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Q9Z1T6

- FYV1_MOUSE

UniProt

Q9Z1T6 - FYV1_MOUSE

Protein

1-phosphatidylinositol 3-phosphate 5-kinase

Gene

Pikfyve

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      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. The product of the reaction it catalyzes functions as an important regulator of vacuole homeostasis perhaps by controlling membrane flux to and/or from the vacuole.1 Publication

    Catalytic activityi

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

    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: Reactome
    2. 1-phosphatidylinositol-4-phosphate 5-kinase activity Source: UniProtKB
    3. 1-phosphatidylinositol-5-kinase activity Source: Reactome
    4. ATP binding Source: UniProtKB-KW
    5. protein binding Source: UniProtKB
    6. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. cellular protein metabolic process Source: InterPro
    2. intracellular signal transduction Source: UniProtKB
    3. myelin assembly Source: MGI
    4. phosphatidylinositol phosphorylation Source: GOC

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    ReactomeiREACT_198970. Synthesis of PIPs at the Golgi membrane.
    REACT_198972. Synthesis of PIPs at the late endosome membrane.
    REACT_198975. Synthesis of PIPs at the early 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
    p235
    Gene namesi
    Name:Pikfyve
    Synonyms:Kiaa0981, Pip5k3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:1335106. Pikfyve.

    Subcellular locationi

    Cytoplasmic vesicle membrane 1 Publication; Peripheral membrane protein 1 Publication. Endosome membrane By similarity
    Note: Associated with vesicle structures. Displays a peripheral vesicular punctate pattern. Mainly associated with membranes of the late endocytic pathway By similarity.By similarity

    GO - Cellular componenti

    1. cell-cell junction Source: MGI
    2. cytoplasmic vesicle Source: MGI
    3. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
    4. cytosol Source: MGI
    5. early endosome membrane Source: Reactome
    6. Golgi membrane Source: Reactome
    7. late endosome membrane Source: Reactome
    8. perinuclear region of cytoplasm Source: MGI
    9. vesicle membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasmic vesicle, Endosome, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 209720961-phosphatidylinositol 3-phosphate 5-kinasePRO_0000185453Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei299 – 2991PhosphoserineBy similarity
    Modified residuei318 – 3181Phosphoserine; by PKB/AKT1 or PKB/AKT2By similarity
    Modified residuei329 – 3291PhosphoserineBy similarity
    Modified residuei1543 – 15431PhosphoserineBy similarity
    Modified residuei1548 – 15481PhosphoserineBy similarity
    Modified residuei1753 – 17531PhosphoserineBy similarity

    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

    PaxDbiQ9Z1T6.
    PRIDEiQ9Z1T6.

    2D gel databases

    SWISS-2DPAGEQ9Z1T6.

    PTM databases

    PhosphoSiteiQ9Z1T6.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    BgeeiQ9Z1T6.
    GenevestigatoriQ9Z1T6.

    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.1 Publication

    Protein-protein interaction databases

    BioGridi202165. 2 interactions.
    IntActiQ9Z1T6. 1 interaction.
    STRINGi10090.ENSMUSP00000109676.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini365 – 44076DEPPROSITE-ProRule annotationAdd
    BLAST
    Domaini1757 – 2083327PIPKPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1841 – 2097257CatalyticBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1222 – 12254Poly-Ser

    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.
    GeneTreeiENSGT00750000117278.
    HOGENOMiHOG000059273.
    HOVERGENiHBG005775.
    KOiK00921.
    OMAiWTEKMQA.
    OrthoDBiEOG757CWH.
    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 (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Z1T6-2) [UniParc]FASTAAdd to Basket

    Also known as: p235S

    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

    MATDDKSSPT LDSANDLPRS PASPSHLTHF KPLTPDQDEP PFKSAYSSFV     50
    NLFRFNKERG EGGQGEQQSP SSSWASPQIP SRTQSVRSPV PYKKQLNEEL 100
    HRRSSVLDSR RKAEPACGGH DPRTAVQLRS LSTVLKRLKE IMEGKSQDSD 150
    LKQYWMPDSQ CKECYDCSEK FTTFRRRHHC RLCGQIFCSR CCNQEIPGKF 200
    MGYTGDLRAC TYCRKIALSY AHSTDSNSIG EDLNALSDST CSVSILDPSE 250
    PRTPVGSRKA SRNIFLEDDL AWQSLIHPDS SNSALSTRLV SVQEDAGKSP 300
    ARNRSASITN LSLDRSGSPM VPSYETSVSP QANRNYIRTE TTEDERKILL 350
    DSAQLKDLWK KICHHTSGME FQDHRYWLRT HPNCIVGKEL VNWLIRNGHI 400
    ATRAQAIAIG QAMVDGRWLD CVSHHDQLFR DEYALYRPLQ STEFSETPSP 450
    DSDSVNSVEG HSEPSWFKDI KFDDSDTEQI AEEGDDNLAN SASPSKRTSV 500
    SSFQSTVDSD SAASISLNVE LDNVNFHIKK PSKYPHVPPH PADQKEYLVS 550
    DTGGQQLSIS DAFIKESLFN RRVEEKSKEL PFTPLGWHHN NLELLREENE 600
    EKQAMERLLS ANHNHMMALL QQLLQNESLS SSWRDIIVSL VCQVVQTVRP 650
    DVKHQDDDMD IRQFVHIKKI PGGKKFDSVV VNGFVCTKNI AHKKMNSCIK 700
    NPKILLLKCS IEYLYREETK FTCIDPIVLQ EREFLKNYVQ RIVDVRPTLV 750
    LVEKTVSRIA QDMLLEHGIT LVINVKSQVL ERISRMTQGD LVVSMDQLLT 800
    KPHLGTCHKF YMQIFQLPNE QTKTLMFFEG CPQHLGCTIK LRGGSDYELA 850
    RVKEILIFMI CVAYHSQLEI SFLMDEFAMP PTLMQSPSFH LLTEGRGEEG 900
    ASQEQVSGSS LPQDPECPRE ALSSEDSTLL ESRTVLEKGE LDNKSIPQAV 950
    ASLKHQDYTT PTCPAGIPCA LFALVPESLL PLHMDQQDAV GNEQPETSQQ 1000
    TDEQQDPKSQ MKAFRDPLQD DTGMYVTEEV TSSEDQRKTY ALTFKQELKD 1050
    VILCISPVIT FREPFLLTEK GMRCSTRDYF PEQIYWSPLL NKEVKEMESR 1100
    RKKQLLRDLS GLQGMNGSVQ AKSIQVLPSH ELVSTRIAEH LGDSQTLGRM 1150
    LADYRARGGR IQSKHLDPFV HSKDASCTSG GKSGNKTESD EERGLIPSDV 1200
    IWPTKVDCLN PANHQRLCVL FSSSSAQSSN APSACVSPWI VTMEFYGKND 1250
    LTLGIFLERY CFRSSYQCPS MFCDTPMVHH IRRFVHGQGC VQIILKELDS 1300
    PVPGYQHTIL TYSWCRICKQ VTPVVALSNE SWSMSFAKYL ELRFYGHQYT 1350
    RRANAEPCGH SIHHDYHQYF SYNQMVASFS YSPIRLLEVC VPLPKIFIKR 1400
    QAPLKVSLLQ DLKDFFQKVS QVYLAVDERL ASLKTDTFSK TREEKMEDIF 1450
    AQKEMEEGEF KNWTEKMQAR LMSSSVDTPQ QLQSIFESLI AKKQSLCEVL 1500
    QAWNSRLQDL FQQEKGRKRP SVPPSPGRLR QGEESKINAM DTSPRNISPG 1550
    LHNGEKEDRF LTTLSSQSST SSTHLQLPTP PEALAEQVVG GPTDLDSASG 1600
    SEDVFDGHLL GSTDSQVKEK STMKAIFANL LPGNSYNPIP FPFDPDKHYL 1650
    MYEHERVPIA VCEKEPSSII AFALSCKEYR NALEELSKAT LRNSAEEGLP 1700
    ANSALDNRPK SSSPIRLPEI SGGQTNRTVE AEPQPTKKAS GMLSFFRGTA 1750
    GKSPDLSSQK RETLRGADSA YYQVGQAGKE GLESQGLEPQ DEVDGGDTQK 1800
    KQLTNPHVEL QFSDANAKFY CRLYYAGEFH KMREVILGSS EEEFIRSLSH 1850
    SSPWQARGGK SGAAFYATED DRFILKQMPR LEVQSFLDFA PHYFNYITNA 1900
    VQQKRPTALA KILGVYRIGY KNSQNNTEKK LDLLVMENLF YGRKMAQVFD 1950
    LKGSLRNRNV KTDTGKESCD VVLLDENLLK MVRDNPLYIR SHSKSVLRTS 2000
    IHSDAHFLSS HLIIDYSLLV GRDDTSNELV VGIIDYIRTF TWDKKLEMVV 2050
    KSTGILGGQG KMPTVVSPEL YRTRFCEAMD KYFLMVPDHW TGLDLNC 2097
    Length:2,097
    Mass (Da):236,877
    Last modified:July 27, 2011 - v3
    Checksum:i8C529E86FBEED8E6
    GO
    Isoform 2 (identifier: Q9Z1T6-1) [UniParc]FASTAAdd to Basket

    Also known as: p235L

    The sequence of this isoform differs from the canonical sequence as follows:
         107-107: L → LENTLPHPQEST
         490-545: Missing.

    Show »
    Length:2,052
    Mass (Da):232,081
    Checksum:iC7FA5897A3319DA0
    GO
    Isoform 3 (identifier: Q9Z1T6-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         490-497: NSASPSKR → SKFGFLML
         498-2097: Missing.

    Show »
    Length:497
    Mass (Da):55,999
    Checksum:i5BB1E9BE48047A7A
    GO

    Sequence cautioni

    The sequence AAD10191.1 differs from that shown. Reason: Frameshift at several positions.
    The sequence BAB30626.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAD32355.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti546 – 5461E → K in AAD10191. (PubMed:9858586)Curated
    Sequence conflicti944 – 9441K → Q in BAD32355. (PubMed:15368895)Curated
    Sequence conflicti994 – 9952QP → HR in AAD10191. (PubMed:9858586)Curated
    Sequence conflicti1107 – 11071R → T in BAB30626. (PubMed:16141072)Curated
    Sequence conflicti1141 – 11411L → V in AAD10191. (PubMed:9858586)Curated
    Sequence conflicti1264 – 12641S → Y in AAD10191. (PubMed:9858586)Curated
    Sequence conflicti1996 – 19961V → E in AAD10191. (PubMed:9858586)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei107 – 1071L → LENTLPHPQEST in isoform 2. 1 PublicationVSP_034953
    Alternative sequencei490 – 54556Missing in isoform 2. 1 PublicationVSP_034954Add
    BLAST
    Alternative sequencei490 – 4978NSASPSKR → SKFGFLML in isoform 3. 1 PublicationVSP_034955
    Alternative sequencei498 – 20971600Missing in isoform 3. 1 PublicationVSP_034956Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF102777 mRNA. Translation: AAD10191.1. Frameshift.
    AK173077 mRNA. Translation: BAD32355.1. Different initiation.
    AK017186 mRNA. Translation: BAB30626.3. Different initiation.
    AK139116 mRNA. Translation: BAE23894.1.
    AK165350 mRNA. Translation: BAE38145.1.
    AC164079 Genomic DNA. No translation available.
    CCDSiCCDS35601.1. [Q9Z1T6-1]
    PIRiT18290.
    RefSeqiNP_035216.2. NM_011086.2.
    XP_006495843.1. XM_006495780.1. [Q9Z1T6-2]
    XP_006495844.1. XM_006495781.1. [Q9Z1T6-2]
    UniGeneiMm.38370.

    Genome annotation databases

    EnsembliENSMUST00000097707; ENSMUSP00000095314; ENSMUSG00000025949. [Q9Z1T6-2]
    GeneIDi18711.
    KEGGimmu:18711.
    UCSCiuc007bho.1. mouse. [Q9Z1T6-3]
    uc007bht.1. mouse. [Q9Z1T6-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF102777 mRNA. Translation: AAD10191.1 . Frameshift.
    AK173077 mRNA. Translation: BAD32355.1 . Different initiation.
    AK017186 mRNA. Translation: BAB30626.3 . Different initiation.
    AK139116 mRNA. Translation: BAE23894.1 .
    AK165350 mRNA. Translation: BAE38145.1 .
    AC164079 Genomic DNA. No translation available.
    CCDSi CCDS35601.1. [Q9Z1T6-1 ]
    PIRi T18290.
    RefSeqi NP_035216.2. NM_011086.2.
    XP_006495843.1. XM_006495780.1. [Q9Z1T6-2 ]
    XP_006495844.1. XM_006495781.1. [Q9Z1T6-2 ]
    UniGenei Mm.38370.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202165. 2 interactions.
    IntActi Q9Z1T6. 1 interaction.
    STRINGi 10090.ENSMUSP00000109676.

    Chemistry

    ChEMBLi CHEMBL2176842.

    PTM databases

    PhosphoSitei Q9Z1T6.

    2D gel databases

    SWISS-2DPAGE Q9Z1T6.

    Proteomic databases

    PaxDbi Q9Z1T6.
    PRIDEi Q9Z1T6.

    Protocols and materials databases

    DNASUi 18711.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000097707 ; ENSMUSP00000095314 ; ENSMUSG00000025949 . [Q9Z1T6-2 ]
    GeneIDi 18711.
    KEGGi mmu:18711.
    UCSCi uc007bho.1. mouse. [Q9Z1T6-3 ]
    uc007bht.1. mouse. [Q9Z1T6-2 ]

    Organism-specific databases

    CTDi 200576.
    MGIi MGI:1335106. Pikfyve.
    Rougei Search...

    Phylogenomic databases

    eggNOGi COG0459.
    GeneTreei ENSGT00750000117278.
    HOGENOMi HOG000059273.
    HOVERGENi HBG005775.
    KOi K00921.
    OMAi WTEKMQA.
    OrthoDBi EOG757CWH.
    TreeFami TF321717.

    Enzyme and pathway databases

    Reactomei REACT_198970. Synthesis of PIPs at the Golgi membrane.
    REACT_198972. Synthesis of PIPs at the late endosome membrane.
    REACT_198975. Synthesis of PIPs at the early endosome membrane.

    Miscellaneous databases

    NextBioi 294793.
    PROi Q9Z1T6.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9Z1T6.
    Genevestigatori Q9Z1T6.

    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. "Cloning, characterization, and expression of a novel Zn2+-binding FYVE finger-containing phosphoinositide kinase in insulin-sensitive cells."
      Shisheva A., Sbrissa D., Ikonomov O.
      Mol. Cell. Biol. 19:623-634(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), CHARACTERIZATION.
      Tissue: Adipose tissue.
    2. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
      DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Pancreatic islet.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Strain: C57BL/6J.
      Tissue: Cerebellum, Ovary, Spleen and Uterus.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    5. "Complementation analysis in PtdInsP kinase-deficient yeast mutants demonstrates that Schizosaccharomyces pombe and murine Fab1p homologues are phosphatidylinositol 3-phosphate 5-kinases."
      McEwen R.K., Dove S.K., Cooke F.T., Painter G.F., Holmes A.B., Shisheva A., Ohya Y., Parker P.J., Michell R.H.
      J. Biol. Chem. 274:33905-33912(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    7. "Loss of Vac14, a regulator of the signaling lipid phosphatidylinositol 3,5-bisphosphate, results in neurodegeneration in mice."
      Zhang Y., Zolov S.N., Chow C.Y., Slutsky S.G., Richardson S.C., Piper R.C., Yang B., Nau J.J., Westrick R.J., Morrison S.J., Meisler M.H., Weisman L.S.
      Proc. Natl. Acad. Sci. U.S.A. 104:17518-17523(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    8. "VAC14 nucleates a protein complex essential for the acute interconversion of PI3P and PI(3,5)P(2) in yeast and mouse."
      Jin N., Chow C.Y., Liu L., Zolov S.N., Bronson R., Davisson M., Petersen J.L., Zhang Y., Park S., Duex J.E., Goldowitz D., Meisler M.H., Weisman L.S.
      EMBO J. 27:3221-3234(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE PI(3,5)P2 REGULATORY COMPLEX, FUNCTION, SUBCELLULAR LOCATION.
    9. "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.

    Entry informationi

    Entry nameiFYV1_MOUSE
    AccessioniPrimary (citable) accession number: Q9Z1T6
    Secondary accession number(s): E9QL40
    , Q3TNE4, Q3UTT6, Q69ZU1, Q9CU94
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 133 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3