCCHHHHHHHHHHHH	64.77	-
100	Ubiquitination	GTRREEQKELQRAAS CCCHHHHHHHHHHHH	64.77	-
107	Phosphorylation	KELQRAASQDHVRGF HHHHHHHHHHHHHHH	34.85	25159151
112	Methylation	AASQDHVRGFLEKES HHHHHHHHHHHHHHH	27.08	115485425
117	Sumoylation	HVRGFLEKESAIVSR HHHHHHHHHHCEEEC	60.15	-
117	Sumoylation	HVRGFLEKESAIVSR HHHHHHHHHHCEEEC	60.15	-
117	Ubiquitination	HVRGFLEKESAIVSR HHHHHHHHHHCEEEC	60.15	-
132	Ubiquitination	PLNPFTAKALSGTSP CCCHHHHHHHCCCCC	46.96	-
135	Phosphorylation	PFTAKALSGTSPDDV HHHHHHHCCCCCCCC	44.90	30266825
137	Phosphorylation	TAKALSGTSPDDVQP HHHHHCCCCCCCCCC	33.44	30266825
138	Phosphorylation	AKALSGTSPDDVQPG HHHHCCCCCCCCCCC	29.83	25159151
147	Phosphorylation	DDVQPGPSVGPPSKD CCCCCCCCCCCCCCC	45.69	24732914
152	Phosphorylation	GPSVGPPSKDKDKVL CCCCCCCCCCCCCCC	57.53	25159151
153	Ubiquitination	PSVGPPSKDKDKVLP CCCCCCCCCCCCCCC	74.66	21890473
155	Ubiquitination	VGPPSKDKDKVLPSF CCCCCCCCCCCCCCC	64.28	-
157	Sumoylation	PPSKDKDKVLPSFWI CCCCCCCCCCCCCCC	51.95	-
157	Ubiquitination	PPSKDKDKVLPSFWI CCCCCCCCCCCCCCC	51.95	21890473
157	Sumoylation	PPSKDKDKVLPSFWI CCCCCCCCCCCCCCC	51.95	-
161	Phosphorylation	DKDKVLPSFWIPSLT CCCCCCCCCCCCCCC	29.11	23403867
166	Phosphorylation	LPSFWIPSLTPEAKA CCCCCCCCCCHHHHC	35.42	22115753
168	Phosphorylation	SFWIPSLTPEAKATK CCCCCCCCHHHHCCC	24.34	25159151
172	Sumoylation	PSLTPEAKATKLEKP CCCCHHHHCCCCCCC	55.73	-
172	Sumoylation	PSLTPEAKATKLEKP CCCCHHHHCCCCCCC	55.73	-
172	Ubiquitination	PSLTPEAKATKLEKP CCCCHHHHCCCCCCC	55.73	-
175	Sumoylation	TPEAKATKLEKPSRT CHHHHCCCCCCCCCE	60.55	-
175	Ubiquitination	TPEAKATKLEKPSRT CHHHHCCCCCCCCCE	60.55	-
175	Acetylation	TPEAKATKLEKPSRT CHHHHCCCCCCCCCE	60.55	25953088
175	Sumoylation	TPEAKATKLEKPSRT CHHHHCCCCCCCCCE	60.55	-
178	Sumoylation	AKATKLEKPSRTVTC HHCCCCCCCCCEEEC	59.74	-
178	Ubiquitination	AKATKLEKPSRTVTC HHCCCCCCCCCEEEC	59.74	-
178	Sumoylation	AKATKLEKPSRTVTC HHCCCCCCCCCEEEC	59.74	-
190	Sumoylation	VTCPMSGKPLRMSDL EECCCCCCCCCHHCC	33.31	-
190	Ubiquitination	VTCPMSGKPLRMSDL EECCCCCCCCCHHCC	33.31	-
190	Sumoylation	VTCPMSGKPLRMSDL EECCCCCCCCCHHCC	33.31	-
195	Phosphorylation	SGKPLRMSDLTPVHF CCCCCCHHCCCCCCC	24.04	29449344
198	Phosphorylation	PLRMSDLTPVHFTPL CCCHHCCCCCCCCCC	28.40	27050516
203	Phosphorylation	DLTPVHFTPLDSSVD CCCCCCCCCCCCCCC	14.20	28348404
207	Phosphorylation	VHFTPLDSSVDRVGL CCCCCCCCCCCEEEE	39.69	28555341
208	Phosphorylation	HFTPLDSSVDRVGLI CCCCCCCCCCEEEEE	27.92	28348404
216	Phosphorylation	VDRVGLITRSERYVC CCEEEEEECCCEEEE	32.93	-
218	Phosphorylation	RVGLITRSERYVCAV EEEEEECCCEEEEEE	20.13	-
253	Ubiquitination	VTLECVEKLIRKDMV EEHHHHHHHHHCCCC	28.90	-
253	Acetylation	VTLECVEKLIRKDMV EEHHHHHHHHHCCCC	28.90	26051181
257	Sumoylation	CVEKLIRKDMVDPVT HHHHHHHCCCCCCCC	43.09	-
257	Sumoylation	CVEKLIRKDMVDPVT HHHHHHHCCCCCCCC	43.09	-
267	Ubiquitination	VDPVTGDKLTDRDII CCCCCCCCCCCCCEE	55.41	-
278	Methylation	RDIIVLQRGGTGFAG CCEEEEECCCCCCCC	41.15	115485433
286	Phosphorylation	GGTGFAGSGVKLQAE CCCCCCCCCCEEEEE	36.66	25159151
289	Ubiquitination	GFAGSGVKLQAEKSR CCCCCCCEEEEECCC	38.11	-
289	Acetylation	GFAGSGVKLQAEKSR CCCCCCCEEEEECCC	38.11	25953088
289	Sumoylation	GFAGSGVKLQAEKSR CCCCCCCEEEEECCC	38.11	-
289	Sumoylation	GFAGSGVKLQAEKSR CCCCCCCEEEEECCC	38.11	-
294	Ubiquitination	GVKLQAEKSRPVMQA CCEEEEECCCCCCCC	55.57	-
294	Acetylation	GVKLQAEKSRPVMQA CCEEEEECCCCCCCC	55.57	23749302
294	Sumoylation	GVKLQAEKSRPVMQA CCEEEEECCCCCCCC	55.57	-
294	Sumoylation	GVKLQAEKSRPVMQA CCEEEEECCCCCCCC	55.57	-

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 NOSIP_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EPOR_HUMAN	EPOR	physical	12746455
NOS3_HUMAN	NOS3	physical	16135813
NOS1_RAT	Nos1	physical	15548660
NOS3_HUMAN	NOS3	physical	11149895
TNNC2_HUMAN	TNNC2	physical	26186194
HMCES_HUMAN	HMCES	physical	26344197
PP2AA_HUMAN	PPP2CA	physical	25546391
PP2AB_HUMAN	PPP2CB	physical	25546391
2AAA_HUMAN	PPP2R1A	physical	25546391
2ABA_HUMAN	PPP2R2A	physical	25546391
UB2D3_HUMAN	UBE2D3	physical	25546391
TNNC2_HUMAN	TNNC2	physical	28514442
CUL5_HUMAN	CUL5	physical	28514442
PTN11_HUMAN	PTPN11	physical	28514442

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 NOSIP_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, AND MASSSPECTROMETRY.	17287340 [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-168, AND MASSSPECTROMETRY.	19413330 [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 THR-30, AND MASSSPECTROMETRY.	17525332 [Abstract]