Reviewed, UniProtKB/Swiss-Prot Q9UBF8 (PI4KB_HUMAN)

Names and origin

Protein names

Recommended name:
    Phosphatidylinositol 4-kinase beta
      Short name=PtdIns 4-kinase beta
      Short name=PI4K-beta
      Short name=PI4Kbeta
    EC=2.7.1.67
Alternative name(s):
    NPIK
    PI4K92

Gene names

Name:	PI4KB
Synonyms:	PIK4CB

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	816 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Phosphorylates phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate (PIP). May regulate Golgi disintegration/reorganization during mitosis, possibly via its phosphorylation. Ref.1 Ref.9 Ref.11
Catalytic activity	ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo-inositol 4-phosphate. Ref.1
Enzyme regulation	Inhibited by wortmannin. Ref.3
Subcellular location	Endomembrane system. Mitochondrion outer membrane; Peripheral membrane protein. Rough endoplasmic reticulum membrane; Peripheral membrane protein. Golgi apparatus. Note: Found in the outer membrane of mitochondria and membranes of the rough endoplasmic reticulum. Recruited to the Golgi complex by the small GTPase ARF to stimulate the synthesis of phosphatidylinositol 4,5-biphosphate (PIP2) on the Golgi complex.
Tissue specificity	Widely expressed with highest levels in heart, skeletal muscle, pancreas, testis and ovary. Weakly expressed in liver. Ref.1 Ref.3 Ref.2
Sequence similarities	Belongs to the PI3/PI4-kinase family. Type III PI4K subfamily. Contains 1 PI3K/PI4K domain.
Sequence caution	The sequence CAH70326.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence EAW53450.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Golgi apparatus Membrane Mitochondrion Mitochondrion outer membrane
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	phosphatidylinositol biosynthetic process Ref.3 Traceable author statement. Source: ProtInc phosphoinositide phosphorylation Inferred from electronic annotation. Source: InterPro phosphoinositide-mediated signaling Inferred from electronic annotation. Source: InterPro receptor-mediated endocytosis Traceable author statement. Source: ProtInc
Cellular component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell endosome Traceable author statement. Source: ProtInc mitochondrial outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell rough endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	1-phosphatidylinositol 4-kinase activity Traceable author statement. Source: ProtInc ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
YWHAB	P31946	1	EBI-1053214,EBI-359815
YWHAG	P61981	1	EBI-1053214,EBI-359832
YWHAQ	P27348	1	EBI-1053214,EBI-359854

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 Ref.1 (identifier: Q9UBF8-1)

Also known as: NPIK-B;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 Ref.1 (identifier: Q9UBF8-2)

Also known as: NPIK-C;

The sequence of this isoform differs from the canonical sequence as follows:
     304-318: Missing.

Isoform 3 (identifier: Q9UBF8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-332: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 816	816	Phosphatidylinositol 4-kinase beta		PRO_0000088829
Regions
	Domain	558 – 765	208	PI3K/PI4K
Amino acid modifications
	Modified residue	258	1	Phosphoserine Ref.15 Ref.10
	Modified residue	263	1	Phosphothreonine Ref.15 Ref.10
	Modified residue	266	1	Phosphoserine Ref.14 Ref.10
	Modified residue	277	1	Phosphoserine Ref.15 Ref.13 Ref.10
	Modified residue	294	1	Phosphoserine Ref.15 Ref.10
	Modified residue	428	1	Phosphoserine Ref.15 Ref.12
	Modified residue	438	1	Phosphothreonine Ref.10
	Modified residue	511	1	Phosphoserine Ref.15 Ref.14 Ref.12 Ref.10
	Modified residue	517	1	Phosphothreonine Ref.14
	Modified residue	519	1	Phosphothreonine Ref.10
Natural variations
	Alternative sequence	1 – 332	332	Missing in isoform 3.		VSP_037133
	Alternative sequence	304 – 318	15	Missing in isoform 2. Ref.1		VSP_050627
Experimental info
	Sequence conflict	216	1	L → V in AAC51156. Ref.3
	Sequence conflict	339	1	L → V in AAC51156. Ref.3
	Sequence conflict	340	1	A → V in AAC51156. Ref.3
	Sequence conflict	370	1	P → S in AAC51156. Ref.3
	Sequence conflict	446	1	F → S in BAG57793. Ref.4
	Sequence conflict	754	1	M → L in BAG57793. Ref.4
	Sequence conflict	796	1	S → G in BAG57793. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (NPIK-B) [UniParc]. Last modified May 1, 2000. Version 1. Checksum: CAD8791729BB4308	FASTA	816	91,379
	10 20 30 40 50 60 MGDTVVEPAP LKPTSEPTSG PPGNNGGSLL SVITEGVGEL SVIDPEVAQK ACQEVLEKVK 70 80 90 100 110 120 LLHGGVAVSS RGTPLELVNG DGVDSEIRCL DDPPAQIREE EDEMGAAVAS GTAKGARRRR 130 140 150 160 170 180 QNNSAKQSWL LRLFESKLFD ISMAISYLYN SKEPGVQAYI GNRLFCFRNE DVDFYLPQLL 190 200 210 220 230 240 NMYIHMDEDV GDAIKPYIVH RCRQSINFSL QCALLLGAYS SDMHISTQRH SRGTKLRKLI 250 260 270 280 290 300 LSDELKPAHR KRELPSLSPA PDTGLSPSKR THQRSKSDAT ASISLSSNLK RTASNPKVEN 310 320 330 340 350 360 EDEELSSSTE SIDNSFSSPV RLAPEREFIK SLMAIGKRLA TLPTKEQKTQ RLISELSLLN 370 380 390 400 410 420 HKLPARVWLP TAGFDHHVVR VPHTQAVVLN SKDKAPYLIY VEVLECENFD TTSVPARIPE 430 440 450 460 470 480 NRIRSTRSVE NLPECGITHE QRAGSFSTVP NYDNDDEAWS VDDIGELQVE LPEVHTNSCD 490 500 510 520 530 540 NISQFSVDSI TSQESKEPVF IAAGDIRRRL SEQLAHTPTA FKRDPEDPSA VALKEPWQEK 550 560 570 580 590 600 VRRIREGSPY GHLPNWRLLS VIVKCGDDLR QELLAFQVLK QLQSIWEQER VPLWIKPYKI 610 620 630 640 650 660 LVISADSGMI EPVVNAVSIH QVKKQSQLSL LDYFLQEHGS YTTEAFLSAQ RNFVQSCAGY 670 680 690 700 710 720 CLVCYLLQVK DRHNGNILLD AEGHIIHIDF GFILSSSPRN LGFETSAFKL TTEFVDVMGG 730 740 750 760 770 780 LDGDMFNYYK MLMLQGLIAA RKHMDKVVQI VEIMQQGSQL PCFHGSSTIR NLKERFHMSM 790 800 810 TEEQLQLLVE QMVDGSMRSI TTKLYDGFQY LTNGIM
	Isoform 2 (NPIK-C). Checksum: 22E1ABA37AA9A2BD	FASTA	801	89,807
	10 20 30 40 50 60 MGDTVVEPAP LKPTSEPTSG PPGNNGGSLL SVITEGVGEL SVIDPEVAQK ACQEVLEKVK 70 80 90 100 110 120 LLHGGVAVSS RGTPLELVNG DGVDSEIRCL DDPPAQIREE EDEMGAAVAS GTAKGARRRR 130 140 150 160 170 180 QNNSAKQSWL LRLFESKLFD ISMAISYLYN SKEPGVQAYI GNRLFCFRNE DVDFYLPQLL 190 200 210 220 230 240 NMYIHMDEDV GDAIKPYIVH RCRQSINFSL QCALLLGAYS SDMHISTQRH SRGTKLRKLI 250 260 270 280 290 300 LSDELKPAHR KRELPSLSPA PDTGLSPSKR THQRSKSDAT ASISLSSNLK RTASNPKVEN 310 320 330 340 350 360 EDEPVRLAPE REFIKSLMAI GKRLATLPTK EQKTQRLISE LSLLNHKLPA RVWLPTAGFD 370 380 390 400 410 420 HHVVRVPHTQ AVVLNSKDKA PYLIYVEVLE CENFDTTSVP ARIPENRIRS TRSVENLPEC 430 440 450 460 470 480 GITHEQRAGS FSTVPNYDND DEAWSVDDIG ELQVELPEVH TNSCDNISQF SVDSITSQES 490 500 510 520 530 540 KEPVFIAAGD IRRRLSEQLA HTPTAFKRDP EDPSAVALKE PWQEKVRRIR EGSPYGHLPN 550 560 570 580 590 600 WRLLSVIVKC GDDLRQELLA FQVLKQLQSI WEQERVPLWI KPYKILVISA DSGMIEPVVN 610 620 630 640 650 660 AVSIHQVKKQ SQLSLLDYFL QEHGSYTTEA FLSAQRNFVQ SCAGYCLVCY LLQVKDRHNG 670 680 690 700 710 720 NILLDAEGHI IHIDFGFILS SSPRNLGFET SAFKLTTEFV DVMGGLDGDM FNYYKMLMLQ 730 740 750 760 770 780 GLIAARKHMD KVVQIVEIMQ QGSQLPCFHG SSTIRNLKER FHMSMTEEQL QLLVEQMVDG 790 800 SMRSITTKLY DGFQYLTNGI M
	Isoform 3. Checksum: 395A9DF64FC58A8C	FASTA	484	54,976
	10 20 30 40 50 60 MAIGKRLATL PTKEQKTQRL ISELSLLNHK LPARVWLPTA GFDHHVVRVP HTQAVVLNSK 70 80 90 100 110 120 DKAPYLIYVE VLECENFDTT SVPARIPENR IRSTRSVENL PECGITHEQR AGSFSTVPNY 130 140 150 160 170 180 DNDDEAWSVD DIGELQVELP EVHTNSCDNI SQFSVDSITS QESKEPVFIA AGDIRRRLSE 190 200 210 220 230 240 QLAHTPTAFK RDPEDPSAVA LKEPWQEKVR RIREGSPYGH LPNWRLLSVI VKCGDDLRQE 250 260 270 280 290 300 LLAFQVLKQL QSIWEQERVP LWIKPYKILV ISADSGMIEP VVNAVSIHQV KKQSQLSLLD 310 320 330 340 350 360 YFLQEHGSYT TEAFLSAQRN FVQSCAGYCL VCYLLQVKDR HNGNILLDAE GHIIHIDFGF 370 380 390 400 410 420 ILSSSPRNLG FETSAFKLTT EFVDVMGGLD GDMFNYYKML MLQGLIAARK HMDKVVQIVE 430 440 450 460 470 480 IMQQGSQLPC FHGSSTIRNL KERFHMSMTE EQLQLLVEQM VDGSMRSITT KLYDGFQYLT NGIM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and characterization of a novel human phosphatidylinositol 4-kinase." Suzuki K., Hirano H., Okutomi K., Suzuki M., Kuga Y., Fujiwara T., Kanemoto N., Isono K., Horie M. DNA Res. 4:273-280(1997) [PubMed: 9405935] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Fetal brain.
[2]	"Complementary DNA cloning and chromosomal mapping of a novel phosphatidylinositol kinase gene." Saito T., Seki N., Ishii H., Ohira M., Hayashi A., Kozuma S., Hori T.-A. DNA Res. 4:301-305(1997) [PubMed: 9405938] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY. Tissue: Brain.
[3]	"Cloning and characterization of a wortmannin-sensitive human phosphatidylinositol 4-kinase." Meyers R., Cantley L.C. J. Biol. Chem. 272:4384-4390(1997) [PubMed: 9020160] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ENZYME REGULATION, TISSUE SPECIFICITY. Tissue: Heart.
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Brain.
[5]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain and Testis.
[8]	"Subcellular locations of phosphatidylinositol 4-kinase isoforms." Wong K., Meyers R., Cantley L.C. J. Biol. Chem. 272:13236-13241(1997) [PubMed: 9148941] [Abstract] Cited for: SUBCELLULAR LOCATION.
[9]	"ARF mediates recruitment of PtdIns-4-OH kinase-beta and stimulates synthesis of PtdIns(4,5)P2 on the Golgi complex." Godi A., Pertile P., Meyers R., Marra P., Di Tullio G., Iurisci C., Luini A., Corda D., De Matteis M.A. Nat. Cell Biol. 1:280-287(1999) [PubMed: 10559940] [Abstract] Cited for: FUNCTION.
[10]	"Human phosphatidylinositol 4-kinase isoform PI4K92. Expression of the recombinant enzyme and determination of multiple phosphorylation sites." Suer S., Sickmann A., Meyer H.E., Herberg F.W., Heilmeyer L.M.G. Jr. Eur. J. Biochem. 268:2099-2106(2001) [PubMed: 11277933] [Abstract] Cited for: PHOSPHORYLATION.
[11]	"Mammalian phosphatidylinositol 4-kinases." Heilmeyer L.M.G. Jr., Vereb G. Jr., Vereb G., Kakuk A., Szivak I. IUBMB Life 55:59-65(2003) [PubMed: 12749687] [Abstract] Cited for: FUNCTION.
[12]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428 AND SER-511, MASS SPECTROMETRY. Tissue: Epithelium.
[13]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, MASS SPECTROMETRY.
[14]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266; SER-511 AND THR-517, MASS SPECTROMETRY.
[15]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258; THR-263; SER-277; SER-294; SER-428 AND SER-511, MASS SPECTROMETRY.
[16]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ011121 mRNA. Translation: CAA09495.1. AJ011122 mRNA. No translation available. AJ011123 mRNA. Translation: CAA09496.1. AB005910 mRNA. Translation: BAA21661.1. Different initiation. U81802 mRNA. Translation: AAC51156.1. AK294606 mRNA. Translation: BAG57793.1. AL391069 Genomic DNA. Translation: CAH70324.1. AL391069 Genomic DNA. Translation: CAH70325.1. AL391069 Genomic DNA. Translation: CAH70326.1. Sequence problems. CH471121 Genomic DNA. Translation: EAW53449.1. CH471121 Genomic DNA. Translation: EAW53450.1. Sequence problems. BC000029 mRNA. Translation: AAH00029.1. BC040300 mRNA. Translation: AAH40300.1.
IPI	IPI00002591. IPI00165547.
PIR	JC5706.
RefSeq	NP_002642.1.
UniGene	Hs.632465
3D structure databases
HSSP	HSSP built from PDB template 1E8Y based on UniProtKB P48736.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UBF8. 3 interactions.
PTM databases
PhosphoSite	Q9UBF8.
Proteomic databases
PRIDE	Q9UBF8.
Genome annotation databases
Ensembl	ENSG00000143393. Homo sapiens. [Contig view]
GeneID	5298.
KEGG	hsa:5298.
Organism-specific databases
GeneCards	GC01M149532.
H-InvDB	HIX0001056.
HGNC	HGNC:8984. PI4KB.
HPA	HPA006280. HPA006281.
MIM	602758. gene.
PharmGKB	PA33317.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	Q9UBF8.
Enzyme and pathway databases
BRENDA	2.7.1.67. 247.
Pathway_Interaction_DB	avb3_integrin_pathway. Integrins in angiogenesis.
Gene expression databases
ArrayExpress	Q9UBF8.
Bgee	Q9UBF8.
CleanEx	HS_PI4KB.
GermOnline	ENSG00000143393. Homo sapiens.
Family and domain databases
InterPro	IPR000403. PI3/4_kinase_cat. IPR018936. PI3/4_kinase_CS. IPR015433. PI_Kinase. [Graphical view]
Gene3D	G3DSA:1.10.1070.11. PI3/4_kinase_cat. 1 hit.
PANTHER	PTHR10048. PI_Kinase. 1 hit.
Pfam	PF00454. PI3_PI4_kinase. 1 hit. [Graphical view]
SMART	SM00146. PI3Kc. 1 hit. [Graphical view]
PROSITE	PS00915. PI3_4_KINASE_1. 1 hit. PS00916. PI3_4_KINASE_2. 1 hit. PS50290. PI3_4_KINASE_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	20482.
PMAP-CutDB	Q9UBF8.
SOURCE	Search...

Entry information

Entry name

PI4KB_HUMAN

Accession

Primary (citable) accession number: Q9UBF8
Secondary accession number(s): B4DGI2 , O15096, P78405, Q5VWB9, Q5VWC0, Q5VWC1, Q9BWR6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 14, 2003
Last sequence update:	May 1, 2000
Last modified:	June 16, 2009
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)