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Protein

Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma

Gene

PIP5K1C

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

GO - Biological processi

  • actin cytoskeleton organization Source: UniProtKB
  • adherens junction assembly Source: UniProtKB
  • clathrin-dependent endocytosis Source: UniProtKB
  • neutrophil chemotaxis Source: UniProtKB
  • phagocytosis Source: UniProtKB
  • phosphatidylinositol biosynthetic process Source: Reactome
  • regulation of phosphatidylinositol 3-kinase signaling Source: Reactome
  • single organismal cell-cell adhesion Source: UniProtKB
  • synaptic vesicle endocytosis Source: UniProtKB
  • 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.
ZFISH:HS02710-MONOMER.
ReactomeiR-HSA-1660499. Synthesis of PIPs at the plasma membrane.
R-HSA-399955. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
R-HSA-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-HSA-8856828. Clathrin-mediated endocytosis.
SIGNORiO60331.

Chemistry databases

SwissLipidsiSLP:000000551. [O60331-4]

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
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:8996. PIP5K1C.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • endomembrane system Source: UniProtKB-SubCell
  • focal adhesion Source: UniProtKB
  • nucleus Source: UniProtKB-SubCell
  • phagocytic cup Source: UniProtKB-SubCell
  • presynapse Source: GOC
  • ruffle membrane Source: UniProtKB-SubCell
  • 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)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:611369
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_036996253D → N in LCCS3; loss of activity. 1 PublicationCorresponds to variant rs121908315dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi650S → D: Abolishes binding to TLN2. Affects localization to focal adhesions. 1 Publication1
Mutagenesisi650S → N: Does not affect binding to TLN2 and localization to focal adhesions. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi23396.
MalaCardsiPIP5K1C.
MIMi611369. phenotype.
OpenTargetsiENSG00000186111.
Orphaneti137783. Lethal congenital contracture syndrome type 3.
PharmGKBiPA33329.

Chemistry databases

ChEMBLiCHEMBL1908383.
GuidetoPHARMACOLOGYi2165.

Polymorphism and mutation databases

BioMutaiPIP5K1C.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001854621 – 668Phosphatidylinositol 4-phosphate 5-kinase type-1 gammaAdd BLAST668

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei265N6-acetyllysine1 Publication1
Modified residuei268N6-acetyllysine1 Publication1
Modified residuei459Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei459Omega-N-methylarginine; alternateBy similarity1
Modified residuei555PhosphoserineBy similarity1
Modified residuei639Phosphotyrosine; by EGFRBy similarity1
Modified residuei649Phosphotyrosine; by CSK1 Publication1
Modified residuei650Phosphoserine; by CDK5, MAPK1 and CDK11 Publication1
Modified residuei662PhosphoserineBy similarity1
Modified residuei666PhosphoserineBy similarity1
Modified residuei668PhosphothreonineBy similarity1

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 PubMed:15738269 phosphorylation at Tyr-649 does not directly enhance binding to tailins (TLN1 and TLN2) but may act indirectly by inhibiting phosphorylation at Ser-650.By similarity1 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, Methylation, Phosphoprotein

Proteomic databases

EPDiO60331.
MaxQBiO60331.
PaxDbiO60331.
PeptideAtlasiO60331.
PRIDEiO60331.

PTM databases

iPTMnetiO60331.
PhosphoSitePlusiO60331.
SwissPalmiO60331.

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

BgeeiENSG00000186111.
CleanExiHS_PIP5K1C.
GenevisibleiO60331. HS.

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).By similarity

Binary interactionsi

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

Protein-protein interaction databases

BioGridi116969. 12 interactors.
DIPiDIP-39809N.
IntActiO60331. 1 interactor.
STRINGi9606.ENSP00000335333.

Chemistry databases

BindingDBiO60331.

Structurei

Secondary structure

1668
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi644 – 646Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2G35NMR-B646-653[»]
3H1ZX-ray1.83P639-653[»]
3H85X-ray2.60P646-653[»]
ProteinModelPortaliO60331.
SMRiO60331.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO60331.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini75 – 443PIPKPROSITE-ProRule annotationAdd BLAST369

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni641 – 668Mediates interaction with TLN21 PublicationAdd BLAST28

Sequence similaritiesi

Contains 1 PIPK domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0229. Eukaryota.
COG5253. LUCA.
GeneTreeiENSGT00760000119184.
HOGENOMiHOG000193876.
HOVERGENiHBG052818.
InParanoidiO60331.
KOiK00889.
OMAiPTDERSW.
OrthoDBiEOG091G0A6L.
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.
[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. AlignAdd to basket

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

        10         20         30         40         50
MELEVPDEAE SAEAGAVPSE AAWAAESGAA AGLAQKKAAP TEVLSMTAQP
60 70 80 90 100
GPGHGKKLGH RGVDASGETT YKKTTSSTLK GAIQLGIGYT VGHLSSKPER
110 120 130 140 150
DVLMQDFYVV ESIFFPSEGS NLTPAHHFQD FRFKTYAPVA FRYFRELFGI
160 170 180 190 200
RPDDYLYSLC NEPLIELSNP GASGSLFYVT SDDEFIIKTV MHKEAEFLQK
210 220 230 240 250
LLPGYYMNLN QNPRTLLPKF YGLYCVQSGG KNIRVVVMNN ILPRVVKMHL
260 270 280 290 300
KFDLKGSTYK RRASKKEKEK SFPTYKDLDF MQDMPEGLLL DADTFSALVK
310 320 330 340 350
TLQRDCLVLE SFKIMDYSLL LGVHNIDQHE RERQAQGAQS TSDEKRPVGQ
360 370 380 390 400
KALYSTAMES IQGGAARGEA IESDDTMGGI PAVNGRGERL LLHIGIIDIL
410 420 430 440 450
QSYRFIKKLE HTWKALVHDG DTVSVHRPSF YAERFFKFMS NTVFRKNSSL
460 470 480 490 500
KSSPSKKGRG GALLAVKPLG PTAAFSASQI PSEREEAQYD LRGARSYPTL
510 520 530 540 550
EDEGRPDLLP CTPPSFEEAT TASIATTLSS TSLSIPERSP SETSEQPRYR
560 570 580 590 600
RRTQSSGQDG RPQEEPPAEE DLQQITVQVE PACSVEIVVP KEEDAGVEAS
610 620 630 640 650
PAGASAAVEV ETASQASDEE GAPASQASDE EDAPATDIYF PTDERSWVYS
660
PLHYSAQAPP ASDGESDT
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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti236V → M in BAH14283 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_036996253D → N in LCCS3; loss of activity. 1 PublicationCorresponds to variant rs121908315dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_042078640 – 668FPTDE…GESDT → FWRLWGPHAPTWPWRREGRA ACLCPYPPHVVTPFPGTGLC ASWSPDGTGGLGAMSCCVSV S in isoform 2. 1 PublicationAdd BLAST29
Alternative sequenceiVSP_042080641 – 668PTDER…GESDT → FTDGRYWIYSPRHRRLRAVT LSASGTVSDRSRPPWGEGAV PLGQQGAAGPRPEAQCLTSV VFQKGFG in isoform 3. 1 PublicationAdd BLAST28
Alternative sequenceiVSP_042079641 – 668Missing in isoform 4. 1 PublicationAdd BLAST28

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
CCDS74257.1. [O60331-3]
RefSeqiNP_001182662.1. NM_001195733.1. [O60331-4]
NP_001287778.1. NM_001300849.1. [O60331-3]
NP_036530.1. NM_012398.2. [O60331-1]
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.3. human. [O60331-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
CCDS74257.1. [O60331-3]
RefSeqiNP_001182662.1. NM_001195733.1. [O60331-4]
NP_001287778.1. NM_001300849.1. [O60331-3]
NP_036530.1. NM_012398.2. [O60331-1]
UniGeneiHs.282177.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2G35NMR-B646-653[»]
3H1ZX-ray1.83P639-653[»]
3H85X-ray2.60P646-653[»]
ProteinModelPortaliO60331.
SMRiO60331.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116969. 12 interactors.
DIPiDIP-39809N.
IntActiO60331. 1 interactor.
STRINGi9606.ENSP00000335333.

Chemistry databases

BindingDBiO60331.
ChEMBLiCHEMBL1908383.
GuidetoPHARMACOLOGYi2165.
SwissLipidsiSLP:000000551. [O60331-4]

PTM databases

iPTMnetiO60331.
PhosphoSitePlusiO60331.
SwissPalmiO60331.

Polymorphism and mutation databases

BioMutaiPIP5K1C.

Proteomic databases

EPDiO60331.
MaxQBiO60331.
PaxDbiO60331.
PeptideAtlasiO60331.
PRIDEiO60331.

Protocols and materials databases

DNASUi23396.
Structural Biology KnowledgebaseSearch...

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.3. human. [O60331-1]

Organism-specific databases

CTDi23396.
DisGeNETi23396.
GeneCardsiPIP5K1C.
HGNCiHGNC:8996. PIP5K1C.
HPAiHPA017168.
MalaCardsiPIP5K1C.
MIMi606102. gene.
611369. phenotype.
neXtProtiNX_O60331.
OpenTargetsiENSG00000186111.
Orphaneti137783. Lethal congenital contracture syndrome type 3.
PharmGKBiPA33329.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0229. Eukaryota.
COG5253. LUCA.
GeneTreeiENSGT00760000119184.
HOGENOMiHOG000193876.
HOVERGENiHBG052818.
InParanoidiO60331.
KOiK00889.
OMAiPTDERSW.
OrthoDBiEOG091G0A6L.
PhylomeDBiO60331.
TreeFamiTF319618.

Enzyme and pathway databases

BioCyciMetaCyc:HS02710-MONOMER.
ZFISH:HS02710-MONOMER.
ReactomeiR-HSA-1660499. Synthesis of PIPs at the plasma membrane.
R-HSA-399955. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
R-HSA-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-HSA-8856828. Clathrin-mediated endocytosis.
SIGNORiO60331.

Miscellaneous databases

ChiTaRSiPIP5K1C. human.
EvolutionaryTraceiO60331.
GeneWikiiPIP5K1C.
GenomeRNAii23396.
PROiO60331.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000186111.
CleanExiHS_PIP5K1C.
GenevisibleiO60331. HS.

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.
[Graphical view]
PANTHERiPTHR23086. PTHR23086. 1 hit.
PfamiPF01504. PIP5K. 1 hit.
[Graphical view]
SMARTiSM00330. PIPKc. 1 hit.
[Graphical view]
PROSITEiPS51455. PIPK. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 138 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.