dbPTM

NP1L1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NP1L1_HUMAN
UniProt AC	P55209
Protein Name	Nucleosome assembly protein 1-like 1
Gene Name	NAP1L1
Organism	Homo sapiens (Human).
Sequence Length	391
Subcellular Localization	Nucleus . Melanosome . Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Protein Description	May be involved in modulating chromatin formation and contribute to regulation of cell proliferation..
Protein Sequence	MADIDNKEQSELDQDLDDVEEVEEEETGEETKLKARQLTVQMMQNPQILAALQERLDGLVETPTGYIESLPRVVKRRVNALKNLQVKCAQIEAKFYEEVHDLERKYAVLYQPLFDKRFEIINAIYEPTEEECEWKPDEEDEISEELKEKAKIEDEKKDEEKEDPKGIPEFWLTVFKNVDLLSDMVQEHDEPILKHLKDIKVKFSDAGQPMSFVLEFHFEPNEYFTNEVLTKTYRMRSEPDDSDPFSFDGPEIMGCTGCQIDWKKGKNVTLKTIKKKQKHKGRGTVRTVTKTVSNDSFFNFFAPPEVPESGDLDDDAEAILAADFEIGHFLRERIIPRSVLYFTGEAIEDDDDDYDEEGEEADEEGEEEGDEENDPDYDPKKDQNPAECKQQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1 (in isoform 3)	Acetylation	-	7.35	22814378
2	Acetylation	------MADIDNKEQ ------CCCCCHHHH	23.59	19413330
10	Phosphorylation	DIDNKEQSELDQDLD CCCHHHHHHHCCCCC	41.01	29255136
27	Phosphorylation	EEVEEEETGEETKLK HHHHHHHCCHHHHHH	53.85	27251275
31	Phosphorylation	EEETGEETKLKARQL HHHCCHHHHHHHHHH	37.06	20068231
32	Ubiquitination	EETGEETKLKARQLT HHCCHHHHHHHHHHH	51.80	21906983
32	Ubiquitination	EETGEETKLKARQLT HHCCHHHHHHHHHHH	51.80	21890473
39	Phosphorylation	KLKARQLTVQMMQNP HHHHHHHHHHHHHCH	10.60	27273156
41	Ubiquitination	KARQLTVQMMQNPQI HHHHHHHHHHHCHHH	19.18	21890473
62	Phosphorylation	RLDGLVETPTGYIES HHHCCCCCCCCHHHH	20.76	19664994
64	Phosphorylation	DGLVETPTGYIESLP HCCCCCCCCHHHHHH	50.46	22167270
66	Phosphorylation	LVETPTGYIESLPRV CCCCCCCHHHHHHHH	12.18	30183078
69	Phosphorylation	TPTGYIESLPRVVKR CCCCHHHHHHHHHHH	33.83	29255136
82	Ubiquitination	KRRVNALKNLQVKCA HHHHHHHHHHHHHHH	53.88	21890473
82	Acetylation	KRRVNALKNLQVKCA HHHHHHHHHHHHHHH	53.88	25953088
82	2-Hydroxyisobutyrylation	KRRVNALKNLQVKCA HHHHHHHHHHHHHHH	53.88	-
82	Ubiquitination	KRRVNALKNLQVKCA HHHHHHHHHHHHHHH	53.88	21906983
87	Acetylation	ALKNLQVKCAQIEAK HHHHHHHHHHHHHHH	15.76	25953088
87	Ubiquitination	ALKNLQVKCAQIEAK HHHHHHHHHHHHHHH	15.76	-
87	Ubiquitination	ALKNLQVKCAQIEAK HHHHHHHHHHHHHHH	15.76	-
87	2-Hydroxyisobutyrylation	ALKNLQVKCAQIEAK HHHHHHHHHHHHHHH	15.76	-
94	Ubiquitination	KCAQIEAKFYEEVHD HHHHHHHHHHHHHHH	35.37	-
94	Acetylation	KCAQIEAKFYEEVHD HHHHHHHHHHHHHHH	35.37	26051181
96	Phosphorylation	AQIEAKFYEEVHDLE HHHHHHHHHHHHHHH	15.52	28796482
97	Ubiquitination	QIEAKFYEEVHDLER HHHHHHHHHHHHHHH	57.59	21890473
105	Acetylation	EVHDLERKYAVLYQP HHHHHHHHHHHHHHH	28.34	26051181
105	Ubiquitination	EVHDLERKYAVLYQP HHHHHHHHHHHHHHH	28.34	21890473
105	2-Hydroxyisobutyrylation	EVHDLERKYAVLYQP HHHHHHHHHHHHHHH	28.34	-
105	Ubiquitination	EVHDLERKYAVLYQP HHHHHHHHHHHHHHH	28.34	21906983
106	Phosphorylation	VHDLERKYAVLYQPL HHHHHHHHHHHHHHH	14.25	28152594
110	Phosphorylation	ERKYAVLYQPLFDKR HHHHHHHHHHHHHHH	11.07	28152594
116	2-Hydroxyisobutyrylation	LYQPLFDKRFEIINA HHHHHHHHHHHHHHH	52.21	-
116	Acetylation	LYQPLFDKRFEIINA HHHHHHHHHHHHHHH	52.21	-
116	Ubiquitination	LYQPLFDKRFEIINA HHHHHHHHHHHHHHH	52.21	21890473
116	Acetylation	LYQPLFDKRFEIINA HHHHHHHHHHHHHHH	52.21	19608861
116	Ubiquitination	LYQPLFDKRFEIINA HHHHHHHHHHHHHHH	52.21	21890473
116	Succinylation	LYQPLFDKRFEIINA HHHHHHHHHHHHHHH	52.21	23954790
125	Phosphorylation	FEIINAIYEPTEEEC HHHHHHHCCCCHHHC	17.28	20873877
128	Phosphorylation	INAIYEPTEEECEWK HHHHCCCCHHHCCCC	44.05	30140170
135	Acetylation	TEEECEWKPDEEDEI CHHHCCCCCCCCCHH	21.94	26051181
135	Ubiquitination	TEEECEWKPDEEDEI CHHHCCCCCCCCCHH	21.94	-
135	Ubiquitination	TEEECEWKPDEEDEI CHHHCCCCCCCCCHH	21.94	-
143	Phosphorylation	PDEEDEISEELKEKA CCCCCHHCHHHHHHH	23.99	25159151
147	Acetylation	DEISEELKEKAKIED CHHCHHHHHHHCCCC	61.52	26051181
147	Ubiquitination	DEISEELKEKAKIED CHHCHHHHHHHCCCC	61.52	-
147	Ubiquitination	DEISEELKEKAKIED CHHCHHHHHHHCCCC	61.52	-
149	Ubiquitination	ISEELKEKAKIEDEK HCHHHHHHHCCCCCC	54.08	-
151	Acetylation	EELKEKAKIEDEKKD HHHHHHHCCCCCCCH	58.66	7822237
156	Ubiquitination	KAKIEDEKKDEEKED HHCCCCCCCHHHCCC	77.25	-
161	Ubiquitination	DEKKDEEKEDPKGIP CCCCHHHCCCCCCCC	66.43	-
165	Acetylation	DEEKEDPKGIPEFWL HHHCCCCCCCCHHHH	80.11	20167786
165	Ubiquitination	DEEKEDPKGIPEFWL HHHCCCCCCCCHHHH	80.11	21906983
165	Ubiquitination	DEEKEDPKGIPEFWL HHHCCCCCCCCHHHH	80.11	21890473
182	Phosphorylation	FKNVDLLSDMVQEHD HCCCHHHHHHHHHCC	30.84	22199227
184	Sulfoxidation	NVDLLSDMVQEHDEP CCHHHHHHHHHCCHH	2.77	21406390
194	Ubiquitination	EHDEPILKHLKDIKV HCCHHHHHHHHHCEE	47.84	19608861
194	Ubiquitination	EHDEPILKHLKDIKV HCCHHHHHHHHHCEE	47.84	-
194	Acetylation	EHDEPILKHLKDIKV HCCHHHHHHHHHCEE	47.84	-
194	Acetylation	EHDEPILKHLKDIKV HCCHHHHHHHHHCEE	47.84	23749302
223	Phosphorylation	FHFEPNEYFTNEVLT EEECCCCCCCHHHHH	23.49	-
232	Phosphorylation	TNEVLTKTYRMRSEP CHHHHHHEECCCCCC	15.89	23403867
237	Phosphorylation	TKTYRMRSEPDDSDP HHEECCCCCCCCCCC	44.10	23403867
242	Phosphorylation	MRSEPDDSDPFSFDG CCCCCCCCCCCCCCC	55.34	28102081
246	Phosphorylation	PDDSDPFSFDGPEIM CCCCCCCCCCCCCCC	28.02	23403867
253	Sulfoxidation	SFDGPEIMGCTGCQI CCCCCCCCCCCCCCE	3.25	30846556
256	Phosphorylation	GPEIMGCTGCQIDWK CCCCCCCCCCCEEEC	34.95	23403867
263	Acetylation	TGCQIDWKKGKNVTL CCCCEEECCCCCEEE	48.15	26051181
264	Acetylation	GCQIDWKKGKNVTLK CCCEEECCCCCEEEE	71.51	70387
266	Acetylation	QIDWKKGKNVTLKTI CEEECCCCCEEEEEH	58.06	129495
269	Phosphorylation	WKKGKNVTLKTIKKK ECCCCCEEEEEHHHH	31.75	20873877
271	Acetylation	KGKNVTLKTIKKKQK CCCCEEEEEHHHHHH	38.55	-
271	Ubiquitination	KGKNVTLKTIKKKQK CCCCEEEEEHHHHHH	38.55	-
271	Malonylation	KGKNVTLKTIKKKQK CCCCEEEEEHHHHHH	38.55	32601280
271	Acetylation	KGKNVTLKTIKKKQK CCCCEEEEEHHHHHH	38.55	23236377
272	Phosphorylation	GKNVTLKTIKKKQKH CCCEEEEEHHHHHHC	40.93	20873877
313	Ubiquitination	VPESGDLDDDAEAIL CCCCCCCCCCHHHHH	57.39	-
321	Ubiquitination	DDAEAILAADFEIGH CCHHHHHHHHHHHHH	10.00	-
343	Phosphorylation	PRSVLYFTGEAIEDD CCHHEEEECCCCCCC	22.13	29457462
354	Phosphorylation	IEDDDDDYDEEGEEA CCCCCCCCCCCCHHC	32.05	28176443
377	Phosphorylation	DEENDPDYDPKKDQN CCCCCCCCCCCCCCC	39.26	28176443
381	Ubiquitination	DPDYDPKKDQNPAEC CCCCCCCCCCCHHHH	70.68	21906983
388	Farnesylation	KDQNPAECKQQ---- CCCCHHHHHCC----	5.39	15308774
388	Methylation	KDQNPAECKQQ---- CCCCHHHHHCC----	5.39	-
388	Farnesylation	KDQNPAECKQQ---- CCCCHHHHHCC----	5.39	15308774
389	Ubiquitination	DQNPAECKQQ----- CCCHHHHHCC-----	43.15	21906983

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 NP1L1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NP1L1_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 NP1L1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NP1L1_HUMAN	NAP1L1	physical	16169070
ODO2_HUMAN	DLST	physical	16169070
MED10_HUMAN	MED10	physical	21900206
CSN2_HUMAN	COPS2	physical	17339334
RL6_HUMAN	RPL6	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RL10A_HUMAN	RPL10A	physical	22939629
NPM_HUMAN	NPM1	physical	22939629
RS3A_HUMAN	RPS3A	physical	22939629
RL5_HUMAN	RPL5	physical	22939629
RL15_HUMAN	RPL15	physical	22939629
RL9_HUMAN	RPL9	physical	22939629
RL31_HUMAN	RPL31	physical	22939629
RL11_HUMAN	RPL11	physical	22939629
RL14_HUMAN	RPL14	physical	22939629
RL12_HUMAN	RPL12	physical	22939629
RL37A_HUMAN	RPL37A	physical	22939629
RS4X_HUMAN	RPS4X	physical	22939629
RS3_HUMAN	RPS3	physical	22939629
NP1L4_HUMAN	NAP1L4	physical	22939629
PESC_HUMAN	PES1	physical	22939629
SET_HUMAN	SET	physical	22939629
PDCD4_HUMAN	PDCD4	physical	22939629
SAE2_HUMAN	UBA2	physical	22939629
RBBP4_HUMAN	RBBP4	physical	22939629
TPX2_HUMAN	TPX2	physical	21988832
POTE1_HUMAN	POT1	physical	21988832
RL24_HUMAN	RPL24	physical	26186194
NP1L4_HUMAN	NAP1L4	physical	26186194
MAGD2_HUMAN	MAGED2	physical	26186194
NOP16_HUMAN	NOP16	physical	26186194
UBE2O_HUMAN	UBE2O	physical	26186194
H2A2B_HUMAN	HIST2H2AB	physical	26186194
IF1AX_HUMAN	EIF1AX	physical	26186194
FNTA_HUMAN	FNTA	physical	26186194
RL36L_HUMAN	RPL36AL	physical	26186194
RL36A_HUMAN	RPL36A	physical	26186194
RIC8B_HUMAN	RIC8B	physical	26186194
RL17_HUMAN	RPL17	physical	26186194
FNTB_HUMAN	FNTB	physical	26186194
E41L5_HUMAN	EPB41L5	physical	26186194
SDA1_HUMAN	SDAD1	physical	26186194
PESC_HUMAN	PES1	physical	26344197
SPT4H_HUMAN	SUPT4H1	physical	26344197
FNTB_HUMAN	FNTB	physical	28514442
RL36L_HUMAN	RPL36AL	physical	28514442
FNTA_HUMAN	FNTA	physical	28514442
RL24_HUMAN	RPL24	physical	28514442
NP1L4_HUMAN	NAP1L4	physical	28514442
SDA1_HUMAN	SDAD1	physical	28514442
RL17_HUMAN	RPL17	physical	28514442
UBE2O_HUMAN	UBE2O	physical	28514442
E41L5_HUMAN	EPB41L5	physical	28514442
RIC8B_HUMAN	RIC8B	physical	28514442
H2A2B_HUMAN	HIST2H2AB	physical	28514442
RL36A_HUMAN	RPL36A	physical	28514442
GNAS3_HUMAN	GNAS	physical	28514442
GNAS2_HUMAN	GNAS	physical	28514442
ALEX_HUMAN	GNAS	physical	28514442
GNAS1_HUMAN	GNAS	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 NP1L1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-62, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-116, AND MASS SPECTROMETRY.	19608861 [Abstract]
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 THR-62 AND SER-69, 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-10; THR-62; SER-69 ANDSER-143, AND MASS SPECTROMETRY.	18669648 [Abstract]
"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-10 AND THR-62, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-62, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-62, AND MASSSPECTROMETRY.	17924679 [Abstract]
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-62, AND MASSSPECTROMETRY.	16565220 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-62, AND MASSSPECTROMETRY.	16964243 [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 THR-62, AND MASSSPECTROMETRY.	17081983 [Abstract]
Prenylation
Reference	PubMed
"A tagging-via-substrate technology for detection and proteomics offarnesylated proteins."; Kho Y., Kim S.C., Jiang C., Barma D., Kwon S.W., Cheng J.,Jaunbergs J., Weinbaum C., Tamanoi F., Falck J., Zhao Y.; Proc. Natl. Acad. Sci. U.S.A. 101:12479-12484(2004). Cited for: ISOPRENYLATION AT CYS-388.	15308774 [Abstract]