Skip Header

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

P48426

- PI42A_HUMAN

UniProt

P48426 - PI42A_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha

Gene

PIP4K2A

Organism
Homo sapiens (Human)
Status
Reviewed - 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

Vmax=466 pmol/min/µg enzyme1 Publication

GO - Molecular functioni

  1. 1-phosphatidylinositol-4-phosphate 5-kinase activity Source: UniProtKB
  2. 1-phosphatidylinositol-5-phosphate 4-kinase activity Source: UniProtKB-EC
  3. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. megakaryocyte development Source: Ensembl
  2. phosphatidylinositol biosynthetic process Source: Reactome
  3. phosphatidylinositol phosphorylation Source: GOC
  4. phospholipid metabolic process Source: Reactome
  5. 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: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: 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

  1. cytosol Source: Reactome
  2. nucleus Source: UniProtKB-KW
  3. plasma membrane Source: UniProtKB-KW
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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 406406Phosphatidylinositol 5-phosphate 4-kinase type-2 alphaPRO_0000185465Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei89 – 891N6-acetyllysine1 Publication
Modified residuei145 – 1451N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

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. 8 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:
PDBe
RCSB PDB
PDBj
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.

This entry describes 2 isoformsi produced by alternative splicing. Align

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:
EMBL
GenBank
DDBJ
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.
UniGeneiHs.57079.

Genome annotation databases

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

Polymorphism databases

DMDMi18266879.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS7141.1. [P48426-1 ]
PIRi A55967.
S57217.
RefSeqi NP_005019.2. NM_005028.4.
UniGenei Hs.57079.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2YBX X-ray 2.56 A/B 35-405 [» ]
ProteinModelPortali P48426.
SMRi P48426. Positions 31-405.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111322. 8 interactions.
IntActi P48426. 4 interactions.
MINTi MINT-1507380.
STRINGi 9606.ENSP00000365757.

Chemistry

ChEMBLi CHEMBL1795194.

PTM databases

PhosphoSitei P48426.

Polymorphism databases

DMDMi 18266879.

2D gel databases

OGPi P48426.

Proteomic databases

MaxQBi P48426.
PaxDbi P48426.
PeptideAtlasi P48426.
PRIDEi P48426.

Protocols and materials databases

DNASUi 5305.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000376573 ; ENSP00000365757 ; ENSG00000150867 . [P48426-1 ]
ENST00000545335 ; ENSP00000442098 ; ENSG00000150867 . [P48426-2 ]
GeneIDi 5305.
KEGGi hsa:5305.
UCSCi uc001irl.4. human. [P48426-1 ]

Organism-specific databases

CTDi 5305.
GeneCardsi GC10M022823.
HGNCi HGNC:8997. PIP4K2A.
MIMi 603140. gene.
neXtProti NX_P48426.
Orphaneti 99860. Precursor B-cell acute lymphoblastic leukemia.
PharmGKBi PA162399615.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5253.
GeneTreei ENSGT00760000119184.
HOGENOMi HOG000007832.
HOVERGENi HBG000072.
InParanoidi P48426.
KOi K00920.
OMAi IVECHGV.
OrthoDBi EOG708VZZ.
PhylomeDBi P48426.
TreeFami TF354315.

Enzyme and pathway databases

BioCyci MetaCyc:HS07693-MONOMER.
Reactomei REACT_121025. Synthesis of PIPs at the plasma membrane.

Miscellaneous databases

ChiTaRSi PIP4K2A. human.
GeneWikii PIP4K2A.
GenomeRNAii 5305.
NextBioi 20506.
PROi P48426.
SOURCEi Search...

Gene expression databases

Bgeei P48426.
CleanExi HS_PIP4K2A.
ExpressionAtlasi P48426. baseline and differential.
Genevestigatori P48426.

Family and domain databases

Gene3Di 3.30.800.10. 1 hit.
3.30.810.10. 1 hit.
InterProi IPR023610. 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 ]
PANTHERi PTHR23086. PTHR23086. 1 hit.
Pfami PF01504. PIP5K. 1 hit.
[Graphical view ]
SMARTi SM00330. PIPKc. 1 hit.
[Graphical view ]
PROSITEi PS51455. PIPK. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. "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].
  12. "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.
  13. "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.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [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: October 29, 2014
This is version 126 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

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