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

Nascent polypeptide-associated complex subunit alpha

Gene

NACA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Prevents inappropriate targeting of non-secretory polypeptides to the endoplasmic reticulum (ER). Binds to nascent polypeptide chains as they emerge from the ribosome and blocks their interaction with the signal recognition particle (SRP), which normally targets nascent secretory peptides to the ER. Also reduces the inherent affinity of ribosomes for protein translocation sites in the ER membrane (M sites). May act as a specific coactivator for JUN, binding to DNA and stabilizing the interaction of JUN homodimers with target gene promoters.3 Publications

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • transcription coactivator activity Source: BHF-UCL

GO - Biological processi

Keywordsi

Molecular functionChaperone, DNA-binding
Biological processHost-virus interaction, Protein transport, Transcription, Transport

Enzyme and pathway databases

SIGNORiQ13765.

Names & Taxonomyi

Protein namesi
Recommended name:
Nascent polypeptide-associated complex subunit alpha
Short name:
NAC-alpha
Alternative name(s):
Alpha-NAC
Allergen: Hom s 2
Gene namesi
Name:NACA
ORF Names:HSD48
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

EuPathDBiHostDB:ENSG00000196531.10.
HGNCiHGNC:7629. NACA.

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

Cytoplasm, Nucleus

Pathology & Biotechi

Allergenic propertiesi

Causes an allergic reaction in human. Binds to IgE from atopic dermatitis (AD) patients. Identified as an IgE autoantigen in atopic dermatitis (AD) patients with severe skin manifestations.1 Publication

Keywords - Diseasei

Allergen

Organism-specific databases

DisGeNETi4666.
OpenTargetsiENSG00000196531.
PharmGKBiPA31433.

Protein family/group databases

Allergomei3323. Hom s 2.0101.
412. Hom s 2.

Polymorphism and mutation databases

BioMutaiNACA.
DMDMi71151996.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001355761 – 215Nascent polypeptide-associated complex subunit alphaAdd BLAST215

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei43Phosphoserine; by ILK11 Publication1
Modified residuei132PhosphoserineND:1
Modified residuei142N6-acetyllysine; alternateND:1
Cross-linki142Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateND:
Modified residuei159Phosphothreonine; by GSK3-betaHMP:1
Modified residuei161PhosphothreonineND:1
Modified residuei166PhosphoserineND:1 Publication1
Modified residuei186PhosphoserineND:1
Modified residuei191PhosphoserineND:1
Modified residuei203PhosphoserineND:1
Modified residuei214PhosphothreonineHMP:1

Post-translational modificationi

Phosphorylation of Thr-159 by GSK3B may promote proteasome mediated degradation (By similarity). Phosphorylation of Ser-43 by ILK during cell adhesion may promote nuclear localization.HMP:2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ13765.
MaxQBiQ13765.
PaxDbiQ13765.
PeptideAtlasiQ13765.
PRIDEiQ13765.
TopDownProteomicsiQ13765-1. [Q13765-1]

PTM databases

iPTMnetiQ13765.
SwissPalmiQ13765.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiENSG00000196531.
CleanExiHS_NACA.
ExpressionAtlasiQ13765. baseline and differential.
GenevisibleiQ13765. HS.

Organism-specific databases

HPAiHPA073152.
HPA073648.

Interactioni

Subunit structurei

Interacts with TBP and JUN (By similarity). Part of the nascent polypeptide-associated complex (NAC), which is a heterodimer of NACA and BTF3 (via NAC-A/B domains). NAC associates with ribosomes through the BTF3/NACB subunit and contacts the ribosomal protein L23, which is positioned near the exiting site. Both subunits can contact nascent polypeptide chains. NACA may also form homodimers, and only this form binds DNA. Interacts with ASFV protein H339R.HMP:4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TXLNAP402222EBI-712216,EBI-359793

Protein-protein interaction databases

BioGridi110748. 49 interactors.
DIPiDIP-43878N.
IntActiQ13765. 28 interactors.
MINTiMINT-5000033.

Structurei

Secondary structure

1215
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi80 – 83ND:4
Beta strandi86 – 88ND:3
Beta strandi91 – 108ND:18
Beta strandi110 – 113ND:4
Beta strandi117 – 124ND:8
Beta strandi126 – 130ND:5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3LKXX-ray2.50B84-136[»]
3MCBX-ray1.90A79-132[»]
3MCEX-ray2.40A/B/C/D81-133[»]
ProteinModelPortaliQ13765.
SMRiQ13765.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13765.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini70 – 135NAC-A/BIEP:Add BLAST66
Domaini176 – 213UBAAdd BLAST38

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni69 – 80Required for DNA-bindingHMP:Add BLAST12
Regioni93 – 108RNA/DNA-bindingAdd BLAST16

Domaini

The positively charged inner surface of the NAC-A/B domain is crucial for NACA localization in the nucleus and DNA-binding. This region is blocked from binding nucleic acids in the heterodimeric complex by a helix region in the beta-subunit, it also displays much higher affinity for RNA than DNA.

Sequence similaritiesi

Belongs to the NAC-alpha family.IKR:

Phylogenomic databases

eggNOGiKOG2239. Eukaryota.
COG1308. LUCA.
GeneTreeiENSGT00440000033468.
HOVERGENiHBG082004.
InParanoidiQ13765.
KOiK03626.
PhylomeDBiQ13765.
TreeFamiTF313348.

Family and domain databases

InterProiView protein in InterPro
IPR016641. EGD2/NACA.
IPR002715. Nas_poly-pep-assoc_cplx_dom.
PANTHERiPTHR21713. PTHR21713. 1 hit.
PfamiView protein in Pfam
PF01849. NAC. 1 hit.
PIRSFiPIRSF015901. NAC_alpha. 1 hit.
SMARTiView protein in SMART
SM01407. NAC. 1 hit.
PROSITEiView protein in PROSITE
PS51151. NAC_AB. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q13765-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPGEATETVP ATEQELPQPQ AETGSGTESD SDESVPELEE QDSTQATTQQ
60 70 80 90 100
AQLAAAAEID EEPVSKAKQS RSEKKARKAM SKLGLRQVTG VTRVTIRKSK
110 120 130 140 150
NILFVITKPD VYKSPASDTY IVFGEAKIED LSQQAQLAAA EKFKVQGEAV
160 170 180 190 200
SNIQENTQTP TVQEESEEEE VDETGVEVKD IELVMSQANV SRAKAVRALK
210
NNSNDIVNAI MELTM
Length:215
Mass (Da):23,384
Last modified:November 1, 1996 - v1
Checksum:i05DC563A8BEF307C
GO
Isoform 2 (identifier: E9PAV3-2) [UniParc]FASTAAdd to basket
The sequence of this isoform can be found in the external entry E9PAV3.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: No experimental confirmation available.
Length:
Mass (Da):
GO
Isoform skNAC (identifier: E9PAV3-1) [UniParc]FASTAAdd to basket
The sequence of this isoform can be found in the external entry E9PAV3.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Length:
Mass (Da):
GO

Sequence cautioni

The sequence AAV83778 differs from that shown. Reason: Erroneous initiation.IKR:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti213L → S in BAD96805 (Ref. 7) IKR:1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY034001 mRNA. Translation: AAK57544.1.
AY911673 mRNA. Translation: AAX14393.1.
X80909 mRNA. Translation: CAA56869.1.
AF054187 mRNA. Translation: AAC99403.1.
AK090650 mRNA. Translation: BAG52208.1.
AK311904 mRNA. Translation: BAG34845.1.
CR450295 mRNA. Translation: CAG29291.1.
AK223085 mRNA. Translation: BAD96805.1.
AC117378 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW96960.1.
BC105120 mRNA. Translation: AAI05121.1.
BC105122 mRNA. Translation: AAI05123.1.
BC106041 mRNA. Translation: AAI06042.1.
AY605660 mRNA. Translation: AAV83778.1. Different initiation.
CCDSiCCDS31837.1. [Q13765-1]
PIRiS49326.
RefSeqiNP_001106672.1. NM_001113201.2. [Q13765-1]
NP_001106673.1. NM_001113202.1. [Q13765-1]
NP_001106674.2. NM_001113203.2.
NP_001307122.1. NM_001320193.1. [Q13765-1]
NP_001307123.1. NM_001320194.1.
NP_005585.1. NM_005594.5. [Q13765-1]
UniGeneiHs.505735.

Genome annotation databases

EnsembliENST00000356769; ENSP00000349212; ENSG00000196531. [Q13765-1]
ENST00000393891; ENSP00000377469; ENSG00000196531. [Q13765-1]
ENST00000546392; ENSP00000446801; ENSG00000196531. [Q13765-1]
ENST00000552540; ENSP00000447821; ENSG00000196531. [Q13765-1]
GeneIDi4666.
KEGGihsa:4666.
UCSCiuc001sly.3. human. [Q13765-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiNACA_HUMAN
AccessioniPrimary (citable) accession number: Q13765
Secondary accession number(s): A8MTN7
, B2R4P8, F8VU71, Q3KQV4, Q53A18, Q53G46
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: November 1, 1996
Last modified: October 25, 2017
This is version 158 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Allergens
    Nomenclature of allergens and list of entries
  2. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families