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Protein

Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha

Gene

PIP5K1A

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 4-phosphate (PtdIns4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). PtdIns(4,5)P2 is involved in a variety of cellular processes and is the substrate to form phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3), another second messenger. The majority of PtdIns(4,5)P2 is thought to occur via type I phosphatidylinositol 4-phosphate 5-kinases given the abundance of PtdIns4P. Participates in a variety of cellular processes such as actin cytoskeleton organization, cell adhesion, migration and phagocytosis. Required for membrane ruffling formation, actin organization and focal adhesion formation during directional cell migration by controlling integrin-induced translocation of RAC1 to the plasma membrane. Together with PIP5K1C is required for phagocytosis, but they regulate different types of actin remodeling at sequential steps. Promotes particle ingestion by activating WAS that induces Arp2/3 dependent actin polymerization at the nascent phagocytic cup. Together with PIP5K1B is required after stimulation of G-protein coupled receptors for stable platelet adhesion. Plays a role during calcium-induced keratinocyte differentiation. Recruited to the plasma membrane by the E-cadherin/beta-catenin complex where it provides the substrate PtdIns(4,5)P2 for the production of PtdIns(3,4,5)P3, diacylglycerol and inositol 1,4,5-trisphosphate that mobilize internal calcium and drive keratinocyte differentiation. Together with PIP5K1C have a role during embryogenesis. Functions also in the nucleus where acts as an activator of TUT1 adenylyltransferase activity in nuclear speckles, thereby regulating mRNA polyadenylation of a select set of mRNAs.3 Publications

Catalytic activityi

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

GO - Molecular functioni

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

GO - Biological processi

  1. actin cytoskeleton reorganization Source: UniProtKB
  2. activation of GTPase activity Source: UniProtKB
  3. cell chemotaxis Source: UniProtKB
  4. cell migration Source: UniProtKB
  5. fibroblast migration Source: Ensembl
  6. focal adhesion assembly Source: UniProtKB
  7. glycerophospholipid metabolic process Source: ProtInc
  8. keratinocyte differentiation Source: UniProtKB
  9. phagocytosis Source: UniProtKB
  10. phosphatidylinositol biosynthetic process Source: Reactome
  11. phosphatidylinositol phosphorylation Source: GOC
  12. phospholipid biosynthetic process Source: UniProtKB
  13. phospholipid metabolic process Source: Reactome
  14. protein targeting to plasma membrane Source: UniProtKB
  15. ruffle assembly Source: UniProtKB
  16. signal transduction Source: ProtInc
  17. 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:HS07047-MONOMER.
BRENDAi2.7.1.68. 2681.
ReactomeiREACT_121025. Synthesis of PIPs at the plasma membrane.
SignaLinkiQ99755.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha (EC:2.7.1.68)
Short name:
PIP5K1-alpha
Short name:
PtdIns(4)P-5-kinase 1 alpha
Alternative name(s):
68 kDa type I phosphatidylinositol 4-phosphate 5-kinase alpha
Phosphatidylinositol 4-phosphate 5-kinase type I alpha
Short name:
PIP5KIalpha
Gene namesi
Name:PIP5K1A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:8994. PIP5K1A.

Subcellular locationi

  1. Cell membrane
  2. Cytoplasm By similarity
  3. Nucleus speckle
  4. Cell projectionruffle

  5. Note: Colocalizes with RAC1 at actin-rich membrane ruffles. Localizes to nuclear speckles and associates with TUT1 to regulate polyadenylation of selected mRNAs.

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. focal adhesion Source: UniProtKB
  4. lamellipodium Source: UniProtKB
  5. nuclear speck Source: UniProtKB
  6. nucleoplasm Source: HPA
  7. nucleus Source: UniProtKB
  8. plasma membrane Source: UniProtKB
  9. ruffle membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi322 – 3221D → N: Does not affect targeting of RAC1 to the plasma membrane; when associated with Q-440. 1 Publication
Mutagenesisi440 – 4401R → Q: Does not affect targeting of RAC1 to the plasma membrane; when associated with N-322. 1 Publication

Organism-specific databases

PharmGKBiPA33327.

Polymorphism and mutation databases

BioMutaiPIP5K1A.
DMDMi74752158.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 562562Phosphatidylinositol 4-phosphate 5-kinase type-1 alphaPRO_0000185456Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki103 – 103Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ99755.
PaxDbiQ99755.
PRIDEiQ99755.

PTM databases

PhosphoSiteiQ99755.

Miscellaneous databases

PMAP-CutDBQ99755.

Expressioni

Tissue specificityi

Highly expressed in heart, placenta, skeletal muscle, kidney and pancreas. Detected at lower levels in brain, lung and liver.

Gene expression databases

BgeeiQ99755.
CleanExiHS_PIP5K1A.
ExpressionAtlasiQ99755. baseline and differential.
GenevestigatoriQ99755.

Organism-specific databases

HPAiHPA029366.

Interactioni

Subunit structurei

Interacts with RAC1 (By similarity). Interacts with TUT1. Forms a complex with CDH1/E-cadherin, CTNNB1/beta-catenin and CTNND1 at the plasma membrane upon calcium stimulation.By similarity2 Publications

Protein-protein interaction databases

BioGridi113983. 31 interactions.
DIPiDIP-60649N.
IntActiQ99755. 3 interactions.
MINTiMINT-1406942.
STRINGi9606.ENSP00000357883.

Structurei

3D structure databases

ProteinModelPortaliQ99755.
SMRiQ99755. Positions 82-367.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini81 – 449369PIPKPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 PIPK domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5148.
GeneTreeiENSGT00760000119184.
HOGENOMiHOG000193876.
HOVERGENiHBG052818.
InParanoidiQ99755.
KOiK00889.
OMAiETEDHMG.
OrthoDBiEOG70W3DM.
PhylomeDBiQ99755.
TreeFamiTF319618.

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 (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q99755-1) [UniParc]FASTAAdd to basket

Also known as: PIP5KIalpha2

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
MASASSGPSS SVGFSSFDPA VPSCTLSSAA SGIKRPMASE VLEARQDSYI
60 70 80 90 100
SLVPYASGMP IKKIGHRSVD SSGETTYKKT TSSALKGAIQ LGITHTVGSL
110 120 130 140 150
STKPERDVLM QDFYVVESIF FPSEGSNLTP AHHYNDFRFK TYAPVAFRYF
160 170 180 190 200
RELFGIRPDD YLYSLCSEPL IELCSSGASG SLFYVSSDDE FIIKTVQHKE
210 220 230 240 250
AEFLQKLLPG YYMNLNQNPR TLLPKFYGLY CVQAGGKNIR IVVMNNLLPR
260 270 280 290 300
SVKMHIKYDL KGSTYKRRAS QKEREKPLPT FKDLDFLQDI PDGLFLDADM
310 320 330 340 350
YNALCKTLQR DCLVLQSFKI MDYSLLMSIH NIDHAQREPL SSETQYSVDT
360 370 380 390 400
RRPAPQKALY STAMESIQGE ARRGGTMETD DHMGGIPARN SKGERLLLYI
410 420 430 440 450
GIIDILQSYR FVKKLEHSWK ALVHDGDTVS VHRPGFYAER FQRFMCNTVF
460 470 480 490 500
KKIPLKPSPS KKFRSGSSFS RRAGSSGNSC ITYQPSVSGE HKAQVTTKAE
510 520 530 540 550
VEPGVHLGRP DVLPQTPPLE EISEGSPIPD PSFSPLVGET LQMLTTSTTL
560
EKLEVAESEF TH
Length:562
Mass (Da):62,633
Last modified:May 1, 1997 - v1
Checksum:iA8F7988EB73506A0
GO
Isoform 2 (identifier: Q99755-2) [UniParc]FASTAAdd to basket

Also known as: PIP5KIalpha3

The sequence of this isoform differs from the canonical sequence as follows:
     30-52: ASGIKRPMASEVLEARQDSYISL → SGIKRPMASE
     455-504: LKPSPSKKFRSGSSFSRRAGSSGNSCITYQPSVSGEHKAQVTTKAEVEPG → C

Show »
Length:500
Mass (Da):56,053
Checksum:i684F0C9C2DBE9EC4
GO
Isoform 3 (identifier: Q99755-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     30-52: ASGIKRPMASEVLEARQDSYISL → SGIKRPMASE

Show »
Length:549
Mass (Da):61,187
Checksum:i7CD48BFE175564A0
GO
Isoform 4 (identifier: Q99755-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     41-52: Missing.
     382-410: HMGGIPARNSKGERLLLYIGIIDILQSYR → Q

Show »
Length:522
Mass (Da):58,119
Checksum:i693CE47DBFC72B5F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti257 – 2571K → E in BAG58542 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei30 – 5223ASGIK…SYISL → SGIKRPMASE in isoform 2 and isoform 3. 3 PublicationsVSP_016007Add
BLAST
Alternative sequencei41 – 5212Missing in isoform 4. 1 PublicationVSP_041912Add
BLAST
Alternative sequencei382 – 41029HMGGI…LQSYR → Q in isoform 4. 1 PublicationVSP_041913Add
BLAST
Alternative sequencei455 – 50450LKPSP…EVEPG → C in isoform 2. 2 PublicationsVSP_016008Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U78575 mRNA. Translation: AAC50910.1.
U78576 mRNA. Translation: AAC50911.1.
U78577 mRNA. Translation: AAC50912.1.
AK291015 mRNA. Translation: BAF83704.1.
AK295691 mRNA. Translation: BAG58542.1.
AL592424 Genomic DNA. Translation: CAI16386.1.
AL592424 Genomic DNA. Translation: CAI16387.1.
AL592424 Genomic DNA. Translation: CAI16388.1.
CH471121 Genomic DNA. Translation: EAW53461.1.
BC007833 mRNA. Translation: AAH07833.1.
CCDSiCCDS44219.1. [Q99755-1]
CCDS44220.1. [Q99755-4]
CCDS44221.1. [Q99755-2]
CCDS990.1. [Q99755-3]
RefSeqiNP_001129108.1. NM_001135636.1. [Q99755-4]
NP_001129109.1. NM_001135637.1. [Q99755-2]
NP_001129110.1. NM_001135638.1. [Q99755-1]
NP_003548.1. NM_003557.2. [Q99755-3]
UniGeneiHs.655131.
Hs.661888.

Genome annotation databases

EnsembliENST00000349792; ENSP00000271663; ENSG00000143398. [Q99755-3]
ENST00000368888; ENSP00000357883; ENSG00000143398. [Q99755-1]
ENST00000368890; ENSP00000357885; ENSG00000143398. [Q99755-2]
ENST00000441902; ENSP00000415648; ENSG00000143398. [Q99755-4]
GeneIDi8394.
KEGGihsa:8394.
UCSCiuc001exi.3. human. [Q99755-3]
uc001exj.3. human. [Q99755-1]
uc001exk.3. human. [Q99755-2]
uc010pcu.2. human. [Q99755-4]

Polymorphism and mutation databases

BioMutaiPIP5K1A.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U78575 mRNA. Translation: AAC50910.1.
U78576 mRNA. Translation: AAC50911.1.
U78577 mRNA. Translation: AAC50912.1.
AK291015 mRNA. Translation: BAF83704.1.
AK295691 mRNA. Translation: BAG58542.1.
AL592424 Genomic DNA. Translation: CAI16386.1.
AL592424 Genomic DNA. Translation: CAI16387.1.
AL592424 Genomic DNA. Translation: CAI16388.1.
CH471121 Genomic DNA. Translation: EAW53461.1.
BC007833 mRNA. Translation: AAH07833.1.
CCDSiCCDS44219.1. [Q99755-1]
CCDS44220.1. [Q99755-4]
CCDS44221.1. [Q99755-2]
CCDS990.1. [Q99755-3]
RefSeqiNP_001129108.1. NM_001135636.1. [Q99755-4]
NP_001129109.1. NM_001135637.1. [Q99755-2]
NP_001129110.1. NM_001135638.1. [Q99755-1]
NP_003548.1. NM_003557.2. [Q99755-3]
UniGeneiHs.655131.
Hs.661888.

3D structure databases

ProteinModelPortaliQ99755.
SMRiQ99755. Positions 82-367.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113983. 31 interactions.
DIPiDIP-60649N.
IntActiQ99755. 3 interactions.
MINTiMINT-1406942.
STRINGi9606.ENSP00000357883.

Chemistry

BindingDBiQ99755.
ChEMBLiCHEMBL5969.
GuidetoPHARMACOLOGYi2164.

PTM databases

PhosphoSiteiQ99755.

Polymorphism and mutation databases

BioMutaiPIP5K1A.
DMDMi74752158.

Proteomic databases

MaxQBiQ99755.
PaxDbiQ99755.
PRIDEiQ99755.

Protocols and materials databases

DNASUi8394.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000349792; ENSP00000271663; ENSG00000143398. [Q99755-3]
ENST00000368888; ENSP00000357883; ENSG00000143398. [Q99755-1]
ENST00000368890; ENSP00000357885; ENSG00000143398. [Q99755-2]
ENST00000441902; ENSP00000415648; ENSG00000143398. [Q99755-4]
GeneIDi8394.
KEGGihsa:8394.
UCSCiuc001exi.3. human. [Q99755-3]
uc001exj.3. human. [Q99755-1]
uc001exk.3. human. [Q99755-2]
uc010pcu.2. human. [Q99755-4]

Organism-specific databases

CTDi8394.
GeneCardsiGC01P151170.
HGNCiHGNC:8994. PIP5K1A.
HPAiHPA029366.
MIMi603275. gene.
neXtProtiNX_Q99755.
PharmGKBiPA33327.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5148.
GeneTreeiENSGT00760000119184.
HOGENOMiHOG000193876.
HOVERGENiHBG052818.
InParanoidiQ99755.
KOiK00889.
OMAiETEDHMG.
OrthoDBiEOG70W3DM.
PhylomeDBiQ99755.
TreeFamiTF319618.

Enzyme and pathway databases

BioCyciMetaCyc:HS07047-MONOMER.
BRENDAi2.7.1.68. 2681.
ReactomeiREACT_121025. Synthesis of PIPs at the plasma membrane.
SignaLinkiQ99755.

Miscellaneous databases

ChiTaRSiPIP5K1A. human.
GeneWikiiPIP5K1A.
GenomeRNAii8394.
NextBioi31416.
PMAP-CutDBQ99755.
PROiQ99755.
SOURCEiSearch...

Gene expression databases

BgeeiQ99755.
CleanExiHS_PIP5K1A.
ExpressionAtlasiQ99755. baseline and differential.
GenevestigatoriQ99755.

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. "Type I phosphatidylinositol-4-phosphate 5-kinases are distinct members of this novel lipid kinase family."
    Loijens J.C., Anderson R.A.
    J. Biol. Chem. 271:32937-32943(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
    Tissue: Fetal brain.
  2. "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] (ISOFORMS 3 AND 4).
    Tissue: Hippocampus.
  3. "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].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Muscle.
  6. "A PtdIns4,5P2-regulated nuclear poly(A) polymerase controls expression of select mRNAs."
    Mellman D.L., Gonzales M.L., Song C., Barlow C.A., Wang P., Kendziorski C., Anderson R.A.
    Nature 451:1013-1017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TUT1.
  7. "Phosphatidylinositol-4-phosphate 5-kinase 1alpha mediates extracellular calcium-induced keratinocyte differentiation."
    Xie Z., Chang S.M., Pennypacker S.D., Liao E.-Y., Bikle D.D.
    Mol. Biol. Cell 20:1695-1704(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN KERATINOCYTE DIFFERENTIATION, SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH CDH1; CTNNB1 AND CTNND1.
  8. "Type I PIPK-alpha regulates directed cell migration by modulating Rac1 plasma membrane targeting and activation."
    Chao W.-T., Daquinag A.C., Ashcroft F., Kunz J.
    J. Cell Biol. 190:247-262(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL MIGRATION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-322 AND ARG-440.
  9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPI51A_HUMAN
AccessioniPrimary (citable) accession number: Q99755
Secondary accession number(s): A8K4Q0
, B4DIN0, Q99754, Q99756
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: May 1, 1997
Last modified: April 29, 2015
This is version 131 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

Caution

There is confusion in the literature with phosphatidylinositol 4-phosphate 5-kinase type I nomenclature due to the fact that frequently mouse PIP5K1B is named Phosphatidylinositol 4-phosphate 5-kinase type I alpha.Curated

Keywords - Technical termi

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. 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.