O14986 (PI51B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Phosphatidylinositol 4-phosphate 5-kinase type I beta
Short name=PIP5KIbeta
Protein STM-7
Type I phosphatidylinositol 4-phosphate 5-kinase beta

Gene names

Name:	PIP5K1B
Synonyms:	STM7

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	540 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Participates in the biosynthesis of phosphatidylinositol 4,5-bisphosphate. Mediates RAC1-dependent reorganization of actin filaments. Contributes to the activation of PLD2. Together with PIP5K1A is required after stimulation of G-protein coupled receptors for stable platelet adhesion By similarity.
Catalytic activity	ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate.
Subunit structure	Interacts with RAC1, AJUBA, PLD1, PLD2 and ARF1 By similarity.
Subcellular location	Endomembrane system By similarity. Note: Associated with membranes By similarity.
Tissue specificity	Detected in heart, pancreas, brain, kidney, skeletal muscle and lung. Ref.7
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	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	phosphatidylinositol biosynthetic process Traceable author statement. Source: Reactome small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome endomembrane system Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: UniProtKB-KW uropod Inferred from direct assay PubMed 20442317. Source: UniProtKB
Molecular_function	1-phosphatidylinositol-4-phosphate 5-kinase activity Non-traceable author statement Ref.7. Source: UniProtKB ATP binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O14986-1)

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: O14986-2)

Also known as: Isoform 1;

The sequence of this isoform differs from the canonical sequence as follows:
     24-24: T → TQVKNQILSRLPKIPCTFIQAWTNTEMITLLACYYFRSVST
     501-540: SKGLPSSSTFTLEEGTIYLTAEPNTLEVQDDNASVLDVYL → RFKMATSEH

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 540	540	Phosphatidylinositol 4-phosphate 5-kinase type-1 beta		PRO_0000185458
Regions
	Domain	25 – 395	371	PIPK
Natural variations
	Alternative sequence	24	1	T → TQVKNQILSRLPKIPCTFIQ AWTNTEMITLLACYYFRSVS T in isoform 2.		VSP_016010
	Alternative sequence	501 – 540	40	SKGLP…LDVYL → RFKMATSEH in isoform 2.		VSP_016011
	Natural variant	415	1	A → T. Ref.2 Corresponds to variant rs55897616 [ dbSNP | Ensembl ].		VAR_023712
Experimental info
	Sequence conflict	346	1	M → T in AAH30587. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 25, 2005. Version 2. Checksum: 7A683794A39A20B6	FASTA	540	61,036
	10 20 30 40 50 60 MSSAAENGEA APGKQNEEKT YKKTASSAIK GAIQLGIGYT VGNLTSKPER DVLMQDFYVV 70 80 90 100 110 120 ESVFLPSEGS NLTPAHHYPD FRFKTYAPLA FRYFRELFGI KPDDYLYSIC SEPLIELSNP 130 140 150 160 170 180 GASGSLFFVT SDDEFIIKTV QHKEAEFLQK LLPGYYMNLN QNPRTLLPKF YGLYCMQSGG 190 200 210 220 230 240 INIRIVVMNN VLPRSMRMHF TYDLKGSTYK RRASRKEREK SNPTFKDLDF LQDMHEGLYF 250 260 270 280 290 300 DTETYNALMK TLQRDCRVLE SFKIMDYSLL LGIHFLDHSL KEKEEETPQN VPDAKRTGMQ 310 320 330 340 350 360 KVLYSTAMES IQGPGKSGDG IITENPDTMG GIPAKSHRGE KLLLFMGIID ILQSYRLMKK 370 380 390 400 410 420 LEHSWKALVY DGDTVSVHRP SFYADRFLKF MNSRVFKKIQ ALKASPSKKR CNSIAALKAT 430 440 450 460 470 480 SQEIVSSISQ EWKDEKRDLL TEGQSFSSLD EEALGSRHRP DLVPSTPSLF EAASLATTIS 490 500 510 520 530 540 SSSLYVNEHY PHDRPTLYSN SKGLPSSSTF TLEEGTIYLT AEPNTLEVQD DNASVLDVYL
	Isoform 2 (Isoform 1) [UniParc]. Checksum: B12247947FAAB6B1	FASTA	549	62,485
	10 20 30 40 50 60 MSSAAENGEA APGKQNEEKT YKKTQVKNQI LSRLPKIPCT FIQAWTNTEM ITLLACYYFR 70 80 90 100 110 120 SVSTASSAIK GAIQLGIGYT VGNLTSKPER DVLMQDFYVV ESVFLPSEGS NLTPAHHYPD 130 140 150 160 170 180 FRFKTYAPLA FRYFRELFGI KPDDYLYSIC SEPLIELSNP GASGSLFFVT SDDEFIIKTV 190 200 210 220 230 240 QHKEAEFLQK LLPGYYMNLN QNPRTLLPKF YGLYCMQSGG INIRIVVMNN VLPRSMRMHF 250 260 270 280 290 300 TYDLKGSTYK RRASRKEREK SNPTFKDLDF LQDMHEGLYF DTETYNALMK TLQRDCRVLE 310 320 330 340 350 360 SFKIMDYSLL LGIHFLDHSL KEKEEETPQN VPDAKRTGMQ KVLYSTAMES IQGPGKSGDG 370 380 390 400 410 420 IITENPDTMG GIPAKSHRGE KLLLFMGIID ILQSYRLMKK LEHSWKALVY DGDTVSVHRP 430 440 450 460 470 480 SFYADRFLKF MNSRVFKKIQ ALKASPSKKR CNSIAALKAT SQEIVSSISQ EWKDEKRDLL 490 500 510 520 530 540 TEGQSFSSLD EEALGSRHRP DLVPSTPSLF EAASLATTIS SSSLYVNEHY PHDRPTLYSN RFKMATSEH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Friedreich's ataxia gene encodes a novel phosphatidylinositol-4-phosphate 5-kinase." Carvajal J.J., Pook M.A., dos Santos M., Doudney K., Hillermann R., Minogue S., Williamson R., Hsuan J.J., Chamberlain S. Nat. Genet. 14:157-162(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain.
[2]	"Exon-intron structure of a 2.7-kb transcript of the STM7 gene with phosphatidylinositol-4-phosphate 5-kinase activity." Pook M.A., Carvajal J.J., Doudney K., Hillermann R., Chamberlain S. Genomics 42:170-172(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-415, ALTERNATIVE SPLICING.
[3]	"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 1). Tissue: Kidney.
[4]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: Testis.
[7]	"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] OF 340-540 (ISOFORM 1), TISSUE SPECIFICITY. Tissue: Fetal brain.
[8]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X92493 mRNA. Translation: CAA63224.1. U52387 , U52376, U52377, U52378, U52379, U52380, U52381, U52382, U52383, U52384, U52385, U52386 Genomic DNA. Translation: AAC51327.1. AK292734 mRNA. Translation: BAF85423.1. AL162730, AL354794, AL356219 Genomic DNA. Translation: CAH71831.1. AL354794, AL356219 Genomic DNA. Translation: CAI12622.1. AL354794, AL356219 Genomic DNA. Translation: CAI12623.1. AL354794, AL356219 Genomic DNA. Translation: CAI12624.1. AL354794, AL162730, AL356219 Genomic DNA. Translation: CAI12625.1. AL356219, AL354794 Genomic DNA. Translation: CAI14092.1. AL356219, AL354794 Genomic DNA. Translation: CAI14093.1. AL356219, AL354794 Genomic DNA. Translation: CAI14094.1. AL356219, AL162730, AL354794 Genomic DNA. Translation: CAI14095.1. CH471089 Genomic DNA. Translation: EAW62465.1. BC030587 mRNA. Translation: AAH30587.1. U78580 mRNA. Translation: AAC50915.1.
IPI	IPI00304025. IPI00465236.
RefSeq	NP_003549.1. NM_003558.2.
UniGene	Hs.534371.
3D structure databases
ProteinModelPortal	O14986.
ModBase	Search...
PTM databases
PhosphoSite	O14986.
Proteomic databases
PaxDb	O14986.
PRIDE	O14986.
Protocols and materials databases
DNASU	8395.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000265382; ENSP00000265382; ENSG00000107242. ENST00000377284; ENSP00000366498; ENSG00000107242. ENST00000377290; ENSP00000366505; ENSG00000107242. ENST00000437200; ENSP00000398587; ENSG00000107242. ENST00000440050; ENSP00000411477; ENSG00000107242. ENST00000478500; ENSP00000435778; ENSG00000107242.
GeneID	8395.
KEGG	hsa:8395.
UCSC	uc004agu.3. human.
Organism-specific databases
CTD	8395.
GeneCards	GC09P071320.
HGNC	HGNC:8995. PIP5K1B.
HPA	HPA009687.
MIM	602745. gene.
neXtProt	NX_O14986.
PharmGKB	PA33328.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5253.
HOVERGEN	HBG052818.
KO	K00889.
OMA	EHYPHDR.
Enzyme and pathway databases
BioCyc	MetaCyc:HS02982-MONOMER.
Reactome	REACT_111217. Metabolism.
SABIO-RK	O14986.
Gene expression databases
ArrayExpress	O14986.
Bgee	O14986.
Genevestigator	O14986.
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
GenomeRNAi	8395.
NextBio	31420.
SOURCE	Search...

Entry information

Entry name

PI51B_HUMAN

Accession

Primary (citable) accession number: O14986
Secondary accession number(s): A8K9L9 , P78518, P78519, Q5T5K6, Q5T5K8, Q5T5K9, Q5VZ00, Q7KYT5, Q8NHQ5, Q92749

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
Last sequence update:	October 25, 2005
Last modified:	May 1, 2013
This is version 92 of the entry and version 2 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.