Q99733 (NP1L4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nucleosome assembly protein 1-like 4

Alternative name(s):
Nucleosome assembly protein 2
Short name=NAP-2

Gene names

Name:	NAP1L4
Synonyms:	NAP2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	375 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Subcellular location	Nucleus.
Tissue specificity	Ubiquitous. Biallelically expressed in fetal and adult tissues. Highest levels in testis.
Post-translational modification	Polyglutamylated by TTLL4, a modification that occurs exclusively on glutamate residues and results in polyglutamate chains on the gamma-carboxyl group. Some residues may also be monoglycylated but not polyglycylated due to the absence of functional TTLL10 in human By similarity.
Sequence similarities	Belongs to the nucleosome assembly protein (NAP) family.

Ontologies

Keywords
Cellular component	Nucleus
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	nucleosome assembly Traceable author statement. Source: ProtInc
Cellular component	chromatin assembly complex Traceable author statement. Source: ProtInc cytoplasm Traceable author statement. Source: ProtInc
Molecular function	unfolded protein binding Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 375	374	Nucleosome assembly protein 1-like 4		PRO_0000185658
Regions
	Motif	265 – 271	7	Nuclear localization signal Potential
	Compositional bias	126 – 131	6	Poly-Glu
	Compositional bias	301 – 310	10	Asp/Glu-rich (acidic)
	Compositional bias	347 – 370	24	Asp/Glu-rich (acidic)
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.8 Ref.11
	Modified residue	5	1	Phosphoserine Ref.3 Ref.8 Ref.11
	Modified residue	7	1	Phosphoserine Ref.11
	Modified residue	12	1	Phosphoserine Ref.11
	Modified residue	51	1	Phosphothreonine Ref.6 Ref.9 Ref.12
	Modified residue	53	1	Phosphoserine Ref.4 Ref.9
	Modified residue	125	1	Phosphoserine Ref.3 Ref.4 Ref.5 Ref.7 Ref.9 Ref.10 Ref.11 Ref.12
	Modified residue	139	1	Phosphoserine Ref.7
	Modified residue	304	1	Phosphoserine Ref.12

Sequences

	Sequence		Length	Mass (Da)
	Q99733 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: 788E1F9F5BC8FD45	FASTA	375	42,823
	10 20 30 40 50 60 MADHSFSDGV PSDSVEAAKN ASNTEKLTDQ VMQNPRVLAA LQERLDNVPH TPSSYIETLP 70 80 90 100 110 120 KAVKRRINAL KQLQVRCAHI EAKFYEEVHD LERKYAALYQ PLFDKRREFI TGDVEPTDAE 130 140 150 160 170 180 SEWHSENEEE EKLAGDMKSK VVVTEKAAAT AEEPDPKGIP EFWFTIFRNV DMLSELVQEY 190 200 210 220 230 240 DEPILKHLQD IKVKFSDPGQ PMSFVLEFHF EPNDYFTNSV LTKTYKMKSE PDKADPFSFE 250 260 270 280 290 300 GPEIVDCDGC TIDWKKGKNV TVKTIKKKQK HKGRGTVRTI TKQVPNESFF NFFNPLKASG 310 320 330 340 350 360 DGESLDEDSE FTLASDFEIG HFFRERIVPR AVLYFTGEAI EDDDNFEEGE EGEEEELEGD 370 EEGEDEDDAE INPKV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel human homologue of yeast nucleosome assembly protein, 65 kb centromeric to the p57KIP2 gene, is biallelically expressed in fetal and adult tissues." Hu R.-J., Lee M.P., Johnson L.A., Feinberg A.P. Hum. Mol. Genet. 5:1743-1748(1996) [PubMed: 8923002] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Muscle.
[3]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5 AND SER-125, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[4]	"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) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53 AND SER-125, MASS SPECTROMETRY. Tissue: Cervix adenocarcinoma.
[5]	"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line." Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S. Electrophoresis 28:2027-2034(2007) [PubMed: 17487921] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, MASS SPECTROMETRY. Tissue: Prostate cancer.
[6]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells 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) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-51, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation 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) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125 AND SER-139, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[8]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-51; SER-53 AND SER-125, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange 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) [PubMed: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, MASS SPECTROMETRY. Tissue: Liver.
[11]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-7; SER-12 AND SER-125, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[12]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-51; SER-125 AND SER-304, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[13]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U77456 mRNA. Translation: AAC50870.1. BC022090 mRNA. Translation: AAH22090.1.
IPI	IPI00941463.
RefSeq	NP_005960.1. NM_005969.3.
UniGene	Hs.501684. Hs.695395.
3D structure databases
ProteinModelPortal	Q99733.
SMR	Q99733. Positions 41-344.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q99733. 3 interactions.
STRING	Q99733.
PTM databases
PhosphoSite	Q99733.
Polymorphism databases
DMDM	2498672.
Proteomic databases
PRIDE	Q99733.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000380542; ENSP00000369915; ENSG00000205531.
GeneID	4676.
KEGG	hsa:4676.
UCSC	uc001lxc.1. human.
Organism-specific databases
CTD	4676.
GeneCards	GC11M002965.
H-InvDB	HIX0201638.
HGNC	HGNC:7640. NAP1L4.
HPA	CAB011567.
MIM	601651. gene.
neXtProt	NX_Q99733.
PharmGKB	PA31442.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG08673.
GeneTree	ENSGT00480000042668.
HOVERGEN	HBG052653.
OrthoDB	EOG46WZ99.
PhylomeDB	Q99733.
Gene expression databases
ArrayExpress	Q99733.
Bgee	Q99733.
CleanEx	HS_NAP1L4.
Genevestigator	Q99733.
GermOnline	ENSG00000205531. Homo sapiens.
Family and domain databases
InterPro	IPR002164. NAP_family. [Graphical view]
KO	K11282.
PANTHER	PTHR11875. NAP_family. 1 hit.
Pfam	PF00956. NAP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	18024.
PMAP-CutDB	Q99733.
SOURCE	Search...

Entry information

Entry name

NP1L4_HUMAN

Accession

Primary (citable) accession number: Q99733

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 1, 1997
Last modified:	January 25, 2012
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.