Q99755 (PI51A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha
Short name=PIP5K1-alpha
Short name=PtdIns(4)P-5-kinase 1 alpha
EC=2.7.1.68

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 names

Name:

PIP5K1A

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	562 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.7 Ref.8 Ref.9
Catalytic activity	ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate.
Subunit structure	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. Ref.7 Ref.8
Subcellular location	Cell membrane. Cytoplasm By similarity. Nucleus speckle. Cell projection › ruffle. Note: Colocalizes with RAC1 at actin-rich membrane ruffles. Localizes to nuclear speckles and associates with TUT1 to regulate polyadenylation of selected mRNAs. Ref.8 Ref.9
Tissue specificity	Highly expressed in heart, placenta, skeletal muscle, kidney and pancreas. Detected at lower levels in brain, lung and liver.
Sequence similarities	Contains 1 PIPK domain.
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.

Ontologies

Keywords
Cellular component	Cell membrane Cell projection Cytoplasm Membrane Nucleus
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Isopeptide bond Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin cytoskeleton reorganization Inferred from mutant phenotype Ref.9. Source: UniProtKB activation of Rac GTPase activity Inferred from mutant phenotype Ref.9. Source: UniProtKB cell chemotaxis Inferred from mutant phenotype Ref.9. Source: UniProtKB fibroblast migration Inferred from electronic annotation. Source: Compara focal adhesion assembly Inferred from mutant phenotype Ref.9. Source: UniProtKB keratinocyte differentiation Traceable author statement PubMed 19889969. Source: UniProtKB phagocytosis Traceable author statement PubMed 19889969. Source: UniProtKB phosphatidylinositol biosynthetic process Traceable author statement. Source: Reactome protein targeting to plasma membrane Inferred from mutant phenotype Ref.9. Source: UniProtKB ruffle assembly Inferred from mutant phenotype Ref.9. Source: UniProtKB signal transduction Traceable author statement Ref.1. Source: ProtInc small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome lamellipodium Inferred from direct assay PubMed 15157668. Source: UniProtKB nuclear speck Inferred from direct assay Ref.7. Source: UniProtKB ruffle membrane Inferred from direct assay Ref.9. Source: UniProtKB
Molecular_function	1-phosphatidylinositol-4-phosphate 5-kinase activity Inferred from direct assay PubMed 15157668. Source: UniProtKB ATP binding Inferred from electronic annotation. Source: UniProtKB-KW kinase binding Inferred from direct assay PubMed 15157668. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q99755-1)

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.

Isoform 2 (identifier: Q99755-2)

Also known as: PIP5KIalpha3;

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

Isoform 3 (identifier: Q99755-3)

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

Isoform 4 (identifier: Q99755-4)

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 562	562	Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha		PRO_0000185456
Regions
	Domain	81 – 449	369	PIPK
Amino acid modifications
	Cross-link	103		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.6
Natural variations
	Alternative sequence	30 – 52	23	ASGIK…SYISL → SGIKRPMASE in isoform 2 and isoform 3.		VSP_016007
	Alternative sequence	41 – 52	12	Missing in isoform 4.		VSP_041912
	Alternative sequence	382 – 410	29	HMGGI…LQSYR → Q in isoform 4.		VSP_041913
	Alternative sequence	455 – 504	50	LKPSP…EVEPG → C in isoform 2.		VSP_016008
Experimental info
	Mutagenesis	322	1	D → N: Does not affect targeting of RAC1 to the plasma membrane; when associated with Q-440. Ref.9
	Mutagenesis	440	1	R → Q: Does not affect targeting of RAC1 to the plasma membrane; when associated with N-322. Ref.9
	Sequence conflict	257	1	K → E in BAG58542. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (PIP5KIalpha2) [UniParc]. Last modified May 1, 1997. Version 1. Checksum: A8F7988EB73506A0	FASTA	562	62,633
	10 20 30 40 50 60 MASASSGPSS SVGFSSFDPA VPSCTLSSAA SGIKRPMASE VLEARQDSYI SLVPYASGMP 70 80 90 100 110 120 IKKIGHRSVD SSGETTYKKT TSSALKGAIQ LGITHTVGSL STKPERDVLM QDFYVVESIF 130 140 150 160 170 180 FPSEGSNLTP AHHYNDFRFK TYAPVAFRYF RELFGIRPDD YLYSLCSEPL IELCSSGASG 190 200 210 220 230 240 SLFYVSSDDE FIIKTVQHKE AEFLQKLLPG YYMNLNQNPR TLLPKFYGLY CVQAGGKNIR 250 260 270 280 290 300 IVVMNNLLPR SVKMHIKYDL KGSTYKRRAS QKEREKPLPT FKDLDFLQDI PDGLFLDADM 310 320 330 340 350 360 YNALCKTLQR DCLVLQSFKI MDYSLLMSIH NIDHAQREPL SSETQYSVDT RRPAPQKALY 370 380 390 400 410 420 STAMESIQGE ARRGGTMETD DHMGGIPARN SKGERLLLYI GIIDILQSYR FVKKLEHSWK 430 440 450 460 470 480 ALVHDGDTVS VHRPGFYAER FQRFMCNTVF KKIPLKPSPS KKFRSGSSFS RRAGSSGNSC 490 500 510 520 530 540 ITYQPSVSGE HKAQVTTKAE VEPGVHLGRP DVLPQTPPLE EISEGSPIPD PSFSPLVGET 550 560 LQMLTTSTTL EKLEVAESEF TH
	Isoform 2 (PIP5KIalpha3) [UniParc]. Checksum: 684F0C9C2DBE9EC4	FASTA	500	56,053
	10 20 30 40 50 60 MASASSGPSS SVGFSSFDPA VPSCTLSSAS GIKRPMASEV PYASGMPIKK IGHRSVDSSG 70 80 90 100 110 120 ETTYKKTTSS ALKGAIQLGI THTVGSLSTK PERDVLMQDF YVVESIFFPS EGSNLTPAHH 130 140 150 160 170 180 YNDFRFKTYA PVAFRYFREL FGIRPDDYLY SLCSEPLIEL CSSGASGSLF YVSSDDEFII 190 200 210 220 230 240 KTVQHKEAEF LQKLLPGYYM NLNQNPRTLL PKFYGLYCVQ AGGKNIRIVV MNNLLPRSVK 250 260 270 280 290 300 MHIKYDLKGS TYKRRASQKE REKPLPTFKD LDFLQDIPDG LFLDADMYNA LCKTLQRDCL 310 320 330 340 350 360 VLQSFKIMDY SLLMSIHNID HAQREPLSSE TQYSVDTRRP APQKALYSTA MESIQGEARR 370 380 390 400 410 420 GGTMETDDHM GGIPARNSKG ERLLLYIGII DILQSYRFVK KLEHSWKALV HDGDTVSVHR 430 440 450 460 470 480 PGFYAERFQR FMCNTVFKKI PCVHLGRPDV LPQTPPLEEI SEGSPIPDPS FSPLVGETLQ 490 500 MLTTSTTLEK LEVAESEFTH
	Isoform 3 [UniParc]. Checksum: 7CD48BFE175564A0	FASTA	549	61,187
	10 20 30 40 50 60 MASASSGPSS SVGFSSFDPA VPSCTLSSAS GIKRPMASEV PYASGMPIKK IGHRSVDSSG 70 80 90 100 110 120 ETTYKKTTSS ALKGAIQLGI THTVGSLSTK PERDVLMQDF YVVESIFFPS EGSNLTPAHH 130 140 150 160 170 180 YNDFRFKTYA PVAFRYFREL FGIRPDDYLY SLCSEPLIEL CSSGASGSLF YVSSDDEFII 190 200 210 220 230 240 KTVQHKEAEF LQKLLPGYYM NLNQNPRTLL PKFYGLYCVQ AGGKNIRIVV MNNLLPRSVK 250 260 270 280 290 300 MHIKYDLKGS TYKRRASQKE REKPLPTFKD LDFLQDIPDG LFLDADMYNA LCKTLQRDCL 310 320 330 340 350 360 VLQSFKIMDY SLLMSIHNID HAQREPLSSE TQYSVDTRRP APQKALYSTA MESIQGEARR 370 380 390 400 410 420 GGTMETDDHM GGIPARNSKG ERLLLYIGII DILQSYRFVK KLEHSWKALV HDGDTVSVHR 430 440 450 460 470 480 PGFYAERFQR FMCNTVFKKI PLKPSPSKKF RSGSSFSRRA GSSGNSCITY QPSVSGEHKA 490 500 510 520 530 540 QVTTKAEVEP GVHLGRPDVL PQTPPLEEIS EGSPIPDPSF SPLVGETLQM LTTSTTLEKL EVAESEFTH
	Isoform 4 [UniParc]. Checksum: 693CE47DBFC72B5F	FASTA	522	58,119
	10 20 30 40 50 60 MASASSGPSS SVGFSSFDPA VPSCTLSSAA SGIKRPMASE VPYASGMPIK KIGHRSVDSS 70 80 90 100 110 120 GETTYKKTTS SALKGAIQLG ITHTVGSLST KPERDVLMQD FYVVESIFFP SEGSNLTPAH 130 140 150 160 170 180 HYNDFRFKTY APVAFRYFRE LFGIRPDDYL YSLCSEPLIE LCSSGASGSL FYVSSDDEFI 190 200 210 220 230 240 IKTVQHKEAE FLQKLLPGYY MNLNQNPRTL LPKFYGLYCV QAGGKNIRIV VMNNLLPRSV 250 260 270 280 290 300 KMHIKYDLKG STYKRRASQK EREKPLPTFK DLDFLQDIPD GLFLDADMYN ALCKTLQRDC 310 320 330 340 350 360 LVLQSFKIMD YSLLMSIHNI DHAQREPLSS ETQYSVDTRR PAPQKALYST AMESIQGEAR 370 380 390 400 410 420 RGGTMETDDQ FVKKLEHSWK ALVHDGDTVS VHRPGFYAER FQRFMCNTVF KKIPLKPSPS 430 440 450 460 470 480 KKFRSGSSFS RRAGSSGNSC ITYQPSVSGE HKAQVTTKAE VEPGVHLGRP DVLPQTPPLE 490 500 510 520 EISEGSPIPD PSFSPLVGET LQMLTTSTTL EKLEVAESEF TH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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]	"Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry." Meierhofer D., Wang X., Huang L., Kaiser P. J. Proteome Res. 7:4566-4576(2008) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-103, MASS SPECTROMETRY.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00022149. IPI00022150. IPI00163602.
RefSeq	NP_001129108.1. NM_001135636.1. NP_001129109.1. NM_001135637.1. NP_001129110.1. NM_001135638.1. NP_003548.1. NM_003557.2.
UniGene	Hs.655131. Hs.661888.
3D structure databases
ProteinModelPortal	Q99755.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q99755. 2 interactions.
MINT	MINT-1406942.
STRING	9606.ENSP00000357883.
PTM databases
PhosphoSite	Q99755.
Polymorphism databases
DMDM	74752158.
Proteomic databases
PaxDb	Q99755.
PRIDE	Q99755.
Protocols and materials databases
DNASU	8394.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000349792; ENSP00000271663; ENSG00000143398. ENST00000368888; ENSP00000357883; ENSG00000143398. ENST00000368890; ENSP00000357885; ENSG00000143398. ENST00000441902; ENSP00000415648; ENSG00000143398.
GeneID	8394.
KEGG	hsa:8394.
UCSC	uc001exi.3. human. uc001exj.3. human. uc001exk.3. human.
Organism-specific databases
CTD	8394.
GeneCards	GC01P151170.
HGNC	HGNC:8994. PIP5K1A.
HPA	HPA029366.
MIM	603275. gene.
neXtProt	NX_Q99755.
PharmGKB	PA33327.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5148.
HOGENOM	HOG000193876.
HOVERGEN	HBG052818.
InParanoid	Q99755.
KO	K00889.
OMA	RSVKMHM.
Enzyme and pathway databases
BioCyc	MetaCyc:HS07047-MONOMER.
BRENDA	2.7.1.68. 2681.
Pathway_Interaction_DB	arf6downstreampathway. Arf6 downstream pathway. avb3_opn_pathway. Osteopontin-mediated events.
Reactome	REACT_111217. Metabolism.
Gene expression databases
ArrayExpress	Q99755.
Bgee	Q99755.
CleanEx	HS_PIP5K1A.
Genevestigator	Q99755.
GermOnline	ENSG00000143398. Homo sapiens.
Family and domain databases
InterPro	IPR023610. PInositol-4-P-5-kinase. IPR002498. PInositol-4-P-5-kinase_core. IPR016034. PInositol-4P-5-kinase_core_sub. [Graphical view]
PANTHER	PTHR23086. PTHR23086. 1 hit.
Pfam	PF01504. PIP5K. 1 hit. [Graphical view]
SMART	SM00330. PIPKc. 1 hit. [Graphical view]
PROSITE	PS51455. PIPK. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q99755.
ChEMBL	CHEMBL5969.
ChiTaRS	PIP5K1A. human.
GenomeRNAi	8394.
NextBio	31416.
PMAP-CutDB	Q99755.
SOURCE	Search...

Entry information

Entry name

PI51A_HUMAN

Accession

Primary (citable) accession number: Q99755
Secondary accession number(s): A8K4Q0 , B4DIN0, Q99754, Q99756

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
Last sequence update:	May 1, 1997
Last modified:	May 1, 2013
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.