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Protein

Nucleosome assembly protein 1-like 1

Gene

Nap1l1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  • kinase binding Source: RGD

GO - Biological processi

  • cellular response to peptide hormone stimulus Source: RGD
  • nucleosome assembly Source: InterPro
  • Schwann cell proliferation Source: RGD
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleosome assembly protein 1-like 1
Alternative name(s):
NAP-1-related protein
Gene namesi
Name:Nap1l1
Synonyms:Nrp
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi71094. Nap1l1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
  • melanosome Source: UniProtKB-SubCell
  • neuron projection Source: RGD
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001856542 – 387Nucleosome assembly protein 1-like 1Add BLAST386
PropeptideiPRO_0000396688388 – 390Removed in mature formBy similarity3

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei10PhosphoserineCombined sources1
Modified residuei62PhosphothreonineCombined sources1
Modified residuei64PhosphothreonineBy similarity1
Modified residuei69PhosphoserineBy similarity1
Modified residuei116N6-acetyllysineBy similarity1
Modified residuei143PhosphoserineBy similarity1
Modified residuei3585-glutamyl polyglycineBy similarity1
Modified residuei3595-glutamyl polyglycineBy similarity1
Modified residuei387Cysteine methyl esterCurated1
Lipidationi387S-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.By similarity
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.By similarity

Keywords - PTMi

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

Proteomic databases

PaxDbiQ9Z2G8.
PeptideAtlasiQ9Z2G8.
PRIDEiQ9Z2G8.

PTM databases

iPTMnetiQ9Z2G8.
PhosphoSitePlusiQ9Z2G8.

Interactioni

GO - Molecular functioni

  • kinase binding Source: RGD

Protein-protein interaction databases

BioGridi250147. 2 interactors.
STRINGi10116.ENSRNOP00000005286.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi272 – 278Nuclear localization signalSequence analysis7

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi10 – 30Asp/Glu-rich (acidic)Add BLAST21
Compositional biasi129 – 145Asp/Glu-rich (acidic)Add BLAST17
Compositional biasi347 – 377Asp/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.
HOVERGENiHBG052653.
InParanoidiQ9Z2G8.
KOiK11279.
PhylomeDBiQ9Z2G8.

Family and domain databases

InterProiIPR002164. NAP_family.
[Graphical view]
PANTHERiPTHR11875. PTHR11875. 2 hits.
PfamiPF00956. NAP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9Z2G8-1 [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 WLTVFKNDLL SDMVQEHDEP ILKHLKDIKV
210 220 230 240 250
KFSDAGQPMS FILEFHFEPN EYFTNEVLTK TYRMRSEPDD SDPFSFDGPE
260 270 280 290 300
IMGCTGCQID WKKGKNVTLK TIKKKQKHKG RGTVRTVTKT VSKTSFFNFF
310 320 330 340 350
APPEVPENGD LDDDXEAILA ADFEIGHFLR ERIIPRSVLY FTGEAIEDDD
360 370 380 390
DDYDEEGEEA DEEGEEEGDE ENDPDYDPKK DQNPAECKQQ
Length:390
Mass (Da):45,314
Last modified:May 1, 1999 - v1
Checksum:i3D59D3C2AE1A71EB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF062594 mRNA. Translation: AAC67388.1.
RefSeqiNP_446013.2. NM_053561.2.
UniGeneiRn.162938.

Genome annotation databases

GeneIDi89825.
KEGGirno:89825.
UCSCiRGD:71094. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF062594 mRNA. Translation: AAC67388.1.
RefSeqiNP_446013.2. NM_053561.2.
UniGeneiRn.162938.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250147. 2 interactors.
STRINGi10116.ENSRNOP00000005286.

PTM databases

iPTMnetiQ9Z2G8.
PhosphoSitePlusiQ9Z2G8.

Proteomic databases

PaxDbiQ9Z2G8.
PeptideAtlasiQ9Z2G8.
PRIDEiQ9Z2G8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi89825.
KEGGirno:89825.
UCSCiRGD:71094. rat.

Organism-specific databases

CTDi4673.
RGDi71094. Nap1l1.

Phylogenomic databases

eggNOGiKOG1507. Eukaryota.
ENOG410XQN9. LUCA.
HOVERGENiHBG052653.
InParanoidiQ9Z2G8.
KOiK11279.
PhylomeDBiQ9Z2G8.

Miscellaneous databases

PROiQ9Z2G8.

Family and domain databases

InterProiIPR002164. NAP_family.
[Graphical view]
PANTHERiPTHR11875. PTHR11875. 2 hits.
PfamiPF00956. NAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNP1L1_RAT
AccessioniPrimary (citable) accession number: Q9Z2G8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: May 1, 1999
Last modified: November 2, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.