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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

  1. DNA binding Source: UniProtKB-KW
  2. TBP-class protein binding Source: BHF-UCL
  3. transcription coactivator activity Source: BHF-UCL

GO - Biological processi

  1. cardiac ventricle development Source: BHF-UCL
  2. heart trabecula morphogenesis Source: BHF-UCL
  3. negative regulation of striated muscle cell apoptotic process Source: BHF-UCL
  4. negative regulation of transcription from RNA polymerase II promoter involved in heart development Source: BHF-UCL
  5. positive regulation of cell proliferation involved in heart morphogenesis Source: BHF-UCL
  6. positive regulation of skeletal muscle tissue growth Source: BHF-UCL
  7. positive regulation of transcription from RNA polymerase II promoter involved in heart development Source: BHF-UCL
  8. protein transport Source: UniProtKB-KW
  9. regulation of skeletal muscle fiber development Source: BHF-UCL
  10. skeletal muscle tissue regeneration Source: BHF-UCL
  11. transcription, DNA-templated Source: UniProtKB-KW
  12. translation Source: ProtInc
  13. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Host-virus interaction, Protein transport, Transcription, Transport

Keywords - Ligandi

DNA-binding

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
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:7629. NACA.

Subcellular locationi

Cytoplasm. Nucleus
Note: The heterodimer is located mainly in the cytosol, and the homodimer in the nucleus.

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. extracellular vesicular exosome Source: UniProtKB
  3. nascent polypeptide-associated complex Source: ProtInc
  4. nucleus Source: BHF-UCL
Complete GO annotation...

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

PharmGKBiPA31433.

Protein family/group databases

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 215215Nascent polypeptide-associated complex subunit alphaPRO_0000135576Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431Phosphoserine; by ILK11 Publication
Modified residuei142 – 1421N6-acetyllysine1 Publication
Modified residuei159 – 1591Phosphothreonine; by GSK3-betaBy similarity
Modified residuei161 – 1611Phosphothreonine1 Publication
Modified residuei166 – 1661Phosphoserine5 Publications
Modified residuei186 – 1861Phosphoserine2 Publications
Modified residuei191 – 1911Phosphoserine2 Publications
Modified residuei203 – 2031Phosphoserine1 Publication

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.By similarity2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ13765.
PaxDbiQ13765.
PRIDEiQ13765.

PTM databases

PhosphoSiteiQ13765.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiQ13765.
CleanExiHS_NACA.
ExpressionAtlasiQ13765. baseline and differential.
GenevestigatoriQ13765.

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.By similarity4 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi110748. 38 interactions.
DIPiDIP-43878N.
IntActiQ13765. 24 interactions.
MINTiMINT-5000033.
STRINGi9606.ENSP00000403817.

Structurei

Secondary structure

1
215
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi80 – 834Combined sources
Beta strandi86 – 883Combined sources
Beta strandi91 – 10818Combined sources
Beta strandi110 – 1134Combined sources
Beta strandi117 – 1248Combined sources
Beta strandi126 – 1305Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LKXX-ray2.50B84-136[»]
3MCBX-ray1.90A79-132[»]
3MCEX-ray2.40A/B/C/D81-133[»]
ProteinModelPortaliQ13765.
SMRiQ13765. Positions 79-132.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13765.

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-bindingBy similarityAdd
BLAST
Regioni93 – 10816RNA/DNA-bindingAdd
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.

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

eggNOGiCOG1308.
GeneTreeiENSGT00440000033468.
HOVERGENiHBG082004.
InParanoidiQ13765.
KOiK03626.
OrthoDBiEOG7RNK24.
PhylomeDBiQ13765.
TreeFamiTF313348.

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.
PROSITEiPS51151. NAC_AB. 1 hit.
[Graphical view]

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:925
Mass (Da):94,681
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:2,078
Mass (Da):205,422
GO

Sequence cautioni

The sequence AAV83778.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti213 – 2131L → S in BAD96805 (Ref. 7) Curated

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_001106673.1. NM_001113202.1. [Q13765-1]
NP_001106674.2. NM_001113203.2.
XP_006719484.1. XM_006719421.1. [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.2. human. [Q13765-1]

Polymorphism databases

DMDMi71151996.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

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_001106673.1. NM_001113202.1. [Q13765-1]
NP_001106674.2. NM_001113203.2.
XP_006719484.1. XM_006719421.1. [Q13765-1]
UniGeneiHs.505735.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LKXX-ray2.50B84-136[»]
3MCBX-ray1.90A79-132[»]
3MCEX-ray2.40A/B/C/D81-133[»]
ProteinModelPortaliQ13765.
SMRiQ13765. Positions 79-132.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110748. 38 interactions.
DIPiDIP-43878N.
IntActiQ13765. 24 interactions.
MINTiMINT-5000033.
STRINGi9606.ENSP00000403817.

Protein family/group databases

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

PTM databases

PhosphoSiteiQ13765.

Polymorphism databases

DMDMi71151996.

Proteomic databases

MaxQBiQ13765.
PaxDbiQ13765.
PRIDEiQ13765.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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.2. human. [Q13765-1]

Organism-specific databases

CTDi4666.
GeneCardsiGC12M057106.
H-InvDBHIX0034277.
HGNCiHGNC:7629. NACA.
MIMi601234. gene.
neXtProtiNX_Q13765.
PharmGKBiPA31433.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1308.
GeneTreeiENSGT00440000033468.
HOVERGENiHBG082004.
InParanoidiQ13765.
KOiK03626.
OrthoDBiEOG7RNK24.
PhylomeDBiQ13765.
TreeFamiTF313348.

Miscellaneous databases

ChiTaRSiNACA. human.
EvolutionaryTraceiQ13765.
GeneWikiiNACA_(gene).
GenomeRNAii4666.
NextBioi17982.
PROiQ13765.
SOURCEiSearch...

Gene expression databases

BgeeiQ13765.
CleanExiHS_NACA.
ExpressionAtlasiQ13765. baseline and differential.
GenevestigatoriQ13765.

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.
PROSITEiPS51151. NAC_AB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Novel products of the HuD, HuC, NNP-1 and alpha-internexin genes identified by autologous antibody screening of a pediatric neuroblastoma library."
    Behrends U., Jandl T., Golbeck A., Lechner B., Mueller-Weihrich S., Schmid I., Till H., Berthold F., Voltz R., Mautner J.M.
    Int. J. Cancer 100:669-677(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Neuroblastoma.
  2. "Investigation of alpha nascent polypeptide-associated complex functions in a human CD8(+) T cell ex vivo expansion model using antisense oligonucleotides."
    Al-Shanti N., Steward C.G., Garland R.J., Rowbottom A.W.
    Immunology 112:397-403(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Nascent polypeptide-associate complex (NAC): a novel type of polypeptide binding protein."
    Sakai H., Chew C., Wang S., Wiedmann B., Geromanos S., Tempst P., Wiedmann M.
    Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain.
  4. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Umbilical cord blood.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Cerebellum and Synovium.
  6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  7. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  8. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain and Cervix.
  11. "A new spermatogenesis-related gene."
    Yuan L.G., Tian Y.Q., Qiao Y., Miao S.Y., Wang L.F.
    Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-173 (ISOFORM 1).
    Tissue: Testis.
  12. Lubec G., Chen W.-Q., Sun Y.
    Submitted (NOV-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 101-142 AND 180-192, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Fetal brain cortex.
  13. Bienvenut W.V., Waridel P., Quadroni M.
    Submitted (FEB-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 101-142; 145-192 AND 201-215, PHOSPHORYLATION AT SER-166, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Cervix carcinoma.
  14. "Isolation of cDNA clones coding for IgE autoantigens with serum IgE from atopic dermatitis patients."
    Natter S., Seiberler S., Hufnagl P., Binder B.R., Hirschl A.M., Ring J., Abeck D., Schmidt T., Valent P., Valenta R.
    FASEB J. 12:1559-1569(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALLERGEN.
  15. "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(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "The alpha and beta subunit of the nascent polypeptide-associated complex have distinct functions."
    Beatrix B., Sakai H., Wiedmann M.
    J. Biol. Chem. 275:37838-37845(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BTF3, ASSOCIATION WITH RIBOSOMES, SUBCELLULAR LOCATION.
  17. "The alpha-chain of the nascent polypeptide-associated complex binds to and regulates FADD function."
    Stilo R., Liguoro D., di Jeso B., Leonardi A., Vito P.
    Biochem. Biophys. Res. Commun. 303:1034-1041(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FADD.
  18. "Activation of the JNK-AP-1 signal transduction pathway is associated with pathogenesis and progression of human osteosarcomas."
    Papachristou D.J., Batistatou A., Sykiotis G.P., Varakis I., Papavassiliou A.G.
    Bone 32:364-371(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, POSSIBLE INVOLVEMENT IN OSTEOSARCOMA.
  19. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-43, SUBCELLULAR LOCATION.
  20. Cited for: FUNCTION.
  21. "Emergence of young human genes after a burst of retroposition in primates."
    Marques A.C., Dupanloup I., Vinckenbosch N., Reymond A., Kaessmann H.
    PLoS Biol. 3:E357-E357(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  22. "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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  24. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  25. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161; SER-166 AND SER-191, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  26. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  28. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-142, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  29. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186; SER-191 AND SER-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  30. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  31. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  32. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  33. "The crystal structure of the human nascent polypeptide-associated complex domain reveals a nucleic acid-binding region on the NACA subunit."
    Liu Y., Hu Y., Li X., Niu L., Teng M.
    Biochemistry 49:2890-2896(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 84-136, SUBUNIT, DNA/RNA-BINDING REGION, SUBCELLULAR LOCATION.
  34. "Crystal structures of NAC domains of human nascent polypeptide-associated complex (NAC) and its alphaNAC subunit."
    Wang L., Zhang W., Wang L., Zhang X.C., Li X., Rao Z.
    Protein Cell 1:406-416(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 79-132, SUBUNIT.

Entry informationi

Entry nameiNACA_HUMAN
AccessioniPrimary (citable) accession number: Q13765
Secondary accession number(s): A8MTN7
, B2R4P8, F8VU71, Q3KQV4, Q53A18, Q53G46
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: November 1, 1996
Last modified: March 4, 2015
This is version 134 of the entry and version 1 of the sequence. [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

External Data

Dasty 3

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 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.