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Q9Y2I7

- FYV1_HUMAN

UniProt

Q9Y2I7 - FYV1_HUMAN

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Protein
1-phosphatidylinositol 3-phosphate 5-kinase
Gene
PIKFYVE, KIAA0981, PIP5K3
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Catalyzes the phosphorylation of phosphatidylinositol 3-phosphate on the fifth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 3,5-bisphosphate. Required for endocytic-vacuolar pathway and nuclear migration. Plays a role in the biogenesis of endosome carrier vesicles (ECV)/ multivesicular bodies (MVB) transport intermediates from early endosomes.1 Publication

Catalytic activityi

ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri158 – 21861FYVE-type
Add
BLAST

GO - Molecular functioni

  1. 1-phosphatidylinositol-3-phosphate 5-kinase activity Source: UniProtKB-EC
  2. 1-phosphatidylinositol-4-phosphate 5-kinase activity Source: HGNC
  3. ATP binding Source: UniProtKB-KW
  4. metal ion binding Source: UniProtKB-KW
  5. phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity Source: Reactome
  6. protein binding Source: UniProtKB

GO - Biological processi

  1. cellular protein metabolic process Source: InterPro
  2. intracellular signal transduction Source: InterPro
  3. myelin assembly Source: Ensembl
  4. phosphatidylinositol biosynthetic process Source: Reactome
  5. phosphatidylinositol phosphorylation Source: GOC
  6. phosphatidylinositol-3-phosphate biosynthetic process Source: GOC
  7. phospholipid metabolic process Source: Reactome
  8. protein localization to nucleus Source: UniProtKB
  9. retrograde transport, endosome to Golgi Source: UniProtKB
  10. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:HS03825-MONOMER.
BRENDAi2.7.1.68. 2681.
ReactomeiREACT_120756. Synthesis of PIPs at the early endosome membrane.
REACT_120836. Synthesis of PIPs at the Golgi membrane.
REACT_120918. Synthesis of PIPs at the late endosome membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
1-phosphatidylinositol 3-phosphate 5-kinase (EC:2.7.1.150)
Short name:
Phosphatidylinositol 3-phosphate 5-kinase
Alternative name(s):
FYVE finger-containing phosphoinositide kinase
PIKfyve
Phosphatidylinositol 3-phosphate 5-kinase type III
Short name:
PIPkin-III
Short name:
Type III PIP kinase
Gene namesi
Name:PIKFYVE
Synonyms:KIAA0981, PIP5K3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:23785. PIKFYVE.

Subcellular locationi

Endosome membrane
Note: Mainly associated with membranes of the late endocytic pathway.2 Publications

GO - Cellular componenti

  1. Golgi membrane Source: Reactome
  2. cytoplasmic vesicle Source: Ensembl
  3. cytosol Source: Ensembl
  4. early endosome membrane Source: UniProtKB
  5. endosome membrane Source: UniProtKB
  6. late endosome membrane Source: Reactome
  7. membrane raft Source: HGNC
  8. perinuclear region of cytoplasm Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Membrane

Pathology & Biotechi

Involvement in diseasei

Corneal dystrophy, fleck (CFD) [MIM:121850]: A form of stromal corneal dystrophy characterized by numerous small white flecks scattered in all levels of the stroma, with configurations varying from semicircular to wreath-like, curvilinear, or punctate. Although CFD may occasionally cause mild photophobia, patients are typically asymptomatic and have normal vision.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1103 – 11031K → R in CFD. 1 Publication
VAR_025309

Keywords - Diseasei

Corneal dystrophy, Disease mutation

Organism-specific databases

MIMi121850. phenotype.
Orphaneti98970. Fleck corneal dystrophy.
PharmGKBiPA165697116.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 209820971-phosphatidylinositol 3-phosphate 5-kinase
PRO_0000185452Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei299 – 2991Phosphoserine2 Publications
Modified residuei318 – 3181Phosphoserine; by PKB/AKT1 or PKB/AKT21 Publication
Modified residuei329 – 3291Phosphoserine1 Publication
Modified residuei1544 – 15441Phosphoserine2 Publications
Modified residuei1549 – 15491Phosphoserine1 Publication
Modified residuei1754 – 17541Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated in response to insulin at Ser-318 in a protein kinase B (PKB)-dependent manner.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9Y2I7.
PaxDbiQ9Y2I7.
PRIDEiQ9Y2I7.

PTM databases

PhosphoSiteiQ9Y2I7.

Expressioni

Gene expression databases

ArrayExpressiQ9Y2I7.
BgeeiQ9Y2I7.
CleanExiHS_PIP5K3.
GenevestigatoriQ9Y2I7.

Organism-specific databases

HPAiHPA042604.

Interactioni

Subunit structurei

Component of the PI(3,5)P2 regulatory complex/PAS complex, at least composed of PIKFYVE, FIG4 and VAC14. VAC14 nucleates the assembly of the complex and serves as a scaffold.2 Publications

Protein-protein interaction databases

BioGridi128336. 9 interactions.
IntActiQ9Y2I7. 3 interactions.
MINTiMINT-3084529.
STRINGi9606.ENSP00000264380.

Structurei

3D structure databases

ProteinModelPortaliQ9Y2I7.
SMRiQ9Y2I7. Positions 155-191, 540-872, 1819-2025.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini365 – 44076DEP
Add
BLAST
Domaini1758 – 2084327PIPK
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1842 – 2098257Catalytic
Add
BLAST

Sequence similaritiesi

Contains 1 DEP domain.
Contains 1 PIPK domain.

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG0459.
HOGENOMiHOG000059273.
HOVERGENiHBG072055.
InParanoidiQ9Y2I7.
KOiK00921.
OMAiWTEKMQA.
OrthoDBiEOG757CWH.
PhylomeDBiQ9Y2I7.
TreeFamiTF321717.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.30.260.10. 2 hits.
3.30.40.10. 1 hit.
3.30.800.10. 1 hit.
3.30.810.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR002423. Cpn60/TCP-1.
IPR000591. DEP_dom.
IPR027409. GroEL-like_apical_dom.
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.
IPR027410. TCP-1-like_intermed.
IPR011991. WHTH_DNA-bd_dom.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR11353. PTHR11353. 1 hit.
PfamiPF00118. Cpn60_TCP1. 1 hit.
PF00610. DEP. 1 hit.
PF01363. FYVE. 1 hit.
PF01504. PIP5K. 1 hit.
[Graphical view]
SMARTiSM00049. DEP. 1 hit.
SM00064. FYVE. 1 hit.
SM00330. PIPKc. 1 hit.
[Graphical view]
SUPFAMiSSF52029. SSF52029. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEiPS50186. DEP. 1 hit.
PS51455. PIPK. 1 hit.
PS50178. ZF_FYVE. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y2I7-1) [UniParc]FASTAAdd to Basket

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

MATDDKTSPT LDSANDLPRS PTSPSHLTHF KPLTPDQDEP PFKSAYSSFV     50
NLFRFNKERA EGGQGEQQPL SGSWTSPQLP SRTQSVRSPT PYKKQLNEEL 100
QRRSSALDTR RKAEPTFGGH DPRTAVQLRS LSTVLKRLKE IMEGKSQDSD 150
LKQYWMPDSQ CKECYDCSEK FTTFRRRHHC RLCGQIFCSR CCNQEIPGKF 200
MGYTGDLRAC TYCRKIALSY AHSTDSNSIG EDLNALSDSA CSVSVLDPSE 250
PRTPVGSRKA SRNIFLEDDL AWQSLIHPDS SNTPLSTRLV SVQEDAGKSP 300
ARNRSASITN LSLDRSGSPM VPSYETSVSP QANRTYVRTE TTEDERKILL 350
DSVQLKDLWK KICHHSSGME FQDHRYWLRT HPNCIVGKEL VNWLIRNGHI 400
ATRAQAIAIG QAMVDGRWLD CVSHHDQLFR DEYALYRPLQ STEFSETPSP 450
DSDSVNSVEG HSEPSWFKDI KFDDSDTEQI AEEGDDNLAN SASPSKRTSV 500
SSFQSTVDSD SAASISLNVE LDNVNFHIKK PSKYPHVPPH PADQKEYLIS 550
DTGGQQLSIS DAFIKESLFN RRVEEKSKEL PFTPLGWHHN NLELLREENG 600
EKQAMERLLS ANHNHMMALL QQLLHSDSLS SSWRDIIVSL VCQVVQTVRP 650
DVKNQDDDMD IRQFVHIKKI PGGKKFDSVV VNGFVCTKNI AHKKMSSCIK 700
NPKILLLKCS IEYLYREETK FTCIDPIVLQ EREFLKNYVQ RIVDVRPTLV 750
LVEKTVSRIA QDMLLEHGIT LVINVKSQVL ERISRMTQGD LVMSMDQLLT 800
KPHLGTCHKF YMQIFQLPNE QTKTLMFFEG CPQHLGCTIK LRGGSDYELA 850
RVKEILIFMI CVAYHSQLEI SFLMDEFAMP PTLMQNPSFH SLIEGRGHEG 900
AVQEQYGGGS IPWDPDIPPE SLPCDDSSLL ELRIVFEKGE QENKNLPQAV 950
ASVKHQEHST TACPAGLPCA FFAPVPESLL PLPVDDQQDA LGSEQPETLQ 1000
QTVVLQDPKS QIRAFRDPLQ DDTGLYVTEE VTSSEDKRKT YSLAFKQELK 1050
DVILCISPVI TFREPFLLTE KGMRCSTRDY FAEQVYWSPL LNKEFKEMEN 1100
RRKKQLLRDL SGLQGMNGSI QAKSIQVLPS HELVSTRIAE HLGDSQSLGR 1150
MLADYRARGG RIQPKNSDPF AHSKDASSTS SGQSGSKNEG DEERGLILSD 1200
AVWSTKVDCL NPINHQRLCV LFSSSSAQSS NAPSACVSPW IVTMEFYGKN 1250
DLTLGIFLER YCFRPSYQCP SMFCDTPMVH HIRRFVHGQG CVQIILKELD 1300
SPVPGYQHTI LTYSWCRICK QVTPVVALSN ESWSMSFAKY LELRFYGHQY 1350
TRRANAEPCG HSIHHDYHQY FSYNQMVASF SYSPIRLLEV CVPLPKIFIK 1400
RQAPLKVSLL QDLKDFFQKV SQVYVAIDER LASLKTDTFS KTREEKMEDI 1450
FAQKEMEEGE FKNWIEKMQA RLMSSSVDTP QQLQSVFESL IAKKQSLCEV 1500
LQAWNNRLQD LFQQEKGRKR PSVPPSPGRL RQGEESKISA MDASPRNISP 1550
GLQNGEKEDR FLTTLSSQSS TSSTHLQLPT PPEVMSEQSV GGPPELDTAS 1600
SSEDVFDGHL LGSTDSQVKE KSTMKAIFAN LLPGNSYNPI PFPFDPDKHY 1650
LMYEHERVPI AVCEKEPSSI IAFALSCKEY RNALEELSKA TQWNSAEEGL 1700
PTNSTSDSRP KSSSPIRLPE MSGGQTNRTT ETEPQPTKKA SGMLSFFRGT 1750
AGKSPDLSSQ KRETLRGADS AYYQVGQTGK EGTENQGVEP QDEVDGGDTQ 1800
KKQLINPHVE LQFSDANAKF YCRLYYAGEF HKMREVILDS SEEDFIRSLS 1850
HSSPWQARGG KSGAAFYATE DDRFILKQMP RLEVQSFLDF APHYFNYITN 1900
AVQQKRPTAL AKILGVYRIG YKNSQNNTEK KLDLLVMENL FYGRKMAQVF 1950
DLKGSLRNRN VKTDTGKESC DVVLLDENLL KMVRDNPLYI RSHSKAVLRT 2000
SIHSDSHFLS SHLIIDYSLL VGRDDTSNEL VVGIIDYIRT FTWDKKLEMV 2050
VKSTGILGGQ GKMPTVVSPE LYRTRFCEAM DKYFLMVPDH WTGLGLNC 2098
Length:2,098
Mass (Da):237,136
Last modified:July 13, 2010 - v3
Checksum:i390C43530D3B1E81
GO
Isoform 2 (identifier: Q9Y2I7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     108-204: Missing.
     546-548: EYL → GRR
     549-2098: Missing.

Note: No experimental confirmation available.

Show »
Length:451
Mass (Da):50,211
Checksum:iE5C7D123475EA30E
GO
Isoform 3 (identifier: Q9Y2I7-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     109-203: TRRKAEPTFG...QEIPGKFMGY → NSLQHPQEN
     546-548: EYL → GRR
     549-2098: Missing.

Note: No experimental confirmation available.

Show »
Length:462
Mass (Da):51,476
Checksum:i60E516304C47A038
GO
Isoform 4 (identifier: Q9Y2I7-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     546-548: EYL → GRR
     549-2098: Missing.

Note: No experimental confirmation available.

Show »
Length:548
Mass (Da):61,595
Checksum:i46091F5266458F67
GO

Sequence cautioni

The sequence BAC03674.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti617 – 6171M → V.
Corresponds to variant rs16840913 [ dbSNP | Ensembl ].
VAR_057097
Natural varianti696 – 6961S → N.2 Publications
Corresponds to variant rs10932258 [ dbSNP | Ensembl ].
VAR_063406
Natural varianti932 – 9321L → S.2 Publications
Corresponds to variant rs2363468 [ dbSNP | Ensembl ].
VAR_063407
Natural varianti995 – 9951Q → L.2 Publications
Corresponds to variant rs893254 [ dbSNP | Ensembl ].
VAR_063408
Natural varianti998 – 9981T → S.2 Publications
Corresponds to variant rs893253 [ dbSNP | Ensembl ].
VAR_063409
Natural varianti1033 – 10331S → A.
Corresponds to variant rs999890 [ dbSNP | Ensembl ].
VAR_057098
Natural varianti1103 – 11031K → R in CFD. 1 Publication
VAR_025309
Natural varianti1183 – 11831Q → K.3 Publications
Corresponds to variant rs1529979 [ dbSNP | Ensembl ].
VAR_063410
Natural varianti1858 – 18581R → Q.
Corresponds to variant rs2289170 [ dbSNP | Ensembl ].
VAR_057099

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei108 – 20497Missing in isoform 2.
VSP_040108Add
BLAST
Alternative sequencei109 – 20395TRRKA…KFMGY → NSLQHPQEN in isoform 3.
VSP_040109Add
BLAST
Alternative sequencei546 – 5483EYL → GRR in isoform 2, isoform 3 and isoform 4.
VSP_040110
Alternative sequencei549 – 20981550Missing in isoform 2, isoform 3 and isoform 4.
VSP_040111Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1335 – 13351M → I in BAC03674. 1 Publication
Sequence conflicti2019 – 20191L → S in BAC03674. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY457063 mRNA. Translation: AAR19397.1.
AC012362 Genomic DNA. Translation: AAY14870.1.
AC016697 Genomic DNA. Translation: AAX93222.1.
CH471063 Genomic DNA. Translation: EAW70444.1.
CH471063 Genomic DNA. Translation: EAW70445.1.
BC032389 mRNA. Translation: AAH32389.1.
BC125052 mRNA. Translation: AAI25053.1.
BC125053 mRNA. Translation: AAI25054.1.
AK091482 mRNA. Translation: BAC03674.1. Different initiation.
AB023198 mRNA. Translation: BAA76825.1.
CCDSiCCDS2382.1. [Q9Y2I7-1]
CCDS33368.1. [Q9Y2I7-2]
CCDS54431.1. [Q9Y2I7-4]
RefSeqiNP_001171471.1. NM_001178000.1. [Q9Y2I7-4]
NP_055855.2. NM_015040.3. [Q9Y2I7-1]
NP_689884.1. NM_152671.3. [Q9Y2I7-2]
UniGeneiHs.744997.

Genome annotation databases

EnsembliENST00000264380; ENSP00000264380; ENSG00000115020. [Q9Y2I7-1]
ENST00000308862; ENSP00000308715; ENSG00000115020. [Q9Y2I7-3]
ENST00000392202; ENSP00000376038; ENSG00000115020. [Q9Y2I7-2]
ENST00000407449; ENSP00000384356; ENSG00000115020. [Q9Y2I7-4]
GeneIDi200576.
KEGGihsa:200576.
UCSCiuc002vcv.3. human. [Q9Y2I7-2]
uc002vcw.3. human. [Q9Y2I7-4]
uc002vcx.3. human. [Q9Y2I7-3]
uc002vcz.3. human. [Q9Y2I7-1]

Polymorphism databases

DMDMi300669693.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY457063 mRNA. Translation: AAR19397.1 .
AC012362 Genomic DNA. Translation: AAY14870.1 .
AC016697 Genomic DNA. Translation: AAX93222.1 .
CH471063 Genomic DNA. Translation: EAW70444.1 .
CH471063 Genomic DNA. Translation: EAW70445.1 .
BC032389 mRNA. Translation: AAH32389.1 .
BC125052 mRNA. Translation: AAI25053.1 .
BC125053 mRNA. Translation: AAI25054.1 .
AK091482 mRNA. Translation: BAC03674.1 . Different initiation.
AB023198 mRNA. Translation: BAA76825.1 .
CCDSi CCDS2382.1. [Q9Y2I7-1 ]
CCDS33368.1. [Q9Y2I7-2 ]
CCDS54431.1. [Q9Y2I7-4 ]
RefSeqi NP_001171471.1. NM_001178000.1. [Q9Y2I7-4 ]
NP_055855.2. NM_015040.3. [Q9Y2I7-1 ]
NP_689884.1. NM_152671.3. [Q9Y2I7-2 ]
UniGenei Hs.744997.

3D structure databases

ProteinModelPortali Q9Y2I7.
SMRi Q9Y2I7. Positions 155-191, 540-872, 1819-2025.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 128336. 9 interactions.
IntActi Q9Y2I7. 3 interactions.
MINTi MINT-3084529.
STRINGi 9606.ENSP00000264380.

Chemistry

ChEMBLi CHEMBL1938222.

PTM databases

PhosphoSitei Q9Y2I7.

Polymorphism databases

DMDMi 300669693.

Proteomic databases

MaxQBi Q9Y2I7.
PaxDbi Q9Y2I7.
PRIDEi Q9Y2I7.

Protocols and materials databases

DNASUi 200576.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264380 ; ENSP00000264380 ; ENSG00000115020 . [Q9Y2I7-1 ]
ENST00000308862 ; ENSP00000308715 ; ENSG00000115020 . [Q9Y2I7-3 ]
ENST00000392202 ; ENSP00000376038 ; ENSG00000115020 . [Q9Y2I7-2 ]
ENST00000407449 ; ENSP00000384356 ; ENSG00000115020 . [Q9Y2I7-4 ]
GeneIDi 200576.
KEGGi hsa:200576.
UCSCi uc002vcv.3. human. [Q9Y2I7-2 ]
uc002vcw.3. human. [Q9Y2I7-4 ]
uc002vcx.3. human. [Q9Y2I7-3 ]
uc002vcz.3. human. [Q9Y2I7-1 ]

Organism-specific databases

CTDi 200576.
GeneCardsi GC02P209130.
HGNCi HGNC:23785. PIKFYVE.
HPAi HPA042604.
MIMi 121850. phenotype.
609414. gene.
neXtProti NX_Q9Y2I7.
Orphaneti 98970. Fleck corneal dystrophy.
PharmGKBi PA165697116.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0459.
HOGENOMi HOG000059273.
HOVERGENi HBG072055.
InParanoidi Q9Y2I7.
KOi K00921.
OMAi WTEKMQA.
OrthoDBi EOG757CWH.
PhylomeDBi Q9Y2I7.
TreeFami TF321717.

Enzyme and pathway databases

BioCyci MetaCyc:HS03825-MONOMER.
BRENDAi 2.7.1.68. 2681.
Reactomei REACT_120756. Synthesis of PIPs at the early endosome membrane.
REACT_120836. Synthesis of PIPs at the Golgi membrane.
REACT_120918. Synthesis of PIPs at the late endosome membrane.

Miscellaneous databases

ChiTaRSi PIKFYVE. human.
GeneWikii PIKFYVE.
GenomeRNAii 200576.
NextBioi 89946.
PROi Q9Y2I7.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Y2I7.
Bgeei Q9Y2I7.
CleanExi HS_PIP5K3.
Genevestigatori Q9Y2I7.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
3.30.260.10. 2 hits.
3.30.40.10. 1 hit.
3.30.800.10. 1 hit.
3.30.810.10. 2 hits.
3.50.7.10. 1 hit.
InterProi IPR002423. Cpn60/TCP-1.
IPR000591. DEP_dom.
IPR027409. GroEL-like_apical_dom.
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.
IPR027410. TCP-1-like_intermed.
IPR011991. WHTH_DNA-bd_dom.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view ]
PANTHERi PTHR11353. PTHR11353. 1 hit.
Pfami PF00118. Cpn60_TCP1. 1 hit.
PF00610. DEP. 1 hit.
PF01363. FYVE. 1 hit.
PF01504. PIP5K. 1 hit.
[Graphical view ]
SMARTi SM00049. DEP. 1 hit.
SM00064. FYVE. 1 hit.
SM00330. PIPKc. 1 hit.
[Graphical view ]
SUPFAMi SSF52029. SSF52029. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEi PS50186. DEP. 1 hit.
PS51455. PIPK. 1 hit.
PS50178. ZF_FYVE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human PIKfyve, a PI3P 5-kinase that regulates endocytic trafficking."
    Cabezas A., Pattni K., Stenmark H.
    Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ASN-696; SER-932; LEU-995; SER-998 AND LYS-1183.
    Tissue: Brain.
  2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS ASN-696; SER-932; LEU-995; SER-998 AND LYS-1183.
  4. "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] (ISOFORMS 2; 3 AND 4).
    Tissue: Brain.
  5. "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] OF 1037-2098 (ISOFORM 1), VARIANT LYS-1183.
    Tissue: Brain.
  6. "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1521-2098 (ISOFORM 1).
    Tissue: Brain.
  7. "Phosphatidylinositol 3-phosphate-interacting domains in PIKfyve. Binding specificity and role in PIKfyve endomembrane localization."
    Sbrissa D., Ikonomov O.C., Shisheva A.
    J. Biol. Chem. 277:6073-6079(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
    Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
    Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Core protein machinery for mammalian phosphatidylinositol 3,5-bisphosphate synthesis and turnover that regulates the progression of endosomal transport. Novel Sac phosphatase joins the ArPIKfyve-PIKfyve complex."
    Sbrissa D., Ikonomov O.C., Fu Z., Ijuin T., Gruenberg J., Takenawa T., Shisheva A.
    J. Biol. Chem. 282:23878-23891(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE PI(3,5)P2 REGULATORY COMPLEX.
  11. "ArPIKfyve homomeric and heteromeric interactions scaffold PIKfyve and Sac3 in a complex to promote PIKfyve activity and functionality."
    Sbrissa D., Ikonomov O.C., Fenner H., Shisheva A.
    J. Mol. Biol. 384:766-779(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE PI(3,5)P2 REGULATORY COMPLEX.
  12. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299 AND SER-1544, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299; SER-1544; SER-1549 AND SER-1754, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  15. "Regulation of PIKfyve phosphorylation by insulin and osmotic stress."
    Hill E.V., Hudson C.A., Vertommen D., Rider M.H., Tavare J.M.
    Biochem. Biophys. Res. Commun. 397:650-655(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-318.
  16. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Mutations in PIP5K3 are associated with Francois-Neetens mouchetee fleck corneal dystrophy."
    Li S., Tiab L., Jiao X., Munier F.L., Zografos L., Frueh B.E., Sergeev Y., Smith J., Rubin B., Meallet M.A., Forster R.K., Hejtmancik J.F., Schorderet D.F.
    Am. J. Hum. Genet. 77:54-63(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CFD ARG-1103.

Entry informationi

Entry nameiFYV1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2I7
Secondary accession number(s): Q08AR7
, Q08AR8, Q53ST3, Q53T36, Q8N5H0, Q8NB67
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 13, 2010
Last modified: September 3, 2014
This is version 141 of the entry and version 3 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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