Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q99755 (PI51A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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-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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length562 AA.
Sequence statusComplete.
Protein existenceEvidence 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.6 Ref.7 Ref.8

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.6 Ref.7

Subcellular location

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. Ref.7 Ref.8

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 componentCell membrane
Cell projection
Cytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMIsopeptide bond
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton reorganization

Inferred from mutant phenotype Ref.8. Source: UniProtKB

activation of Rac GTPase activity

Inferred from mutant phenotype Ref.8. Source: UniProtKB

cell chemotaxis

Inferred from mutant phenotype Ref.8. Source: UniProtKB

cell migration

Non-traceable author statement PubMed 15157668. Source: UniProtKB

fibroblast migration

Inferred from electronic annotation. Source: Ensembl

focal adhesion assembly

Inferred from mutant phenotype Ref.8. Source: UniProtKB

glycerophospholipid metabolic process

Traceable author statement Ref.1. Source: ProtInc

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

phosphatidylinositol phosphorylation

Inferred from direct assay PubMed 15157668. Source: GOC

phospholipid biosynthetic process

Inferred from direct assay PubMed 15157668. Source: UniProtKB

phospholipid metabolic process

Traceable author statement. Source: Reactome

protein targeting to plasma membrane

Inferred from mutant phenotype Ref.8. Source: UniProtKB

ruffle assembly

Inferred from mutant phenotype Ref.8. Source: UniProtKB

signal transduction

Traceable author statement Ref.1. Source: ProtInc

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

lamellipodium

Inferred from direct assay PubMed 15157668. Source: UniProtKB

nuclear speck

Inferred from direct assay Ref.6. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 15157668. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.8. Source: UniProtKB

ruffle membrane

Inferred from direct assay Ref.8. Source: UniProtKB

   Molecular_function1-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 562562Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha
PRO_0000185456

Regions

Domain81 – 449369PIPK

Amino acid modifications

Cross-link103Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Natural variations

Alternative sequence30 – 5223ASGIK…SYISL → SGIKRPMASE in isoform 2 and isoform 3.
VSP_016007
Alternative sequence41 – 5212Missing in isoform 4.
VSP_041912
Alternative sequence382 – 41029HMGGI…LQSYR → Q in isoform 4.
VSP_041913
Alternative sequence455 – 50450LKPSP…EVEPG → C in isoform 2.
VSP_016008

Experimental info

Mutagenesis3221D → N: Does not affect targeting of RAC1 to the plasma membrane; when associated with Q-440. Ref.8
Mutagenesis4401R → Q: Does not affect targeting of RAC1 to the plasma membrane; when associated with N-322. Ref.8
Sequence conflict2571K → E in BAG58542. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (PIP5KIalpha2) [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: A8F7988EB73506A0

FASTA56262,633
        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 

« Hide

Isoform 2 (PIP5KIalpha3) [UniParc].

Checksum: 684F0C9C2DBE9EC4
Show »

FASTA50056,053
Isoform 3 [UniParc].

Checksum: 7CD48BFE175564A0
Show »

FASTA54961,187
Isoform 4 [UniParc].

Checksum: 693CE47DBFC72B5F
Show »

FASTA52258,119

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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]"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]"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.
RefSeqNP_001129108.1. NM_001135636.1.
NP_001129109.1. NM_001135637.1.
NP_001129110.1. NM_001135638.1.
NP_003548.1. NM_003557.2.
UniGeneHs.655131.
Hs.661888.

3D structure databases

ProteinModelPortalQ99755.
SMRQ99755. Positions 81-449.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113983. 7 interactions.
DIPDIP-60649N.
IntActQ99755. 2 interactions.
MINTMINT-1406942.
STRING9606.ENSP00000357883.

Chemistry

BindingDBQ99755.
ChEMBLCHEMBL5969.
GuidetoPHARMACOLOGY2164.

PTM databases

PhosphoSiteQ99755.

Polymorphism databases

DMDM74752158.

Proteomic databases

PaxDbQ99755.
PRIDEQ99755.

Protocols and materials databases

DNASU8394.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000349792; ENSP00000271663; ENSG00000143398. [Q99755-3]
ENST00000368888; ENSP00000357883; ENSG00000143398. [Q99755-1]
ENST00000368890; ENSP00000357885; ENSG00000143398. [Q99755-2]
ENST00000441902; ENSP00000415648; ENSG00000143398. [Q99755-4]
GeneID8394.
KEGGhsa:8394.
UCSCuc001exi.3. human. [Q99755-3]
uc001exj.3. human. [Q99755-1]
uc001exk.3. human. [Q99755-2]
uc010pcu.2. human. [Q99755-4]

Organism-specific databases

CTD8394.
GeneCardsGC01P151170.
HGNCHGNC:8994. PIP5K1A.
HPAHPA029366.
MIM603275. gene.
neXtProtNX_Q99755.
PharmGKBPA33327.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5148.
HOGENOMHOG000193876.
HOVERGENHBG052818.
InParanoidQ99755.
KOK00889.
OMAETEDHMG.
OrthoDBEOG70W3DM.
PhylomeDBQ99755.
TreeFamTF319618.

Enzyme and pathway databases

BioCycMetaCyc:HS07047-MONOMER.
BRENDA2.7.1.68. 2681.
ReactomeREACT_111217. Metabolism.
SignaLinkQ99755.

Gene expression databases

ArrayExpressQ99755.
BgeeQ99755.
CleanExHS_PIP5K1A.
GenevestigatorQ99755.

Family and domain databases

Gene3D3.30.800.10. 1 hit.
3.30.810.10. 1 hit.
InterProIPR023610. 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]
PANTHERPTHR23086. PTHR23086. 1 hit.
PfamPF01504. PIP5K. 1 hit.
[Graphical view]
SMARTSM00330. PIPKc. 1 hit.
[Graphical view]
PROSITEPS51455. PIPK. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPIP5K1A. human.
GeneWikiPIP5K1A.
GenomeRNAi8394.
NextBio31416.
PMAP-CutDBQ99755.
PROQ99755.
SOURCESearch...

Entry information

Entry namePI51A_HUMAN
AccessionPrimary (citable) accession number: Q99755
Secondary accession number(s): A8K4Q0 expand/collapse secondary AC list , B4DIN0, Q99754, Q99756
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: May 1, 1997
Last modified: April 16, 2014
This is version 121 of the entry and version 1 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

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM