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Q13765 (NACA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nascent polypeptide-associated complex subunit alpha

Short name=NAC-alpha
Alternative name(s):
Alpha-NAC
Allergen=Hom s 2
Gene names
Name:NACA
ORF Names:HSD48
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length215 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.15 Ref.16 Ref.20

Subunit structure

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. Ref.16 Ref.17 Ref.33 Ref.34

Subcellular location

Cytoplasm. Nucleus. Note: The heterodimer is located mainly in the cytosol, and the homodimer in the nucleus. Ref.16 Ref.18 Ref.19 Ref.33

Tissue specificity

Ubiquitously expressed. Ref.21

Domain

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.

Post-translational modification

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.

Allergenic properties

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. Ref.14

Sequence similarities

Belongs to the NAC-alpha family.

Contains 1 NAC-A/B (NAC-alpha/beta) domain.

Contains 1 UBA domain.

Sequence caution

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

Ontologies

Keywords
   Biological processHost-virus interaction
Protein transport
Transcription
Transport
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DiseaseAllergen
   LigandDNA-binding
   Molecular functionChaperone
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcardiac ventricle development

Inferred from sequence or structural similarity. Source: BHF-UCL

heart trabecula morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of striated muscle cell apoptotic process

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of transcription from RNA polymerase II promoter involved in heart development

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of cell proliferation involved in heart morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of skeletal muscle tissue growth

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter involved in heart development

Inferred from sequence or structural similarity. Source: BHF-UCL

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of skeletal muscle fiber development

Inferred from sequence or structural similarity. Source: BHF-UCL

skeletal muscle tissue regeneration

Inferred from sequence or structural similarity. Source: BHF-UCL

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

translation

Traceable author statement PubMed 8047162. Source: ProtInc

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: BHF-UCL

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

nascent polypeptide-associated complex

Traceable author statement PubMed 8047162. Source: ProtInc

nucleus

Inferred from sequence or structural similarity. Source: BHF-UCL

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

TBP-class protein binding

Inferred from sequence or structural similarity. Source: BHF-UCL

transcription coactivator activity

Inferred from sequence or structural similarity. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TXLNAP402222EBI-712216,EBI-359793

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13765-1)

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.
Isoform 2 (identifier: E9PAV3-2)

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.
Isoform skNAC (identifier: E9PAV3-1)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 215215Nascent polypeptide-associated complex subunit alpha
PRO_0000135576

Regions

Domain70 – 13566NAC-A/B
Domain176 – 21338UBA
Region69 – 8012Required for DNA-binding By similarity
Region93 – 10816RNA/DNA-binding

Amino acid modifications

Modified residue431Phosphoserine; by ILK1 Ref.19
Modified residue1421N6-acetyllysine Ref.28
Modified residue1591Phosphothreonine; by GSK3-beta By similarity
Modified residue1611Phosphothreonine Ref.25
Modified residue1661Phosphoserine Ref.13 Ref.24 Ref.25 Ref.27 Ref.31
Modified residue1861Phosphoserine Ref.23 Ref.29
Modified residue1911Phosphoserine Ref.25 Ref.29
Modified residue2031Phosphoserine Ref.29

Experimental info

Sequence conflict2131L → S in BAD96805. Ref.7

Secondary structure

............. 215
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 05DC563A8BEF307C

FASTA21523,384
        10         20         30         40         50         60 
MPGEATETVP ATEQELPQPQ AETGSGTESD SDESVPELEE QDSTQATTQQ AQLAAAAEID 

        70         80         90        100        110        120 
EEPVSKAKQS RSEKKARKAM SKLGLRQVTG VTRVTIRKSK NILFVITKPD VYKSPASDTY 

       130        140        150        160        170        180 
IVFGEAKIED LSQQAQLAAA EKFKVQGEAV SNIQENTQTP TVQEESEEEE VDETGVEVKD 

       190        200        210 
IELVMSQANV SRAKAVRALK NNSNDIVNAI MELTM 

« Hide

Isoform 2 [UniParc].

See E9PAV3.

Isoform skNAC [UniParc].

See E9PAV3.

References

« Hide 'large scale' references
[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(2002) [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(2004) [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 (AUG-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. expand/collapse author list , Gu J., Chen S.-J., Chen Z.
Genome Res. 10:1546-1560(2000) [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. expand/collapse author list , 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(2004) [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 (MAY-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 (APR-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. expand/collapse author list , 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(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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(2004) [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 (APR-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 (DEC-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 (MAR-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(1998) [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(1998) [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(2000) [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(2003) [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(2003) [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(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-43, SUBCELLULAR LOCATION.
[20]"NACA is a positive regulator of human erythroid-cell differentiation."
Lopez S., Stuhl L., Fichelson S., Dubart-Kupperschmitt A., St Arnaud R., Galindo J.-R., Murati A., Berda N., Dubreuil P., Gomez S.
J. Cell Sci. 118:1595-1605(2005) [PubMed] [Europe PMC] [Abstract]
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(2005) [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(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
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(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[25]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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(2009) [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(2009) [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(2009) [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(2010) [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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[32]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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(2010) [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(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 79-132, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS49326.
RefSeqNP_001106673.1. NM_001113202.1.
NP_001106674.2. NM_001113203.2.
UniGeneHs.505735.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3LKXX-ray2.50B84-136[»]
3MCBX-ray1.90A79-132[»]
3MCEX-ray2.40A/B/C/D81-133[»]
ProteinModelPortalQ13765.
SMRQ13765. Positions 79-213.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110748. 37 interactions.
IntActQ13765. 23 interactions.
MINTMINT-5000033.
STRING9606.ENSP00000403817.

Protein family/group databases

Allergome3323. Hom s 2.0101.
412. Hom s 2.

PTM databases

PhosphoSiteQ13765.

Polymorphism databases

DMDM71151996.

Proteomic databases

PaxDbQ13765.
PRIDEQ13765.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000356769; ENSP00000349212; ENSG00000196531. [Q13765-1]
ENST00000393891; ENSP00000377469; ENSG00000196531. [Q13765-1]
ENST00000546392; ENSP00000446801; ENSG00000196531. [Q13765-1]
ENST00000552540; ENSP00000447821; ENSG00000196531. [Q13765-1]
GeneID4666.
KEGGhsa:4666.
UCSCuc001sly.2. human. [Q13765-1]

Organism-specific databases

CTD4666.
GeneCardsGC12M057106.
H-InvDBHIX0034277.
HGNCHGNC:7629. NACA.
MIM601234. gene.
neXtProtNX_Q13765.
PharmGKBPA31433.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1308.
HOVERGENHBG082004.
KOK03626.
OrthoDBEOG7RNK24.
PhylomeDBQ13765.
TreeFamTF313348.

Gene expression databases

ArrayExpressQ13765.
BgeeQ13765.
CleanExHS_NACA.
GenevestigatorQ13765.

Family and domain databases

InterProIPR016641. EGD2/NACA.
IPR002715. Nas_poly-pep-assoc_cplx_dom.
[Graphical view]
PANTHERPTHR21713. PTHR21713. 1 hit.
PfamPF01849. NAC. 1 hit.
[Graphical view]
PIRSFPIRSF015901. NAC_alpha. 1 hit.
PROSITEPS51151. NAC_AB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNACA. human.
EvolutionaryTraceQ13765.
GeneWikiNACA_(gene).
GenomeRNAi4666.
NextBio17982.
PROQ13765.
SOURCESearch...

Entry information

Entry nameNACA_HUMAN
AccessionPrimary (citable) accession number: Q13765
Secondary accession number(s): A8MTN7 expand/collapse secondary AC list , B2R4P8, F8VU71, Q3KQV4, Q53A18, Q53G46
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM

Allergens

Nomenclature of allergens and list of entries