NACAM_HUMAN
ID NACAM_HUMAN Reviewed; 2078 AA.
AC E9PAV3;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Nascent polypeptide-associated complex subunit alpha, muscle-specific form;
DE AltName: Full=Alpha-NAC, muscle-specific form;
DE Short=skNAC;
GN Name=NACA;
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 [LARGE SCALE MRNA] (ISOFORM SKNAC-2), AND VARIANTS
RP GLU-336; SER-405; SER-519; THR-1795 AND PRO-1841.
RC TISSUE=Pericardium;
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 [2]
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 [3]
RP IDENTIFICATION, REPEATS, AND ALTERNATIVE SPLICING.
RX PubMed=19211926; DOI=10.1096/fj.08-125542;
RA Li H., Randall W.R., Du S.J.;
RT "skNAC (skeletal Naca), a muscle-specific isoform of Naca (nascent
RT polypeptide-associated complex alpha), is required for myofibril
RT organization.";
RL FASEB J. 23:1988-2000(2009).
RN [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2049, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2029, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2024; SER-2029 AND SER-2054,
RP AND 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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2029, 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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2005, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2049; SER-2054 AND SER-2066,
RP AND 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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2029, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1995, 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 [15]
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 [16]
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 [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-2005, 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).
CC -!- FUNCTION: Cardiac- and muscle-specific transcription factor. May act to
CC regulate the expression of genes involved in the development of
CC myotubes. Plays a critical role in ventricular cardiomyocyte expansion
CC and regulates postnatal skeletal muscle growth and regeneration.
CC Involved in the organized assembly of thick and thin filaments of
CC myofibril sarcomeres (By similarity). {ECO:0000250|UniProtKB:P70670}.
CC -!- SUBUNIT: Interacts (via PXLXP motif) with the muscle-restricted histone
CC methyltransferase SMYD1 (via MYND-type zinc finger).
CC {ECO:0000250|UniProtKB:P70670}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P70670}. Nucleus
CC {ECO:0000250|UniProtKB:P70670}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=skNAC;
CC IsoId=E9PAV3-1; Sequence=Displayed;
CC Name=1;
CC IsoId=Q13765-1; Sequence=External;
CC Name=skNAC-2; Synonyms=2;
CC IsoId=E9PAV3-2; Sequence=VSP_053722, VSP_053723;
CC -!- DOMAIN: The proline-rich muscle-specific exon 3 contains eighteen
CC approximate 23-AA repeats. {ECO:0000269|PubMed:19211926}.
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DR EMBL; AK096699; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC117378; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS44925.2; -. [E9PAV3-2]
DR RefSeq; XP_011536691.1; XM_011538389.1.
DR AlphaFoldDB; E9PAV3; -.
DR SMR; E9PAV3; -.
DR BioGRID; 110748; 157.
DR IntAct; E9PAV3; 10.
DR GlyGen; E9PAV3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; E9PAV3; -.
DR MetOSite; E9PAV3; -.
DR PhosphoSitePlus; E9PAV3; -.
DR SwissPalm; E9PAV3; -.
DR BioMuta; NACA; -.
DR EPD; E9PAV3; -.
DR jPOST; E9PAV3; -.
DR MassIVE; E9PAV3; -.
DR PaxDb; E9PAV3; -.
DR PeptideAtlas; E9PAV3; -.
DR PRIDE; E9PAV3; -.
DR ProteomicsDB; 19086; -. [E9PAV3-1]
DR Antibodypedia; 28384; 97 antibodies from 17 providers.
DR Ensembl; ENST00000454682.6; ENSP00000403817.1; ENSG00000196531.14. [E9PAV3-1]
DR Ensembl; ENST00000550952.6; ENSP00000448035.1; ENSG00000196531.14. [E9PAV3-2]
DR MANE-Select; ENST00000454682.6; ENSP00000403817.1; NM_001365896.1; NP_001352825.1.
DR UCSC; uc001sma.3; human. [E9PAV3-1]
DR GeneCards; NACA; -.
DR HGNC; HGNC:7629; NACA.
DR HPA; ENSG00000196531; Low tissue specificity.
DR neXtProt; NX_E9PAV3; -.
DR OpenTargets; ENSG00000196531; -.
DR VEuPathDB; HostDB:ENSG00000196531; -.
DR eggNOG; KOG2239; Eukaryota.
DR GeneTree; ENSGT00440000033468; -.
DR HOGENOM; CLU_237256_0_0_1; -.
DR OMA; PHKGAPT; -.
DR OrthoDB; 1331328at2759; -.
DR PhylomeDB; E9PAV3; -.
DR PathwayCommons; E9PAV3; -.
DR SignaLink; E9PAV3; -.
DR SIGNOR; E9PAV3; -.
DR BioGRID-ORCS; 4666; 509 hits in 1079 CRISPR screens.
DR ChiTaRS; NACA; human.
DR GenomeRNAi; 4666; -.
DR Pharos; E9PAV3; Tbio.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; E9PAV3; protein.
DR Bgee; ENSG00000196531; Expressed in tendon of biceps brachii and 209 other tissues.
DR ExpressionAtlas; E9PAV3; baseline and differential.
DR Genevisible; E9PAV3; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005854; C:nascent polypeptide-associated complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR Gene3D; 2.20.70.30; -; 1.
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; 2.
DR Pfam; PF19026; HYPK_UBA; 1.
DR Pfam; PF01849; NAC; 1.
DR SMART; SM01407; NAC; 1.
DR PROSITE; PS51151; NAC_AB; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; Cytoplasm; DNA-binding;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..2078
FT /note="Nascent polypeptide-associated complex subunit
FT alpha, muscle-specific form"
FT /id="PRO_0000425571"
FT DOMAIN 1933..1998
FT /note="NAC-A/B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00507"
FT DOMAIN 2039..2078
FT /note="UBA"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 37..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..1944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1932..1943
FT /note="Required for DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P70670"
FT MOTIF 1841..1845
FT /note="PXLXP"
FT /evidence="ECO:0000250|UniProtKB:P70670"
FT COMPBIAS 55..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..809
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..853
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..868
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..1060
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1117
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1126..1186
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1195..1209
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1218..1232
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1241..1271
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1287..1348
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1349..1364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1382..1405
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1466..1480
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1555..1569
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1573..1588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1601..1640
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1641..1663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1698..1719
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1797..1815
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1877..1894
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1903..1917
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1924..1943
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 917
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70670"
FT MOD_RES 1181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70670"
FT MOD_RES 1397
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70670"
FT MOD_RES 1474
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70670"
FT MOD_RES 1906
FT /note="Phosphoserine; by ILK1"
FT /evidence="ECO:0000250|UniProtKB:P70670"
FT MOD_RES 1995
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2005
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 2022
FT /note="Phosphothreonine; by GSK3-beta"
FT /evidence="ECO:0000250|UniProtKB:P70670"
FT MOD_RES 2024
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 2029
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 2049
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 2054
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 2066
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CROSSLNK 2005
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 602..644
FT /note="Missing (in isoform skNAC-2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053722"
FT VAR_SEQ 665..1774
FT /note="Missing (in isoform skNAC-2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053723"
FT VARIANT 336
FT /note="V -> E (in dbSNP:rs2958127)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_070547"
FT VARIANT 405
FT /note="F -> S (in dbSNP:rs2926743)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_070548"
FT VARIANT 519
FT /note="P -> S (in dbSNP:rs185561121)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_070549"
FT VARIANT 1795
FT /note="S -> T (in dbSNP:rs2926747)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_070550"
FT VARIANT 1841
FT /note="L -> P (in dbSNP:rs2958149)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_070551"
FT CONFLICT 417
FT /note="S -> N (in Ref. 1; AK096699)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2078 AA; 205422 MW; 9A07C05D3F24C34B CRC64;
MPGEATETVP ATEQELPQPQ AETAVLPMSS ALSVTAALGQ PGPTLPPPCS PAPQQCPLSA
ANQASPFPSP STIASTPLEV PFPQSSSGTA LPLGTAPEAP TFLPNLIGPP ISPAALALAS
PMIAPTLKGT PSSSAPLALV ALAPHSVQKS SAFPPNLLTS PPSVAVAESG SVITLSAPIA
PSEPKTNLNK VPSEVVPNPK GTPSPPCIVS TVPYHCVTPM ASIQSGVASL PQTTPTTTLA
IASPQVKDTT ISSVLISPQN PGSLSLKGPV SPPAALSLST QSLPVVTSSQ KTAGPNTPPD
FPISLGSHLA PLHQSSFGSV QLLGQTGPSA LSDPTVKTIS VDHSSTGASY PSQRSVIPPL
PSRNEVVPAT VAAFPVVAPS VDKGPSTISS ITCSPSGSLN VATSFSLSPT TSLILKSSPN
ATYHYPLVAQ MPVSSVGTTP LVVTNPCTIA AAPTTTFEVA TCVSPPMSSG PISNIEPTSP
AALVMAPVAP KEPSTQVATT LRIPVSPPLP DPEDLKNLPS SVLVKFPTQK DLQTVPASLE
GAPFSPAQAG LTTKKDPTVL PLVQAAPKNS PSFQSTSSSP EIPLSPEATL AKKSLGEPLP
IGKPASSMTS PLGVNSSASV IKTDSYAGPD SAGPLLKSSL ITPTVAAFPL ESADPAGVAP
TTAKGTSTYT TTASPFLEGT VSLAPKNHPV KEGTLTTLPL VPTASENCPV APSPQNTCAP
LATLVLAPEI PKSVPSPSLP PAGTPPGTKK VDGISHTSAL APVASSPKEC PTEDSGASAT
ASSKGTLTYL ADSPSPLGVS VSPQTKRPPT KKGSAGPDTP IGNLSSPVSP VEASFLPENS
LSFQGSKDSP ATTHSPTPPS PKGAPTPSAV TPLSPKGVTL PPKETPTPSV VNLPFPKEGP
ATPAPKQAPA LSMTSSSPKK ARATPAPKGI PASPSPKGAP TPPAATPPSP KGGPATPSPK
WAPTPPAATP PSPKGGPATP SPKGAPTPPA ATPPSPKGGP ATPSPKGAPT PPAVTPPSPK
GSPAATPFPK GASTPPAATP PSPKGSPAAT PLPKGAPTTP AATLPSPKGG PATPSLKGAP
TPPAATPPSP KGGPATPSPK GAPMPPAATP PSPKGGLATP PHKGAPTTPA ATPPSPKGGL
ATPPPKGAPT TPAATPPSPK GGLATPPPKG APTTPAATPP SPKGGLATPS PKGAPTTPAA
TPPSPKGGLA TPSPKGAPTT PAATPPSPKG GLATPSPKGA PTTPAATPPS PKGGPATPPP
KGAPTPPAAT PPSLKGGLAT PPHKGAPNPA VVTPPSPKGG PATSPPKGAP TPPAATPPSP
KGSPGTPPPK GAPTPPAVTP PSPKGTPTLP ATTPSSKGGP TTPSSKEGPT PPAATPSHKG
GPAMTPPSPK RGPAIPSPKG DPTSPAVIPL SPKKAPATPV TREGAATPSK GDLTPPAVTP
VSLKKAPATS APKGGPATPS SKGDPTLPAV TPPSPKEPPA PKQVATSSSP KKAPATPAPM
GAPTLPAVIP SSPKEVPATP SSRRDPIAPT ATLLSKKTPA TLAPKEALIP PAMTVPSPKK
TPAIPTPKEA PATPSSKEAS SPPAVTPSTY KGAPSPKELL IPPAVTSPSP KEAPTPPAVT
PPSPEKGPAT PAPKGTPTSP PVTPSSLKDS PTSPASVTCK MGATVPQASK GLPAKKGPTA
LKEVLVAPAP ESTPIITAPT RKGPQTKKSS ATSPPICPDP SAKNGSKGPL STVAPAPLLP
VQKDSSKTAK GKDASHSPKG PLAPPESKAS TPLTAAAFEK VLPKPESASV SAAPSPPVSL
PLAPSPVPTL PPKQQFLPSS PGLVLESPSK PLAPADEDEL LPLIPPEPIS GGVPFQSVLV
NMPTPKSAGI PVPTPSAKQP VTKNNKGSGT ESDSDESVPE LEEQDSTQAT TQQAQLAAAA
EIDEEPVSKA KQSRSEKKAR KAMSKLGLRQ VTGVTRVTIR KSKNILFVIT KPDVYKSPAS
DTYIVFGEAK IEDLSQQAQL AAAEKFKVQG EAVSNIQENT QTPTVQEESE EEEVDETGVE
VKDIELVMSQ ANVSRAKAVR ALKNNSNDIV NAIMELTM
