dbPTM

SNIP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SNIP1_HUMAN
UniProt AC	Q8TAD8
Protein Name	Smad nuclear-interacting protein 1
Gene Name	SNIP1
Organism	Homo sapiens (Human).
Sequence Length	396
Subcellular Localization	Nucleus .
Protein Description	Down-regulates NF-kappa-B signaling by competing with RELA for CREBBP/EP300 binding. Involved in the microRNA (miRNA) biogenesis. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA..
Protein Sequence	MKAVKSERERGSRRRHRDGDVVLPAGVVVKQERLSPEVAPPAHRRPDHSGGSPSPPTSEPARSGHRGNRARGVSRSPPKKKNKASGRRSKSPRSKRNRSPHHSTVKVKQEREDHPRRGREDRQHREPSEQEHRRARNSDRDRHRGHSHQRRTSNERPGSGQGQGRDRDTQNLQAQEEEREFYNARRREHRQRNDVGGGGSESQELVPRPGGNNKEKEVPAKEKPSFELSGALLEDTNTFRGVVIKYSEPPEARIPKKRWRLYPFKNDEVLPVMYIHRQSAYLLGRHRRIADIPIDHPSCSKQHAVFQYRLVEYTRADGTVGRRVKPYIIDLGSGNGTFLNNKRIEPQRYYELKEKDVLKFGFSSREYVLLHESSDTSEIDRKDDEDEEEEEEVSDS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MKAVKSERE ------CCCCCCCHH	62.98	25953088
5	Sumoylation	---MKAVKSERERGS ---CCCCCCCHHHCC	52.00	-
5	Acetylation	---MKAVKSERERGS ---CCCCCCCHHHCC	52.00	25953088
6	Phosphorylation	--MKAVKSERERGSR --CCCCCCCHHHCCC	34.97	26437602
12	Phosphorylation	KSERERGSRRRHRDG CCCHHHCCCCCCCCC	28.92	-
30	Sumoylation	LPAGVVVKQERLSPE ECCEEEEEECCCCCC	34.53	-
30	Sumoylation	LPAGVVVKQERLSPE ECCEEEEEECCCCCC	34.53	25114211
30	Acetylation	LPAGVVVKQERLSPE ECCEEEEEECCCCCC	34.53	25953088
35	Phosphorylation	VVKQERLSPEVAPPA EEEECCCCCCCCCCC	25.82	29255136
49	Phosphorylation	AHRRPDHSGGSPSPP CCCCCCCCCCCCCCC	52.83	29255136
52	Phosphorylation	RPDHSGGSPSPPTSE CCCCCCCCCCCCCCC	26.23	29255136
54	Phosphorylation	DHSGGSPSPPTSEPA CCCCCCCCCCCCCCC	45.25	29255136
57	Phosphorylation	GGSPSPPTSEPARSG CCCCCCCCCCCCCCC	49.45	30266825
58	Phosphorylation	GSPSPPTSEPARSGH CCCCCCCCCCCCCCC	47.56	29255136
63	Phosphorylation	PTSEPARSGHRGNRA CCCCCCCCCCCCCCC	40.85	28111955
74	Phosphorylation	GNRARGVSRSPPKKK CCCCCCCCCCCCCCC	29.84	23401153
76	Phosphorylation	RARGVSRSPPKKKNK CCCCCCCCCCCCCCC	37.74	23401153
79	Acetylation	GVSRSPPKKKNKASG CCCCCCCCCCCCCCC	78.68	12432625
80	Acetylation	VSRSPPKKKNKASGR CCCCCCCCCCCCCCC	68.31	12432635
89	Phosphorylation	NKASGRRSKSPRSKR CCCCCCCCCCCCHHC	35.80	17081983
91	Phosphorylation	ASGRRSKSPRSKRNR CCCCCCCCCCHHCCC	27.13	17081983
99	Phosphorylation	PRSKRNRSPHHSTVK CCHHCCCCCCCCCCC	31.94	22167270
103	Phosphorylation	RNRSPHHSTVKVKQE CCCCCCCCCCCCCHH	31.68	20068231
104	Phosphorylation	NRSPHHSTVKVKQER CCCCCCCCCCCCHHH	21.71	20068231
108	Sumoylation	HHSTVKVKQEREDHP CCCCCCCCHHHCCCC	40.50	28112733
108	Sumoylation	HHSTVKVKQEREDHP CCCCCCCCHHHCCCC	40.50	-
128	Phosphorylation	DRQHREPSEQEHRRA HHCCCCCCHHHHHHH	47.35	21955146
147	Phosphorylation	RDRHRGHSHQRRTSN HHHHHCCCCCCCCCC	24.92	26329039
152	Phosphorylation	GHSHQRRTSNERPGS CCCCCCCCCCCCCCC	37.79	22167270
153	Phosphorylation	HSHQRRTSNERPGSG CCCCCCCCCCCCCCC	34.58	22167270
159	Phosphorylation	TSNERPGSGQGQGRD CCCCCCCCCCCCCCC	30.53	21955146
169	Phosphorylation	GQGRDRDTQNLQAQE CCCCCCHHHHHHHHH	21.91	17525332
200	Phosphorylation	NDVGGGGSESQELVP CCCCCCCCCCCCCCC	37.03	23401153
202	Phosphorylation	VGGGGSESQELVPRP CCCCCCCCCCCCCCC	30.56	17525332
223	Acetylation	KEVPAKEKPSFELSG CCCCCCCCCCEEECC	45.30	25953088
223	Ubiquitination	KEVPAKEKPSFELSG CCCCCCCCCCEEECC	45.30	-
223	Sumoylation	KEVPAKEKPSFELSG CCCCCCCCCCEEECC	45.30	28112733
225	Phosphorylation	VPAKEKPSFELSGAL CCCCCCCCEEECCEE	42.28	28450419
229	Phosphorylation	EKPSFELSGALLEDT CCCCEEECCEEEECC	18.15	28450419
236	Phosphorylation	SGALLEDTNTFRGVV CCEEEECCCCEEEEE	27.12	20068231
238	Phosphorylation	ALLEDTNTFRGVVIK EEEECCCCEEEEEEE	19.46	29759185
246	Phosphorylation	FRGVVIKYSEPPEAR EEEEEEECCCCCCCC	13.72	29759185
247	Phosphorylation	RGVVIKYSEPPEARI EEEEEECCCCCCCCC	38.33	29759185
301	Ubiquitination	IDHPSCSKQHAVFQY CCCCCHHCCCEEEEE	50.89	-
301	Acetylation	IDHPSCSKQHAVFQY CCCCCHHCCCEEEEE	50.89	25953088
308	Phosphorylation	KQHAVFQYRLVEYTR CCCEEEEEEEEEEEC	8.41	-
313	Phosphorylation	FQYRLVEYTRADGTV EEEEEEEEECCCCCC	8.27	-
314	Phosphorylation	QYRLVEYTRADGTVG EEEEEEEECCCCCCC	13.08	-
325	Acetylation	GTVGRRVKPYIIDLG CCCCCEECCEEEEEC	30.23	26051181
325	Ubiquitination	GTVGRRVKPYIIDLG CCCCCEECCEEEEEC	30.23	-
342	Ubiquitination	NGTFLNNKRIEPQRY CCCCCCCCCCCCCEE	54.39	-
349	Phosphorylation	KRIEPQRYYELKEKD CCCCCCEEEECCHHC	8.95	27251275
350	Phosphorylation	RIEPQRYYELKEKDV CCCCCEEEECCHHCC	19.58	27251275
353	Ubiquitination	PQRYYELKEKDVLKF CCEEEECCHHCCEEE	51.26	-
367	Phosphorylation	FGFSSREYVLLHESS ECCCCCCEEEEECCC	8.69	20873877
373	Phosphorylation	EYVLLHESSDTSEID CEEEEECCCCCCCCC	23.83	30108239
374	Phosphorylation	YVLLHESSDTSEIDR EEEEECCCCCCCCCC	41.75	30108239
376	Phosphorylation	LLHESSDTSEIDRKD EEECCCCCCCCCCCC	30.15	30108239
377	Phosphorylation	LHESSDTSEIDRKDD EECCCCCCCCCCCCC	37.23	30108239
394	Phosphorylation	EEEEEEVSDS----- HHHHHHHCCC-----	35.10	30266825
396	Phosphorylation	EEEEVSDS------- HHHHHCCC-------	34.32	30266825

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 SNIP1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SNIP1_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 SNIP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SMAD4_HUMAN	SMAD4	physical	10887155
EP300_HUMAN	EP300	physical	10887155
CBP_HUMAN	CREBBP	physical	10887155
TF65_HUMAN	RELA	physical	11567019
ATR_HUMAN	ATR	physical	17260016
MYC_HUMAN	MYC	physical	17157259
MAX_HUMAN	MAX	physical	17157259
PR40A_HUMAN	PRPF40A	physical	22365833
SF3B1_HUMAN	SF3B1	physical	22365833
CHERP_HUMAN	CHERP	physical	22365833
SRRM2_HUMAN	SRRM2	physical	22365833
PRPF3_HUMAN	PRPF3	physical	22365833
SNW1_HUMAN	SNW1	physical	22365833
MFAP1_HUMAN	MFAP1	physical	22365833
RED_HUMAN	IK	physical	22365833
NCBP3_HUMAN	C17orf85	physical	22365833
TTC14_HUMAN	TTC14	physical	22365833
ZCH10_HUMAN	ZCCHC10	physical	22365833
SRPK2_HUMAN	SRPK2	physical	22365833
BCLF1_HUMAN	BCLAF1	physical	26186194
TR150_HUMAN	THRAP3	physical	26186194
ACINU_HUMAN	ACIN1	physical	26186194
NCBP3_HUMAN	C17orf85	physical	26186194
SRRM2_HUMAN	SRRM2	physical	26186194
ZC3HE_HUMAN	ZC3H14	physical	26186194
PININ_HUMAN	PNN	physical	26186194
GPTC8_HUMAN	GPATCH8	physical	26186194
NCBP1_HUMAN	NCBP1	physical	26186194
CRNL1_HUMAN	CRNKL1	physical	26186194
RBM22_HUMAN	RBM22	physical	26186194
AQR_HUMAN	AQR	physical	26186194
GPAM1_HUMAN	GPALPP1	physical	26186194
PPIG_HUMAN	PPIG	physical	26186194
SRSF9_HUMAN	SRSF9	physical	26186194
SRSF1_HUMAN	SRSF1	physical	26186194
RNPS1_HUMAN	RNPS1	physical	26186194
CLASR_HUMAN	CLASRP	physical	26186194
SNW1_HUMAN	SNW1	physical	26186194
LARP1_HUMAN	LARP1	physical	26186194
CCDC9_HUMAN	CCDC9	physical	26186194
CCD12_HUMAN	CCDC12	physical	26186194
SRRT_HUMAN	SRRT	physical	26186194
PRP17_HUMAN	CDC40	physical	26186194
MGN_HUMAN	MAGOH	physical	26186194
ISY1_HUMAN	ISY1	physical	26186194
IF4A3_HUMAN	EIF4A3	physical	26186194
CLK3_HUMAN	CLK3	physical	26186194
CASC3_HUMAN	CASC3	physical	26186194
YTDC1_HUMAN	YTHDC1	physical	26186194
NKTR_HUMAN	NKTR	physical	26186194
SRSF6_HUMAN	SRSF6	physical	26186194
MKRN1_HUMAN	MKRN1	physical	26186194
TRA2A_HUMAN	TRA2A	physical	26186194
TRA2B_HUMAN	TRA2B	physical	26186194
SRSF8_HUMAN	SRSF8	physical	26186194
BUD31_HUMAN	BUD31	physical	26186194
SPT2_HUMAN	SPTY2D1	physical	26186194
SRS12_HUMAN	SRSF12	physical	26186194
SRS10_HUMAN	SRSF10	physical	26186194
DHX8_HUMAN	DHX8	physical	26186194
CLK2_HUMAN	CLK2	physical	26186194
NKAP_HUMAN	NKAP	physical	26186194
CLASR_HUMAN	CLASRP	physical	28514442
ACINU_HUMAN	ACIN1	physical	28514442
RNPS1_HUMAN	RNPS1	physical	28514442
PININ_HUMAN	PNN	physical	28514442
CCDC9_HUMAN	CCDC9	physical	28514442
SRSF8_HUMAN	SRSF8	physical	28514442
NKTR_HUMAN	NKTR	physical	28514442
ZC3HE_HUMAN	ZC3H14	physical	28514442
CASC3_HUMAN	CASC3	physical	28514442
CLK2_HUMAN	CLK2	physical	28514442
PPIG_HUMAN	PPIG	physical	28514442
YTDC1_HUMAN	YTHDC1	physical	28514442
SRS12_HUMAN	SRSF12	physical	28514442
NCBP3_HUMAN	C17orf85	physical	28514442
GPTC8_HUMAN	GPATCH8	physical	28514442
CLK3_HUMAN	CLK3	physical	28514442
TR150_HUMAN	THRAP3	physical	28514442
CRNL1_HUMAN	CRNKL1	physical	28514442
MKRN1_HUMAN	MKRN1	physical	28514442
GPAM1_HUMAN	GPALPP1	physical	28514442
PRP17_HUMAN	CDC40	physical	28514442
TRA2A_HUMAN	TRA2A	physical	28514442
SRSF1_HUMAN	SRSF1	physical	28514442
SRS10_HUMAN	SRSF10	physical	28514442
BCLF1_HUMAN	BCLAF1	physical	28514442
RBM22_HUMAN	RBM22	physical	28514442
ISY1_HUMAN	ISY1	physical	28514442
AQR_HUMAN	AQR	physical	28514442
BUD31_HUMAN	BUD31	physical	28514442
PAI2B_HUMAN	PAIP2B	physical	28514442
NCBP1_HUMAN	NCBP1	physical	28514442
SRRM2_HUMAN	SRRM2	physical	28514442
CCD12_HUMAN	CCDC12	physical	28514442
CDK3_HUMAN	CDK3	physical	28514442
TRA2B_HUMAN	TRA2B	physical	28514442
DHX8_HUMAN	DHX8	physical	28514442
PPIE_HUMAN	PPIE	physical	28514442
SRSF9_HUMAN	SRSF9	physical	28514442
SNW1_HUMAN	SNW1	physical	28514442
IF4A3_HUMAN	EIF4A3	physical	28514442
RALY_HUMAN	RALY	physical	28514442
RL5_HUMAN	RPL5	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614501	Psychomotor retardation, epilepsy, and craniofacial dysmorphism (PMRED)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of SNIP1_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-52 AND SER-54, 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-35; SER-49; SER-52 ANDSER-54, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment."; Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; J. Proteome Res. 7:5167-5176(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, AND MASSSPECTROMETRY.	19367720 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND MASSSPECTROMETRY.	18220336 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND MASSSPECTROMETRY.	19007248 [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-169 AND SER-202, ANDMASS SPECTROMETRY.	17525332 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; SER-89; SER-91 ANDSER-153, AND MASS SPECTROMETRY.	17081983 [Abstract]
Sumoylation
Reference	PubMed
"PDSM, a motif for phosphorylation-dependent SUMO modification."; Hietakangas V., Anckar J., Blomster H.A., Fujimoto M., Palvimo J.J.,Nakai A., Sistonen L.; Proc. Natl. Acad. Sci. U.S.A. 103:45-50(2006). Cited for: SUMOYLATION AT LYS-30, AND MUTAGENESIS OF LYS-30.	16371476 [Abstract]