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Q14207

- NPAT_HUMAN

UniProt

Q14207 - NPAT_HUMAN

Protein

Protein NPAT

Gene

NPAT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 3 (18 May 2010)
      Previous versions | rss
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    Functioni

    Required for progression through the G1 and S phases of the cell cycle and for S phase entry. Activates transcription of the histone H2A, histone H2B, histone H3 and histone H4 genes in conjunction with MIZF. Also positively regulates the ATM, MIZF and PRKDC promoters. Transcriptional activation may be accomplished at least in part by the recruitment of the NuA4 histone acetyltransferase (HAT) complex to target gene promoters.14 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein C-terminus binding Source: UniProtKB
    3. protein N-terminus binding Source: UniProtKB
    4. sequence-specific DNA binding transcription factor activity Source: UniProtKB
    5. transcription coactivator activity Source: UniProtKB
    6. transcription corepressor activity Source: UniProtKB

    GO - Biological processi

    1. positive regulation of transcription, DNA-templated Source: UniProtKB
    2. regulation of gene expression Source: UniProtKB
    3. regulation of transcription involved in G1/S transition of mitotic cell cycle Source: UniProtKB
    4. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Cell cycle, Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein NPAT
    Alternative name(s):
    Nuclear protein of the ataxia telangiectasia mutated locus
    Short name:
    Nuclear protein of the ATM locus
    p220
    Gene namesi
    Name:NPAT
    Synonyms:CAND3, E14
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:7896. NPAT.

    Subcellular locationi

    Nucleus. NucleusCajal body
    Note: Concentrates in two Cajal bodies tethered to histone gene clusters at chromosome 6p21 during G1, S and G2 phases. Also concentrates in two additional Cajal bodies tethered to histone gene clusters at chromosome 1q21 specifically during S and G2 phases.

    GO - Cellular componenti

    1. Cajal body Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. Gemini of coiled bodies Source: UniProtKB
    4. nucleoplasm Source: UniProtKB
    5. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi7 – 71V → A: Impairs activation of histone gene transcription; when associated with A-10; A-11; A-15 and A-18. 2 Publications
    Mutagenesisi10 – 101L → A: Impairs activation of histone gene transcription; when associated with A-7; A-11; A-15 and A-18. 2 Publications
    Mutagenesisi11 – 111V → A: Impairs activation of histone gene transcription; when associated with A-7; A-10; A-15 and A-18. 2 Publications
    Mutagenesisi15 – 151L → A: Impairs activation of histone gene transcription; when associated with A-7; A-10; A-11 and A-18. 2 Publications
    Mutagenesisi18 – 181E → A: Impairs activation of histone gene transcription; when associated with A-7; A-10; A-11 and A-15. 2 Publications
    Mutagenesisi27 – 271F → A: Impairs activation of histone gene transcription; when associated with A-30. 2 Publications
    Mutagenesisi30 – 301E → A: Impairs activation of histone gene transcription; when associated with A-27. 2 Publications
    Mutagenesisi331 – 3333LFD → AAA: Impairs activation of histone gene transcription. Impairs interaction with BZW1, RUVBL1, RUVBL2 and TRRAP. 1 Publication
    Mutagenesisi775 – 7751S → A: Impairs activation of histone gene transcription; when associated with A-779; A-1100; A-1270 and A-1350. 5 Publications
    Mutagenesisi779 – 7791S → A: Impairs activation of histone gene transcription; when associated with A-775; A-1100; A-1270 and A-1350. 5 Publications
    Mutagenesisi1100 – 11001S → A: Impairs activation of histone gene transcription; when associated with A-775; A-779; A-1270 and A-1350. 5 Publications
    Mutagenesisi1270 – 12701T → A: Impairs activation of histone gene transcription; when associated with A-775; A-779; A-1100 and A-1350. 5 Publications
    Mutagenesisi1350 – 13501T → A: Impairs activation of histone gene transcription; when associated with A-775; A-779; A-1100 and A-1270. 5 Publications

    Organism-specific databases

    PharmGKBiPA31697.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14271427Protein NPATPRO_0000318163Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei775 – 7751Phosphoserine; by CDK21 Publication
    Modified residuei779 – 7791Phosphoserine; by CDK21 Publication
    Modified residuei1100 – 11001Phosphoserine; by CDK21 Publication
    Modified residuei1228 – 12281N6-acetyllysine1 Publication
    Modified residuei1270 – 12701Phosphothreonine; by CDK21 Publication
    Modified residuei1350 – 13501Phosphothreonine; by CDK21 Publication

    Post-translational modificationi

    Phosphorylated at Ser-775, Ser-779, Ser-1100, Thr-1270 and Thr-1350 by CCNE1/CDK2 at G1-S transition and until prophase, which promotes association with histone gene clusters and stimulates activation of histone transcription. Also phosphorylated by CCNA1/CDK2 in vitro.3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ14207.
    PaxDbiQ14207.
    PRIDEiQ14207.

    PTM databases

    PhosphoSiteiQ14207.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.2 Publications

    Developmental stagei

    Expressed throughout the cell cycle. Expression peaks at the G1/S phase boundary and declines during S phase.2 Publications

    Inductioni

    By expression of E2F1, E2F2, E2F3 and E2F4. Expression is reduced in response to radiation-induced DNA damage.2 Publications

    Gene expression databases

    ArrayExpressiQ14207.
    BgeeiQ14207.
    CleanExiHS_NPAT.
    GenevestigatoriQ14207.

    Organism-specific databases

    HPAiHPA056823.

    Interactioni

    Subunit structurei

    Interacts with the cylin/CDK complexes CCNE1/CDK2 and CCNA1/CDK2. Interacts with BZW1, CASP8AP2, CREBBP, MIZF and YY1. Interacts with the RUVBL1, RUVBL2 and TRRAP subunits of the NuA4 complex. May also interact with GAPDH, NME1, NME2 and STIP1.7 Publications

    Protein-protein interaction databases

    BioGridi110924. 15 interactions.
    DIPiDIP-59961N.
    IntActiQ14207. 1 interaction.
    STRINGi9606.ENSP00000278612.

    Structurei

    3D structure databases

    ProteinModelPortaliQ14207.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 3533LisHPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 318318Interaction with MIZFAdd
    BLAST
    Regioni5 – 2521Required for activation of histone gene transcription and interaction with MIZFAdd
    BLAST
    Regioni121 – 14525Required for activation of histone gene transcription and interaction with MIZFAdd
    BLAST
    Regioni262 – 33877Mediates transcriptional activationAdd
    BLAST
    Regioni629 – 65325Required for acceleration of G1 phaseAdd
    BLAST
    Regioni828 – 85326Required for acceleration of G1 phaseAdd
    BLAST
    Regioni1039 – 105416Required for acceleration of G1 phaseAdd
    BLAST
    Regioni1228 – 125225Required for acceleration of G1 phaseAdd
    BLAST
    Regioni1325 – 134925Required for acceleration of G1 phaseAdd
    BLAST

    Domaini

    The LisH domain is required for the activation of histone gene transcription.1 Publication

    Sequence similaritiesi

    Belongs to the NPAT family.Curated
    Contains 1 LisH domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG29266.
    HOVERGENiHBG108198.
    InParanoidiQ14207.
    OMAiFDLFDYG.
    OrthoDBiEOG7JDQX0.
    PhylomeDBiQ14207.
    TreeFamiTF332825.

    Family and domain databases

    InterProiIPR006594. LisH_dimerisation.
    [Graphical view]
    SMARTiSM00667. LisH. 1 hit.
    [Graphical view]
    PROSITEiPS50896. LISH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q14207-1 [UniParc]FASTAAdd to Basket

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    MLLPSDVARL VLGYLQQENL ISTCQTFILE SSDLKEYAEH CTDEGFIPAC     50
    LLSLFGKNLT TILNEYVAMK TKETSNNVPA IMSSLWKKLD HTLSQIRSMQ 100
    SSPRFAGSQR ARTRTGIAEI KRQRKLASQT APASAELLTL PYLSGQFTTP 150
    PSTGTQVTRP SGQISDPSRS YFVVVNHSQS QDTVTTGEAL NVIPGAQEKK 200
    AHASLMSPGR RKSESQRKST TLSGPHSTIR NFQDPNAFAV EKQMVIENAR 250
    EKILSNKSLQ EKLAENINKF LTSDNNIAQV PKQTDNNPTE PETSIDEFLG 300
    LPSEIHMSEE AIQDILEQTE SDPAFQALFD LFDYGKTKNN KNISQSISSQ 350
    PMESNPSIVL ADETNLAVKG SFETEESDGQ SGQPAFCTSY QNDDPLNALK 400
    NSNNHDVLRQ EDQENFSQIS TSIQKKAFKT AVPTEQKCDI DITFESVPNL 450
    NDFNQRGNSN AECNPHCAEL YTNQMSTETE MAIGIEKNSL SSNVPSESQL 500
    QPDQPDIPIT SFVSLGCEAN NENLILSGKS SQLLSQDTSL TGKPSKKSQF 550
    CENSNDTVKL KINFHGSKSS DSSEVHKSKI EINVLEPVMS QLSNCQDNSC 600
    LQSEILPVSV ESSHLNVSGQ VEIHLGDSLS STKQPSNDSA SVELNHTENE 650
    AQASKSENSQ EPSSSVKEEN TIFLSLGGNA NCEKVALTPP EGTPVENSHS 700
    LPPESVCSSV GDSHPESQNT DDKPSSNNSA EIDASNIVSL KVIISDDPFV 750
    SSDTELTSAV SSINGENLPT IILSSPTKSP TKNAELVKCL SSEETVGAVV 800
    YAEVGDSASM EQSLLTFKSE DSAVNNTQNE DGIAFSANVT PCVSKDGGYI 850
    QLMPATSTAF GNSNNILIAT CVTDPTALGT SVSQSNVVVL PGNSAPMTAQ 900
    PLPPQLQTPP RSNSVFAVNQ AVSPNFSQGS AIIIASPVQP VLQGMVGMIP 950
    VSVVGQNGNN FSTPPRQVLH MPLTAPVCNR SIPQFPVPPK SQKAQGLRNK 1000
    PCIGKQVNNL VDSSGHSVGC HAQKTEVSDK SIATDLGKKS EETTVPFPEE 1050
    SIVPAAKPCH RRVLCFDSTT APVANTQGPN HKMVSQNKER NAVSFPNLDS 1100
    PNVSSTLKPP SNNAIKREKE KPPLPKILSK SESAISRHTT IRETQSEKKV 1150
    SPTEIVLESF HKATANKENE LCSDVERQKN PENSKLSIGQ QNGGLRSEKS 1200
    IASLQEMTKK QGTSSNNKNV LSVGTAVKDL KQEQTKSASS LITTEMLQDI 1250
    QRHSSVSRLA DSSDLPVPRT PGSGAGEKHK EEPIDIIKAP SSRRFSEDSS 1300
    TSKVMVPPVT PDLPACSPAS ETGSENSVNM AAHTLMILSR AAISRTTSAT 1350
    PLKDNTQQFR ASSRSTTKKR KIEELDERER NSRPSSKNLT NSSIPMKKKK 1400
    IKKKKLPSSF PAGMDVDKFL LSLHYDE 1427
    Length:1,427
    Mass (Da):154,290
    Last modified:May 18, 2010 - v3
    Checksum:iD5C5E630A56227F9
    GO

    Sequence cautioni

    The sequence AAB02735.1 differs from that shown. Reason: Chimeric cDNA. A chimeric cDNA originating from chromosomes 11 and 4.
    The sequence AAH40356.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAH50561.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti22 – 221S → Y in AAB02735. (PubMed:9060412)Curated
    Sequence conflicti101 – 1011S → N in BAF84376. (PubMed:14702039)Curated
    Sequence conflicti329 – 3291F → L in BAF84376. (PubMed:14702039)Curated
    Sequence conflicti471 – 4711Y → N in CAA65824. (PubMed:8923007)Curated
    Sequence conflicti785 – 7851E → G in BAF82709. (PubMed:14702039)Curated
    Sequence conflicti1145 – 11451Q → R in BAF82709. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti295 – 2951I → L.1 Publication
    Corresponds to variant rs1131748 [ dbSNP | Ensembl ].
    VAR_038696
    Natural varianti399 – 3991L → M.1 Publication
    Corresponds to variant rs1051521 [ dbSNP | Ensembl ].
    VAR_038697
    Natural varianti447 – 4471V → M.
    Corresponds to variant rs35504388 [ dbSNP | Ensembl ].
    VAR_038698
    Natural varianti483 – 4831I → L.
    Corresponds to variant rs968207 [ dbSNP | Ensembl ].
    VAR_038699
    Natural varianti540 – 5401L → F.1 Publication
    Corresponds to variant rs4144901 [ dbSNP | Ensembl ].
    VAR_038700
    Natural varianti575 – 5751V → I.5 Publications
    Corresponds to variant rs2070661 [ dbSNP | Ensembl ].
    VAR_038701
    Natural varianti608 – 6081V → A.
    Corresponds to variant rs35095430 [ dbSNP | Ensembl ].
    VAR_038702
    Natural varianti621 – 6211V → I.1 Publication
    Corresponds to variant rs1051522 [ dbSNP | Ensembl ].
    VAR_038703
    Natural varianti967 – 9671Q → E.1 Publication
    Corresponds to variant rs1131750 [ dbSNP | Ensembl ].
    VAR_038704
    Natural varianti973 – 9731L → V.1 Publication
    Corresponds to variant rs1131751 [ dbSNP | Ensembl ].
    VAR_038705
    Natural varianti987 – 9871V → A.1 Publication
    Corresponds to variant rs1051524 [ dbSNP | Ensembl ].
    VAR_038706
    Natural varianti999 – 9991N → K.1 Publication
    Corresponds to variant rs34052882 [ dbSNP | Ensembl ].
    VAR_038707
    Natural varianti1191 – 11911Q → R.1 Publication
    Corresponds to variant rs1051525 [ dbSNP | Ensembl ].
    VAR_038708

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D83243 mRNA. Translation: BAA11861.1.
    X97186 mRNA. Translation: CAA65824.1.
    D89854 Genomic DNA. Translation: BAA21367.1.
    AK290020 mRNA. Translation: BAF82709.1.
    AK291687 mRNA. Translation: BAF84376.1.
    BC040356 mRNA. Translation: AAH40356.1. Sequence problems.
    BC050561 mRNA. Translation: AAH50561.1. Sequence problems.
    U58852 mRNA. Translation: AAB02735.1. Sequence problems.
    CCDSiCCDS41710.1.
    RefSeqiNP_002510.2. NM_002519.2.
    UniGeneiHs.171061.
    Hs.367437.

    Genome annotation databases

    EnsembliENST00000278612; ENSP00000278612; ENSG00000149308.
    GeneIDi4863.
    KEGGihsa:4863.
    UCSCiuc001pjz.4. human.

    Polymorphism databases

    DMDMi296439285.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D83243 mRNA. Translation: BAA11861.1 .
    X97186 mRNA. Translation: CAA65824.1 .
    D89854 Genomic DNA. Translation: BAA21367.1 .
    AK290020 mRNA. Translation: BAF82709.1 .
    AK291687 mRNA. Translation: BAF84376.1 .
    BC040356 mRNA. Translation: AAH40356.1 . Sequence problems.
    BC050561 mRNA. Translation: AAH50561.1 . Sequence problems.
    U58852 mRNA. Translation: AAB02735.1 . Sequence problems.
    CCDSi CCDS41710.1.
    RefSeqi NP_002510.2. NM_002519.2.
    UniGenei Hs.171061.
    Hs.367437.

    3D structure databases

    ProteinModelPortali Q14207.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110924. 15 interactions.
    DIPi DIP-59961N.
    IntActi Q14207. 1 interaction.
    STRINGi 9606.ENSP00000278612.

    PTM databases

    PhosphoSitei Q14207.

    Polymorphism databases

    DMDMi 296439285.

    Proteomic databases

    MaxQBi Q14207.
    PaxDbi Q14207.
    PRIDEi Q14207.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000278612 ; ENSP00000278612 ; ENSG00000149308 .
    GeneIDi 4863.
    KEGGi hsa:4863.
    UCSCi uc001pjz.4. human.

    Organism-specific databases

    CTDi 4863.
    GeneCardsi GC11M108062.
    H-InvDB HIX0035981.
    HGNCi HGNC:7896. NPAT.
    HPAi HPA056823.
    MIMi 601448. gene.
    neXtProti NX_Q14207.
    PharmGKBi PA31697.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG29266.
    HOVERGENi HBG108198.
    InParanoidi Q14207.
    OMAi FDLFDYG.
    OrthoDBi EOG7JDQX0.
    PhylomeDBi Q14207.
    TreeFami TF332825.

    Miscellaneous databases

    GeneWikii NPAT_(gene).
    GenomeRNAii 4863.
    NextBioi 18734.
    PROi Q14207.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14207.
    Bgeei Q14207.
    CleanExi HS_NPAT.
    Genevestigatori Q14207.

    Family and domain databases

    InterProi IPR006594. LisH_dimerisation.
    [Graphical view ]
    SMARTi SM00667. LisH. 1 hit.
    [Graphical view ]
    PROSITEi PS50896. LISH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and characterization of a new gene physically linked to the ATM gene."
      Imai T., Yamauchi M., Seki N., Sugawara T., Saito T., Matsuda Y., Ito H., Nagase T., Nomura N., Hori T.
      Genome Res. 6:439-447(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANT ILE-575.
    2. "A gene transcribed from the bidirectional ATM promoter coding for a serine rich protein: amino acid sequence, structure and expression studies."
      Byrd P.J., Cooper P.R., Stankovic T., Kullar H.S., Watts G.D.J., Robinson P.J., Taylor A.M.R.
      Hum. Mol. Genet. 5:1785-1791(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANTS LEU-295; MET-399; ILE-575; ILE-621; GLU-967; VAL-973; ALA-987 AND ARG-1191.
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-575.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS PHE-540; ILE-575 AND LYS-999.
      Tissue: Hippocampus and Placenta.
    5. "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] OF 1-1369, VARIANT ILE-575.
      Tissue: Lymph and Testis.
    6. "CAND3: a ubiquitously expressed gene immediately adjacent and in opposite transcriptional orientation to the ATM gene at 11q23.1."
      Chen X., Yang L., Udar N., Liang T., Uhrhammer N., Xu S., Bay J.-O., Wang Z., Dandakar S., Chiplunkar S., Klisak I., Telatar M., Yang H., Concannon P., Gatti R.A.
      Mamm. Genome 8:129-133(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1169.
    7. "Expression of NPAT, a novel substrate of cyclin E-CDK2, promotes S-phase entry."
      Zhao J., Dynlacht B., Imai T., Hori T., Harlow E.
      Genes Dev. 12:456-461(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CCNE1 AND CDK2, DEVELOPMENTAL STAGE, PHOSPHORYLATION.
    8. "NPAT links cyclin E-Cdk2 to the regulation of replication-dependent histone gene transcription."
      Zhao J., Kennedy B.K., Lawrence B.D., Barbie D.A., Matera A.G., Fletcher J.A., Harlow E.
      Genes Dev. 14:2283-2297(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    9. "Cell cycle-regulated phosphorylation of p220(NPAT) by cyclin E/Cdk2 in Cajal bodies promotes histone gene transcription."
      Ma T., Van Tine B.A., Wei Y., Garrett M.D., Nelson D., Adams P.D., Wang J., Qin J., Chow L.T., Harper J.W.
      Genes Dev. 14:2298-2313(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CCNA1; CCNE1 AND CDK2, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-775; SER-779; SER-1100; THR-1270 AND THR-1350 BY CDK2, MUTAGENESIS OF SER-775; SER-779; SER-1100; THR-1270 AND THR-1350.
    10. "Aberrant methylation of the ATM promoter correlates with increased radiosensitivity in a human colorectal tumor cell line."
      Kim W.-J., Vo Q.N., Shrivastav M., Lataxes T.A., Brown K.D.
      Oncogene 21:3864-3871(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    11. "S phase activation of the histone H2B promoter by OCA-S, a coactivator complex that contains GAPDH as a key component."
      Zheng L., Roeder R.G., Luo Y.
      Cell 114:255-266(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GAPDH; NME1; NME2 AND STIP1.
    12. "NPAT expression is regulated by E2F and is essential for cell cycle progression."
      Gao G., Bracken A.P., Burkard K., Pasini D., Classon M., Attwooll C., Sagara M., Imai T., Helin K., Zhao J.
      Mol. Cell. Biol. 23:2821-2833(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION.
    13. "The cyclin E/Cdk2 substrate and Cajal body component p220(NPAT) activates histone transcription through a novel LisH-like domain."
      Wei Y., Jin J., Harper J.W.
      Mol. Cell. Biol. 23:3669-3680(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF VAL-7; LEU-10; VAL-11; LEU-15; GLU-18; PHE-27 AND GLU-30.
    14. "Identification of HiNF-P, a key activator of cell cycle-controlled histone H4 genes at the onset of S phase."
      Mitra P., Xie R.-L., Medina R., Hovhannisyan H., Zaidi S.K., Wei Y., Harper J.W., Stein J.L., van Wijnen A.J., Stein G.S.
      Mol. Cell. Biol. 23:8110-8123(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF SER-775; SER-779; SER-1100; THR-1270 AND THR-1350.
    15. "The cyclin E/Cdk2 substrate p220(NPAT) is required for S-phase entry, histone gene expression, and Cajal body maintenance in human somatic cells."
      Ye X., Wei Y., Nalepa G., Harper J.W.
      Mol. Cell. Biol. 23:8586-8600(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    16. "Dynamic interaction of p220(NPAT) and CBP/p300 promotes S-phase entry."
      Wang A., Ikura T., Eto K., Ota M.S.
      Biochem. Biophys. Res. Commun. 325:1509-1516(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CCNE1 AND CREBBP, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-775; SER-779; SER-1100; THR-1270 AND THR-1350.
    17. "DNA damage induces downregulation of histone gene expression through the G1 checkpoint pathway."
      Su C., Gao G., Schneider S., Helt C., Weiss C., O'Reilly M.A., Bohmann D., Zhao J.
      EMBO J. 23:1133-1143(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION.
    18. "Coordinate control and selective expression of the full complement of replication-dependent histone H4 genes in normal and cancer cells."
      Holmes W.F., Braastad C.D., Mitra P., Hampe C., Doenecke D., Albig W., Stein J.L., van Wijnen A.J., Stein G.S.
      J. Biol. Chem. 280:37400-37407(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. "HiNF-P directly links the cyclin E/CDK2/p220NPAT pathway to histone H4 gene regulation at the G1/S phase cell cycle transition."
      Miele A., Braastad C.D., Holmes W.F., Mitra P., Medina R., Xie R.-L., Zaidi S.K., Ye X., Wei Y., Harper J.W., van Wijnen A.J., Stein J.L., Stein G.S.
      Mol. Cell. Biol. 25:6140-6153(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MIZF, SUBCELLULAR LOCATION.
    20. "Deficiency of the zinc finger protein ZPR1 causes defects in transcription and cell cycle progression."
      Gangwani L.
      J. Biol. Chem. 281:40330-40340(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    21. "Self-renewal of human embryonic stem cells is supported by a shortened G1 cell cycle phase."
      Becker K.A., Ghule P.N., Therrien J.A., Lian J.B., Stein J.L., van Wijnen A.J., Stein G.S.
      J. Cell. Physiol. 209:883-893(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    22. Cited for: INTERACTION WITH CASP8AP2, SUBCELLULAR LOCATION.
    23. "The HiNF-P/p220NPAT cell cycle signaling pathway controls nonhistone target genes."
      Medina R., van der Deen M., Miele-Chamberland A., Xie R.-L., van Wijnen A.J., Stein J.L., Stein G.S.
      Cancer Res. 67:10334-10342(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    24. "Transcriptional activation of the histone nuclear factor P (HiNF-P) gene by HiNF-P and its cyclin E/CDK2 responsive co-factor p220NPAT defines a novel autoregulatory loop at the G1/S phase transition."
      Xie R.-L., Liu L., Mitra P., Stein J.L., van Wijnen A.J., Stein G.S.
      Gene 402:94-102(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    25. "HiNF-P is a bifunctional regulator of cell cycle controlled histone H4 gene transcription."
      Mitra P., Xie R.-L., Harper J.W., Stein J.L., Stein G.S., van Wijnen A.J.
      J. Cell. Biochem. 101:181-191(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF SER-775; SER-779; SER-1100; THR-1270 AND THR-1350.
    26. "Establishment of histone gene regulation and cell cycle checkpoint control in human embryonic stem cells."
      Becker K.A., Stein J.L., Lian J.B., van Wijnen A.J., Stein G.S.
      J. Cell. Physiol. 210:517-526(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE, INDUCTION.
    27. "Cell cycle dependent phosphorylation and subnuclear organization of the histone gene regulator p220(NPAT) in human embryonic stem cells."
      Ghule P.N., Becker K.A., Harper J.W., Lian J.B., Stein J.L., van Wijnen A.J., Stein G.S.
      J. Cell. Physiol. 213:9-17(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    28. "Transcriptional activation of histone genes requires NPAT-dependent recruitment of TRRAP-Tip60 complex to histone promoters during the G1/S phase transition."
      DeRan M., Pulvino M., Greene E., Su C., Zhao J.
      Mol. Cell. Biol. 28:435-447(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BZW1; RUVBL1; RUVBL2; TRRAP AND YY1, MUTAGENESIS OF 331-LEU--ASP-333.
    29. "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].
    30. "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-1228, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    31. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.

    Entry informationi

    Entry nameiNPAT_HUMAN
    AccessioniPrimary (citable) accession number: Q14207
    Secondary accession number(s): A8K1V5
    , A8K6M2, Q13632, Q14967, Q16580, Q86W55, Q8IWE9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 5, 2008
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 90 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3