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Q99755

- PI51A_HUMAN

UniProt

Q99755 - PI51A_HUMAN

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Protein

Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha

Gene
PIP5K1A
Organism
Homo sapiens (Human)
Status
Reviewed - 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
  4. protein binding Source: UniProtKB

GO - Biological processi

  1. actin cytoskeleton reorganization Source: UniProtKB
  2. activation of Rac 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: Chromosome 1

Organism-specific databases

HGNCiHGNC:8994. PIP5K1A.

Subcellular locationi

Cell membrane. Cytoplasm By similarity. Nucleus speckle. Cell projectionruffle
Note: Colocalizes with RAC1 at actin-rich membrane ruffles. Localizes to nuclear speckles and associates with TUT1 to regulate polyadenylation of selected mRNAs.2 Publications

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. lamellipodium Source: UniProtKB
  4. nuclear speck Source: UniProtKB
  5. nucleus Source: UniProtKB
  6. plasma membrane Source: UniProtKB
  7. 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.

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

ArrayExpressiQ99755.
BgeeiQ99755.
CleanExiHS_PIP5K1A.
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.2 Publications

Protein-protein interaction databases

BioGridi113983. 7 interactions.
DIPiDIP-60649N.
IntActiQ99755. 2 interactions.
MINTiMINT-1406942.
STRINGi9606.ENSP00000357883.

Structurei

3D structure databases

ProteinModelPortaliQ99755.
SMRiQ99755. Positions 82-367.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini81 – 449369PIPKAdd
BLAST

Sequence similaritiesi

Contains 1 PIPK domain.

Phylogenomic databases

eggNOGiCOG5148.
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. Align

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

MASASSGPSS SVGFSSFDPA VPSCTLSSAA SGIKRPMASE VLEARQDSYI    50
SLVPYASGMP IKKIGHRSVD SSGETTYKKT TSSALKGAIQ LGITHTVGSL 100
STKPERDVLM QDFYVVESIF FPSEGSNLTP AHHYNDFRFK TYAPVAFRYF 150
RELFGIRPDD YLYSLCSEPL IELCSSGASG SLFYVSSDDE FIIKTVQHKE 200
AEFLQKLLPG YYMNLNQNPR TLLPKFYGLY CVQAGGKNIR IVVMNNLLPR 250
SVKMHIKYDL KGSTYKRRAS QKEREKPLPT FKDLDFLQDI PDGLFLDADM 300
YNALCKTLQR DCLVLQSFKI MDYSLLMSIH NIDHAQREPL SSETQYSVDT 350
RRPAPQKALY STAMESIQGE ARRGGTMETD DHMGGIPARN SKGERLLLYI 400
GIIDILQSYR FVKKLEHSWK ALVHDGDTVS VHRPGFYAER FQRFMCNTVF 450
KKIPLKPSPS KKFRSGSSFS RRAGSSGNSC ITYQPSVSGE HKAQVTTKAE 500
VEPGVHLGRP DVLPQTPPLE EISEGSPIPD PSFSPLVGET LQMLTTSTTL 550
EKLEVAESEF TH 562
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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei30 – 5223ASGIK…SYISL → SGIKRPMASE in isoform 2 and isoform 3. VSP_016007Add
BLAST
Alternative sequencei41 – 5212Missing in isoform 4. VSP_041912Add
BLAST
Alternative sequencei382 – 41029HMGGI…LQSYR → Q in isoform 4. VSP_041913Add
BLAST
Alternative sequencei455 – 50450LKPSP…EVEPG → C in isoform 2. VSP_016008Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti257 – 2571K → E in BAG58542. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 databases

DMDMi74752158.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS44219.1. [Q99755-1 ]
CCDS44220.1. [Q99755-4 ]
CCDS44221.1. [Q99755-2 ]
CCDS990.1. [Q99755-3 ]
RefSeqi NP_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 ]
UniGenei Hs.655131.
Hs.661888.

3D structure databases

ProteinModelPortali Q99755.
SMRi Q99755. Positions 82-367.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113983. 7 interactions.
DIPi DIP-60649N.
IntActi Q99755. 2 interactions.
MINTi MINT-1406942.
STRINGi 9606.ENSP00000357883.

Chemistry

BindingDBi Q99755.
ChEMBLi CHEMBL5969.
GuidetoPHARMACOLOGYi 2164.

PTM databases

PhosphoSitei Q99755.

Polymorphism databases

DMDMi 74752158.

Proteomic databases

MaxQBi Q99755.
PaxDbi Q99755.
PRIDEi Q99755.

Protocols and materials databases

DNASUi 8394.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000349792 ; ENSP00000271663 ; ENSG00000143398 . [Q99755-3 ]
ENST00000368888 ; ENSP00000357883 ; ENSG00000143398 . [Q99755-1 ]
ENST00000368890 ; ENSP00000357885 ; ENSG00000143398 . [Q99755-2 ]
ENST00000441902 ; ENSP00000415648 ; ENSG00000143398 . [Q99755-4 ]
GeneIDi 8394.
KEGGi hsa:8394.
UCSCi uc001exi.3. human. [Q99755-3 ]
uc001exj.3. human. [Q99755-1 ]
uc001exk.3. human. [Q99755-2 ]
uc010pcu.2. human. [Q99755-4 ]

Organism-specific databases

CTDi 8394.
GeneCardsi GC01P151170.
HGNCi HGNC:8994. PIP5K1A.
HPAi HPA029366.
MIMi 603275. gene.
neXtProti NX_Q99755.
PharmGKBi PA33327.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5148.
HOGENOMi HOG000193876.
HOVERGENi HBG052818.
InParanoidi Q99755.
KOi K00889.
OMAi ETEDHMG.
OrthoDBi EOG70W3DM.
PhylomeDBi Q99755.
TreeFami TF319618.

Enzyme and pathway databases

BioCyci MetaCyc:HS07047-MONOMER.
BRENDAi 2.7.1.68. 2681.
Reactomei REACT_121025. Synthesis of PIPs at the plasma membrane.
SignaLinki Q99755.

Miscellaneous databases

ChiTaRSi PIP5K1A. human.
GeneWikii PIP5K1A.
GenomeRNAii 8394.
NextBioi 31416.
PMAP-CutDB Q99755.
PROi Q99755.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q99755.
Bgeei Q99755.
CleanExi HS_PIP5K1A.
Genevestigatori Q99755.

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. "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. 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: September 3, 2014
This is version 125 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.

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

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