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Q9UBF8 (PI4KB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphatidylinositol 4-kinase beta

Short name=PI4K-beta
Short name=PI4Kbeta
Short name=PtdIns 4-kinase beta
EC=2.7.1.67
Alternative name(s):
NPIK
PI4K92
Gene names
Name:PI4KB
Synonyms:PIK4CB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length816 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Involved in Golgi-to-plasma membrane trafficking By similarity. 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. Increased kinase activity upon interaction with NCS1/FREQ By similarity. Ref.3

Subunit structure

Interacts with ARF1 and ARF3 in the Golgi complex, but not with ARF4, ARF5 or ARF6. Interacts with NCS1/FREQ in a calcium-independent manner By similarity. Interacts with CALN1/CABP8 and CALN2/CABP7; in a calcium-dependent manner By similarity. This binding competes with NCS1/FREQ binding By similarity. Ref.13

Subcellular location

Endomembrane system. Mitochondrion outer membrane; Peripheral membrane protein. Rough endoplasmic reticulum membrane; Peripheral membrane protein. Golgi apparatus. Cytoplasmperinuclear region. 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-bisphosphate (PIP2) on the Golgi complex. Ref.1 Ref.8 Ref.13

Tissue specificity

Widely expressed with highest levels in heart, skeletal muscle, pancreas, testis and ovary. Weakly expressed in liver. Ref.1 Ref.2 Ref.3

Sequence similarities

Belongs to the PI3/PI4-kinase family. Type III PI4K subfamily.

Contains 1 PI3K/PI4K domain.

Contains 1 PIK helical domain.

Sequence caution

The sequence BAA21661.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

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 componentCytoplasm
Endoplasmic reticulum
Golgi apparatus
Membrane
Mitochondrion
Mitochondrion outer membrane
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processphosphatidylinositol biosynthetic process

Traceable author statement. Source: Reactome

phosphatidylinositol-mediated signaling

Inferred from electronic annotation. Source: InterPro

phospholipid metabolic process

Traceable author statement. Source: Reactome

receptor-mediated endocytosis

Traceable author statement PubMed 9584208. Source: ProtInc

signal transduction

Traceable author statement Ref.3. Source: ProtInc

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentGolgi membrane

Traceable author statement. Source: Reactome

cytoplasm

Traceable author statement PubMed 9584208. Source: ProtInc

cytosol

Traceable author statement. Source: Reactome

endosome

Traceable author statement PubMed 9584208. Source: ProtInc

mitochondrial outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: Ensembl

rough endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function1-phosphatidylinositol 4-kinase activity

Traceable author statement. Source: Reactome

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ACBD3Q9H3P74EBI-1053214,EBI-1791792

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.
Note: Contains a phosphoserine at position 294.
Isoform 3 (identifier: Q9UBF8-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 816816Phosphatidylinositol 4-kinase beta
PRO_0000088829

Regions

Domain29 – 242214PIK helical
Domain558 – 765208PI3K/PI4K

Amino acid modifications

Modified residue2581Phosphoserine Ref.10 Ref.15 Ref.17
Modified residue2631Phosphothreonine Ref.10
Modified residue2661Phosphoserine Ref.10 Ref.17
Modified residue2771Phosphoserine Ref.10 Ref.15
Modified residue2941Phosphoserine Ref.10 Ref.15
Modified residue4281Phosphoserine Ref.12 Ref.15 Ref.16 Ref.17 Ref.19
Modified residue4381Phosphothreonine Ref.10
Modified residue5111Phosphoserine Ref.10 Ref.14 Ref.15
Modified residue5191Phosphothreonine Ref.10

Natural variations

Alternative sequence1 – 332332Missing in isoform 3.
VSP_037133
Alternative sequence304 – 31815Missing in isoform 2. Ref.1
VSP_050627

Experimental info

Sequence conflict2161L → V in AAC51156. Ref.3
Sequence conflict3391L → V in AAC51156. Ref.3
Sequence conflict3401A → V in AAC51156. Ref.3
Sequence conflict3701P → S in AAC51156. Ref.3
Sequence conflict4461F → S in BAG57793. Ref.4
Sequence conflict7541M → L in BAG57793. Ref.4
Sequence conflict7961S → G in BAG57793. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (NPIK-B) [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: CAD8791729BB4308

FASTA81691,379
        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 

« Hide

Isoform 2 (NPIK-C) [UniParc].

Checksum: 22E1ABA37AA9A2BD
Show »

FASTA80189,807
Isoform 3 [UniParc].

Checksum: 395A9DF64FC58A8C
Show »

FASTA48454,976

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. 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] (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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-258; THR-263; SER-266; SER-277; SER-294; THR-438; SER-511 AND THR-519.
[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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Specificity, promiscuity and localization of ARF protein interactions with NCS-1 and phosphatidylinositol-4 kinase-III beta."
Haynes L.P., Sherwood M.W., Dolman N.J., Burgoyne R.D.
Traffic 8:1080-1092(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARF1 AND ARF3, SUBCELLULAR LOCATION.
[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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-511, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258; SER-277; SER-428 AND SER-511, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-294 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[17]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258; SER-266 AND SER-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRJC5706.
RefSeqNP_001185702.1. NM_001198773.1.
NP_001185703.1. NM_001198774.1.
NP_001185704.1. NM_001198775.1.
NP_002642.1. NM_002651.2.
XP_005245318.1. XM_005245261.2.
XP_005245319.1. XM_005245262.2.
XP_005245320.1. XM_005245263.2.
UniGeneHs.632465.

3D structure databases

ProteinModelPortalQ9UBF8.
SMRQ9UBF8. Positions 559-804.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111316. 7 interactions.
IntActQ9UBF8. 6 interactions.
MINTMINT-1681077.
STRING9606.ENSP00000271657.

Chemistry

BindingDBQ9UBF8.
ChEMBLCHEMBL2096619.
GuidetoPHARMACOLOGY2149.

PTM databases

PhosphoSiteQ9UBF8.

Polymorphism databases

DMDM38372507.

Proteomic databases

PaxDbQ9UBF8.
PRIDEQ9UBF8.

Protocols and materials databases

DNASU5298.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000271657; ENSP00000271657; ENSG00000143393.
ENST00000368872; ENSP00000357866; ENSG00000143393. [Q9UBF8-2]
ENST00000368873; ENSP00000357867; ENSG00000143393. [Q9UBF8-1]
ENST00000368874; ENSP00000357868; ENSG00000143393. [Q9UBF8-2]
ENST00000368875; ENSP00000357869; ENSG00000143393.
ENST00000529142; ENSP00000433149; ENSG00000143393. [Q9UBF8-3]
GeneID5298.
KEGGhsa:5298.
UCSCuc001exr.3. human. [Q9UBF8-1]
uc001exs.3. human. [Q9UBF8-2]

Organism-specific databases

CTD5298.
GeneCardsGC01M151264.
H-InvDBHIX0001056.
HGNCHGNC:8984. PI4KB.
HPACAB022071.
HPA006280.
HPA006281.
MIM602758. gene.
neXtProtNX_Q9UBF8.
PharmGKBPA162399420.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5032.
HOVERGENHBG053597.
InParanoidQ9UBF8.
KOK00888.
OrthoDBEOG773XFQ.
PhylomeDBQ9UBF8.
TreeFamTF102042.

Enzyme and pathway databases

BioCycMetaCyc:HS07046-MONOMER.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ9UBF8.
BgeeQ9UBF8.
CleanExHS_PI4KB.
GenevestigatorQ9UBF8.

Family and domain databases

Gene3D1.10.1070.11. 1 hit.
InterProIPR011009. Kinase-like_dom.
IPR027003. Phosphatidylino_kinase.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR015433. PI_Kinase.
IPR001263. PInositide-3_kin_accessory_dom.
[Graphical view]
PANTHERPTHR10048. PTHR10048. 1 hit.
PTHR10048:SF22. PTHR10048:SF22. 1 hit.
PfamPF00454. PI3_PI4_kinase. 1 hit.
[Graphical view]
SMARTSM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 2 hits.
PROSITEPS00915. PI3_4_KINASE_1. 1 hit.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
PS51545. PIK_HELICAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPI4KB. human.
GeneWikiPI4KB.
GenomeRNAi5298.
NextBio20482.
PMAP-CutDBQ9UBF8.
PROQ9UBF8.
SOURCESearch...

Entry information

Entry namePI4KB_HUMAN
AccessionPrimary (citable) accession number: Q9UBF8
Secondary accession number(s): B4DGI2 expand/collapse secondary AC list , O15096, P78405, Q5VWB9, Q5VWC0, Q5VWC1, Q9BWR6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 117 of the entry and version 1 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 chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM