dbPTM

NP1L4_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NP1L4_MOUSE
UniProt AC	Q78ZA7
Protein Name	Nucleosome assembly protein 1-like 4
Gene Name	Nap1l4
Organism	Mus musculus (Mouse).
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. Phosphorylated form localizes in the cytoplasm during the G0/G1 transition, whereas depho
Protein Description	Acts as histone chaperone in nucleosome assembly. [PubMed: 28366643 In condensing spermatids, mediates the loading of the heterodimer composed of histones H2AFB1 and HIST1H2BA/TH2B onto the nucleosomes, thereby promoting the replacement of histones to protamine in male germ cells]
Protein Sequence	MAENSLSDGGPADSVEAAKNASNTEKLTDQVMQNPQVLAALQERLDNVSHTPSSYIETLPKAVKRRINALKQLQVRCAHIEAKFYEEVHDLERKYAALYQPLFDKRREFITGDVEPTDAESAWHSENEEEDKLAGDMKNKVVIAEKEAATVEELNPKGIPEFWFTIFRNVDMLSELVQEYDEPILKHLQDIKVKFSDPGQPMSFVLEFHFEPNDYFTNPVLTKTYKMKSEPDKADPFSFEGPEIVDCDGCTIDWKKGKNVTVKTIKKKQKHKGRGTVRTITKQVPNESFFNFFSPLKASGDGESLDEDSEFTLASDFEIGHFFRERIVPRAVLYFTGEAIEDDDNFEEGEEGEEEELEGDEEGEDEDDADVNPKV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAENSLSDG ------CCCCCCCCC	25.36	-
5	Phosphorylation	---MAENSLSDGGPA ---CCCCCCCCCCCC	22.28	26824392
7	Phosphorylation	-MAENSLSDGGPADS -CCCCCCCCCCCCHH	33.75	26824392
14	Phosphorylation	SDGGPADSVEAAKNA CCCCCCHHHHHHHHC	24.78	25619855
49	Phosphorylation	QERLDNVSHTPSSYI HHHHHCCCCCCHHHH	28.09	26824392
51	Phosphorylation	RLDNVSHTPSSYIET HHHCCCCCCHHHHHH	19.84	22942356
53	Phosphorylation	DNVSHTPSSYIETLP HCCCCCCHHHHHHHH	36.61	21082442
54	Phosphorylation	NVSHTPSSYIETLPK CCCCCCHHHHHHHHH	31.19	26824392
55	Phosphorylation	VSHTPSSYIETLPKA CCCCCHHHHHHHHHH	13.71	21082442
58	Phosphorylation	TPSSYIETLPKAVKR CCHHHHHHHHHHHHH	38.51	25266776
71	Ubiquitination	KRRINALKQLQVRCA HHHHHHHHHHHHHHH	46.69	-
94	Ubiquitination	EVHDLERKYAALYQP HHHHHHHHHHHHHHH	29.84	-
105	Acetylation	LYQPLFDKRREFITG HHHHHHHHCCHHHCC	46.12	-
105	Ubiquitination	LYQPLFDKRREFITG HHHHHHHHCCHHHCC	46.12	-
111	Phosphorylation	DKRREFITGDVEPTD HHCCHHHCCCCCCCC	32.42	24925903
117	Phosphorylation	ITGDVEPTDAESAWH HCCCCCCCCHHHHCC	34.04	24925903
121	Phosphorylation	VEPTDAESAWHSENE CCCCCHHHHCCCCCH	38.08	24925903
125	Phosphorylation	DAESAWHSENEEEDK CHHHHCCCCCHHHHH	31.26	27087446
146	Acetylation	NKVVIAEKEAATVEE CCEEEEEHHHCCHHH	43.56	23806337
146	Ubiquitination	NKVVIAEKEAATVEE CCEEEEEHHHCCHHH	43.56	-
255	Acetylation	DGCTIDWKKGKNVTV CCCEEEECCCCCEEE	48.15	69901
256	Acetylation	GCTIDWKKGKNVTVK CCEEEECCCCCEEEE	71.51	69905
282	Ubiquitination	GTVRTITKQVPNESF CCEEEEEEECCCCHH	45.51	-
294	Phosphorylation	ESFFNFFSPLKASGD CHHHHHHCCCCCCCC	25.78	26745281
299	Phosphorylation	FFSPLKASGDGESLD HHCCCCCCCCCCCCC	35.51	23984901
304	Phosphorylation	KASGDGESLDEDSEF CCCCCCCCCCCCCCE	46.80	26239621
309	Phosphorylation	GESLDEDSEFTLASD CCCCCCCCCEEECCC	32.34	26239621
312	Phosphorylation	LDEDSEFTLASDFEI CCCCCCEEECCCCEE	19.84	26239621

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_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NP1L4_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
NP1L2_MOUSE	Nap1l2	physical	21333655

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of NP1L4_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND MASSSPECTROMETRY.	19131326 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49 AND SER-125, AND MASSSPECTROMETRY.	17242355 [Abstract]
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry."; Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; J. Proteome Res. 6:250-262(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND MASSSPECTROMETRY.	17203969 [Abstract]