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Q9Y2I7

- FYV1_HUMAN

UniProt

Q9Y2I7 - FYV1_HUMAN

Protein

1-phosphatidylinositol 3-phosphate 5-kinase

Gene

PIKFYVE

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 3 (13 Jul 2010)
      Previous versions | rss
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    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-typePROSITE-ProRule annotationAdd
    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-3-phosphate biosynthetic process Source: GOC
    5. phosphatidylinositol biosynthetic process Source: Reactome
    6. phosphatidylinositol phosphorylation 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

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

    GO - Cellular componenti

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

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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 – 11Removed2 Publications
    Chaini2 – 209820971-phosphatidylinositol 3-phosphate 5-kinasePRO_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.4 Publications

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini365 – 44076DEPPROSITE-ProRule annotationAdd
    BLAST
    Domaini1758 – 2084327PIPKPROSITE-ProRule annotationAdd
    BLAST

    Region

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

    Sequence similaritiesi

    Contains 1 DEP domain.PROSITE-ProRule annotation
    Contains 1 FYVE-type zinc finger.PROSITE-ProRule annotation
    Contains 1 PIPK domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri158 – 21861FYVE-typePROSITE-ProRule annotationAdd
    BLAST

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1335 – 13351M → I in BAC03674. (PubMed:14702039)Curated
    Sequence conflicti2019 – 20191L → S in BAC03674. (PubMed:14702039)Curated

    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. 1 PublicationVSP_040108Add
    BLAST
    Alternative sequencei109 – 20395TRRKA…KFMGY → NSLQHPQEN in isoform 3. 1 PublicationVSP_040109Add
    BLAST
    Alternative sequencei546 – 5483EYL → GRR in isoform 2, isoform 3 and isoform 4. 1 PublicationVSP_040110
    Alternative sequencei549 – 20981550Missing in isoform 2, isoform 3 and isoform 4. 1 PublicationVSP_040111Add
    BLAST

    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

    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: October 1, 2014
    This is version 142 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