NP1L4_HUMAN - dbPTM
NP1L4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NP1L4_HUMAN
UniProt AC Q99733
Protein Name Nucleosome assembly protein 1-like 4
Gene Name NAP1L4 {ECO:0000312|HGNC:HGNC:7640}
Organism Homo sapiens (Human).
Sequence Length 375
Subcellular Localization Nucleus . Cytoplasm . Present in the cytoplasm and excluded from the nucleus during G0/G1 phase, then relocates to the nucleus by the time cells are in S phase (PubMed:9325046). Phosphorylated form localizes in the cytoplasm during the G0/G1 transiti
Protein Description Acts as histone chaperone in nucleosome assembly..
Protein Sequence MADHSFSDGVPSDSVEAAKNASNTEKLTDQVMQNPRVLAALQERLDNVPHTPSSYIETLPKAVKRRINALKQLQVRCAHIEAKFYEEVHDLERKYAALYQPLFDKRREFITGDVEPTDAESEWHSENEEEEKLAGDMKSKVVVTEKAAATAEEPDPKGIPEFWFTIFRNVDMLSELVQEYDEPILKHLQDIKVKFSDPGQPMSFVLEFHFEPNDYFTNSVLTKTYKMKSEPDKADPFSFEGPEIVDCDGCTIDWKKGKNVTVKTIKKKQKHKGRGTVRTITKQVPNESFFNFFNPLKASGDGESLDEDSEFTLASDFEIGHFFRERIVPRAVLYFTGEAIEDDDNFEEGEEGEEEELEGDEEGEDEDDAEINPKV
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MADHSFSDG
------CCCCCCCCC		24.1920068231
5Phosphorylation---MADHSFSDGVPS
---CCCCCCCCCCCH		27.3029255136
7Phosphorylation-MADHSFSDGVPSDS
-CCCCCCCCCCCHHH		36.1529255136
12PhosphorylationSFSDGVPSDSVEAAK
CCCCCCCHHHHHHHH		39.8629255136
14PhosphorylationSDGVPSDSVEAAKNA
CCCCCHHHHHHHHHC		26.6230266825
19UbiquitinationSDSVEAAKNASNTEK
HHHHHHHHHCCCHHH		61.16-
22PhosphorylationVEAAKNASNTEKLTD
HHHHHHCCCHHHHHH		54.3926074081
24PhosphorylationAAKNASNTEKLTDQV
HHHHCCCHHHHHHHH		31.8126074081
26UbiquitinationKNASNTEKLTDQVMQ
HHCCCHHHHHHHHHH		55.4321890473
26UbiquitinationKNASNTEKLTDQVMQ
HHCCCHHHHHHHHHH		55.4321906983
26UbiquitinationKNASNTEKLTDQVMQ
HHCCCHHHHHHHHHH		55.4321890473
28PhosphorylationASNTEKLTDQVMQNP
CCCHHHHHHHHHHCH		35.1421601212
32SulfoxidationEKLTDQVMQNPRVLA
HHHHHHHHHCHHHHH		2.3721406390
51PhosphorylationRLDNVPHTPSSYIET
HHHCCCCCCHHHHHH		20.8529255136
53PhosphorylationDNVPHTPSSYIETLP
HCCCCCCHHHHHHHH		36.6129255136
54PhosphorylationNVPHTPSSYIETLPK
CCCCCCHHHHHHHHH		31.1929255136
55PhosphorylationVPHTPSSYIETLPKA
CCCCCHHHHHHHHHH		13.7129255136
58PhosphorylationTPSSYIETLPKAVKR
CCHHHHHHHHHHHHH		38.5129255136
61UbiquitinationSYIETLPKAVKRRIN
HHHHHHHHHHHHHHH		69.77-
71UbiquitinationKRRINALKQLQVRCA
HHHHHHHHHHHHHHH		46.6921890473
71UbiquitinationKRRINALKQLQVRCA
HHHHHHHHHHHHHHH		46.6921890473
71AcetylationKRRINALKQLQVRCA
HHHHHHHHHHHHHHH		46.6925953088
83AcetylationRCAHIEAKFYEEVHD
HHHHHHHHHHHHHHH		35.3725953088
85PhosphorylationAHIEAKFYEEVHDLE
HHHHHHHHHHHHHHH		15.5228796482
94UbiquitinationEVHDLERKYAALYQP
HHHHHHHHHHHHHHH		29.8421890473
94UbiquitinationEVHDLERKYAALYQP
HHHHHHHHHHHHHHH		29.8421890473
94AcetylationEVHDLERKYAALYQP
HHHHHHHHHHHHHHH		29.8426051181
95PhosphorylationVHDLERKYAALYQPL
HHHHHHHHHHHHHHH		11.8828152594
99PhosphorylationERKYAALYQPLFDKR
HHHHHHHHHHHHHHC		11.8928152594
105AcetylationLYQPLFDKRREFITG
HHHHHHHHCCHHHCC		46.1227452117
105UbiquitinationLYQPLFDKRREFITG
HHHHHHHHCCHHHCC		46.1221890473
105UbiquitinationLYQPLFDKRREFITG
HHHHHHHHCCHHHCC		46.1221890473
111PhosphorylationDKRREFITGDVEPTD
HHCCHHHCCCCCCCC		32.4223927012
117PhosphorylationITGDVEPTDAESEWH
HCCCCCCCCCCCCCC		34.0423927012
121PhosphorylationVEPTDAESEWHSENE
CCCCCCCCCCCCCCH		47.9422167270
125PhosphorylationDAESEWHSENEEEEK
CCCCCCCCCCHHHHH		43.1019664994
139PhosphorylationKLAGDMKSKVVVTEK
HHHHCCCCCEEEEEH		24.8417287340
140UbiquitinationLAGDMKSKVVVTEKA
HHHCCCCCEEEEEHH		33.27-
146UbiquitinationSKVVVTEKAAATAEE
CCEEEEEHHHHCCCC		33.6821890473
146AcetylationSKVVVTEKAAATAEE
CCEEEEEHHHHCCCC		33.6825953088
146UbiquitinationSKVVVTEKAAATAEE
CCEEEEEHHHHCCCC		33.6821906983
150PhosphorylationVTEKAAATAEEPDPK
EEEHHHHCCCCCCCC		29.8520860994
172SulfoxidationTIFRNVDMLSELVQE
HHHCCHHHHHHHHHH		3.7530846556
186AcetylationEYDEPILKHLQDIKV
HCCHHHHHHHHHCEE		42.8826822725
192UbiquitinationLKHLQDIKVKFSDPG
HHHHHHCEEEECCCC		47.89-
215PhosphorylationFHFEPNDYFTNSVLT
EECCCCCCCCHHHHH		20.95-
255AcetylationDGCTIDWKKGKNVTV
CCCEEEECCCCCEEE		48.1526051181
255UbiquitinationDGCTIDWKKGKNVTV
CCCEEEECCCCCEEE		48.15-
256AcetylationGCTIDWKKGKNVTVK
CCEEEECCCCCEEEE		71.5169903
263UbiquitinationKGKNVTVKTIKKKQK
CCCCEEEEECCCCHH		34.86-
263AcetylationKGKNVTVKTIKKKQK
CCCCEEEEECCCCHH		34.8625953088
264PhosphorylationGKNVTVKTIKKKQKH
CCCEEEEECCCCHHC		33.4228857561
282UbiquitinationGTVRTITKQVPNESF
CCEEEEEECCCCCHH		45.51-
282UbiquitinationGTVRTITKQVPNESF
CCEEEEEECCCCCHH		45.5121890473
282UbiquitinationGTVRTITKQVPNESF
CCEEEEEECCCCCHH		45.5121890473
288PhosphorylationTKQVPNESFFNFFNP
EECCCCCHHHHHCCC		41.6028857561
299PhosphorylationFFNPLKASGDGESLD
HCCCCCCCCCCCCCC		35.5122115753
304PhosphorylationKASGDGESLDEDSEF
CCCCCCCCCCCCCCE		46.8027362937
309PhosphorylationGESLDEDSEFTLASD
CCCCCCCCCEEECCC		32.3427362937
312PhosphorylationLDEDSEFTLASDFEI
CCCCCCEEECCCCEE		19.8428464451
315PhosphorylationDSEFTLASDFEIGHF
CCCEEECCCCEEHHH		46.0420873877
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 NP1L4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NP1L4_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 NP1L4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
H11_HUMANHIST1H1Aphysical
9325046
H31T_HUMANHIST3H3physical
9325046
H2A1B_HUMANHIST1H2AEphysical
9325046
H2B2E_HUMANHIST2H2BEphysical
9325046
NP1L4_HUMANNAP1L4physical
11073993
H2A2C_HUMANHIST2H2ACphysical
11073993
H32_HUMANHIST2H3Cphysical
11073993
NUCL_HUMANNCLphysical
22939629
PESC_HUMANPES1physical
22939629
NPM_HUMANNPM1physical
22939629
SYK_HUMANKARSphysical
22863883
NP1L1_HUMANNAP1L1physical
22863883
PESC_HUMANPES1physical
26344197
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 NP1L4_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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 SER-5; SER-7; SER-12 AND SER-125, AND MASSSPECTROMETRY.
"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-5, ACETYLATION [LARGESCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-51; SER-125 AND SER-304,AND MASS SPECTROMETRY.
"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 SER-5; SER-7; SER-12 AND SER-125, AND MASSSPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND MASSSPECTROMETRY.
"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 THR-51; SER-53 AND SER-125,AND MASS SPECTROMETRY.
"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-5, ACETYLATION [LARGESCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"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-125 AND SER-139, ANDMASS SPECTROMETRY.
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline.";
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
Electrophoresis 28:2027-2034(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND MASSSPECTROMETRY.
"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 SER-53 AND SER-125, AND MASSSPECTROMETRY.
"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-5 AND SER-125, AND MASSSPECTROMETRY.
"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-51, AND MASSSPECTROMETRY.

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