Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha

Gene

PIP4K2A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the phosphorylation of phosphatidylinositol 5-phosphate (PtdIns5P) on the fourth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). May exert its function by regulating the levels of PtdIns5P, which functions in the cytosol by increasing AKT activity and in the nucleus signals through ING2. May regulate the pool of cytosolic PtdIns5P in response to the activation of tyrosine phosphorylation. May negatively regulate insulin-stimulated glucose uptake by lowering the levels of PtdIns5P. May be involved in thrombopoiesis, and the terminal maturation of megakaryocytes and regulation of their size.1 Publication

Catalytic activityi

ATP + 1-phosphatidyl-1D-myo-inositol 5-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate.1 Publication

Kineticsi

  1. KM=50 µM for phosphatidylinositol-5- phosphate1 Publication
  1. Vmax=466 pmol/min/µg enzyme1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS07693-MONOMER.
ReactomeiREACT_121025. Synthesis of PIPs at the plasma membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha (EC:2.7.1.149)
Alternative name(s):
1-phosphatidylinositol 5-phosphate 4-kinase 2-alpha
Diphosphoinositide kinase 2-alpha
PIP5KIII
Phosphatidylinositol 5-phosphate 4-kinase type II alpha
Short name:
PI(5)P 4-kinase type II alpha
Short name:
PIP4KII-alpha
PtdIns(4)P-5-kinase B isoform
PtdIns(4)P-5-kinase C isoform
PtdIns(5)P-4-kinase isoform 2-alpha
Gene namesi
Name:PIP4K2A
Synonyms:PIP5K2, PIP5K2A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:8997. PIP4K2A.

Subcellular locationi

  • Cell membrane By similarity
  • Nucleus 1 Publication
  • Cytoplasm 1 Publication

  • Note: May translocate from the cytosol to the cell membrane upon activation of tyrosine phosphorylation. May translocate from the inner to the outer segments of the rod photoreceptor cells in response to light (By similarity). Localization to the nucleus is modulated by the interaction with PIP4K2B.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi131 – 1311G → L: Abolishes catalytic activity; when associated with F-138. 1 Publication
Mutagenesisi138 – 1381Y → F: Abolishes catalytic activity; when associated with L-131. 1 Publication

Organism-specific databases

Orphaneti99860. Precursor B-cell acute lymphoblastic leukemia.
PharmGKBiPA162399615.

Polymorphism and mutation databases

BioMutaiPIP4K2A.
DMDMi18266879.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed4 Publications
Chaini2 – 406405Phosphatidylinositol 5-phosphate 4-kinase type-2 alphaPRO_0000185465Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine4 Publications
Modified residuei3 – 31Phosphothreonine1 Publication
Modified residuei14 – 141Phosphoserine3 Publications
Modified residuei89 – 891N6-acetyllysine1 Publication
Modified residuei145 – 1451N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP48426.
PaxDbiP48426.
PeptideAtlasiP48426.
PRIDEiP48426.

2D gel databases

OGPiP48426.

PTM databases

PhosphoSiteiP48426.

Expressioni

Tissue specificityi

Expressed ubiquitously, with high levels in the brain. Present in most tissues, except notably skeletal muscle and small intestine.2 Publications

Gene expression databases

BgeeiP48426.
CleanExiHS_PIP4K2A.
ExpressionAtlasiP48426. baseline and differential.
GenevestigatoriP48426.

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with PIP4K2B. Interaction with PIP4K2B may regulate localization to the nucleus.By similarity1 Publication

Protein-protein interaction databases

BioGridi111322. 15 interactions.
IntActiP48426. 4 interactions.
MINTiMINT-1507380.
STRINGi9606.ENSP00000365757.

Structurei

Secondary structure

1
406
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi36 – 5217Combined sources
Helixi63 – 675Combined sources
Beta strandi69 – 8012Combined sources
Turni81 – 833Combined sources
Beta strandi86 – 949Combined sources
Helixi95 – 10410Combined sources
Helixi109 – 1179Combined sources
Beta strandi134 – 1363Combined sources
Beta strandi140 – 1478Combined sources
Helixi149 – 16820Combined sources
Turni169 – 1713Combined sources
Beta strandi178 – 1869Combined sources
Beta strandi189 – 1979Combined sources
Beta strandi202 – 2043Combined sources
Beta strandi207 – 2126Combined sources
Beta strandi215 – 2173Combined sources
Helixi223 – 2264Combined sources
Beta strandi228 – 2303Combined sources
Helixi235 – 2406Combined sources
Helixi249 – 26820Combined sources
Beta strandi271 – 2733Combined sources
Beta strandi275 – 2828Combined sources
Helixi283 – 2919Combined sources
Turni334 – 3363Combined sources
Beta strandi340 – 3423Combined sources
Beta strandi351 – 3588Combined sources
Beta strandi362 – 3643Combined sources
Helixi390 – 40415Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YBXX-ray2.56A/B35-405[»]
ProteinModelPortaliP48426.
SMRiP48426. Positions 31-405.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 405373PIPKPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 PIPK domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5253.
GeneTreeiENSGT00760000119184.
HOGENOMiHOG000007832.
HOVERGENiHBG000072.
InParanoidiP48426.
KOiK00920.
OMAiIVECHGV.
OrthoDBiEOG708VZZ.
PhylomeDBiP48426.
TreeFamiTF354315.

Family and domain databases

Gene3Di3.30.800.10. 1 hit.
3.30.810.10. 1 hit.
InterProiIPR023610. PInositol-4-P-5-kinase.
IPR027483. PInositol-4-P-5-kinase_C.
IPR002498. PInositol-4-P-5-kinase_core.
IPR027484. PInositol-4-P-5-kinase_N.
IPR016034. PInositol-4P-5-kinase_core_sub.
[Graphical view]
PANTHERiPTHR23086. PTHR23086. 1 hit.
PfamiPF01504. PIP5K. 1 hit.
[Graphical view]
SMARTiSM00330. PIPKc. 1 hit.
[Graphical view]
PROSITEiPS51455. PIPK. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P48426-1) [UniParc]FASTAAdd to basket

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

        10         20         30         40         50
MATPGNLGSS VLASKTKTKK KHFVAQKVKL FRASDPLLSV LMWGVNHSIN
60 70 80 90 100
ELSHVQIPVM LMPDDFKAYS KIKVDNHLFN KENMPSHFKF KEYCPMVFRN
110 120 130 140 150
LRERFGIDDQ DFQNSLTRSA PLPNDSQARS GARFHTSYDK RYIIKTITSE
160 170 180 190 200
DVAEMHNILK KYHQYIVECH GITLLPQFLG MYRLNVDGVE IYVIVTRNVF
210 220 230 240 250
SHRLSVYRKY DLKGSTVARE ASDKEKAKEL PTLKDNDFIN EGQKIYIDDN
260 270 280 290 300
NKKVFLEKLK KDVEFLAQLK LMDYSLLVGI HDVERAEQEE VECEENDGEE
310 320 330 340 350
EGESDGTHPV GTPPDSPGNT LNSSPPLAPG EFDPNIDVYG IKCHENSPRK
360 370 380 390 400
EVYFMAIIDI LTHYDAKKKA AHAAKTVKHG AGAEISTVNP EQYSKRFLDF

IGHILT
Length:406
Mass (Da):46,225
Last modified:August 14, 2001 - v2
Checksum:i5BAF0A27CC9EF376
GO
Isoform 2 (identifier: P48426-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-59: Missing.

Note: No experimental confirmation available.

Show »
Length:347
Mass (Da):39,802
Checksum:iE8E3F2DADE991A74
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti101 – 1033LRE → CGK in AAB35041 (PubMed:7639683).Curated
Sequence conflicti109 – 1091D → V in AAB35041 (PubMed:7639683).Curated
Sequence conflicti143 – 1431I → M in AAB35041 (PubMed:7639683).Curated
Sequence conflicti177 – 1782QF → HL in AAB35041 (PubMed:7639683).Curated
Sequence conflicti333 – 3331D → E in AAB35041 (PubMed:7639683).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti7 – 71L → I.
Corresponds to variant rs11813789 [ dbSNP | Ensembl ].
VAR_059764
Natural varianti251 – 2511N → S.1 Publication
Corresponds to variant rs10828317 [ dbSNP | Ensembl ].
VAR_024565

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5959Missing in isoform 2. 1 PublicationVSP_056458Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14957 mRNA. Translation: AAA64835.2.
S78798 mRNA. Translation: AAB35041.1.
AL513128, AL157707, AL390318 Genomic DNA. Translation: CAH72211.1.
AK294817 mRNA. Translation: BAG57933.1.
EF445009 Genomic DNA. Translation: ACA06044.1.
EF445009 Genomic DNA. Translation: ACA06045.1.
AL157707, AL390318, AL513128 Genomic DNA. Translation: CAI39585.1.
AL390318, AL157707, AL513128 Genomic DNA. Translation: CAH70526.1.
CH471072 Genomic DNA. Translation: EAW86140.1.
CH471072 Genomic DNA. Translation: EAW86141.1.
BC018034 mRNA. Translation: AAH18034.1.
CCDSiCCDS7141.1. [P48426-1]
PIRiA55967.
S57217.
RefSeqiNP_005019.2. NM_005028.4. [P48426-1]
UniGeneiHs.57079.

Genome annotation databases

EnsembliENST00000376573; ENSP00000365757; ENSG00000150867. [P48426-1]
ENST00000545335; ENSP00000442098; ENSG00000150867. [P48426-2]
GeneIDi5305.
KEGGihsa:5305.
UCSCiuc001irl.4. human. [P48426-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14957 mRNA. Translation: AAA64835.2.
S78798 mRNA. Translation: AAB35041.1.
AL513128, AL157707, AL390318 Genomic DNA. Translation: CAH72211.1.
AK294817 mRNA. Translation: BAG57933.1.
EF445009 Genomic DNA. Translation: ACA06044.1.
EF445009 Genomic DNA. Translation: ACA06045.1.
AL157707, AL390318, AL513128 Genomic DNA. Translation: CAI39585.1.
AL390318, AL157707, AL513128 Genomic DNA. Translation: CAH70526.1.
CH471072 Genomic DNA. Translation: EAW86140.1.
CH471072 Genomic DNA. Translation: EAW86141.1.
BC018034 mRNA. Translation: AAH18034.1.
CCDSiCCDS7141.1. [P48426-1]
PIRiA55967.
S57217.
RefSeqiNP_005019.2. NM_005028.4. [P48426-1]
UniGeneiHs.57079.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YBXX-ray2.56A/B35-405[»]
ProteinModelPortaliP48426.
SMRiP48426. Positions 31-405.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111322. 15 interactions.
IntActiP48426. 4 interactions.
MINTiMINT-1507380.
STRINGi9606.ENSP00000365757.

Chemistry

ChEMBLiCHEMBL1795194.

PTM databases

PhosphoSiteiP48426.

Polymorphism and mutation databases

BioMutaiPIP4K2A.
DMDMi18266879.

2D gel databases

OGPiP48426.

Proteomic databases

MaxQBiP48426.
PaxDbiP48426.
PeptideAtlasiP48426.
PRIDEiP48426.

Protocols and materials databases

DNASUi5305.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000376573; ENSP00000365757; ENSG00000150867. [P48426-1]
ENST00000545335; ENSP00000442098; ENSG00000150867. [P48426-2]
GeneIDi5305.
KEGGihsa:5305.
UCSCiuc001irl.4. human. [P48426-1]

Organism-specific databases

CTDi5305.
GeneCardsiGC10M022823.
HGNCiHGNC:8997. PIP4K2A.
MIMi603140. gene.
neXtProtiNX_P48426.
Orphaneti99860. Precursor B-cell acute lymphoblastic leukemia.
PharmGKBiPA162399615.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5253.
GeneTreeiENSGT00760000119184.
HOGENOMiHOG000007832.
HOVERGENiHBG000072.
InParanoidiP48426.
KOiK00920.
OMAiIVECHGV.
OrthoDBiEOG708VZZ.
PhylomeDBiP48426.
TreeFamiTF354315.

Enzyme and pathway databases

BioCyciMetaCyc:HS07693-MONOMER.
ReactomeiREACT_121025. Synthesis of PIPs at the plasma membrane.

Miscellaneous databases

ChiTaRSiPIP4K2A. human.
GeneWikiiPIP4K2A.
GenomeRNAii5305.
NextBioi20506.
PROiP48426.
SOURCEiSearch...

Gene expression databases

BgeeiP48426.
CleanExiHS_PIP4K2A.
ExpressionAtlasiP48426. baseline and differential.
GenevestigatoriP48426.

Family and domain databases

Gene3Di3.30.800.10. 1 hit.
3.30.810.10. 1 hit.
InterProiIPR023610. PInositol-4-P-5-kinase.
IPR027483. PInositol-4-P-5-kinase_C.
IPR002498. PInositol-4-P-5-kinase_core.
IPR027484. PInositol-4-P-5-kinase_N.
IPR016034. PInositol-4P-5-kinase_core_sub.
[Graphical view]
PANTHERiPTHR23086. PTHR23086. 1 hit.
PfamiPF01504. PIP5K. 1 hit.
[Graphical view]
SMARTiSM00330. PIPKc. 1 hit.
[Graphical view]
PROSITEiPS51455. PIPK. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The sequence of phosphatidylinositol-4-phosphate 5-kinase defines a novel family of lipid kinases."
    Boronenkov I.V., Anderson R.A.
    J. Biol. Chem. 270:2881-2884(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 30-42; 74-88; 93-112; 141-145; 254-259; 281-297 AND 383-406, TISSUE SPECIFICITY.
    Tissue: Placenta.
  2. Boronenkov I.V.
    Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 298-310 AND 381-382.
  3. "The cloning and sequence of the C isoform of PtdIns4P 5-kinase."
    Divecha N., Truong O., Hsuan J.J., Hinchliffe K.A., Irvine R.F.
    Biochem. J. 309:715-719(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT SER-251.
    Tissue: Leukocyte.
  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 2).
    Tissue: Brain.
  5. NHLBI resequencing and genotyping service (RS&G)
    Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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 1).
    Tissue: Hippocampus.
  9. "A new pathway for synthesis of phosphatidylinositol-4,5-bisphosphate."
    Rameh L.E., Tolias K.F., Duckworth B.C., Cantley L.C.
    Nature 390:192-196(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY.
  10. "Regulation of extranuclear PtdIns5P production by phosphatidylinositol phosphate 4-kinase 2alpha."
    Wilcox A., Hinchliffe K.A.
    FEBS Lett. 582:1391-1394(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3 AND SER-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  14. "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-89 AND LYS-145, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "PIP4Kbeta interacts with and modulates nuclear localization of the high-activity PtdIns5P-4-kinase isoform PIP4Kalpha."
    Bultsma Y., Keune W.-J., Divecha N.
    Biochem. J. 430:223-235(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH PIP4K2B, SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-131 AND TYR-138, IDENTIFICATION BY MASS SPECTROMETRY.
  16. "Localization, regulation and function of type II phosphatidylinositol 5-phosphate 4-kinases."
    Clarke J.H., Wang M., Irvine R.F.
    Adv. Enzyme Regul. 50:12-18(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPI42A_HUMAN
AccessioniPrimary (citable) accession number: P48426
Secondary accession number(s): B0YJ66
, B4DGX2, D3DRV1, P53807, Q5VUX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: August 14, 2001
Last modified: April 29, 2015
This is version 130 of the entry and version 2 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

Caution

This protein was previously thought to be a phosphatidylinositol 4-phosphate 5-kinase.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.