LOCUS       NP_002510               1427 aa            linear   PRI 27-APR-2025
DEFINITION  protein NPAT isoform 2 [Homo sapiens].
ACCESSION   NP_002510
VERSION     NP_002510.2
DBSOURCE    REFSEQ: accession NM_002519.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1427)
  AUTHORS   Terradas,M., Schubert,S.A., Viana-Errasti,J., Ruano,D., Aiza,G.,
            Nielsen,M., Marciel,P., Tops,C.M., Parra,G., Morreau,H.,
            Torrents,D., van Leerdam,M.E., Capella,G., de Miranda,N.F.C.C.,
            Valle,L. and van Wezel,T.
  TITLE     Germline NPAT inactivating variants as cause of hereditary
            colorectal cancer
  JOURNAL   Eur J Hum Genet 32 (7), 871-875 (2024)
   PUBMED   38778081
  REMARK    GeneRIF: Germline NPAT inactivating variants as cause of hereditary
            colorectal cancer.
REFERENCE   2  (residues 1 to 1427)
  AUTHORS   Chen,C., Gallagher,J.R., Tarlton,J., van Aalten,L., Bray,S.E.,
            Ashford,M.L.J., McCrimmon,R.J., Pearson,E.R., McNeilly,A.D. and
            Sutherland,C.
  TITLE     The genetic association of the transcription factor NPAT with
            glycemic response to metformin involves regulation of fuel
            selection
  JOURNAL   PLoS One 16 (7), e0253533 (2021)
   PUBMED   34197485
  REMARK    GeneRIF: The genetic association of the transcription factor NPAT
            with glycemic response to metformin involves regulation of fuel
            selection.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1427)
  AUTHORS   Bucholc,K., Skrajna,A., Adamska,K., Yang,X.C., Krajewski,K.,
            Poznanski,J., Dadlez,M., Dominski,Z. and Zhukov,I.
  TITLE     Structural Analysis of the SANT/Myb Domain of FLASH and YARP
            Proteins and Their Complex with the C-Terminal Fragment of NPAT by
            NMR Spectroscopy and Computer Simulations
  JOURNAL   Int J Mol Sci 21 (15), 5268 (2020)
   PUBMED   32722282
  REMARK    GeneRIF: Structural Analysis of the SANT/Myb Domain of FLASH and
            YARP Proteins and Their Complex with the C-Terminal Fragment of
            NPAT by NMR Spectroscopy and Computer Simulations.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1427)
  AUTHORS   Ling Zheng,L., Wang,F.Y., Cong,X.X., Shen,Y., Rao,X.S., Huang,D.S.,
            Fan,W., Yi,P., Wang,X.B., Zheng,L., Zhou,Y.T. and Luo,Y.
  TITLE     Interaction of Heat Shock Protein Cpn10 with the Cyclin E/Cdk2
            Substrate Nuclear Protein Ataxia-Telangiectasia (NPAT) Is Involved
            in Regulating Histone Transcription
  JOURNAL   J Biol Chem 290 (49), 29290-29300 (2015)
   PUBMED   26429916
  REMARK    GeneRIF: Cpn10 has a role in the spatial regulation of NPAT
            signaling
REFERENCE   5  (residues 1 to 1427)
  AUTHORS   Yang,X.C., Sabath,I., Kunduru,L., van Wijnen,A.J., Marzluff,W.F.
            and Dominski,Z.
  TITLE     A conserved interaction that is essential for the biogenesis of
            histone locus bodies
  JOURNAL   J Biol Chem 289 (49), 33767-33782 (2014)
   PUBMED   25339177
  REMARK    GeneRIF: The conserved C-terminal domain shared by FLASH, YARP, and
            Mute recognizes the C-terminal sequence of NPAT orthologues, thus
            acting as a signal targeting proteins to histone locus bodies.
REFERENCE   6  (residues 1 to 1427)
  AUTHORS   Imai,T., Sugawara,T., Nishiyama,A., Shimada,R., Ohki,R., Seki,N.,
            Sagara,M., Ito,H., Yamauchi,M. and Hori,T.
  TITLE     The structure and organization of the human NPAT gene
  JOURNAL   Genomics 42 (3), 388-392 (1997)
   PUBMED   9205109
REFERENCE   7  (residues 1 to 1427)
  AUTHORS   Platzer,M., Rotman,G., Bauer,D., Uziel,T., Savitsky,K.,
            Bar-Shira,A., Gilad,S., Shiloh,Y. and Rosenthal,A.
  TITLE     Ataxia-telangiectasia locus: sequence analysis of 184 kb of human
            genomic DNA containing the entire ATM gene
  JOURNAL   Genome Res 7 (6), 592-605 (1997)
   PUBMED   9199932
REFERENCE   8  (residues 1 to 1427)
  AUTHORS   Byrd,P.J., Cooper,P.R., Stankovic,T., Kullar,H.S., Watts,G.D.,
            Robinson,P.J. and Taylor,M.R.
  TITLE     A gene transcribed from the bidirectional ATM promoter coding for a
            serine rich protein: amino acid sequence, structure and expression
            studies
  JOURNAL   Hum Mol Genet 5 (11), 1785-1791 (1996)
   PUBMED   8923007
REFERENCE   9  (residues 1 to 1427)
  AUTHORS   Imai,T., Yamauchi,M., Seki,N., Sugawara,T., Saito,T., Matsuda,Y.,
            Ito,H., Nagase,T., Nomura,N. and Hori,T.
  TITLE     Identification and characterization of a new gene physically linked
            to the ATM gene
  JOURNAL   Genome Res 6 (5), 439-447 (1996)
   PUBMED   8743993
REFERENCE   10 (residues 1 to 1427)
  AUTHORS   Byrd,P.J., McConville,C.M., Cooper,P., Parkhill,J., Stankovic,T.,
            McGuire,G.M., Thick,J.A. and Taylor,A.M.
  TITLE     Mutations revealed by sequencing the 5' half of the gene for ataxia
            telangiectasia
  JOURNAL   Hum Mol Genet 5 (1), 145-149 (1996)
   PUBMED   8789452
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA338219.1, BC050561.2, BC094769.1, X97186.1 and AP002433.5.
            
            On Aug 15, 2007 this sequence version replaced NP_002510.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK290020.1, SRR1660803.14079.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000278612.9/ ENSP00000278612.8
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1427
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q22.3"
     Protein         1..1427
                     /product="protein NPAT isoform 2"
                     /note="protein NPAT; nuclear protein of the ATM locus;
                     nuclear protein of the ataxia telangiectasia mutated
                     locus; nuclear protein, ataxia-telangiectasia locus;
                     nuclear protein, co-activator of histone transcription"
                     /calculated_mol_wt=154160
     Region          1..318
                     /region_name="Interaction with MIZF.
                     /evidence=ECO:0000269|PubMed:15988025"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14207.3)"
     Region          5..25
                     /region_name="Required for activation of histone gene
                     transcription and interaction with MIZF.
                     /evidence=ECO:0000269|PubMed:15988025"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14207.3)"
     Region          121..145
                     /region_name="Required for activation of histone gene
                     transcription and interaction with MIZF.
                     /evidence=ECO:0000269|PubMed:15988025"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14207.3)"
     Region          199..231
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14207.3)"
     Site            207
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14207.3)"
     Region          262..338
                     /region_name="Mediates transcriptional activation"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14207.3)"
     Site            554
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14207.3)"
     Site            599
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BMA5; propagated from
                     UniProtKB/Swiss-Prot (Q14207.3)"
     Region          628..669
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14207.3)"
     Region          629..653
                     /region_name="Required for acceleration of G1 phase"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14207.3)"
     Region          683..732
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14207.3)"
     Region          758..1427
                     /region_name="NPAT_C"
                     /note="NPAT C terminus; pfam15712"
                     /db_xref="CDD:434876"
     Site            775
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK2.
                     /evidence=ECO:0000269|PubMed:10995387; propagated from
                     UniProtKB/Swiss-Prot (Q14207.3)"
     Site            779
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK2.
                     /evidence=ECO:0000269|PubMed:10995387; propagated from
                     UniProtKB/Swiss-Prot (Q14207.3)"
     Region          828..853
                     /region_name="Required for acceleration of G1 phase"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14207.3)"
     Region          1039..1054
                     /region_name="Required for acceleration of G1 phase"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14207.3)"
     Region          1095..1121
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14207.3)"
     Site            1100
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK2.
                     /evidence=ECO:0000269|PubMed:10995387; propagated from
                     UniProtKB/Swiss-Prot (Q14207.3)"
     Region          1133..1152
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14207.3)"
     Site            1151
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14207.3)"
     Site            1200
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14207.3)"
     Region          1228..1252
                     /region_name="Required for acceleration of G1 phase"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14207.3)"
     Site            1228
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q14207.3)"
     Region          1253..1327
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14207.3)"
     Site            1254
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BMA5; propagated from
                     UniProtKB/Swiss-Prot (Q14207.3)"
     Site            1270
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK2.
                     /evidence=ECO:0000269|PubMed:10995387; propagated from
                     UniProtKB/Swiss-Prot (Q14207.3)"
     Region          1325..1349
                     /region_name="Required for acceleration of G1 phase"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14207.3)"
     Region          1348..1413
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14207.3)"
     Site            1350
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK2.
                     /evidence=ECO:0000269|PubMed:10995387,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14207.3)"
     CDS             1..1427
                     /gene="NPAT"
                     /gene_synonym="E14; E14/NPAT; p220"
                     /coded_by="NM_002519.3:103..4386"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS41710.1"
                     /db_xref="GeneID:4863"
                     /db_xref="HGNC:HGNC:7896"
                     /db_xref="MIM:601448"
ORIGIN      
        1 mllpsdvarl vlgylqqenl istcqtfile ssdlkeyaeh ctdegfipac llslfgknlt
       61 tilneyvamk tketsnnvpa imsslwkkld htlsqirsmq ssprfagsqr artrtgiaei
      121 krqrklasqt apasaelltl pylsgqfttp pstgtqvtrp sgqisdpsrs yfvvvnhsqs
      181 qdtvttgeal nvipgaqekk ahaslmspgr rksesqrkst tlsgphstir nfqdpnafav
      241 ekqmvienar ekilsnkslq eklaeninkf ltsdnniaqv pkqtdnnpte petsideflg
      301 lpseihmsee aiqdileqte sdpafqalfd lfdygktknn knisqsissq pmesnpsivl
      361 adetnlavkg sfeteesdgq sgqpafctsy qnddplnalk nsnnhdvlrq edqenfsqis
      421 tsiqkkafkt avpteqkcdi ditfesvpnl ndfnqrgnsn aecnphcael ytnqmstete
      481 maigieknsl ssnvpsesql qpdqpdipit sfvslgcean nenlilsgks sqllsqdtsl
      541 tgkpskksqf censndtvkl kinfhgskss dssevhkski einvlepvms qlsncqdnsc
      601 lqseilpvsv esshlnvsgq veihlgdsls stkqpsndsa svelnhtene aqasksensq
      661 epsssvkeen tiflslggna ncekvaltpp egtpvenshs lppesvcssv gdshpesqnt
      721 ddkpssnnsa eidasnivsl kviisddpfv ssdteltsav ssingenlpt iilssptksp
      781 tknaelvkcl sseetvgavv yaevgdsasm eqslltfkse dsavnntqne dgiafsanvt
      841 pcvskdggyi qlmpatstaf gnsnniliat cvtdptalgt svsqsnvvvl pgnsapmtaq
      901 plppqlqtpp rsnsvfavnq avspnfsqgs aiiiaspvqp vlqgmvgmip vsvvgqngnn
      961 fstpprqvlh mpltapvcnr sipqfpvppk sqkaqglrnk pcigkqvnnl vdssghsvgc
     1021 haqktevsdk siatdlgkks eettvpfpee sivpaakpch rrvlcfdstt apvantqgpn
     1081 hkmvsqnker navsfpnlds pnvsstlkpp snnaikreke kpplpkilsk sesaisrhtt
     1141 iretqsekkv spteivlesf hkatankene lcsdverqkn pensklsigq qngglrseks
     1201 iaslqemtkk qgtssnnknv lsvgtavkdl kqeqtksass littemlqdi qrhssvsrla
     1261 dssdlpvprt pgsgagekhk eepidiikap ssrrfsedss tskvmvppvt pdlpacspas
     1321 etgsensvnm aahtlmilsr aaisrttsat plkdntqqfr assrsttkkr kieelderer
     1381 nsrpssknlt nssipmkkkk ikkkklpssf pagmdvdkfl lslhyde
//
