P55209 (NP1L1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nucleosome assembly protein 1-like 1

Alternative name(s):
NAP-1-related protein
Short name=hNRP

Gene names

Name:	NAP1L1
Synonyms:	NRP

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	391 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)

Function	May be involved in modulating chromatin formation and contribute to regulation of cell proliferation.
Subcellular location	Nucleus. Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.7
Tissue specificity	Ubiquitously expressed.
Domain	The acidic domains are probably involved in the interaction with histones.
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 Lipoprotein Methylation Phosphoprotein Prenylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA replication Traceable author statement. Source: ProtInc nucleosome assembly Traceable author statement. Source: ProtInc positive regulation of cell proliferation Traceable author statement. Source: ProtInc
Cellular component	chromatin assembly complex Traceable author statement. Source: ProtInc melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CREBBP	Q92793	3	EBI-356392,EBI-81215
EP300	Q09472	3	EBI-356392,EBI-447295
NR2F6	P10588	2	EBI-356392,EBI-2681496

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 388	387	Nucleosome assembly protein 1-like 1		PRO_0000185652
	Propeptide	389 – 391	3	Removed in mature form Probable		PRO_0000393943
Regions
	Motif	273 – 279	7	Nuclear localization signal Potential
	Compositional bias	10 – 30	21	Asp/Glu-rich (acidic)
	Compositional bias	129 – 145	17	Asp/Glu-rich (acidic)
	Compositional bias	348 – 378	31	Asp/Glu-rich (acidic)
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.14
	Modified residue	10	1	Phosphoserine Ref.11 Ref.12
	Modified residue	62	1	Phosphothreonine Ref.6 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15
	Modified residue	69	1	Phosphoserine Ref.12 Ref.15
	Modified residue	116	1	N6-acetyllysine Ref.16
	Modified residue	143	1	Phosphoserine Ref.12
	Modified residue	388	1	Cysteine methyl ester Probable
	Lipidation	388	1	S-farnesyl cysteine Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P55209 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: E5B2EAA4EAE551D2	FASTA	391	45,374
	10 20 30 40 50 60 MADIDNKEQS ELDQDLDDVE EVEEEETGEE TKLKARQLTV QMMQNPQILA ALQERLDGLV 70 80 90 100 110 120 ETPTGYIESL PRVVKRRVNA LKNLQVKCAQ IEAKFYEEVH DLERKYAVLY QPLFDKRFEI 130 140 150 160 170 180 INAIYEPTEE ECEWKPDEED EISEELKEKA KIEDEKKDEE KEDPKGIPEF WLTVFKNVDL 190 200 210 220 230 240 LSDMVQEHDE PILKHLKDIK VKFSDAGQPM SFVLEFHFEP NEYFTNEVLT KTYRMRSEPD 250 260 270 280 290 300 DSDPFSFDGP EIMGCTGCQI DWKKGKNVTL KTIKKKQKHK GRGTVRTVTK TVSNDSFFNF 310 320 330 340 350 360 FAPPEVPESG DLDDDAEAIL AADFEIGHFL RERIIPRSVL YFTGEAIEDD DDDYDEEGEE 370 380 390 ADEEGEEEGD EENDPDYDPK KDQNPAECKQ Q

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular characterization of hNRP, a cDNA encoding a human nucleosome-assembly-protein-I-related gene product involved in the induction of cell proliferation." Simon H.-U., Mills G.B., Kozlowski M., Hogg D., Branch D., Ishimi Y., Siminovitch K.A. Biochem. J. 297:389-397(1994) [PubMed: 8297347] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Thymus.
[2]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Melanoma.
[4]	"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.
[5]	"A tagging-via-substrate technology for detection and proteomics of farnesylated 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) [PubMed: 15308774] [Abstract] Cited for: ISOPRENYLATION AT CYS-388.
[6]	"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 THR-62, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes." Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F. J. Proteome Res. 5:3135-3144(2006) [PubMed: 17081065] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Melanoma.
[8]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-62, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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 THR-62, MASS SPECTROMETRY. Tissue: Cervix adenocarcinoma.
[10]	"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-62, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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-10 AND THR-62, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[12]	"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 SER-10; THR-62; SER-69 AND SER-143, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"The histone chaperone protein Nucleosome Assembly Protein-1 (hNAP-1) binds HIV-1 Tat and promotes viral transcription." Vardabasso C., Manganaro L., Lusic M., Marcello A., Giacca M. Retrovirology 5:8-8(2008) [PubMed: 18226242] [Abstract] Cited for: INTERACTION WITH HIV-1 TAT.
[14]	"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 THR-62, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[15]	"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-62 AND SER-69, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[16]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-116, MASS SPECTROMETRY.
[17]	"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	M86667 mRNA. Translation: AAC37544.1. BT007023 mRNA. Translation: AAP35669.1. AL162068 mRNA. Translation: CAB82405.1. BC002387 mRNA. Translation: AAH02387.1.
IPI	IPI00023860.
PIR	S40510.
RefSeq	NP_004528.1. NM_004537.4. NP_631946.1. NM_139207.2.
UniGene	Hs.524599. Hs.695185.
3D structure databases
ProteinModelPortal	P55209.
SMR	P55209. Positions 52-352.
ModBase	Search...
Protein-protein interaction databases
IntAct	P55209. 32 interactions.
MINT	MINT-150144.
STRING	P55209.
PTM databases
PhosphoSite	P55209.
Polymorphism databases
DMDM	1709337.
2D gel databases
OGP	P55209.
Proteomic databases
PRIDE	P55209.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000261182; ENSP00000261182; ENSG00000187109. ENST00000393263; ENSP00000376947; ENSG00000187109.
GeneID	4673.
KEGG	hsa:4673.
UCSC	uc001sxv.1. human.
Organism-specific databases
CTD	4673.
GeneCards	GC12M076438.
H-InvDB	HIX0010831. HIX0129726.
HGNC	HGNC:7637. NAP1L1.
HPA	HPA028861.
MIM	164060. gene.
neXtProt	NX_P55209.
PharmGKB	PA31439.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG11375.
GeneTree	ENSGT00480000042668.
HOGENOM	HBG619916.
HOVERGEN	HBG052653.
InParanoid	P55209.
OMA	PDYDSKK.
OrthoDB	EOG46WZ99.
PhylomeDB	P55209.
Gene expression databases
ArrayExpress	P55209.
Bgee	P55209.
CleanEx	HS_NAP1L1.
Genevestigator	P55209.
GermOnline	ENSG00000187109. Homo sapiens.
Family and domain databases
InterPro	IPR002164. NAP_family. [Graphical view]
KO	K11279.
PANTHER	PTHR11875. NAP_family. 1 hit.
Pfam	PF00956. NAP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	18010.
PMAP-CutDB	P55209.
SOURCE	Search...

Entry information

Entry name

NP1L1_HUMAN

Accession

Primary (citable) accession number: P55209

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	January 25, 2012
This is version 111 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.