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Reviewed, UniProtKB/Swiss-Prot Q99733 (NP1L4_HUMAN)

Last modified November 4, 2008. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Nucleosome assembly protein 1-like 4
Alternative name(s):
    Nucleosome assembly protein 2
      Short name=NAP2
Gene names
Name: NAP1L4
Synonyms: NAP2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length375 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Subcellular location

Nucleus.

Tissue specificity

Ubiquitous. Biallelically expressed in fetal and adult tissues. Highest levels in testis.

Sequence similarities

Belongs to the nucleosome assembly protein (NAP) family.

Ontologies

Keywords

   Cellular componentNucleus
   PTMPhosphoprotein

Gene Ontology (GO)

   Biological processnucleosome assembly

Traceable author statement. Source: ProtInc

   Cellular componentchromatin assembly complex

Traceable author statement. Source: ProtInc

cytoplasm

Traceable author statement. Source: ProtInc

   Molecular functionunfolded protein binding

Traceable author statement. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 375375Nucleosome assembly protein 1-like 4
PRO_0000185658

Regions

Motif265 – 2717Nuclear localization signal Potential
Compositional bias126 – 1316Poly-Glu
Compositional bias301 – 31010Asp/Glu-rich (acidic)
Compositional bias347 – 37024Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue51Phosphoserine
Modified residue511Phosphothreonine
Modified residue531Phosphoserine
Modified residue1251Phosphoserine
Modified residue1391Phosphoserine

Sequences

Sequence LengthMass (Da)Tools
Q99733-1 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 788E1F9F5BC8FD45

FASTA37542,823
        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 

« Hide

References

« Hide '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: Epithelium.
[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: Epithelium.
[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.
[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: Epithelium.
[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.
[8]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

U77456 mRNA. Translation: AAC50870.1.
BC022090 mRNA. Translation: AAH22090.1.
RefSeqNP_005960.1.
UniGeneHs.501684
Hs.695395

3D structure databases

ModBaseSearch...

PTM databases

PhosphoSiteQ99733.

Genome annotation databases

EnsemblENSG00000205531. Homo sapiens. [Contig view]
GeneID4676.
KEGGhsa:4676.

Organism-specific databases

H-InvDBHIX0009370.
HGNCHGNC:7640. NAP1L4.
HPACAB011567.
MIM601651. gene.
PharmGKBPA31442.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOGENOMQ99733.
HOVERGENQ99733.

Gene expression databases

ArrayExpressQ99733.
CleanExHS_NAP1L4.
GermOnlineENSG00000205531. Homo sapiens.

Family and domain databases

InterProIPR002164. NAP_family.
[Graphical view]
PANTHERPTHR11875. NAP_family. 1 hit.
PfamPF00956. NAP. 1 hit.
[Graphical view]
BLOCKSSearch...
ProtoNetSearch...

Other Resources

LinkHubQ99733.
NextBio18024.
SOURCESearch...

Entry information

Entry nameNP1L4_HUMAN
AccessionPrimary (citable) accession number: Q99733
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: November 4, 2008
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents