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Q9UBF8

- PI4KB_HUMAN

UniProt

Q9UBF8 - PI4KB_HUMAN

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Protein
Phosphatidylinositol 4-kinase beta
Gene
PI4KB, PIK4CB
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo-inositol 4-phosphate.1 Publication

Enzyme regulationi

Inhibited by wortmannin. Increased kinase activity upon interaction with NCS1/FREQ By similarity.1 Publication

GO - Molecular functioni

  1. 1-phosphatidylinositol 4-kinase activity Source: Reactome
  2. ATP binding Source: UniProtKB-KW
  3. protein binding Source: IntAct

GO - Biological processi

  1. phosphatidylinositol biosynthetic process Source: Reactome
  2. phosphatidylinositol-mediated signaling Source: InterPro
  3. phospholipid metabolic process Source: Reactome
  4. receptor-mediated endocytosis Source: ProtInc
  5. signal transduction Source: ProtInc
  6. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS07046-MONOMER.
ReactomeiREACT_120836. Synthesis of PIPs at the Golgi membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol 4-kinase beta (EC:2.7.1.67)
Short name:
PI4K-beta
Short name:
PI4Kbeta
Short name:
PtdIns 4-kinase beta
Alternative name(s):
NPIK
PI4K92
Gene namesi
Name:PI4KB
Synonyms:PIK4CB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:8984. PI4KB.

Subcellular locationi

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.3 Publications

GO - Cellular componenti

  1. Golgi membrane Source: Reactome
  2. cytoplasm Source: ProtInc
  3. cytosol Source: Reactome
  4. endosome Source: ProtInc
  5. mitochondrial outer membrane Source: UniProtKB-SubCell
  6. perinuclear region of cytoplasm Source: UniProtKB-SubCell
  7. plasma membrane Source: Ensembl
  8. rough endoplasmic reticulum membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Golgi apparatus, Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162399420.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 816816Phosphatidylinositol 4-kinase beta
PRO_0000088829Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei258 – 2581Phosphoserine3 Publications
Modified residuei263 – 2631Phosphothreonine1 Publication
Modified residuei266 – 2661Phosphoserine2 Publications
Modified residuei277 – 2771Phosphoserine2 Publications
Modified residuei294 – 2941Phosphoserine2 Publications
Modified residuei428 – 4281Phosphoserine5 Publications
Modified residuei438 – 4381Phosphothreonine1 Publication
Modified residuei511 – 5111Phosphoserine3 Publications
Modified residuei519 – 5191Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UBF8.
PaxDbiQ9UBF8.
PRIDEiQ9UBF8.

PTM databases

PhosphoSiteiQ9UBF8.

Miscellaneous databases

PMAP-CutDBQ9UBF8.

Expressioni

Tissue specificityi

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

Gene expression databases

ArrayExpressiQ9UBF8.
BgeeiQ9UBF8.
CleanExiHS_PI4KB.
GenevestigatoriQ9UBF8.

Organism-specific databases

HPAiCAB022071.
HPA006280.
HPA006281.

Interactioni

Subunit structurei

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.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ACBD3Q9H3P74EBI-1053214,EBI-1791792
NSP034952EBI-1053214,EBI-2548993From a different organism.

Protein-protein interaction databases

BioGridi111316. 7 interactions.
IntActiQ9UBF8. 6 interactions.
MINTiMINT-1681077.
STRINGi9606.ENSP00000271657.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4D0LX-ray2.94A/C/E121-799[»]
4D0MX-ray6.00A/C/G/I/M/O/Q/S/W/Y/c/g121-799[»]
ProteinModelPortaliQ9UBF8.
SMRiQ9UBF8. Positions 523-798.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 242214PIK helical
Add
BLAST
Domaini558 – 765208PI3K/PI4K
Add
BLAST

Sequence similaritiesi

Contains 1 PI3K/PI4K domain.
Contains 1 PIK helical domain.

Phylogenomic databases

eggNOGiCOG5032.
HOVERGENiHBG053597.
InParanoidiQ9UBF8.
KOiK00888.
OrthoDBiEOG773XFQ.
PhylomeDBiQ9UBF8.
TreeFamiTF102042.

Family and domain databases

Gene3Di1.10.1070.11. 1 hit.
InterProiIPR011009. 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]
PANTHERiPTHR10048. PTHR10048. 1 hit.
PTHR10048:SF22. PTHR10048:SF22. 1 hit.
PfamiPF00454. PI3_PI4_kinase. 1 hit.
[Graphical view]
SMARTiSM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS00915. 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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 11 Publication (identifier: Q9UBF8-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MGDTVVEPAP LKPTSEPTSG PPGNNGGSLL SVITEGVGEL SVIDPEVAQK    50
ACQEVLEKVK LLHGGVAVSS RGTPLELVNG DGVDSEIRCL DDPPAQIREE 100
EDEMGAAVAS GTAKGARRRR QNNSAKQSWL LRLFESKLFD ISMAISYLYN 150
SKEPGVQAYI GNRLFCFRNE DVDFYLPQLL NMYIHMDEDV GDAIKPYIVH 200
RCRQSINFSL QCALLLGAYS SDMHISTQRH SRGTKLRKLI LSDELKPAHR 250
KRELPSLSPA PDTGLSPSKR THQRSKSDAT ASISLSSNLK RTASNPKVEN 300
EDEELSSSTE SIDNSFSSPV RLAPEREFIK SLMAIGKRLA TLPTKEQKTQ 350
RLISELSLLN HKLPARVWLP TAGFDHHVVR VPHTQAVVLN SKDKAPYLIY 400
VEVLECENFD TTSVPARIPE NRIRSTRSVE NLPECGITHE QRAGSFSTVP 450
NYDNDDEAWS VDDIGELQVE LPEVHTNSCD NISQFSVDSI TSQESKEPVF 500
IAAGDIRRRL SEQLAHTPTA FKRDPEDPSA VALKEPWQEK VRRIREGSPY 550
GHLPNWRLLS VIVKCGDDLR QELLAFQVLK QLQSIWEQER VPLWIKPYKI 600
LVISADSGMI EPVVNAVSIH QVKKQSQLSL LDYFLQEHGS YTTEAFLSAQ 650
RNFVQSCAGY CLVCYLLQVK DRHNGNILLD AEGHIIHIDF GFILSSSPRN 700
LGFETSAFKL TTEFVDVMGG LDGDMFNYYK MLMLQGLIAA RKHMDKVVQI 750
VEIMQQGSQL PCFHGSSTIR NLKERFHMSM TEEQLQLLVE QMVDGSMRSI 800
TTKLYDGFQY LTNGIM 816
Length:816
Mass (Da):91,379
Last modified:May 1, 2000 - v1
Checksum:iCAD8791729BB4308
GO
Isoform 21 Publication (identifier: Q9UBF8-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:801
Mass (Da):89,807
Checksum:i22E1ABA37AA9A2BD
GO
Isoform 3 (identifier: Q9UBF8-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:484
Mass (Da):54,976
Checksum:i395A9DF64FC58A8C
GO

Sequence cautioni

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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 332332Missing in isoform 3.
VSP_037133Add
BLAST
Alternative sequencei304 – 31815Missing in isoform 2. 1 Publication
VSP_050627Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti216 – 2161L → V in AAC51156. 1 Publication
Sequence conflicti339 – 3391L → V in AAC51156. 1 Publication
Sequence conflicti340 – 3401A → V in AAC51156. 1 Publication
Sequence conflicti370 – 3701P → S in AAC51156. 1 Publication
Sequence conflicti446 – 4461F → S in BAG57793. 1 Publication
Sequence conflicti754 – 7541M → L in BAG57793. 1 Publication
Sequence conflicti796 – 7961S → G in BAG57793. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS55637.1. [Q9UBF8-3]
CCDS55638.1. [Q9UBF8-2]
PIRiJC5706.
RefSeqiNP_001185702.1. NM_001198773.1. [Q9UBF8-2]
NP_001185703.1. NM_001198774.1. [Q9UBF8-2]
NP_001185704.1. NM_001198775.1. [Q9UBF8-3]
NP_002642.1. NM_002651.2.
XP_005245318.1. XM_005245261.2. [Q9UBF8-1]
XP_005245319.1. XM_005245262.2. [Q9UBF8-1]
XP_005245320.1. XM_005245263.2. [Q9UBF8-1]
UniGeneiHs.632465.

Genome annotation databases

EnsembliENST00000271657; 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]
GeneIDi5298.
KEGGihsa:5298.
UCSCiuc001exr.3. human. [Q9UBF8-1]
uc001exs.3. human. [Q9UBF8-2]

Polymorphism databases

DMDMi38372507.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS55637.1. [Q9UBF8-3 ]
CCDS55638.1. [Q9UBF8-2 ]
PIRi JC5706.
RefSeqi NP_001185702.1. NM_001198773.1. [Q9UBF8-2 ]
NP_001185703.1. NM_001198774.1. [Q9UBF8-2 ]
NP_001185704.1. NM_001198775.1. [Q9UBF8-3 ]
NP_002642.1. NM_002651.2.
XP_005245318.1. XM_005245261.2. [Q9UBF8-1 ]
XP_005245319.1. XM_005245262.2. [Q9UBF8-1 ]
XP_005245320.1. XM_005245263.2. [Q9UBF8-1 ]
UniGenei Hs.632465.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4D0L X-ray 2.94 A/C/E 121-799 [» ]
4D0M X-ray 6.00 A/C/G/I/M/O/Q/S/W/Y/c/g 121-799 [» ]
ProteinModelPortali Q9UBF8.
SMRi Q9UBF8. Positions 523-798.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111316. 7 interactions.
IntActi Q9UBF8. 6 interactions.
MINTi MINT-1681077.
STRINGi 9606.ENSP00000271657.

Chemistry

BindingDBi Q9UBF8.
ChEMBLi CHEMBL2096619.
GuidetoPHARMACOLOGYi 2149.

PTM databases

PhosphoSitei Q9UBF8.

Polymorphism databases

DMDMi 38372507.

Proteomic databases

MaxQBi Q9UBF8.
PaxDbi Q9UBF8.
PRIDEi Q9UBF8.

Protocols and materials databases

DNASUi 5298.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000271657 ; 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 ]
GeneIDi 5298.
KEGGi hsa:5298.
UCSCi uc001exr.3. human. [Q9UBF8-1 ]
uc001exs.3. human. [Q9UBF8-2 ]

Organism-specific databases

CTDi 5298.
GeneCardsi GC01M151264.
H-InvDB HIX0001056.
HGNCi HGNC:8984. PI4KB.
HPAi CAB022071.
HPA006280.
HPA006281.
MIMi 602758. gene.
neXtProti NX_Q9UBF8.
PharmGKBi PA162399420.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5032.
HOVERGENi HBG053597.
InParanoidi Q9UBF8.
KOi K00888.
OrthoDBi EOG773XFQ.
PhylomeDBi Q9UBF8.
TreeFami TF102042.

Enzyme and pathway databases

BioCyci MetaCyc:HS07046-MONOMER.
Reactomei REACT_120836. Synthesis of PIPs at the Golgi membrane.

Miscellaneous databases

ChiTaRSi PI4KB. human.
GeneWikii PI4KB.
GenomeRNAii 5298.
NextBioi 20482.
PMAP-CutDB Q9UBF8.
PROi Q9UBF8.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UBF8.
Bgeei Q9UBF8.
CleanExi HS_PI4KB.
Genevestigatori Q9UBF8.

Family and domain databases

Gene3Di 1.10.1070.11. 1 hit.
InterProi IPR011009. 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 ]
PANTHERi PTHR10048. PTHR10048. 1 hit.
PTHR10048:SF22. PTHR10048:SF22. 1 hit.
Pfami PF00454. PI3_PI4_kinase. 1 hit.
[Graphical view ]
SMARTi SM00146. PI3Kc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 2 hits.
PROSITEi PS00915. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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. 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. 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].

Entry informationi

Entry nameiPI4KB_HUMAN
AccessioniPrimary (citable) accession number: Q9UBF8
Secondary accession number(s): B4DGI2
, O15096, P78405, Q5VWB9, Q5VWC0, Q5VWC1, Q9BWR6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: May 1, 2000
Last modified: September 3, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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