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O60331 (PI51C_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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 gamma

Short name=PIP5K1-gamma
Short name=PtdIns(4)P-5-kinase 1 gamma
EC=2.7.1.68
Alternative name(s):
Phosphatidylinositol 4-phosphate 5-kinase type I gamma
Short name=PIP5KIgamma
Gene names
Name:PIP5K1C
Synonyms:KIAA0589
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length668 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 vesicle mediated transport, cell adhesion, cell polarization and cell migration. Together with PIP5K1A is required for phagocytosis, but they regulate different types of actin remodeling at sequential steps. Promotes particle attachment by generating the pool of PtdIns(4,5)P2 that induces controlled actin depolymerization to facilitate Fc-gamma-R clustering. Mediates RAC1-dependent reorganization of actin filaments. Required for synaptic vesicle transport. Controls the plasma membrane pool of PtdIns(4,5)P2 implicated in synaptic vesicle endocytosis and exocytosis. Plays a role in endocytosis mediated by clathrin and AP-2 (adaptor protein complex 2). Required for clathrin-coated pits assembly at the synapse. Participates in cell junction assembly. Modulates adherens junctions formation by facilitating CDH1 trafficking. Required for focal adhesion dynamics. Modulates the targeting of talins (TLN1 and TLN2) to the plasma membrane and their efficient assembly into focal adhesions. Regulates the interaction between talins (TLN1 and TLN2) and beta-integrins. Required for uropodium formation and retraction of the cell rear during directed migration. Has a role in growth factor- stimulated directional cell migration and adhesion. Required for talin assembly into nascent adhesions forming at the leading edge toward the direction of the growth factor. Negative regulator of T-cell activation and adhesion. Negatively regulates integrin alpha-L/beta-2 (LFA-1) polarization and adhesion induced by T-cell receptor. Together with PIP5K1A have a role during embryogenesis and together with PIP5K1B may have a role immediately after birth. Ref.5 Ref.6 Ref.8 Ref.9

Catalytic activity

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

Enzyme regulation

Activated by interaction with TLN2. Ref.5

Subunit structure

Interacts with TLN1 By similarity. Interacts with TLN2; interaction stimulates lipid kinase activity. May compete with beta-integrins for the same binding site on TLN1 and TLN2. Interacts with ARF6. Interacts with AP2B1. Interacts with AP2M1; phosphorylation of PIP5K1C by CSK disrupts the interaction; clathrin competes with PIP5K1C By similarity. Interacts with CDH1. Interacts with CSK By similarity. Interacts with PLCG1; interaction is abolished upon EGF stimulation By similarity. Ref.5 Ref.6 Ref.8

Subcellular location

Cell membrane; Peripheral membrane protein; Cytoplasmic side. Endomembrane system. Cytoplasm. Cell junctionfocal adhesion. Cell junctionadherens junction. Cell projectionruffle membrane. Cell projectionphagocytic cup. Cell projectionuropodium. Note: Detected in plasma membrane invaginations. Isoform 3 is detected in intracellular vesicle-like structures. Ref.1 Ref.5 Ref.6 Ref.8

Isoform 2: Cytoplasm. Nucleus Ref.1 Ref.5 Ref.6 Ref.8.

Tissue specificity

Isoform 1 is strongly expressed in brain and also detected in heart and lung. Isoform 2 is strongly expressed in pancreas and liver and in lesser quantities in brain, heart, lung and kidney. Isoform 3 is detected in large amounts in heart and large intestine, is also present in lung, pancreas and thyroid, and to a lesser extent in brain, stomach and kidney. Ref.1

Post-translational modification

Phosphorylation on Ser-650 negatively regulates binding to TLN2 and is strongly stimulated in mitosis. Phosphorylation on Tyr-649 is necessary for targeting to focal adhesions. Phosphorylation on Ser-650 and Tyr-649 are mutually exclusive. Phosphorylated by SYK and CSK By similarity. Tyrosine phosphorylation is enhanced by PTK2 signaling. Phosphorylated at Tyr-639 upon EGF stimulation. Some studies suggest that phosphorylation on Tyr-649 enhances binding to tailins (TLN1 and TLN2). According to Ref.7 phosphorylation at Tyr-649 does not directly enhance binding to tailins (TLN1 and TLN2) but may act indirectly by inhibiting phosphorylation at Ser-650. Ref.7

Acetylation at Lys-265 and Lys-268 seems to decrease lipid kinase activity. Deacetylation of these sites by SIRT1 positively regulates the exocytosis of TSH-containing granules from pituitary cells. Ref.10

Involvement in disease

Lethal congenital contracture syndrome 3 (LCCS3) [MIM:611369]: A form of lethal congenital contracture syndrome, an autosomal recessive disorder characterized by degeneration of anterior horn neurons, extreme skeletal muscle atrophy, and congenital non-progressive joint contractures (arthrogryposis). The contractures can involve the upper or lower limbs and/or the vertebral column, leading to various degrees of flexion or extension limitations evident at birth. LCCS3 patients present at birth with severe multiple joint contractures and severe muscle wasting and atrophy, mainly in the legs. Death occurs minutes to hours after birth due to respiratory insufficiency. The phenotype can be distinguished from that of LCCS1 by the absence of hydrops, fractures and multiple pterygia, and from LCCS2 by the absence of neurogenic bladder defect.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12

Sequence similarities

Contains 1 PIPK domain.

Sequence caution

The sequence BAA25515.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processCell adhesion
Chemotaxis
Endocytosis
Exocytosis
Phagocytosis
   Cellular componentCell junction
Cell membrane
Cell projection
Cytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton organization

Traceable author statement Ref.11. Source: UniProtKB

adherens junction assembly

Traceable author statement Ref.11. Source: UniProtKB

axon guidance

Traceable author statement. Source: Reactome

cell-cell adhesion

Traceable author statement Ref.11. Source: UniProtKB

clathrin-mediated endocytosis

Traceable author statement Ref.11. Source: UniProtKB

cytoskeletal anchoring at plasma membrane

Inferred from electronic annotation. Source: Ensembl

neutrophil chemotaxis

Traceable author statement Ref.11. Source: UniProtKB

phagocytosis

Traceable author statement Ref.11. Source: UniProtKB

phosphatidylinositol biosynthetic process

Traceable author statement. Source: Reactome

phospholipid metabolic process

Traceable author statement. Source: Reactome

platelet aggregation

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

synaptic vesicle endocytosis

Traceable author statement Ref.11. Source: UniProtKB

synaptic vesicle exocytosis

Traceable author statement Ref.11. Source: UniProtKB

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

endomembrane system

Inferred from electronic annotation. Source: UniProtKB-SubCell

focal adhesion

Traceable author statement Ref.11. Source: UniProtKB

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

phagocytic cup

Inferred from electronic annotation. Source: UniProtKB-SubCell

ruffle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

uropod

Traceable author statement Ref.11. Source: UniProtKB

   Molecular_function1-phosphatidylinositol-4-phosphate 5-kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O60331-1)

Also known as: PIPKIgamma-90; PIPKIgamma-668; PIPkinIgamma-a; PIPKIgamma_i2;

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: O60331-2)

Also known as: variant 700; PIPKIgamma-700; PIPKIgamma_i4;

The sequence of this isoform differs from the canonical sequence as follows:
     640-668: FPTDERSWVYSPLHYSAQAPPASDGESDT → FWRLWGPHAP...GAMSCCVSVS
Isoform 3 (identifier: O60331-3)

Also known as: variant 707; PIPKIgamma-707; PIPKIgamma_i5;

The sequence of this isoform differs from the canonical sequence as follows:
     641-668: PTDERSWVYSPLHYSAQAPPASDGESDT → FTDGRYWIYS...TSVVFQKGFG
Isoform 4 (identifier: O60331-4)

Also known as: PIPKIgamma-87; PIPKIgamma-640; PIPkinIgamma-b; PIPKIgamma_i1;

The sequence of this isoform differs from the canonical sequence as follows:
     641-668: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 668668Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma
PRO_0000185462

Regions

Domain75 – 443369PIPK
Region641 – 66828Mediates interaction with TLN2

Amino acid modifications

Modified residue2651N6-acetyllysine Ref.10
Modified residue2681N6-acetyllysine Ref.10
Modified residue6391Phosphotyrosine; by EGFR By similarity
Modified residue6491Phosphotyrosine; by CSK Ref.7
Modified residue6501Phosphoserine; by CDK5, MAPK1 and CDK1 Ref.7

Natural variations

Alternative sequence640 – 66829FPTDE…GESDT → FWRLWGPHAPTWPWRREGRA ACLCPYPPHVVTPFPGTGLC ASWSPDGTGGLGAMSCCVSV S in isoform 2.
VSP_042078
Alternative sequence641 – 66828PTDER…GESDT → FTDGRYWIYSPRHRRLRAVT LSASGTVSDRSRPPWGEGAV PLGQQGAAGPRPEAQCLTSV VFQKGFG in isoform 3.
VSP_042080
Alternative sequence641 – 66828Missing in isoform 4.
VSP_042079
Natural variant2531D → N in LCCS3; loss of activity. Ref.12
VAR_036996

Experimental info

Mutagenesis6501S → D: Abolishes binding to TLN2. Affects localization to focal adhesions. Ref.7
Mutagenesis6501S → N: Does not affect binding to TLN2 and localization to focal adhesions. Ref.7
Sequence conflict2361V → M in BAH14283. Ref.3

Secondary structure

... 668
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (PIPKIgamma-90) (PIPKIgamma-668) (PIPkinIgamma-a) (PIPKIgamma_i2) [UniParc].

Last modified October 25, 2005. Version 2.
Checksum: 45A9FB32B4E43083

FASTA66873,260
        10         20         30         40         50         60 
MELEVPDEAE SAEAGAVPSE AAWAAESGAA AGLAQKKAAP TEVLSMTAQP GPGHGKKLGH 

        70         80         90        100        110        120 
RGVDASGETT YKKTTSSTLK GAIQLGIGYT VGHLSSKPER DVLMQDFYVV ESIFFPSEGS 

       130        140        150        160        170        180 
NLTPAHHFQD FRFKTYAPVA FRYFRELFGI RPDDYLYSLC NEPLIELSNP GASGSLFYVT 

       190        200        210        220        230        240 
SDDEFIIKTV MHKEAEFLQK LLPGYYMNLN QNPRTLLPKF YGLYCVQSGG KNIRVVVMNN 

       250        260        270        280        290        300 
ILPRVVKMHL KFDLKGSTYK RRASKKEKEK SFPTYKDLDF MQDMPEGLLL DADTFSALVK 

       310        320        330        340        350        360 
TLQRDCLVLE SFKIMDYSLL LGVHNIDQHE RERQAQGAQS TSDEKRPVGQ KALYSTAMES 

       370        380        390        400        410        420 
IQGGAARGEA IESDDTMGGI PAVNGRGERL LLHIGIIDIL QSYRFIKKLE HTWKALVHDG 

       430        440        450        460        470        480 
DTVSVHRPSF YAERFFKFMS NTVFRKNSSL KSSPSKKGRG GALLAVKPLG PTAAFSASQI 

       490        500        510        520        530        540 
PSEREEAQYD LRGARSYPTL EDEGRPDLLP CTPPSFEEAT TASIATTLSS TSLSIPERSP 

       550        560        570        580        590        600 
SETSEQPRYR RRTQSSGQDG RPQEEPPAEE DLQQITVQVE PACSVEIVVP KEEDAGVEAS 

       610        620        630        640        650        660 
PAGASAAVEV ETASQASDEE GAPASQASDE EDAPATDIYF PTDERSWVYS PLHYSAQAPP 


ASDGESDT 

« Hide

Isoform 2 (variant 700) (PIPKIgamma-700) (PIPKIgamma_i4) [UniParc].

Checksum: D3E3DC89BDF2E868
Show »

FASTA70076,620
Isoform 3 (variant 707) (PIPKIgamma-707) (PIPKIgamma_i5) [UniParc].

Checksum: 42BC87A1C20A5037
Show »

FASTA70777,484
Isoform 4 (PIPKIgamma-87) (PIPKIgamma-640) (PIPkinIgamma-b) (PIPKIgamma_i1) [UniParc].

Checksum: 197B427BF16392C8
Show »

FASTA64070,214

References

« Hide 'large scale' references
[1]"Two novel phosphatidylinositol-4-phosphate 5-kinase type Igamma splice variants expressed in human cells display distinctive cellular targeting."
Schill N.J., Anderson R.A.
Biochem. J. 422:473-482(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]"Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[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. 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] (ISOFORM 4).
[4]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"Recruitment and regulation of phosphatidylinositol phosphate kinase type 1 gamma by the FERM domain of talin."
Di Paolo G., Pellegrini L., Letinic K., Cestra G., Zoncu R., Voronov S., Chang S., Guo J., Wenk M.R., De Camilli P.
Nature 420:85-89(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TLN2, SUBCELLULAR LOCATION, ENZYME REGULATION.
[6]"ARF6 stimulates clathrin/AP-2 recruitment to synaptic membranes by activating phosphatidylinositol phosphate kinase type Igamma."
Krauss M., Kinuta M., Wenk M.R., De Camilli P., Takei K., Haucke V.
J. Cell Biol. 162:113-124(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ARF6, SUBCELLULAR LOCATION.
[7]"Regulation of the interaction between PIPKI gamma and talin by proline-directed protein kinases."
Lee S.Y., Voronov S., Letinic K., Nairn A.C., Di Paolo G., De Camilli P.
J. Cell Biol. 168:789-799(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-649 AND SER-650, MUTAGENESIS OF SER-650.
[8]"Type I gamma phosphatidylinositol phosphate kinase modulates adherens junction and E-cadherin trafficking via a direct interaction with mu 1B adaptin."
Ling K., Bairstow S.F., Carbonara C., Turbin D.A., Huntsman D.G., Anderson R.A.
J. Cell Biol. 176:343-353(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CDH1.
[9]"Type I gamma phosphatidylinositol phosphate kinase is required for EGF-stimulated directional cell migration."
Sun Y., Ling K., Wagoner M.P., Anderson R.A.
J. Cell Biol. 178:297-308(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL MIGRATION AND ADHESION.
[10]"SIRT1 regulates thyroid-stimulating hormone release by enhancing PIP5Kgamma activity through deacetylation of specific lysine residues in mammals."
Akieda-Asai S., Zaima N., Ikegami K., Kahyo T., Yao I., Hatanaka T., Iemura S., Sugiyama R., Yokozeki T., Eishi Y., Koike M., Ikeda K., Chiba T., Yamaza H., Shimokawa I., Song S.Y., Matsuno A., Mizutani A. expand/collapse author list , Sawabe M., Chao M.V., Tanaka M., Kanaho Y., Natsume T., Sugimura H., Date Y., McBurney M.W., Guarente L., Setou M.
PLoS ONE 5:E11755-E11755(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-265 AND LYS-268, DEACETYLATION BY SIRT1.
[11]"PIP5K-driven PtdIns(4,5)P2 synthesis: regulation and cellular functions."
van den Bout I., Divecha N.
J. Cell Sci. 122:3837-3850(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[12]"Lethal contractural syndrome type 3 (LCCS3) is caused by a mutation in PIP5K1C, which encodes PIPKI gamma of the phophatidylinositol pathway."
Narkis G., Ofir R., Landau D., Manor E., Volokita M., Hershkowitz R., Elbedour K., Birk O.S.
Am. J. Hum. Genet. 81:530-539(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LCCS3 ASN-253, CHARACTERIZATION OF VARIANT LCCS3 ASN-253.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FJ965536 mRNA. Translation: ACS73483.1.
FJ965537 mRNA. Translation: ACS73484.1.
AB011161 mRNA. Translation: BAA25515.1. Different initiation.
AK315912 mRNA. Translation: BAH14283.1.
AC005542 Genomic DNA. Translation: AAC32904.1.
AC093071 Genomic DNA. No translation available.
AC004637 Genomic DNA. No translation available.
RefSeqNP_001182662.1. NM_001195733.1.
NP_036530.1. NM_012398.2.
XP_005259580.1. XM_005259523.2.
UniGeneHs.282177.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3H1ZX-ray1.83P639-653[»]
3H85X-ray2.60P646-653[»]
ProteinModelPortalO60331.
SMRO60331. Positions 74-443.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116969. 6 interactions.
DIPDIP-39809N.
STRING9606.ENSP00000335333.

Chemistry

BindingDBO60331.
ChEMBLCHEMBL1908383.
GuidetoPHARMACOLOGY2165.

PTM databases

PhosphoSiteO60331.

Proteomic databases

PaxDbO60331.
PRIDEO60331.

Protocols and materials databases

DNASU23396.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000335312; ENSP00000335333; ENSG00000186111. [O60331-1]
ENST00000537021; ENSP00000444779; ENSG00000186111. [O60331-2]
ENST00000539785; ENSP00000445992; ENSG00000186111. [O60331-4]
ENST00000589578; ENSP00000466363; ENSG00000186111. [O60331-3]
GeneID23396.
KEGGhsa:23396.
UCSCuc002lyj.2. human. [O60331-1]
uc010xhr.2. human. [O60331-3]

Organism-specific databases

CTD23396.
GeneCardsGC19M003631.
HGNCHGNC:8996. PIP5K1C.
HPAHPA017168.
MIM606102. gene.
611369. phenotype.
neXtProtNX_O60331.
Orphanet137783. Lethal congenital contracture syndrome type 3.
PharmGKBPA33329.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5253.
HOGENOMHOG000193876.
HOVERGENHBG052818.
InParanoidO60331.
KOK00889.
OMAPTDERSW.
OrthoDBEOG70W3DM.
PhylomeDBO60331.
TreeFamTF319618.

Enzyme and pathway databases

BioCycMetaCyc:HS02710-MONOMER.
ReactomeREACT_111045. Developmental Biology.
REACT_111217. Metabolism.

Gene expression databases

ArrayExpressO60331.
BgeeO60331.
CleanExHS_PIP5K1C.
GenevestigatorO60331.

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

ChiTaRSPIP5K1C. human.
EvolutionaryTraceO60331.
GeneWikiPIP5K1C.
GenomeRNAi23396.
NextBio45537.
PROO60331.
SOURCESearch...

Entry information

Entry namePI51C_HUMAN
AccessionPrimary (citable) accession number: O60331
Secondary accession number(s): B7Z9E7 expand/collapse secondary AC list , C6GIJ7, C6GIJ8, Q7LE07
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 25, 2005
Last modified: April 16, 2014
This is version 113 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM