SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O60331

- PI51C_HUMAN

UniProt

O60331 - PI51C_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma

Gene
PIP5K1C, KIAA0589
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 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.4 Publications

Catalytic activityi

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

Enzyme regulationi

Activated by interaction with TLN2.1 Publication

GO - Molecular functioni

  1. 1-phosphatidylinositol-4-phosphate 5-kinase activity Source: UniProtKB-EC
  2. ATP binding Source: UniProtKB-KW
  3. protein binding Source: IntAct

GO - Biological processi

  1. actin cytoskeleton organization Source: UniProtKB
  2. adherens junction assembly Source: UniProtKB
  3. axon guidance Source: Reactome
  4. clathrin-mediated endocytosis Source: UniProtKB
  5. cytoskeletal anchoring at plasma membrane Source: Ensembl
  6. neutrophil chemotaxis Source: UniProtKB
  7. phagocytosis Source: UniProtKB
  8. phosphatidylinositol biosynthetic process Source: Reactome
  9. phospholipid metabolic process Source: Reactome
  10. platelet aggregation Source: Ensembl
  11. single organismal cell-cell adhesion Source: UniProtKB
  12. small molecule metabolic process Source: Reactome
  13. synaptic vesicle endocytosis Source: UniProtKB
  14. synaptic vesicle exocytosis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Cell adhesion, Chemotaxis, Endocytosis, Exocytosis, Phagocytosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS02710-MONOMER.
ReactomeiREACT_121025. Synthesis of PIPs at the plasma membrane.
REACT_19279. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma (EC:2.7.1.68)
Short name:
PIP5K1-gamma
Short name:
PtdIns(4)P-5-kinase 1 gamma
Alternative name(s):
Phosphatidylinositol 4-phosphate 5-kinase type I gamma
Short name:
PIP5KIgamma
Gene namesi
Name:PIP5K1C
Synonyms:KIAA0589
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:8996. PIP5K1C.

Subcellular locationi

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.4 Publications
Isoform 2 : Cytoplasm. Nucleus 4 Publications

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. endomembrane system Source: UniProtKB-SubCell
  3. focal adhesion Source: UniProtKB
  4. nucleus Source: UniProtKB-SubCell
  5. phagocytic cup Source: UniProtKB-SubCell
  6. ruffle membrane Source: UniProtKB-SubCell
  7. uropod Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti253 – 2531D → N in LCCS3; loss of activity. 1 Publication
VAR_036996

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi650 – 6501S → D: Abolishes binding to TLN2. Affects localization to focal adhesions. 1 Publication
Mutagenesisi650 – 6501S → N: Does not affect binding to TLN2 and localization to focal adhesions. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi611369. phenotype.
Orphaneti137783. Lethal congenital contracture syndrome type 3.
PharmGKBiPA33329.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 668668Phosphatidylinositol 4-phosphate 5-kinase type-1 gammaPRO_0000185462Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei265 – 2651N6-acetyllysine1 Publication
Modified residuei268 – 2681N6-acetyllysine1 Publication
Modified residuei639 – 6391Phosphotyrosine; by EGFR By similarity
Modified residuei649 – 6491Phosphotyrosine; by CSK1 Publication
Modified residuei650 – 6501Phosphoserine; by CDK5, MAPK1 and CDK11 Publication

Post-translational modificationi

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 1 Publication phosphorylation at Tyr-649 does not directly enhance binding to tailins (TLN1 and TLN2) but may act indirectly by inhibiting phosphorylation at Ser-650.1 Publication
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.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO60331.
PaxDbiO60331.
PRIDEiO60331.

PTM databases

PhosphoSiteiO60331.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

ArrayExpressiO60331.
BgeeiO60331.
CleanExiHS_PIP5K1C.
GenevestigatoriO60331.

Organism-specific databases

HPAiHPA017168.

Interactioni

Subunit structurei

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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
IQGAP1P469406EBI-8838062,EBI-297509

Protein-protein interaction databases

BioGridi116969. 7 interactions.
DIPiDIP-39809N.
IntActiO60331. 1 interaction.
STRINGi9606.ENSP00000335333.

Structurei

Secondary structure

1
668
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi644 – 6463

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2G35NMR-B646-653[»]
3H1ZX-ray1.83P639-653[»]
3H85X-ray2.60P646-653[»]
ProteinModelPortaliO60331.
SMRiO60331. Positions 76-328.

Miscellaneous databases

EvolutionaryTraceiO60331.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini75 – 443369PIPKAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni641 – 66828Mediates interaction with TLN2Add
BLAST

Sequence similaritiesi

Contains 1 PIPK domain.

Phylogenomic databases

eggNOGiCOG5253.
HOGENOMiHOG000193876.
HOVERGENiHBG052818.
InParanoidiO60331.
KOiK00889.
OMAiPTDERSW.
OrthoDBiEOG70W3DM.
PhylomeDBiO60331.
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: O60331-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MELEVPDEAE SAEAGAVPSE AAWAAESGAA AGLAQKKAAP TEVLSMTAQP    50
GPGHGKKLGH RGVDASGETT YKKTTSSTLK GAIQLGIGYT VGHLSSKPER 100
DVLMQDFYVV ESIFFPSEGS NLTPAHHFQD FRFKTYAPVA FRYFRELFGI 150
RPDDYLYSLC NEPLIELSNP GASGSLFYVT SDDEFIIKTV MHKEAEFLQK 200
LLPGYYMNLN QNPRTLLPKF YGLYCVQSGG KNIRVVVMNN ILPRVVKMHL 250
KFDLKGSTYK RRASKKEKEK SFPTYKDLDF MQDMPEGLLL DADTFSALVK 300
TLQRDCLVLE SFKIMDYSLL LGVHNIDQHE RERQAQGAQS TSDEKRPVGQ 350
KALYSTAMES IQGGAARGEA IESDDTMGGI PAVNGRGERL LLHIGIIDIL 400
QSYRFIKKLE HTWKALVHDG DTVSVHRPSF YAERFFKFMS NTVFRKNSSL 450
KSSPSKKGRG GALLAVKPLG PTAAFSASQI PSEREEAQYD LRGARSYPTL 500
EDEGRPDLLP CTPPSFEEAT TASIATTLSS TSLSIPERSP SETSEQPRYR 550
RRTQSSGQDG RPQEEPPAEE DLQQITVQVE PACSVEIVVP KEEDAGVEAS 600
PAGASAAVEV ETASQASDEE GAPASQASDE EDAPATDIYF PTDERSWVYS 650
PLHYSAQAPP ASDGESDT 668
Length:668
Mass (Da):73,260
Last modified:October 25, 2005 - v2
Checksum:i45A9FB32B4E43083
GO
Isoform 2 (identifier: O60331-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:700
Mass (Da):76,620
Checksum:iD3E3DC89BDF2E868
GO
Isoform 3 (identifier: O60331-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:707
Mass (Da):77,484
Checksum:i42BC87A1C20A5037
GO
Isoform 4 (identifier: O60331-4) [UniParc]FASTAAdd to Basket

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.

Show »
Length:640
Mass (Da):70,214
Checksum:i197B427BF16392C8
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti253 – 2531D → N in LCCS3; loss of activity. 1 Publication
VAR_036996

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei640 – 66829FPTDE…GESDT → FWRLWGPHAPTWPWRREGRA ACLCPYPPHVVTPFPGTGLC ASWSPDGTGGLGAMSCCVSV S in isoform 2. VSP_042078Add
BLAST
Alternative sequencei641 – 66828PTDER…GESDT → FTDGRYWIYSPRHRRLRAVT LSASGTVSDRSRPPWGEGAV PLGQQGAAGPRPEAQCLTSV VFQKGFG in isoform 3. VSP_042080Add
BLAST
Alternative sequencei641 – 66828Missing in isoform 4. VSP_042079Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti236 – 2361V → M in BAH14283. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS32872.1. [O60331-1]
CCDS56074.1. [O60331-4]
RefSeqiNP_001182662.1. NM_001195733.1. [O60331-4]
NP_036530.1. NM_012398.2. [O60331-1]
XP_005259580.1. XM_005259523.2. [O60331-3]
UniGeneiHs.282177.

Genome annotation databases

EnsembliENST00000335312; ENSP00000335333; ENSG00000186111. [O60331-1]
ENST00000537021; ENSP00000444779; ENSG00000186111. [O60331-2]
ENST00000539785; ENSP00000445992; ENSG00000186111. [O60331-4]
ENST00000589578; ENSP00000466363; ENSG00000186111. [O60331-3]
GeneIDi23396.
KEGGihsa:23396.
UCSCiuc002lyj.2. human. [O60331-1]
uc010xhr.2. human. [O60331-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS32872.1. [O60331-1 ]
CCDS56074.1. [O60331-4 ]
RefSeqi NP_001182662.1. NM_001195733.1. [O60331-4 ]
NP_036530.1. NM_012398.2. [O60331-1 ]
XP_005259580.1. XM_005259523.2. [O60331-3 ]
UniGenei Hs.282177.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2G35 NMR - B 646-653 [» ]
3H1Z X-ray 1.83 P 639-653 [» ]
3H85 X-ray 2.60 P 646-653 [» ]
ProteinModelPortali O60331.
SMRi O60331. Positions 76-328.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116969. 7 interactions.
DIPi DIP-39809N.
IntActi O60331. 1 interaction.
STRINGi 9606.ENSP00000335333.

Chemistry

BindingDBi O60331.
ChEMBLi CHEMBL1908383.
GuidetoPHARMACOLOGYi 2165.

PTM databases

PhosphoSitei O60331.

Proteomic databases

MaxQBi O60331.
PaxDbi O60331.
PRIDEi O60331.

Protocols and materials databases

DNASUi 23396.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000335312 ; ENSP00000335333 ; ENSG00000186111 . [O60331-1 ]
ENST00000537021 ; ENSP00000444779 ; ENSG00000186111 . [O60331-2 ]
ENST00000539785 ; ENSP00000445992 ; ENSG00000186111 . [O60331-4 ]
ENST00000589578 ; ENSP00000466363 ; ENSG00000186111 . [O60331-3 ]
GeneIDi 23396.
KEGGi hsa:23396.
UCSCi uc002lyj.2. human. [O60331-1 ]
uc010xhr.2. human. [O60331-3 ]

Organism-specific databases

CTDi 23396.
GeneCardsi GC19M003631.
HGNCi HGNC:8996. PIP5K1C.
HPAi HPA017168.
MIMi 606102. gene.
611369. phenotype.
neXtProti NX_O60331.
Orphaneti 137783. Lethal congenital contracture syndrome type 3.
PharmGKBi PA33329.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5253.
HOGENOMi HOG000193876.
HOVERGENi HBG052818.
InParanoidi O60331.
KOi K00889.
OMAi PTDERSW.
OrthoDBi EOG70W3DM.
PhylomeDBi O60331.
TreeFami TF319618.

Enzyme and pathway databases

BioCyci MetaCyc:HS02710-MONOMER.
Reactomei REACT_121025. Synthesis of PIPs at the plasma membrane.
REACT_19279. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.

Miscellaneous databases

ChiTaRSi PIP5K1C. human.
EvolutionaryTracei O60331.
GeneWikii PIP5K1C.
GenomeRNAii 23396.
NextBioi 45537.
PROi O60331.
SOURCEi Search...

Gene expression databases

ArrayExpressi O60331.
Bgeei O60331.
CleanExi HS_PIP5K1C.
Genevestigatori O60331.

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. "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.
    , 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.
    , 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. 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.

Entry informationi

Entry nameiPI51C_HUMAN
AccessioniPrimary (citable) accession number: O60331
Secondary accession number(s): B7Z9E7
, C6GIJ7, C6GIJ8, Q7LE07
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 25, 2005
Last modified: September 3, 2014
This is version 117 of the entry and version 2 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi