Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Nucleosome assembly protein 1-like 1

Gene

Nap1l1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

May be involved in modulating chromatin formation and contribute to regulation of cell proliferation.

GO - Molecular functioni

GO - Biological processi

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleosome assembly protein 1-like 1
Alternative name(s):
Brain protein DN38
NAP-1-related protein
Gene namesi
Name:Nap1l1
Synonyms:Nrp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1855693 Nap1l1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi359E → D: Reduced polyglycylation. 1 Publication1
Mutagenesisi360E → D: Reduced polyglycylation. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001856532 – 388Nucleosome assembly protein 1-like 1Add BLAST387
PropeptideiPRO_0000396686389 – 391Removed in mature formBy similarity3

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei10PhosphoserineBy similarity1
Modified residuei62PhosphothreonineCombined sources1
Modified residuei64PhosphothreonineCombined sources1
Modified residuei69PhosphoserineBy similarity1
Modified residuei116N6-acetyllysineCombined sources1
Modified residuei143PhosphoserineCombined sources1
Modified residuei3595-glutamyl polyglycine1 Publication1
Modified residuei3605-glutamyl polyglycine1 Publication1
Modified residuei388Cysteine methyl esterCurated1
Lipidationi388S-farnesyl cysteineBy similarity1

Post-translational modificationi

Polyglycylated by TTLL10 on glutamate residues, resulting in polyglycine chains on the gamma-carboxyl group. Both polyglutamylation and polyglycylation modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally.1 Publication
Polyglutamylated by TTLL4 on glutamate residues, resulting in polyglutamate chains on the gamma-carboxyl group. Both polyglutamylation and polyglycylation modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

EPDiP28656
MaxQBiP28656
PaxDbiP28656
PeptideAtlasiP28656
PRIDEiP28656

PTM databases

iPTMnetiP28656
PhosphoSitePlusiP28656
SwissPalmiP28656

Expressioni

Tissue specificityi

High expression in cerebral cortex, not in cerebellar cortex.

Gene expression databases

BgeeiENSMUSG00000058799
CleanExiMM_NAP1L1
ExpressionAtlasiP28656 baseline and differential
GenevisibleiP28656 MM

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
Map2k5Q9WVS720EBI-645055,EBI-446144

GO - Molecular functioni

Protein-protein interaction databases

BioGridi207325, 6 interactors
IntActiP28656, 6 interactors
MINTiP28656
STRINGi10090.ENSMUSP00000126850

Structurei

3D structure databases

ProteinModelPortaliP28656
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi273 – 279Nuclear localization signalSequence analysis7

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi11 – 30Asp/Glu-rich (acidic)Add BLAST20
Compositional biasi129 – 145Asp/Glu-rich (acidic)Add BLAST17
Compositional biasi348 – 378Asp/Glu-rich (acidic)Add BLAST31

Domaini

The acidic domains are probably involved in the interaction with histones.

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1507 Eukaryota
ENOG410XQN9 LUCA
GeneTreeiENSGT00480000042668
HOGENOMiHOG000171827
HOVERGENiHBG052653
InParanoidiP28656
KOiK11279
PhylomeDBiP28656

Family and domain databases

InterProiView protein in InterPro
IPR037231 NAP-like_sf
IPR002164 NAP_family
PANTHERiPTHR11875 PTHR11875, 1 hit
PfamiView protein in Pfam
PF00956 NAP, 1 hit
SUPFAMiSSF143113 SSF143113, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P28656-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADIDNKEQS ELDQDLEDVE EVEEEETGEE TKIKARQLTV QMMQNPQILA
60 70 80 90 100
ALQERLDGLV DTPTGYIESL PKVVKRRVNA LKNLQVKCAQ IEAKFYEEVH
110 120 130 140 150
DLERKYAVLY QPLFDKRFEI INAIYEPTEE ECEWKPDEED EVSEELKEKA
160 170 180 190 200
KIEDEKKDEE KEDPKGIPEF WLTVFKNVDL LSDMVQEHDE PILKHLKDIK
210 220 230 240 250
VKFSDAGQPM SFVLEFHFEP NDYFTNEVLT KTYRMRSEPD DSDPFSFDGP
260 270 280 290 300
EIMGCTGCQI DWKKGKNVTL KTIKKKQKHK GRGTVRTVTK TVSNDSFFNF
310 320 330 340 350
FAPPEVPENG DLDDDAEAIL AADFEIGHFL RERIIPRSVL YFTGEAIEDD
360 370 380 390
DDDYDEEGEE ADEEGEEEGD EENDPDYDPK KDQNPAECKQ Q
Length:391
Mass (Da):45,345
Last modified:October 1, 1996 - v2
Checksum:i48F17F3A44D9A597
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti377 – 390YDPKK…AECKQ → MTQRRIRTQPSASSSE in CAA43689 (PubMed:12106288).CuratedAdd BLAST14

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D12618 mRNA Translation: BAA02142.1
AK050375 mRNA Translation: BAC34219.1
AK136161 mRNA Translation: BAE22850.1
AK145766 mRNA Translation: BAE26637.1
BC076591 mRNA Translation: AAH76591.1
X61449 mRNA Translation: CAA43689.1
CCDSiCCDS36058.1
PIRiJS0707
RefSeqiNP_056596.1, NM_015781.4
UniGeneiMm.290407

Genome annotation databases

EnsembliENSMUST00000065917; ENSMUSP00000070068; ENSMUSG00000058799
ENSMUST00000217908; ENSMUSP00000151750; ENSMUSG00000058799
ENSMUST00000218828; ENSMUSP00000151972; ENSMUSG00000058799
GeneIDi53605
KEGGimmu:53605
UCSCiuc007hac.2 mouse

Similar proteinsi

Entry informationi

Entry nameiNP1L1_MOUSE
AccessioniPrimary (citable) accession number: P28656
Secondary accession number(s): Q3UL14
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: October 1, 1996
Last modified: June 20, 2018
This is version 143 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health