Q14207 (NPAT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	NPAT
Synonyms:	CAND3, E14

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1427 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Nucleus › Cajal 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 process	Cell cycle Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Molecular function	Activator
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of transcription, DNA-dependent Inferred from direct assay PubMed 18850719. Source: UniProtKB regulation of transcription involved in G1/S phase of mitotic cell cycle Inferred from mutant phenotype Ref.19. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Cajal body Inferred from direct assay Ref.19PubMed 17577209PubMed 19170105. Source: UniProtKB
Molecular_function	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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1427	1427	Protein NPAT		PRO_0000318163
Regions
	Domain	3 – 35	33	LisH
	Region	1 – 318	318	Interaction with MIZF
	Region	5 – 25	21	Required for activation of histone gene transcription and interaction with MIZF
	Region	121 – 145	25	Required for activation of histone gene transcription and interaction with MIZF
	Region	262 – 338	77	Mediates transcriptional activation
	Region	629 – 653	25	Required for acceleration of G1 phase
	Region	828 – 853	26	Required for acceleration of G1 phase
	Region	1039 – 1054	16	Required for acceleration of G1 phase
	Region	1228 – 1252	25	Required for acceleration of G1 phase
	Region	1325 – 1349	25	Required for acceleration of G1 phase
Amino acid modifications
	Modified residue	775	1	Phosphoserine; by CDK2 Ref.9
	Modified residue	779	1	Phosphoserine; by CDK2 Ref.9
	Modified residue	1100	1	Phosphoserine; by CDK2 Ref.9
	Modified residue	1228	1	N6-acetyllysine Ref.29
	Modified residue	1270	1	Phosphothreonine; by CDK2 Ref.9
	Modified residue	1350	1	Phosphothreonine; by CDK2 Ref.9
Natural variations
	Natural variant	295	1	I → L. Ref.2 Corresponds to variant rs1131748 [ dbSNP | Ensembl ].		VAR_038696
	Natural variant	399	1	L → M. Ref.2 Corresponds to variant rs1051521 [ dbSNP | Ensembl ].		VAR_038697
	Natural variant	447	1	V → M. Corresponds to variant rs35504388 [ dbSNP | Ensembl ].		VAR_038698
	Natural variant	483	1	I → L. Corresponds to variant rs968207 [ dbSNP | Ensembl ].		VAR_038699
	Natural variant	540	1	L → F. Ref.4 Corresponds to variant rs4144901 [ dbSNP | Ensembl ].		VAR_038700
	Natural variant	575	1	V → I. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Corresponds to variant rs2070661 [ dbSNP | Ensembl ].		VAR_038701
	Natural variant	608	1	V → A. Corresponds to variant rs35095430 [ dbSNP | Ensembl ].		VAR_038702
	Natural variant	621	1	V → I. Ref.2 Corresponds to variant rs1051522 [ dbSNP | Ensembl ].		VAR_038703
	Natural variant	967	1	Q → E. Ref.2 Corresponds to variant rs1131750 [ dbSNP | Ensembl ].		VAR_038704
	Natural variant	973	1	L → V. Ref.2 Corresponds to variant rs1131751 [ dbSNP | Ensembl ].		VAR_038705
	Natural variant	987	1	V → A. Ref.2 Corresponds to variant rs1051524 [ dbSNP | Ensembl ].		VAR_038706
	Natural variant	999	1	N → K. Ref.4 Corresponds to variant rs34052882 [ dbSNP | Ensembl ].		VAR_038707
	Natural variant	1191	1	Q → R. Ref.2 Corresponds to variant rs1051525 [ dbSNP | Ensembl ].		VAR_038708
Experimental info
	Mutagenesis	7	1	V → A: Impairs activation of histone gene transcription; when associated with A-10; A-11; A-15 and A-18. Ref.13
	Mutagenesis	10	1	L → A: Impairs activation of histone gene transcription; when associated with A-7; A-11; A-15 and A-18. Ref.13
	Mutagenesis	11	1	V → A: Impairs activation of histone gene transcription; when associated with A-7; A-10; A-15 and A-18. Ref.13
	Mutagenesis	15	1	L → A: Impairs activation of histone gene transcription; when associated with A-7; A-10; A-11 and A-18. Ref.13
	Mutagenesis	18	1	E → A: Impairs activation of histone gene transcription; when associated with A-7; A-10; A-11 and A-15. Ref.13
	Mutagenesis	27	1	F → A: Impairs activation of histone gene transcription; when associated with A-30. Ref.13
	Mutagenesis	30	1	E → A: Impairs activation of histone gene transcription; when associated with A-27. Ref.13
	Mutagenesis	331 – 333	3	LFD → AAA: Impairs activation of histone gene transcription. Impairs interaction with BZW1, RUVBL1, RUVBL2 and TRRAP. Ref.28
	Mutagenesis	775	1	S → 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
	Mutagenesis	779	1	S → 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
	Mutagenesis	1100	1	S → 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
	Mutagenesis	1270	1	T → 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
	Mutagenesis	1350	1	T → 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 conflict	22	1	S → Y in AAB02735. Ref.6
	Sequence conflict	101	1	S → N in BAF84376. Ref.4
	Sequence conflict	329	1	F → L in BAF84376. Ref.4
	Sequence conflict	471	1	Y → N in CAA65824. Ref.2
	Sequence conflict	785	1	E → G in BAF82709. Ref.4
	Sequence conflict	1145	1	Q → R in BAF82709. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q14207 [UniParc]. Last modified May 18, 2010. Version 3. Checksum: D5C5E630A56227F9	FASTA	1,427	154,290
	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

References

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[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. , 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]	"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, MASS SPECTROMETRY.
[30]	"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.
IPI	IPI00290547.
RefSeq	NP_002510.2. NM_002519.2.
UniGene	Hs.171061. Hs.367437.
3D structure databases
ProteinModelPortal	Q14207.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-59961N.
IntAct	Q14207. 1 interaction.
STRING	9606.ENSP00000278612.
PTM databases
PhosphoSite	Q14207.
Polymorphism databases
DMDM	296439285.
Proteomic databases
PaxDb	Q14207.
PRIDE	Q14207.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000278612; ENSP00000278612; ENSG00000149308.
GeneID	4863.
KEGG	hsa:4863.
UCSC	uc001pjz.4. human.
Organism-specific databases
CTD	4863.
GeneCards	GC11M108062.
H-InvDB	HIX0035981.
HGNC	HGNC:7896. NPAT.
MIM	601448. gene.
neXtProt	NX_Q14207.
PharmGKB	PA31697.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG29266.
HOVERGEN	HBG108198.
InParanoid	Q14207.
OMA	FDLFDYG.
OrthoDB	EOG4MW856.
Gene expression databases
ArrayExpress	Q14207.
Bgee	Q14207.
CleanEx	HS_NPAT.
Genevestigator	Q14207.
Family and domain databases
InterPro	IPR006594. LisH_dimerisation. [Graphical view]
SMART	SM00667. LisH. 1 hit. [Graphical view]
PROSITE	PS50896. LISH. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	4863.
NextBio	18734.
SOURCE	Search...

Entry information

Entry name

NPAT_HUMAN

Accession

Primary (citable) accession number: Q14207
Secondary accession number(s): A8K1V5 , A8K6M2, Q13632, Q14967, Q16580, Q86W55, Q8IWE9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	May 18, 2010
Last modified:	April 3, 2013
This is version 79 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.