dbPTM

NSF_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NSF_HUMAN
UniProt AC	P46459
Protein Name	Vesicle-fusing ATPase
Gene Name	NSF
Organism	Homo sapiens (Human).
Sequence Length	744
Subcellular Localization	Cytoplasm.
Protein Description	Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack independent of vesicle origin. Interaction with AMPAR subunit GRIA2 leads to influence GRIA2 membrane cycling (By similarity)..
Protein Sequence	MAGRSMQAARCPTDELSLTNCAVVNEKDFQSGQHVIVRTSPNHRYTFTLKTHPSVVPGSIAFSLPQRKWAGLSIGQEIEVSLYTFDKAKQCIGTMTIEIDFLQKKSIDSNPYDTDKMAAEFIQQFNNQAFSVGQQLVFSFNEKLFGLLVKDIEAMDPSILKGEPATGKRQKIEVGLVVGNSQVAFEKAENSSLNLIGKAKTKENRQSIINPDWNFEKMGIGGLDKEFSDIFRRAFASRVFPPEIVEQMGCKHVKGILLYGPPGCGKTLLARQIGKMLNAREPKVVNGPEILNKYVGESEANIRKLFADAEEEQRRLGANSGLHIIIFDEIDAICKQRGSMAGSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRPDLIDEALLRPGRLEVKMEIGLPDEKGRLQILHIHTARMRGHQLLSADVDIKELAVETKNFSGAELEGLVRAAQSTAMNRHIKASTKVEVDMEKAESLQVTRGDFLASLENDIKPAFGTNQEDYASYIMNGIIKWGDPVTRVLDDGELLVQQTKNSDRTPLVSVLLEGPPHSGKTALAAKIAEESNFPFIKICSPDKMIGFSETAKCQAMKKIFDDAYKSQLSCVVVDDIERLLDYVPIGPRFSNLVLQALLVLLKKAPPQGRKLLIIGTTSRKDVLQEMEMLNAFSTTIHVPNIATGEQLLEALELLGNFKDKERTTIAQQVKGKKVWIGIKKLLMLIEMSLQMDPEYRVRKFLALLREEGASPLDFD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
12 (in isoform 2)	Phosphorylation	-	37.01	25159151
13	Phosphorylation	MQAARCPTDELSLTN CCCCCCCCCCCCCCC	45.81	25693802
17	Phosphorylation	RCPTDELSLTNCAVV CCCCCCCCCCCEEEE	30.97	25693802
19	Phosphorylation	PTDELSLTNCAVVNE CCCCCCCCCEEEECH	25.52	25693802
21	S-nitrosocysteine	DELSLTNCAVVNEKD CCCCCCCEEEECHHH	2.27	-
21	S-nitrosylation	DELSLTNCAVVNEKD CCCCCCCEEEECHHH	2.27	22178444
45	Phosphorylation	RTSPNHRYTFTLKTH ECCCCCCEEEEEEEC	9.92	22817900
83	Phosphorylation	QEIEVSLYTFDKAKQ CEEEEEEEEHHHHHH	9.61	22817900
91	S-nitrosocysteine	TFDKAKQCIGTMTIE EHHHHHHEEEEEEEE	2.82	-
91	S-nitrosylation	TFDKAKQCIGTMTIE EHHHHHHEEEEEEEE	2.82	22178444
105	Acetylation	EIDFLQKKSIDSNPY EEEEHHHCCCCCCCC	39.42	-
105	Malonylation	EIDFLQKKSIDSNPY EEEEHHHCCCCCCCC	39.42	26320211
106	Phosphorylation	IDFLQKKSIDSNPYD EEEHHHCCCCCCCCC	38.37	26657352
109	Phosphorylation	LQKKSIDSNPYDTDK HHHCCCCCCCCCHHH	37.73	21406692
112	Phosphorylation	KSIDSNPYDTDKMAA CCCCCCCCCHHHHHH	35.41	21406692
114	Phosphorylation	IDSNPYDTDKMAAEF CCCCCCCHHHHHHHH	31.51	21406692
155	Sulfoxidation	LVKDIEAMDPSILKG HHHCHHHCCHHHHCC	5.16	21406390
158	Phosphorylation	DIEAMDPSILKGEPA CHHHCCHHHHCCCCC	35.97	20068231
166	Phosphorylation	ILKGEPATGKRQKIE HHCCCCCCCCCCEEE	54.68	20860994
172	Ubiquitination	ATGKRQKIEVGLVVG CCCCCCEEEEEEEEC	3.82	-
181	Ubiquitination	VGLVVGNSQVAFEKA EEEEECCCHHHHHHH	21.80	-
198	Acetylation	SSLNLIGKAKTKENR CCCCCCEECCCHHHH	39.45	25953088
198	Malonylation	SSLNLIGKAKTKENR CCCCCCEECCCHHHH	39.45	26320211
201	Phosphorylation	NLIGKAKTKENRQSI CCCEECCCHHHHHCC	48.74	28857561
207	Phosphorylation	KTKENRQSIINPDWN CCHHHHHCCCCCCCC	23.38	30266825
228	Phosphorylation	GGLDKEFSDIFRRAF CCCCHHHHHHHHHHH	30.78	27499020
250	S-nitrosylation	EIVEQMGCKHVKGIL HHHHHHCCCEEEEEE	2.01	22178444
250	S-nitrosocysteine	EIVEQMGCKHVKGIL HHHHHHCCCEEEEEE	2.01	-
254	Acetylation	QMGCKHVKGILLYGP HHCCCEEEEEEEECC	39.70	26051181
259	Phosphorylation	HVKGILLYGPPGCGK EEEEEEEECCCCCCH	24.92	21082442
264	Glutathionylation	LLYGPPGCGKTLLAR EEECCCCCCHHHHHH	6.61	22555962
264	S-nitrosocysteine	LLYGPPGCGKTLLAR EEECCCCCCHHHHHH	6.61	-
264	S-nitrosylation	LLYGPPGCGKTLLAR EEECCCCCCHHHHHH	6.61	22178444
266	Ubiquitination	YGPPGCGKTLLARQI ECCCCCCHHHHHHHH	39.82	-
266	Acetylation	YGPPGCGKTLLARQI ECCCCCCHHHHHHHH	39.82	25953088
267	Phosphorylation	GPPGCGKTLLARQIG CCCCCCHHHHHHHHH	16.58	28857561
275	Ubiquitination	LLARQIGKMLNAREP HHHHHHHHHHCCCCC	41.67	-
293	Acetylation	NGPEILNKYVGESEA CCHHHHHHHCCCCHH	37.56	25953088
294	Phosphorylation	GPEILNKYVGESEAN CHHHHHHHCCCCHHH	16.77	28152594
294	Nitration	GPEILNKYVGESEAN CHHHHHHHCCCCHHH	16.77	-
298	Phosphorylation	LNKYVGESEANIRKL HHHHCCCCHHHHHHH	35.76	20068231
337	Methylation	IDAICKQRGSMAGST HHHHHHHCCCCCCCC	25.34	115485613
339	Phosphorylation	AICKQRGSMAGSTGV HHHHHCCCCCCCCCC	13.98	20873877
340	Sulfoxidation	ICKQRGSMAGSTGVH HHHHCCCCCCCCCCH	5.65	21406390
343	Phosphorylation	QRGSMAGSTGVHDTV HCCCCCCCCCCHHHH	16.67	28857561
344	Phosphorylation	RGSMAGSTGVHDTVV CCCCCCCCCCHHHHH	42.16	28857561
349	Phosphorylation	GSTGVHDTVVNQLLS CCCCCHHHHHHHHHH	16.10	23312004
356	Phosphorylation	TVVNQLLSKIDGVEQ HHHHHHHHCCCCHHH	35.84	23312004
368	Ubiquitination	VEQLNNILVIGMTNR HHHHHCEEEEECCCC	2.20	-
401	Acetylation	EIGLPDEKGRLQILH EECCCCCCCCEEEEE	57.63	25953088
421	Phosphorylation	MRGHQLLSADVDIKE HCCCEEECCCCCHHH	30.89	23898821
434	2-Hydroxyisobutyrylation	KELAVETKNFSGAEL HHHHHCCCCCCHHHH	42.35	-
434	Ubiquitination	KELAVETKNFSGAEL HHHHHCCCCCCHHHH	42.35	-
435	Ubiquitination	ELAVETKNFSGAELE HHHHCCCCCCHHHHH	43.68	-
437	Phosphorylation	AVETKNFSGAELEGL HHCCCCCCHHHHHHH	46.62	21712546
460	Phosphorylation	MNRHIKASTKVEVDM HHHHHCCCCEEEECH	24.61	22210691
461	Phosphorylation	NRHIKASTKVEVDME HHHHCCCCEEEECHH	43.92	22210691
461	Ubiquitination	NRHIKASTKVEVDME HHHHCCCCEEEECHH	43.92	-
462	Ubiquitination	RHIKASTKVEVDMEK HHHCCCCEEEECHHH	33.62	-
472	Phosphorylation	VDMEKAESLQVTRGD ECHHHHHHCCCCCHH	29.03	29255136
476	Phosphorylation	KAESLQVTRGDFLAS HHHHCCCCCHHHHHH	18.90	30622161
483	Phosphorylation	TRGDFLASLENDIKP CCHHHHHHHHCCCCC	38.06	22210691
529	Ubiquitination	ELLVQQTKNSDRTPL CEEEEECCCCCCCCE	50.55	21906983
531	Phosphorylation	LVQQTKNSDRTPLVS EEEECCCCCCCCEEE	29.99	23090842
534	Phosphorylation	QTKNSDRTPLVSVLL ECCCCCCCCEEEEEE	26.43	23090842
538	Phosphorylation	SDRTPLVSVLLEGPP CCCCCEEEEEECCCC	18.09	23090842
547	Phosphorylation	LLEGPPHSGKTALAA EECCCCCCCHHHHHH	48.00	25022875
555	Ubiquitination	GKTALAAKIAEESNF CHHHHHHHHHHHCCC	36.52	-
569	Phosphorylation	FPFIKICSPDKMIGF CCEEEECCCCCCCCC	39.34	30624053
572	2-Hydroxyisobutyrylation	IKICSPDKMIGFSET EEECCCCCCCCCCHH	35.48	-
577	Phosphorylation	PDKMIGFSETAKCQA CCCCCCCCHHHHHHH	28.91	30631047
579	Phosphorylation	KMIGFSETAKCQAMK CCCCCCHHHHHHHHH	30.16	30631047
599	Glutathionylation	AYKSQLSCVVVDDIE HHHHCCCEEEECCHH	3.51	22555962
611	Phosphorylation	DIERLLDYVPIGPRF CHHHHHHCCCCCHHH	14.22	-
639	Acetylation	KAPPQGRKLLIIGTT HCCCCCCEEEEEECC	55.24	26051181
645	Phosphorylation	RKLLIIGTTSRKDVL CEEEEEECCCHHHHH	15.93	-
646	Phosphorylation	KLLIIGTTSRKDVLQ EEEEEECCCHHHHHH	22.71	24114839
693	Phosphorylation	FKDKERTTIAQQVKG CCCHHCCCHHHHHCC	22.12	-
699	Malonylation	TTIAQQVKGKKVWIG CCHHHHHCCCEEEEH	61.75	26320211
699	2-Hydroxyisobutyrylation	TTIAQQVKGKKVWIG CCHHHHHCCCEEEEH	61.75	-
708	2-Hydroxyisobutyrylation	KKVWIGIKKLLMLIE CEEEEHHHHHHHHHH	31.96	-
709	Acetylation	KVWIGIKKLLMLIEM EEEEHHHHHHHHHHH	44.95	25953088
717	Phosphorylation	LLMLIEMSLQMDPEY HHHHHHHHHCCCHHH	11.58	28270605
724	Phosphorylation	SLQMDPEYRVRKFLA HHCCCHHHHHHHHHH	21.57	28270605
728	Acetylation	DPEYRVRKFLALLRE CHHHHHHHHHHHHHH	41.70	25953088
728	Malonylation	DPEYRVRKFLALLRE CHHHHHHHHHHHHHH	41.70	26320211
739	Phosphorylation	LLREEGASPLDFD-- HHHHCCCCCCCCC--	36.53	22617229

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
83	Y	Phosphorylation	Kinase	FER	P16591	PSP
83	Y	Phosphorylation	Kinase	FES	P07332	PSP
569	S	Phosphorylation	Kinase	CDK16	Q00536	Uniprot
645	T	Phosphorylation	Kinase	LRRK2	Q5S007	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
569	S	Phosphorylation		-
Phosphorylation at Ser-569 interferes with homohexamerization.

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 NSF_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EIF3E_HUMAN	EIF3E	physical	16169070
FUND2_HUMAN	FUNDC2	physical	16169070
CE126_HUMAN	KIAA1377	physical	16169070
LC7L2_HUMAN	LUC7L2	physical	16169070
ERG28_HUMAN	C14orf1	physical	16169070
RLA1_HUMAN	RPLP1	physical	16169070
NSF_HUMAN	NSF	physical	8051214
SNAA_HUMAN	NAPA	physical	20562859
SNAG_HUMAN	NAPG	physical	20562859
STX12_HUMAN	STX12	physical	20562859
STX8_HUMAN	STX8	physical	20562859
STX7_HUMAN	STX7	physical	20562859
VTI1B_HUMAN	VTI1B	physical	20562859
SNP29_HUMAN	SNAP29	physical	20562859
SCFD1_HUMAN	SCFD1	physical	20562859
SNP23_HUMAN	SNAP23	physical	20562859
STX6_HUMAN	STX6	physical	20562859
STX5_HUMAN	STX5	physical	20562859
KC1G3_HUMAN	CSNK1G3	physical	20562859
PMS2_HUMAN	PMS2	physical	22939629
STAT1_HUMAN	STAT1	physical	22939629
VA0D1_HUMAN	ATP6V0D1	physical	26344197
RM09_HUMAN	MRPL9	physical	26344197
RAP2A_HUMAN	RAP2A	physical	26344197
SCFD1_HUMAN	SCFD1	physical	26344197
SC31A_HUMAN	SEC31A	physical	26344197
SNP25_HUMAN	SNAP25	physical	26344197
SNP29_HUMAN	SNAP29	physical	26344197
VPS4B_HUMAN	VPS4B	physical	26344197
EXOC5_HUMAN	EXOC5	physical	27173435

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 NSF_HUMAN

Related Literatures of Post-Translational Modification

show