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Protein

Nascent polypeptide-associated complex subunit alpha

Gene

Naca

Organism
Mus musculus (Mouse)
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) (By similarity). Isoform 1 and isoform 2 appear to bind DNA and play roles in transcription. Isoform 1 may function as a specific coactivator for JUN, acting to stabilize the interaction of JUN homodimers with promoter elements.By similarity5 Publications

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • TBP-class protein binding Source: MGI
  • transcription coactivator activity Source: MGI

GO - Biological processi

  • cardiac ventricle development Source: BHF-UCL
  • heart trabecula morphogenesis Source: BHF-UCL
  • myoblast migration Source: MGI
  • negative regulation of striated muscle cell apoptotic process Source: BHF-UCL
  • negative regulation of transcription from RNA polymerase II promoter involved in heart development Source: BHF-UCL
  • positive regulation of cell proliferation involved in heart morphogenesis Source: BHF-UCL
  • positive regulation of skeletal muscle tissue growth Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter involved in heart development Source: BHF-UCL
  • protein transport Source: UniProtKB-KW
  • regulation of skeletal muscle fiber development Source: BHF-UCL
  • skeletal muscle tissue regeneration Source: BHF-UCL
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Protein transport, Transcription, Transport

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Nascent polypeptide-associated complex subunit alpha
Alternative name(s):
Alpha-NAC
Alpha-NAC/1.9.2
Gene namesi
Name:Naca
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:106095. Naca.

Subcellular locationi

  • Cytoplasm
  • Nucleus

  • Note: The heterodimer is located mainly in the cytosol, and the homodimer in the nucleus.By similarity

GO - Cellular componenti

  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 215215Nascent polypeptide-associated complex subunit alphaPRO_0000135577Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431Phosphoserine; by ILK11 Publication
Modified residuei142 – 1421N6-acetyllysineCombined sources
Modified residuei159 – 1591Phosphothreonine; by GSK3-betaCombined sources1 Publication
Modified residuei161 – 1611PhosphothreonineBy similarity
Modified residuei166 – 1661PhosphoserineCombined sources
Modified residuei186 – 1861PhosphoserineBy similarity
Modified residuei191 – 1911PhosphoserineBy similarity
Modified residuei203 – 2031PhosphoserineBy similarity

Post-translational modificationi

Phosphorylation of Ser-43 by ILK during cell adhesion may promote nuclear localization. Phosphorylation of Thr-159 by GSK3B may promote proteasome mediated degradation.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ60817.
MaxQBiQ60817.
PaxDbiQ60817.
PRIDEiQ60817.

PTM databases

iPTMnetiQ60817.

Expressioni

Tissue specificityi

Isoform 1 appears to be ubiquitously expressed.3 Publications

Developmental stagei

Expressed concomitant with the onset of mineralization in ossification centers of developing bone.1 Publication

Gene expression databases

BgeeiQ60817.
ExpressionAtlasiQ60817. baseline.
GenevisibleiQ60817. MM.

Interactioni

Subunit structurei

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 (By similarity). Interacts with TBP and JUN.By similarity3 Publications

GO - Molecular functioni

  • TBP-class protein binding Source: MGI

Protein-protein interaction databases

BioGridi201682. 8 interactions.
IntActiQ60817. 2 interactions.
STRINGi10090.ENSMUSP00000089680.

Structurei

3D structure databases

ProteinModelPortaliQ60817.
SMRiQ60817. Positions 79-132.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini70 – 13566NAC-A/BPROSITE-ProRule annotationAdd
BLAST
Domaini176 – 21338UBAAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni69 – 8012Required for DNA-bindingAdd
BLAST
Regioni93 – 10816RNA/DNA-bindingBy similarityAdd
BLAST

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 (By similarity).By similarity

Sequence similaritiesi

Belongs to the NAC-alpha family.Curated
Contains 1 NAC-A/B (NAC-alpha/beta) domain.PROSITE-ProRule annotation
Contains 1 UBA domain.Curated

Phylogenomic databases

eggNOGiKOG2239. Eukaryota.
COG1308. LUCA.
GeneTreeiENSGT00440000033468.
HOGENOMiHOG000239674.
HOVERGENiHBG082004.

Family and domain databases

InterProiIPR016641. EGD2/NACA.
IPR002715. Nas_poly-pep-assoc_cplx_dom.
[Graphical view]
PANTHERiPTHR21713. PTHR21713. 1 hit.
PfamiPF01849. NAC. 1 hit.
[Graphical view]
PIRSFiPIRSF015901. NAC_alpha. 1 hit.
SMARTiSM01407. NAC. 1 hit.
[Graphical view]
PROSITEiPS51151. NAC_AB. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q60817-1) [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 QDSTQTATQQ
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:i0E7D5D90304E306D
GO
Isoform 2 (identifier: P70670-1) [UniParc]FASTAAdd to basket

Also known as: Gp220, skNAC

The sequence of this isoform can be found in the external entry P70670.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Length:2,187
Mass (Da):220,499
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti52 – 521Q → K in BAE40130 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U22151 mRNA. Translation: AAB80961.1.
U48363 Genomic DNA. Translation: AAB18733.1.
AK146197 mRNA. Translation: BAE26971.1.
AK151928 mRNA. Translation: BAE30804.1.
AK161678 mRNA. Translation: BAE36526.1.
AK168023 mRNA. Translation: BAE40008.1.
AK168169 mRNA. Translation: BAE40130.1.
AK168607 mRNA. Translation: BAE40474.1.
AK169432 mRNA. Translation: BAE41173.1.
AK169435 mRNA. Translation: BAE41176.1.
BC029830 mRNA. Translation: AAH29830.1.
BC083340 mRNA. Translation: AAH83340.1.
BC099375 mRNA. Translation: AAH99375.1.
CCDSiCCDS24258.1. [Q60817-1]
PIRiT30827.
RefSeqiNP_001269905.1. NM_001282976.1. [Q60817-1]
NP_038636.2. NM_013608.3. [Q60817-1]
UniGeneiMm.3746.

Genome annotation databases

EnsembliENSMUST00000073868; ENSMUSP00000073532; ENSMUSG00000061315. [Q60817-1]
GeneIDi17938.
UCSCiuc007hlb.2. mouse. [Q60817-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U22151 mRNA. Translation: AAB80961.1.
U48363 Genomic DNA. Translation: AAB18733.1.
AK146197 mRNA. Translation: BAE26971.1.
AK151928 mRNA. Translation: BAE30804.1.
AK161678 mRNA. Translation: BAE36526.1.
AK168023 mRNA. Translation: BAE40008.1.
AK168169 mRNA. Translation: BAE40130.1.
AK168607 mRNA. Translation: BAE40474.1.
AK169432 mRNA. Translation: BAE41173.1.
AK169435 mRNA. Translation: BAE41176.1.
BC029830 mRNA. Translation: AAH29830.1.
BC083340 mRNA. Translation: AAH83340.1.
BC099375 mRNA. Translation: AAH99375.1.
CCDSiCCDS24258.1. [Q60817-1]
PIRiT30827.
RefSeqiNP_001269905.1. NM_001282976.1. [Q60817-1]
NP_038636.2. NM_013608.3. [Q60817-1]
UniGeneiMm.3746.

3D structure databases

ProteinModelPortaliQ60817.
SMRiQ60817. Positions 79-132.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201682. 8 interactions.
IntActiQ60817. 2 interactions.
STRINGi10090.ENSMUSP00000089680.

PTM databases

iPTMnetiQ60817.

Proteomic databases

EPDiQ60817.
MaxQBiQ60817.
PaxDbiQ60817.
PRIDEiQ60817.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000073868; ENSMUSP00000073532; ENSMUSG00000061315. [Q60817-1]
GeneIDi17938.
UCSCiuc007hlb.2. mouse. [Q60817-1]

Organism-specific databases

CTDi4666.
MGIiMGI:106095. Naca.

Phylogenomic databases

eggNOGiKOG2239. Eukaryota.
COG1308. LUCA.
GeneTreeiENSGT00440000033468.
HOGENOMiHOG000239674.
HOVERGENiHBG082004.

Miscellaneous databases

SOURCEiSearch...

Gene expression databases

BgeeiQ60817.
ExpressionAtlasiQ60817. baseline.
GenevisibleiQ60817. MM.

Family and domain databases

InterProiIPR016641. EGD2/NACA.
IPR002715. Nas_poly-pep-assoc_cplx_dom.
[Graphical view]
PANTHERiPTHR21713. PTHR21713. 1 hit.
PfamiPF01849. NAC. 1 hit.
[Graphical view]
PIRSFiPIRSF015901. NAC_alpha. 1 hit.
SMARTiSM01407. NAC. 1 hit.
[Graphical view]
PROSITEiPS51151. NAC_AB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Differential splicing-in of a proline-rich exon converts alphaNAC into a muscle-specific transcription factor."
    Yotov W.V., St Arnaud R.
    Genes Dev. 10:1763-1772(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), FUNCTION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
  2. "The alpha chain of the nascent polypeptide-associated complex functions as a transcriptional coactivator."
    Yotov W.V., Moreau A., St Arnaud R.
    Mol. Cell. Biol. 18:1303-1311(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH TBP, SUBCELLULAR LOCATION.
  3. Yotov W.V., St Arnaud R.
    Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: BALB/cJ, C57BL/6J and DBA/2.
    Tissue: Bone marrow, Embryo, Heart and Kidney.
  5. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J and Czech II.
    Tissue: Brain, Mammary tumor and Placenta.
  6. "Unregulated exposure of the ribosomal M-site caused by NAC depletion results in delivery of non-secretory polypeptides to the Sec61 complex."
    Moeller I., Beatrix B., Kreibich G., Sakai H., Lauring B., Wiedmann M.
    FEBS Lett. 441:1-5(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  7. "Bone-specific expression of the alpha chain of the nascent polypeptide-associated complex, a coactivator potentiating c-Jun-mediated transcription."
    Moreau A., Yotov W.V., Glorieux F.H., St Arnaud R.
    Mol. Cell. Biol. 18:1312-1321(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH JUN, DEVELOPMENTAL STAGE.
  8. "Cloning of novel injury-regulated genes. Implications for an important role of the muscle-specific protein skNAC in muscle repair."
    Munz B., Wiedmann M., Lochmueller H., Werner S.
    J. Biol. Chem. 274:13305-13310(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
  9. "GSK3 beta-dependent phosphorylation of the alpha NAC coactivator regulates its nuclear translocation and proteasome-mediated degradation."
    Quelo I., Akhouayri O., Prud'homme J., St Arnaud R.
    Biochemistry 43:2906-2914(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, DEGRADATION, PHOSPHORYLATION AT THR-159.
  10. "Integrin-linked kinase regulates the nuclear entry of the c-Jun coactivator alpha-NAC and its coactivation potency."
    Quelo I., Gauthier C., Hannigan G.E., Dedhar S., St-Arnaud R.
    J. Biol. Chem. 279:43893-43899(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ILK, PHOSPHORYLATION AT SER-43.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  12. "Sequence-specific DNA binding by the alphaNAC coactivator is required for potentiation of c-Jun-dependent transcription of the osteocalcin gene."
    Akhouayri O., Quelo I., St-Arnaud R.
    Mol. Cell. Biol. 25:3452-3460(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-159 AND SER-166, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  16. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-142, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiNACA_MOUSE
AccessioniPrimary (citable) accession number: Q60817
Secondary accession number(s): Q3THR6, Q4FZL8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 127 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.