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Q14207 (NPAT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 89. Feed History...

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

Names and origin

Protein namesRecommended name:
Protein NPAT
Alternative name(s):
Nuclear protein of the ataxia telangiectasia mutated locus
Short name=Nuclear protein of the ATM locus
p220
Gene names
Name:NPAT
Synonyms:CAND3, E14
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1427 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7 Ref.8 Ref.9 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19 Ref.23 Ref.24 Ref.25 Ref.28

Subunit structure

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. Ref.7 Ref.9 Ref.11 Ref.16 Ref.19 Ref.22 Ref.28

Subcellular location

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. Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.21 Ref.22 Ref.27

Tissue specificity

Ubiquitously expressed. Ref.1 Ref.2

Developmental stage

Expressed throughout the cell cycle. Expression peaks at the G1/S phase boundary and declines during S phase. Ref.7 Ref.26

Induction

By expression of E2F1, E2F2, E2F3 and E2F4. Expression is reduced in response to radiation-induced DNA damage. Ref.12 Ref.26

Domain

The LisH domain is required for the activation of histone gene transcription. Ref.13

Post-translational modification

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. Ref.7 Ref.9 Ref.17

Sequence similarities

Belongs to the NPAT family.

Contains 1 LisH domain.

Sequence caution

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.

Ontologies

Keywords
   Biological processCell cycle
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   Molecular functionActivator
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpositive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 18850719. Source: UniProtKB

regulation of gene expression

Inferred from mutant phenotype Ref.19. Source: UniProtKB

regulation of transcription involved in G1/S transition of mitotic cell cycle

Inferred from mutant phenotype Ref.19. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentCajal body

Inferred from direct assay Ref.19Ref.20PubMed 17577209PubMed 19170105. Source: UniProtKB

Gemini of coiled bodies

Inferred from direct assay Ref.20. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.20. Source: UniProtKB

nucleoplasm

Inferred from direct assay Ref.20. Source: UniProtKB

nucleus

Inferred from direct assay Ref.19PubMed 19170105. Source: UniProtKB

   Molecular_functionprotein C-terminus binding

Inferred from physical interaction Ref.19. Source: UniProtKB

protein N-terminus binding

Inferred from physical interaction PubMed 19170105. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 18850719. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 18850719. Source: UniProtKB

transcription coactivator activity

Inferred from direct assay Ref.14Ref.23. Source: UniProtKB

transcription corepressor activity

Inferred from mutant phenotype Ref.25. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14271427Protein NPAT
PRO_0000318163

Regions

Domain3 – 3533LisH
Region1 – 318318Interaction with MIZF
Region5 – 2521Required for activation of histone gene transcription and interaction with MIZF
Region121 – 14525Required for activation of histone gene transcription and interaction with MIZF
Region262 – 33877Mediates transcriptional activation
Region629 – 65325Required for acceleration of G1 phase
Region828 – 85326Required for acceleration of G1 phase
Region1039 – 105416Required for acceleration of G1 phase
Region1228 – 125225Required for acceleration of G1 phase
Region1325 – 134925Required for acceleration of G1 phase

Amino acid modifications

Modified residue7751Phosphoserine; by CDK2 Ref.9
Modified residue7791Phosphoserine; by CDK2 Ref.9
Modified residue11001Phosphoserine; by CDK2 Ref.9
Modified residue12281N6-acetyllysine Ref.30
Modified residue12701Phosphothreonine; by CDK2 Ref.9
Modified residue13501Phosphothreonine; by CDK2 Ref.9

Natural variations

Natural variant2951I → L. Ref.2
Corresponds to variant rs1131748 [ dbSNP | Ensembl ].
VAR_038696
Natural variant3991L → M. Ref.2
Corresponds to variant rs1051521 [ dbSNP | Ensembl ].
VAR_038697
Natural variant4471V → M.
Corresponds to variant rs35504388 [ dbSNP | Ensembl ].
VAR_038698
Natural variant4831I → L.
Corresponds to variant rs968207 [ dbSNP | Ensembl ].
VAR_038699
Natural variant5401L → F. Ref.4
Corresponds to variant rs4144901 [ dbSNP | Ensembl ].
VAR_038700
Natural variant5751V → I. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5
Corresponds to variant rs2070661 [ dbSNP | Ensembl ].
VAR_038701
Natural variant6081V → A.
Corresponds to variant rs35095430 [ dbSNP | Ensembl ].
VAR_038702
Natural variant6211V → I. Ref.2
Corresponds to variant rs1051522 [ dbSNP | Ensembl ].
VAR_038703
Natural variant9671Q → E. Ref.2
Corresponds to variant rs1131750 [ dbSNP | Ensembl ].
VAR_038704
Natural variant9731L → V. Ref.2
Corresponds to variant rs1131751 [ dbSNP | Ensembl ].
VAR_038705
Natural variant9871V → A. Ref.2
Corresponds to variant rs1051524 [ dbSNP | Ensembl ].
VAR_038706
Natural variant9991N → K. Ref.4
Corresponds to variant rs34052882 [ dbSNP | Ensembl ].
VAR_038707
Natural variant11911Q → R. Ref.2
Corresponds to variant rs1051525 [ dbSNP | Ensembl ].
VAR_038708

Experimental info

Mutagenesis71V → A: Impairs activation of histone gene transcription; when associated with A-10; A-11; A-15 and A-18. Ref.13
Mutagenesis101L → A: Impairs activation of histone gene transcription; when associated with A-7; A-11; A-15 and A-18. Ref.13
Mutagenesis111V → A: Impairs activation of histone gene transcription; when associated with A-7; A-10; A-15 and A-18. Ref.13
Mutagenesis151L → A: Impairs activation of histone gene transcription; when associated with A-7; A-10; A-11 and A-18. Ref.13
Mutagenesis181E → A: Impairs activation of histone gene transcription; when associated with A-7; A-10; A-11 and A-15. Ref.13
Mutagenesis271F → A: Impairs activation of histone gene transcription; when associated with A-30. Ref.13
Mutagenesis301E → A: Impairs activation of histone gene transcription; when associated with A-27. Ref.13
Mutagenesis331 – 3333LFD → AAA: Impairs activation of histone gene transcription. Impairs interaction with BZW1, RUVBL1, RUVBL2 and TRRAP. Ref.28
Mutagenesis7751S → A: Impairs activation of histone gene transcription; when associated with A-779; A-1100; A-1270 and A-1350. Ref.9 Ref.14 Ref.16 Ref.25
Mutagenesis7791S → A: Impairs activation of histone gene transcription; when associated with A-775; A-1100; A-1270 and A-1350. Ref.9 Ref.14 Ref.16 Ref.25
Mutagenesis11001S → A: Impairs activation of histone gene transcription; when associated with A-775; A-779; A-1270 and A-1350. Ref.9 Ref.14 Ref.16 Ref.25
Mutagenesis12701T → A: Impairs activation of histone gene transcription; when associated with A-775; A-779; A-1100 and A-1350. Ref.9 Ref.14 Ref.16 Ref.25
Mutagenesis13501T → A: Impairs activation of histone gene transcription; when associated with A-775; A-779; A-1100 and A-1270. Ref.9 Ref.14 Ref.16 Ref.25
Sequence conflict221S → Y in AAB02735. Ref.6
Sequence conflict1011S → N in BAF84376. Ref.4
Sequence conflict3291F → L in BAF84376. Ref.4
Sequence conflict4711Y → N in CAA65824. Ref.2
Sequence conflict7851E → G in BAF82709. Ref.4
Sequence conflict11451Q → R in BAF82709. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q14207 [UniParc].

Last modified May 18, 2010. Version 3.
Checksum: D5C5E630A56227F9

FASTA1,427154,290
        10         20         30         40         50         60 
MLLPSDVARL VLGYLQQENL ISTCQTFILE SSDLKEYAEH CTDEGFIPAC LLSLFGKNLT 

        70         80         90        100        110        120 
TILNEYVAMK TKETSNNVPA IMSSLWKKLD HTLSQIRSMQ SSPRFAGSQR ARTRTGIAEI 

       130        140        150        160        170        180 
KRQRKLASQT APASAELLTL PYLSGQFTTP PSTGTQVTRP SGQISDPSRS YFVVVNHSQS 

       190        200        210        220        230        240 
QDTVTTGEAL NVIPGAQEKK AHASLMSPGR RKSESQRKST TLSGPHSTIR NFQDPNAFAV 

       250        260        270        280        290        300 
EKQMVIENAR EKILSNKSLQ EKLAENINKF LTSDNNIAQV PKQTDNNPTE PETSIDEFLG 

       310        320        330        340        350        360 
LPSEIHMSEE AIQDILEQTE SDPAFQALFD LFDYGKTKNN KNISQSISSQ PMESNPSIVL 

       370        380        390        400        410        420 
ADETNLAVKG SFETEESDGQ SGQPAFCTSY QNDDPLNALK NSNNHDVLRQ EDQENFSQIS 

       430        440        450        460        470        480 
TSIQKKAFKT AVPTEQKCDI DITFESVPNL NDFNQRGNSN AECNPHCAEL YTNQMSTETE 

       490        500        510        520        530        540 
MAIGIEKNSL SSNVPSESQL QPDQPDIPIT SFVSLGCEAN NENLILSGKS SQLLSQDTSL 

       550        560        570        580        590        600 
TGKPSKKSQF CENSNDTVKL KINFHGSKSS DSSEVHKSKI EINVLEPVMS QLSNCQDNSC 

       610        620        630        640        650        660 
LQSEILPVSV ESSHLNVSGQ VEIHLGDSLS STKQPSNDSA SVELNHTENE AQASKSENSQ 

       670        680        690        700        710        720 
EPSSSVKEEN TIFLSLGGNA NCEKVALTPP EGTPVENSHS LPPESVCSSV GDSHPESQNT 

       730        740        750        760        770        780 
DDKPSSNNSA EIDASNIVSL KVIISDDPFV SSDTELTSAV SSINGENLPT IILSSPTKSP 

       790        800        810        820        830        840 
TKNAELVKCL SSEETVGAVV YAEVGDSASM EQSLLTFKSE DSAVNNTQNE DGIAFSANVT 

       850        860        870        880        890        900 
PCVSKDGGYI QLMPATSTAF GNSNNILIAT CVTDPTALGT SVSQSNVVVL PGNSAPMTAQ 

       910        920        930        940        950        960 
PLPPQLQTPP RSNSVFAVNQ AVSPNFSQGS AIIIASPVQP VLQGMVGMIP VSVVGQNGNN 

       970        980        990       1000       1010       1020 
FSTPPRQVLH MPLTAPVCNR SIPQFPVPPK SQKAQGLRNK PCIGKQVNNL VDSSGHSVGC 

      1030       1040       1050       1060       1070       1080 
HAQKTEVSDK SIATDLGKKS EETTVPFPEE SIVPAAKPCH RRVLCFDSTT APVANTQGPN 

      1090       1100       1110       1120       1130       1140 
HKMVSQNKER NAVSFPNLDS PNVSSTLKPP SNNAIKREKE KPPLPKILSK SESAISRHTT 

      1150       1160       1170       1180       1190       1200 
IRETQSEKKV SPTEIVLESF HKATANKENE LCSDVERQKN PENSKLSIGQ QNGGLRSEKS 

      1210       1220       1230       1240       1250       1260 
IASLQEMTKK QGTSSNNKNV LSVGTAVKDL KQEQTKSASS LITTEMLQDI QRHSSVSRLA 

      1270       1280       1290       1300       1310       1320 
DSSDLPVPRT PGSGAGEKHK EEPIDIIKAP SSRRFSEDSS TSKVMVPPVT PDLPACSPAS 

      1330       1340       1350       1360       1370       1380 
ETGSENSVNM AAHTLMILSR AAISRTTSAT PLKDNTQQFR ASSRSTTKKR KIEELDERER 

      1390       1400       1410       1420 
NSRPSSKNLT NSSIPMKKKK IKKKKLPSSF PAGMDVDKFL LSLHYDE 

« Hide

References

« Hide 'large scale' references
[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]"The structure and organization of the human NPAT gene."
Imai T., Sugawara T., Nishiyama A., Shimada R., Ohki R., Seki N., Sagara M., Ito H., Yamauchi M., Hori T.
Genomics 42:388-392(1997) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], 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]"FLASH is required for histone transcription and S-phase progression."
Barcaroli D., Bongiorno-Borbone L., Terrinoni A., Hofmann T.G., Rossi M., Knight R.A., Matera A.G., Melino G., De Laurenzi V.
Proc. Natl. Acad. Sci. U.S.A. 103:14808-14812(2006) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS41710.1.
RefSeqNP_002510.2. NM_002519.2.
UniGeneHs.171061.
Hs.367437.

3D structure databases

ProteinModelPortalQ14207.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110924. 15 interactions.
DIPDIP-59961N.
IntActQ14207. 1 interaction.
STRING9606.ENSP00000278612.

PTM databases

PhosphoSiteQ14207.

Polymorphism databases

DMDM296439285.

Proteomic databases

MaxQBQ14207.
PaxDbQ14207.
PRIDEQ14207.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000278612; ENSP00000278612; ENSG00000149308.
GeneID4863.
KEGGhsa:4863.
UCSCuc001pjz.4. human.

Organism-specific databases

CTD4863.
GeneCardsGC11M108062.
H-InvDBHIX0035981.
HGNCHGNC:7896. NPAT.
HPAHPA056823.
MIM601448. gene.
neXtProtNX_Q14207.
PharmGKBPA31697.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG29266.
HOVERGENHBG108198.
InParanoidQ14207.
OMAFDLFDYG.
OrthoDBEOG7JDQX0.
PhylomeDBQ14207.
TreeFamTF332825.

Gene expression databases

ArrayExpressQ14207.
BgeeQ14207.
CleanExHS_NPAT.
GenevestigatorQ14207.

Family and domain databases

InterProIPR006594. LisH_dimerisation.
[Graphical view]
SMARTSM00667. LisH. 1 hit.
[Graphical view]
PROSITEPS50896. LISH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiNPAT_(gene).
GenomeRNAi4863.
NextBio18734.
PROQ14207.
SOURCESearch...

Entry information

Entry nameNPAT_HUMAN
AccessionPrimary (citable) accession number: Q14207
Secondary accession number(s): A8K1V5 expand/collapse secondary AC list , A8K6M2, Q13632, Q14967, Q16580, Q86W55, Q8IWE9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 18, 2010
Last modified: July 9, 2014
This is version 89 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM