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P42356 (PI4KA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphatidylinositol 4-kinase alpha

Short name=PI4-kinase alpha
Short name=PI4K-alpha
Short name=PtdIns-4-kinase alpha
EC=2.7.1.67
Gene names
Name:PI4KA
Synonyms:PIK4, PIK4CA
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2044 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts on phosphatidylinositol (PtdIns) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate.

Catalytic activity

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

Enzyme regulation

This is a type II PtdIns-4-kinase activated by detergents such as triton and inhibited by adenosine.

Tissue specificity

Expressed ubiquitously. Highest levels in placenta and brain. Little or no expression in lung, liver, pancreas, testis or leukocytes. Ref.1 Ref.2

Sequence similarities

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

Contains 1 PI3K/PI4K domain.

Contains 1 PIK helical domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P42356-1)

Also known as: PI4K230;

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 (identifier: P42356-2)

Also known as: PI4K97;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1190: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 20442044Phosphatidylinositol 4-kinase alpha
PRO_0000088827

Regions

Domain1472 – 1660189PIK helical
Domain1788 – 2021234PI3K/PI4K
Region1661 – 1793133Pleckstrin homology (PH) domain conferring phosphoinositide binding specificity By similarity

Amino acid modifications

Modified residue1721Phosphoserine Ref.5 Ref.9
Modified residue1971Phosphothreonine Ref.9
Modified residue1981Phosphoserine Ref.5 Ref.6
Modified residue1991Phosphoserine Ref.6
Modified residue2021Phosphoserine Ref.6
Modified residue2041Phosphoserine Ref.6
Modified residue2071Phosphoserine Ref.5 Ref.6 Ref.10
Modified residue10961Phosphotyrosine Ref.8
Modified residue13781Phosphoserine Ref.10
Modified residue17701Phosphoserine Ref.7

Natural variations

Alternative sequence1 – 11901190Missing in isoform 2.
VSP_008805
Natural variant3221M → V.
Corresponds to variant rs17819211 [ dbSNP | Ensembl ].
VAR_050531
Natural variant17931V → L.
Corresponds to variant rs2539908 [ dbSNP | Ensembl ].
VAR_059549

Experimental info

Sequence conflict3801N → S in AAD13352. Ref.2
Sequence conflict18891S → I in AAH53654. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (PI4K230) [UniParc].

Last modified December 16, 2008. Version 3.
Checksum: 7516EE4AA1E66465

FASTA2,044231,319
        10         20         30         40         50         60 
MCPVDFHGIF QLDERRRDAV IALGIFLIES DLQHKDCVVP YLLRLLKGLP KVYWVEESTA 

        70         80         90        100        110        120 
RKGRGALPVA ESFSFCLVTL LSDVAYRDPS LRDEILEVLL QVLHVLLGMC QALEIQDKEY 

       130        140        150        160        170        180 
LCKYAIPCLI GISRAFGRYS NMEESLLSKL FPKIPPHSLR VLEELEGVRR RSFNDFRSIL 

       190        200        210        220        230        240 
PSNLLTVCQE GTLKRKTSSV SSISQVSPER GMPPPSSPGG SAFHYFEASC LPDGTALEPE 

       250        260        270        280        290        300 
YYFSTISSSF SVSPLFNGVT YKEFNIPLEM LRELLNLVKK IVEEAVLKSL DAIVASVMEA 

       310        320        330        340        350        360 
NPSADLYYTS FSDPLYLTMF KMLRDTLYYM KDLPTSFVKE IHDFVLEQFN TSQGELQKIL 

       370        380        390        400        410        420 
HDADRIHNEL SPLKLRCQAN AACVDLMVWA VKDEQGAENL CIKLSEKLQS KTSSKVIIAH 

       430        440        450        460        470        480 
LPLLICCLQG LGRLCERFPV VVHSVTPSLR DFLVIPSPVL VKLYKYHSQY HTVAGNDIKI 

       490        500        510        520        530        540 
SVTNEHSEST LNVMSGKKSQ PSMYEQLRDI AIDNICRCLK AGLTVDPVIV EAFLASLSNR 

       550        560        570        580        590        600 
LYISQESDKD AHLIPDHTIR ALGHIAVALR DTPKVMEPIL QILQQKFCQP PSPLDVLIID 

       610        620        630        640        650        660 
QLGCLVITGN QYIYQEVWNL FQQISVKASS VVYSATKDYK DHGYRHCSLA VINALANIAA 

       670        680        690        700        710        720 
NIQDEHLVDE LLMNLLELFV QLGLEGKRAS ERASEKGPAL KASSSAGNLG VLIPVIAVLT 

       730        740        750        760        770        780 
RRLPPIKEAK PRLQKLFRDF WLYSVLMGFA VEGSGLWPEE WYEGVCEIAT KSPLLTFPSK 

       790        800        810        820        830        840 
EPLRSVLQYN SAMKNDTVTP AELSELRSTI INLLDPPPEV SALINKLDFA MSTYLLSVYR 

       850        860        870        880        890        900 
LEYMRVLRST DPDRFQVMFC YFEDKAIQKD KSGMMQCVIA VADKVFDAFL NMMADKAKTK 

       910        920        930        940        950        960 
ENEEELERHA QFLLVNFNHI HKRIRRVADK YLSGLVDKFP HLLWSGTVLK TMLDILQTLS 

       970        980        990       1000       1010       1020 
LSLSADIHKD QPYYDIPDAP YRITVPDTYE ARESIVKDFA ARCGMILQEA MKWAPTVTKS 

      1030       1040       1050       1060       1070       1080 
HLQEYLNKHQ NWVSGLSQHT GLAMATESIL HFAGYNKQNT TLGATQLSER PACVKKDYSN 

      1090       1100       1110       1120       1130       1140 
FMASLNLRNR YAGEVYGMIR FSGTTGQMSD LNKMMVQDLH SALDRSHPQH YTQAMFKLTA 

      1150       1160       1170       1180       1190       1200 
MLISSKDCDP QLLHHLCWGP LRMFNEHGME TALACWEWLL AGKDGVEVPF MREMAGAWHM 

      1210       1220       1230       1240       1250       1260 
TVEQKFGLFS AEIKEADPLA ASEASQPKPC PPEVTPHYIW IDFLVQRFEI AKYCSSDQVE 

      1270       1280       1290       1300       1310       1320 
IFSSLLQRSM SLNIGGAKGS MNRHVAAIGP RFKLLTLGLS LLHADVVPNA TIRNVLREKI 

      1330       1340       1350       1360       1370       1380 
YSTAFDYFSC PPKFPTQGEK RLREDISIMI KFWTAMFSDK KYLTASQLVP PDNQDTRSNL 

      1390       1400       1410       1420       1430       1440 
DITVGSRQQA TQGWINTYPL SSGMSTISKK SGMSKKTNRG SQLHKYYMKR RTLLLSLLAT 

      1450       1460       1470       1480       1490       1500 
EIERLITWYN PLSAPELELD QAGENSVANW RSKYISLSEK QWKDNVNLAW SISPYLAVQL 

      1510       1520       1530       1540       1550       1560 
PARFKNTEAI GNEVTRLVRL DPGAVSDVPE AIKFLVTWHT IDADAPELSH VLCWAPTDPP 

      1570       1580       1590       1600       1610       1620 
TGLSYFSSMY PPHPLTAQYG VKVLRSFPPD AILFYIPQIV QALRYDKMGY VREYILWAAS 

      1630       1640       1650       1660       1670       1680 
KSQLLAHQFI WNMKTNIYLD EEGHQKDPDI GDLLDQLVEE ITGSLSGPAK DFYQREFDFF 

      1690       1700       1710       1720       1730       1740 
NKITNVSAII KPYPKGDERK KACLSALSEV KVQPGCYLPS NPEAIVLDID YKSGTPMQSA 

      1750       1760       1770       1780       1790       1800 
AKAPYLAKFK VKRCGVSELE KEGLRCRSDS EDECSTQEAD GQKISWQAAI FKVGDDCRQD 

      1810       1820       1830       1840       1850       1860 
MLALQIIDLF KNIFQLVGLD LFVFPYRVVA TAPGCGVIEC IPDCTSRDQL GRQTDFGMYD 

      1870       1880       1890       1900       1910       1920 
YFTRQYGDES TLAFQQARYN FIRSMAAYSL LLFLLQIKDR HNGNIMLDKK GHIIHIDFGF 

      1930       1940       1950       1960       1970       1980 
MFESSPGGNL GWEPDIKLTD EMVMIMGGKM EATPFKWFME MCVRGYLAVR PYMDAVVSLV 

      1990       2000       2010       2020       2030       2040 
TLMLDTGLPC FRGQTIKLLK HRFSPNMTER EAANFIMKVI QSCFLSNRSR TYDMIQYYQN 


DIPY 

« Hide

Isoform 2 (PI4K97) [UniParc].

Checksum: F519168FA721644E
Show »

FASTA85496,984

References

« Hide 'large scale' references
[1]"Cloning and characterization of a human phosphatidylinositol 4-kinase."
Wong K., Cantley L.C.
J. Biol. Chem. 269:28878-28884(1994) [PubMed: 7961848] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
[2]"Functional expression and characterisation of a new human phosphatidylinositol 4-kinase PI4K230."
Gehrmann T., Guelkan H., Suer S., Herberg F.W., Balla A., Vereb G. Jr., Mayr G.W., Heilmeyer L.M.G. Jr.
Biochim. Biophys. Acta 1437:341-356(1999) [PubMed: 10101268] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[3]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed: 10591208] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1142-2044 (ISOFORM 1).
Tissue: Uterus.
[5]"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: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172; SER-198 AND SER-207, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[6]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198; SER-199; SER-202; SER-204 AND SER-207, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[7]"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: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1770, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[8]"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells."
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J.
J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1096, MASS SPECTROMETRY.
Tissue: Mammary epithelium.
[9]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172 AND THR-197, MASS SPECTROMETRY.
[10]"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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207 AND SER-1378, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[11]"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: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L36151 mRNA. Translation: AAA56839.1.
AF012872 mRNA. Translation: AAD13352.1.
AC007050 Genomic DNA. No translation available.
AC007308 Genomic DNA. No translation available.
BC018120 mRNA. Translation: AAH18120.2.
BC053654 mRNA. Translation: AAH53654.1.
IPIIPI00031424.
IPI00070943.
PIRA55404.
RefSeqNP_002641.1. NM_002650.2.
UniGeneHs.529438.

3D structure databases

ProteinModelPortalP42356.
SMRP42356. Positions 1501-2028.
ModBaseSearch...

Protein-protein interaction databases

IntActP42356. 7 interactions.
MINTMINT-1388461.
STRINGP42356.

PTM databases

PhosphoSiteP42356.

Polymorphism databases

DMDM218512114.

Proteomic databases

PRIDEP42356.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000255882; ENSP00000255882; ENSG00000241973.
GeneID5297.
KEGGhsa:5297.
UCSCuc002zsy.2. human.
uc002zsz.2. human.

Organism-specific databases

CTD5297.
GeneCardsGC22M021061.
H-InvDBHIX0016262.
HGNCHGNC:8983. PI4KA.
HPACAB009092.
MIM600286. gene.
neXtProtNX_P42356.
PharmGKBPA162399305.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG15200.
HOVERGENHBG052742.
InParanoidP42356.
OrthoDBEOG4FJ87V.
PhylomeDBP42356.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000133511-MONOMER.
Pathway_Interaction_DBavb3_integrin_pathway. Integrins in angiogenesis.

Gene expression databases

ArrayExpressP42356.
BgeeP42356.
CleanExHS_PI4KA.
GenevestigatorP42356.
GermOnlineENSG00000133511. Homo sapiens.

Family and domain databases

InterProIPR016024. ARM-type_fold.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat.
IPR018936. PI3/4_kinase_CS.
IPR015433. PI_Kinase.
IPR001263. PInositide-3_kin_accessory_dom.
[Graphical view]
Gene3DG3DSA:1.10.1070.11. PI3/4_kinase_cat. 1 hit.
G3DSA:1.25.40.70. PI3Ka. 1 hit.
KOK00888.
PANTHERPTHR10048. PI_Kinase. 1 hit.
PfamPF00454. PI3_PI4_kinase. 1 hit.
PF00613. PI3Ka. 1 hit.
[Graphical view]
SMARTSM00145. PI3Ka. 1 hit.
SM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMSSF48371. ARM-type_fold. 1 hit.
SSF56112. Kinase_like. 1 hit.
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

NextBio20474.
SOURCESearch...

Entry information

Entry namePI4KA_HUMAN
AccessionPrimary (citable) accession number: P42356
Secondary accession number(s): Q7Z625, Q9UPG2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: December 16, 2008
Last modified: January 25, 2012
This is version 109 of the entry and version 3 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

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families