NACA_HUMAN
ID NACA_HUMAN Reviewed; 215 AA.
AC Q13765; A8MTN7; B2R4P8; F8VU71; Q3KQV4; Q53A18; Q53G46;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Nascent polypeptide-associated complex subunit alpha;
DE Short=NAC-alpha;
DE AltName: Full=Alpha-NAC;
DE AltName: Allergen=Hom s 2;
GN Name=NACA; ORFNames=HSD48;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Neuroblastoma;
RX PubMed=12209604; DOI=10.1002/ijc.10550;
RA Behrends U., Jandl T., Golbeck A., Lechner B., Mueller-Weihrich S.,
RA Schmid I., Till H., Berthold F., Voltz R., Mautner J.M.;
RT "Novel products of the HuD, HuC, NNP-1 and alpha-internexin genes
RT identified by autologous antibody screening of a pediatric neuroblastoma
RT library.";
RL Int. J. Cancer 100:669-677(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=15196207; DOI=10.1111/j.1365-2567.2004.01893.x;
RA Al-Shanti N., Steward C.G., Garland R.J., Rowbottom A.W.;
RT "Investigation of alpha nascent polypeptide-associated complex functions in
RT a human CD8(+) T cell ex vivo expansion model using antisense
RT oligonucleotides.";
RL Immunology 112:397-403(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Sakai H., Chew C., Wang S., Wiedmann B., Geromanos S., Tempst P.,
RA Wiedmann M.;
RT "Nascent polypeptide-associate complex (NAC): a novel type of polypeptide
RT binding protein.";
RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum, and Synovium;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Cervix;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-173 (ISOFORM 1).
RC TISSUE=Testis;
RA Yuan L.G., Tian Y.Q., Qiao Y., Miao S.Y., Wang L.F.;
RT "A new spermatogenesis-related gene.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP PROTEIN SEQUENCE OF 101-142 AND 180-192, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [13]
RP PROTEIN SEQUENCE OF 101-142; 145-192 AND 201-215, PHOSPHORYLATION AT
RP SER-166, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [14]
RP ALLERGEN.
RX PubMed=9806765; DOI=10.1096/fasebj.12.14.1559;
RA Natter S., Seiberler S., Hufnagl P., Binder B.R., Hirschl A.M., Ring J.,
RA Abeck D., Schmidt T., Valent P., Valenta R.;
RT "Isolation of cDNA clones coding for IgE autoantigens with serum IgE from
RT atopic dermatitis patients.";
RL FASEB J. 12:1559-1569(1998).
RN [15]
RP FUNCTION.
RX PubMed=9877153; DOI=10.1016/s0014-5793(98)01440-9;
RA Moeller I., Beatrix B., Kreibich G., Sakai H., Lauring B., Wiedmann M.;
RT "Unregulated exposure of the ribosomal M-site caused by NAC depletion
RT results in delivery of non-secretory polypeptides to the Sec61 complex.";
RL FEBS Lett. 441:1-5(1998).
RN [16]
RP FUNCTION, INTERACTION WITH BTF3, ASSOCIATION WITH RIBOSOMES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=10982809; DOI=10.1074/jbc.m006368200;
RA Beatrix B., Sakai H., Wiedmann M.;
RT "The alpha and beta subunit of the nascent polypeptide-associated complex
RT have distinct functions.";
RL J. Biol. Chem. 275:37838-37845(2000).
RN [17]
RP INTERACTION WITH FADD.
RX PubMed=12684039; DOI=10.1016/s0006-291x(03)00487-x;
RA Stilo R., Liguoro D., di Jeso B., Leonardi A., Vito P.;
RT "The alpha-chain of the nascent polypeptide-associated complex binds to and
RT regulates FADD function.";
RL Biochem. Biophys. Res. Commun. 303:1034-1041(2003).
RN [18]
RP SUBCELLULAR LOCATION, AND POSSIBLE INVOLVEMENT IN OSTEOSARCOMA.
RX PubMed=12689679; DOI=10.1016/s8756-3282(03)00026-7;
RA Papachristou D.J., Batistatou A., Sykiotis G.P., Varakis I.,
RA Papavassiliou A.G.;
RT "Activation of the JNK-AP-1 signal transduction pathway is associated with
RT pathogenesis and progression of human osteosarcomas.";
RL Bone 32:364-371(2003).
RN [19]
RP PHOSPHORYLATION AT SER-43, AND SUBCELLULAR LOCATION.
RX PubMed=15299025; DOI=10.1074/jbc.m406310200;
RA Quelo I., Gauthier C., Hannigan G.E., Dedhar S., St-Arnaud R.;
RT "Integrin-linked kinase regulates the nuclear entry of the c-Jun
RT coactivator alpha-NAC and its coactivation potency.";
RL J. Biol. Chem. 279:43893-43899(2004).
RN [20]
RP FUNCTION.
RX PubMed=15784678; DOI=10.1242/jcs.02295;
RA Lopez S., Stuhl L., Fichelson S., Dubart-Kupperschmitt A., St Arnaud R.,
RA Galindo J.-R., Murati A., Berda N., Dubreuil P., Gomez S.;
RT "NACA is a positive regulator of human erythroid-cell differentiation.";
RL J. Cell Sci. 118:1595-1605(2005).
RN [21]
RP TISSUE SPECIFICITY.
RX PubMed=16201836; DOI=10.1371/journal.pbio.0030357;
RA Marques A.C., Dupanloup I., Vinckenbosch N., Reymond A., Kaessmann H.;
RT "Emergence of young human genes after a burst of retroposition in
RT primates.";
RL PLoS Biol. 3:E357-E357(2005).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161; SER-166 AND SER-191, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [28]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-142, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186; SER-191 AND SER-203, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [30]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [33]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [34]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [35]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-142, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [36]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 84-136, SUBUNIT, DNA/RNA-BINDING
RP REGION, AND SUBCELLULAR LOCATION.
RX PubMed=20214399; DOI=10.1021/bi902050p;
RA Liu Y., Hu Y., Li X., Niu L., Teng M.;
RT "The crystal structure of the human nascent polypeptide-associated complex
RT domain reveals a nucleic acid-binding region on the NACA subunit.";
RL Biochemistry 49:2890-2896(2010).
RN [37]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 79-132, AND SUBUNIT.
RX PubMed=21203952; DOI=10.1007/s13238-010-0049-3;
RA Wang L., Zhang W., Wang L., Zhang X.C., Li X., Rao Z.;
RT "Crystal structures of NAC domains of human nascent polypeptide-associated
RT complex (NAC) and its alphaNAC subunit.";
RL Protein Cell 1:406-416(2010).
CC -!- FUNCTION: Prevents inappropriate targeting of non-secretory
CC polypeptides to the endoplasmic reticulum (ER). Binds to nascent
CC polypeptide chains as they emerge from the ribosome and blocks their
CC interaction with the signal recognition particle (SRP), which normally
CC targets nascent secretory peptides to the ER. Also reduces the inherent
CC affinity of ribosomes for protein translocation sites in the ER
CC membrane (M sites). May act as a specific coactivator for JUN, binding
CC to DNA and stabilizing the interaction of JUN homodimers with target
CC gene promoters. {ECO:0000269|PubMed:10982809,
CC ECO:0000269|PubMed:15784678, ECO:0000269|PubMed:9877153}.
CC -!- SUBUNIT: Interacts with TBP and JUN (By similarity). Part of the
CC nascent polypeptide-associated complex (NAC), which is a heterodimer of
CC NACA and BTF3 (via NAC-A/B domains). NAC associates with ribosomes
CC through the BTF3/NACB subunit and contacts the ribosomal protein L23,
CC which is positioned near the exiting site. Both subunits can contact
CC nascent polypeptide chains. NACA may also form homodimers, and only
CC this form binds DNA. {ECO:0000250, ECO:0000269|PubMed:10982809,
CC ECO:0000269|PubMed:12684039, ECO:0000269|PubMed:20214399,
CC ECO:0000269|PubMed:21203952}.
CC -!- INTERACTION:
CC Q13765; P05067: APP; NbExp=3; IntAct=EBI-712216, EBI-77613;
CC Q13765; P40222: TXLNA; NbExp=2; IntAct=EBI-712216, EBI-359793;
CC Q13765; P13051-2: UNG; NbExp=3; IntAct=EBI-712216, EBI-25834258;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10982809,
CC ECO:0000269|PubMed:12689679, ECO:0000269|PubMed:15299025,
CC ECO:0000269|PubMed:20214399}. Nucleus {ECO:0000269|PubMed:12689679,
CC ECO:0000269|PubMed:15299025, ECO:0000269|PubMed:20214399}. Note=The
CC heterodimer is located mainly in the cytosol, and the homodimer in the
CC nucleus. {ECO:0000269|PubMed:10982809, ECO:0000269|PubMed:20214399}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q13765-1; Sequence=Displayed;
CC Name=skNAC-2; Synonyms=2;
CC IsoId=E9PAV3-2; Sequence=External;
CC Name=skNAC;
CC IsoId=E9PAV3-1; Sequence=External;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:16201836}.
CC -!- DOMAIN: The positively charged inner surface of the NAC-A/B domain is
CC crucial for NACA localization in the nucleus and DNA-binding. This
CC region is blocked from binding nucleic acids in the heterodimeric
CC complex by a helix region in the beta-subunit, it also displays much
CC higher affinity for RNA than DNA.
CC -!- PTM: Phosphorylation of Thr-159 by GSK3B may promote proteasome
CC mediated degradation (By similarity). Phosphorylation of Ser-43 by ILK
CC during cell adhesion may promote nuclear localization. {ECO:0000250,
CC ECO:0000269|PubMed:15299025, ECO:0000269|Ref.13}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE from
CC atopic dermatitis (AD) patients. Identified as an IgE autoantigen in
CC atopic dermatitis (AD) patients with severe skin manifestations.
CC {ECO:0000269|PubMed:9806765}.
CC -!- SIMILARITY: Belongs to the NAC-alpha family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAV83778.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY034001; AAK57544.1; -; mRNA.
DR EMBL; AY911673; AAX14393.1; -; mRNA.
DR EMBL; X80909; CAA56869.1; -; mRNA.
DR EMBL; AF054187; AAC99403.1; -; mRNA.
DR EMBL; AK090650; BAG52208.1; -; mRNA.
DR EMBL; AK311904; BAG34845.1; -; mRNA.
DR EMBL; CR450295; CAG29291.1; -; mRNA.
DR EMBL; AK223085; BAD96805.1; -; mRNA.
DR EMBL; AC117378; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW96960.1; -; Genomic_DNA.
DR EMBL; BC105120; AAI05121.1; -; mRNA.
DR EMBL; BC105122; AAI05123.1; -; mRNA.
DR EMBL; BC106041; AAI06042.1; -; mRNA.
DR EMBL; AY605660; AAV83778.1; ALT_INIT; mRNA.
DR CCDS; CCDS31837.1; -. [Q13765-1]
DR PIR; S49326; S49326.
DR RefSeq; NP_001106672.1; NM_001113201.2. [Q13765-1]
DR RefSeq; NP_001106673.1; NM_001113202.1. [Q13765-1]
DR RefSeq; NP_001106674.2; NM_001113203.2.
DR RefSeq; NP_001307122.1; NM_001320193.1. [Q13765-1]
DR RefSeq; NP_001307123.1; NM_001320194.1.
DR RefSeq; NP_005585.1; NM_005594.5. [Q13765-1]
DR PDB; 3LKX; X-ray; 2.50 A; B=84-136.
DR PDB; 3MCB; X-ray; 1.90 A; A=79-132.
DR PDB; 3MCE; X-ray; 2.40 A; A/B/C/D=81-133.
DR PDB; 7QWQ; EM; 2.83 A; t=1-215.
DR PDB; 7QWR; EM; 2.90 A; t=1-215.
DR PDB; 7QWS; EM; 3.40 A; t=1-215.
DR PDBsum; 3LKX; -.
DR PDBsum; 3MCB; -.
DR PDBsum; 3MCE; -.
DR PDBsum; 7QWQ; -.
DR PDBsum; 7QWR; -.
DR PDBsum; 7QWS; -.
DR AlphaFoldDB; Q13765; -.
DR SMR; Q13765; -.
DR BioGRID; 110748; 157.
DR ComplexPortal; CPX-676; Nascent polypeptide-associated complex.
DR DIP; DIP-43878N; -.
DR IntAct; Q13765; 47.
DR MINT; Q13765; -.
DR Allergome; 3323; Hom s 2.0101.
DR Allergome; 412; Hom s 2.
DR iPTMnet; Q13765; -.
DR MetOSite; Q13765; -.
DR SwissPalm; Q13765; -.
DR BioMuta; NACA; -.
DR DMDM; 71151996; -.
DR EPD; Q13765; -.
DR jPOST; Q13765; -.
DR MassIVE; Q13765; -.
DR MaxQB; Q13765; -.
DR PeptideAtlas; Q13765; -.
DR PRIDE; Q13765; -.
DR ProteomicsDB; 28706; -.
DR ProteomicsDB; 59679; -. [Q13765-1]
DR TopDownProteomics; Q13765-1; -. [Q13765-1]
DR Antibodypedia; 28384; 97 antibodies from 17 providers.
DR DNASU; 4666; -.
DR Ensembl; ENST00000356769.7; ENSP00000349212.3; ENSG00000196531.14. [Q13765-1]
DR Ensembl; ENST00000393891.8; ENSP00000377469.4; ENSG00000196531.14. [Q13765-1]
DR Ensembl; ENST00000546392.6; ENSP00000446801.1; ENSG00000196531.14. [Q13765-1]
DR Ensembl; ENST00000552540.5; ENSP00000447821.1; ENSG00000196531.14. [Q13765-1]
DR Ensembl; ENST00000678066.1; ENSP00000503345.1; ENSG00000196531.14. [Q13765-1]
DR GeneID; 4666; -.
DR KEGG; hsa:4666; -.
DR UCSC; uc001sly.3; human. [Q13765-1]
DR CTD; 4666; -.
DR DisGeNET; 4666; -.
DR GeneCards; NACA; -.
DR HGNC; HGNC:7629; NACA.
DR HPA; ENSG00000196531; Low tissue specificity.
DR MIM; 601234; gene.
DR neXtProt; NX_Q13765; -.
DR OpenTargets; ENSG00000196531; -.
DR PharmGKB; PA31433; -.
DR VEuPathDB; HostDB:ENSG00000196531; -.
DR GeneTree; ENSGT00440000033468; -.
DR HOGENOM; CLU_057806_1_2_1; -.
DR InParanoid; Q13765; -.
DR OrthoDB; 1331328at2759; -.
DR PhylomeDB; Q13765; -.
DR TreeFam; TF313348; -.
DR PathwayCommons; Q13765; -.
DR SignaLink; Q13765; -.
DR SIGNOR; Q13765; -.
DR BioGRID-ORCS; 4666; 509 hits in 1079 CRISPR screens.
DR ChiTaRS; NACA; human.
DR EvolutionaryTrace; Q13765; -.
DR GeneWiki; NACA_(gene); -.
DR GenomeRNAi; 4666; -.
DR Pharos; Q13765; Tbio.
DR Proteomes; UP000005640; Chromosome 12.
DR Bgee; ENSG00000196531; Expressed in tendon of biceps brachii and 209 other tissues.
DR ExpressionAtlas; Q13765; baseline and differential.
DR Genevisible; Q13765; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005854; C:nascent polypeptide-associated complex; IPI:ComplexPortal.
DR GO; GO:0005634; C:nucleus; NAS:BHF-UCL.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003713; F:transcription coactivator activity; NAS:BHF-UCL.
DR GO; GO:0003231; P:cardiac ventricle development; ISS:BHF-UCL.
DR GO; GO:0061384; P:heart trabecula morphogenesis; ISS:BHF-UCL.
DR GO; GO:1905551; P:negative regulation of protein localization to endoplasmic reticulum; IDA:ComplexPortal.
DR GO; GO:0010664; P:negative regulation of striated muscle cell apoptotic process; ISS:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR GO; GO:2000138; P:positive regulation of cell proliferation involved in heart morphogenesis; ISS:BHF-UCL.
DR GO; GO:0048633; P:positive regulation of skeletal muscle tissue growth; ISS:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0048742; P:regulation of skeletal muscle fiber development; ISS:BHF-UCL.
DR GO; GO:0043403; P:skeletal muscle tissue regeneration; ISS:BHF-UCL.
DR GO; GO:0006412; P:translation; TAS:ProtInc.
DR GO; GO:0042060; P:wound healing; ISS:BHF-UCL.
DR Gene3D; 2.20.70.30; -; 1.
DR IDEAL; IID00472; -.
DR InterPro; IPR016641; EGD2/NACA.
DR InterPro; IPR044034; NAC-like_UBA.
DR InterPro; IPR038187; NAC_A/B_dom_sf.
DR InterPro; IPR002715; Nas_poly-pep-assoc_cplx_dom.
DR PANTHER; PTHR21713; PTHR21713; 1.
DR Pfam; PF19026; HYPK_UBA; 1.
DR Pfam; PF01849; NAC; 1.
DR PIRSF; PIRSF015901; NAC_alpha; 1.
DR SMART; SM01407; NAC; 1.
DR PROSITE; PS51151; NAC_AB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Allergen; Alternative splicing; Chaperone;
KW Cytoplasm; Direct protein sequencing; DNA-binding; Isopeptide bond;
KW Nucleus; Phosphoprotein; Protein transport; Reference proteome;
KW Transcription; Transport; Ubl conjugation.
FT CHAIN 1..215
FT /note="Nascent polypeptide-associated complex subunit
FT alpha"
FT /id="PRO_0000135576"
FT DOMAIN 70..135
FT /note="NAC-A/B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00507"
FT DOMAIN 176..213
FT /note="UBA"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..80
FT /note="Required for DNA-binding"
FT /evidence="ECO:0000250"
FT REGION 93..108
FT /note="RNA/DNA-binding"
FT COMPBIAS 11..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 43
FT /note="Phosphoserine; by ILK1"
FT /evidence="ECO:0000269|PubMed:15299025"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 142
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 159
FT /note="Phosphothreonine; by GSK3-beta"
FT /evidence="ECO:0000250|UniProtKB:Q60817"
FT MOD_RES 161
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|Ref.13, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CROSSLNK 142
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CONFLICT 213
FT /note="L -> S (in Ref. 7; BAD96805)"
FT /evidence="ECO:0000305"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:3MCB"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:3LKX"
FT STRAND 91..108
FT /evidence="ECO:0007829|PDB:3MCB"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:3MCB"
FT STRAND 117..124
FT /evidence="ECO:0007829|PDB:3MCB"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:3MCB"
SQ SEQUENCE 215 AA; 23384 MW; 05DC563A8BEF307C CRC64;
MPGEATETVP ATEQELPQPQ AETGSGTESD SDESVPELEE QDSTQATTQQ AQLAAAAEID
EEPVSKAKQS RSEKKARKAM SKLGLRQVTG VTRVTIRKSK NILFVITKPD VYKSPASDTY
IVFGEAKIED LSQQAQLAAA EKFKVQGEAV SNIQENTQTP TVQEESEEEE VDETGVEVKD
IELVMSQANV SRAKAVRALK NNSNDIVNAI MELTM
