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Q9Z1T6

- FYV1_MOUSE

UniProt

Q9Z1T6 - FYV1_MOUSE

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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

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. 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
  5. protein localization to nucleus Source: Ensembl
  6. retrograde transport, endosome to Golgi Source: Ensembl
Complete GO annotation...

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. cytosol Source: MGI
  4. early endosome membrane Source: Reactome
  5. Golgi membrane Source: Reactome
  6. late endosome membrane Source: Reactome
  7. membrane raft Source: Ensembl
  8. perinuclear region of cytoplasm Source: MGI
  9. vesicle membrane Source: UniProtKB
Complete GO annotation...

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

MaxQBiQ9Z1T6.
PaxDbiQ9Z1T6.
PRIDEiQ9Z1T6.

2D gel databases

SWISS-2DPAGEQ9Z1T6.

PTM databases

PhosphoSiteiQ9Z1T6.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ9Z1T6.
ExpressionAtlasiQ9Z1T6. baseline and differential.
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.
GeneTreeiENSGT00770000120535.
HOGENOMiHOG000059273.
HOVERGENiHBG005775.
InParanoidiQ9Z1T6.
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

        10         20         30         40         50
MATDDKSSPT LDSANDLPRS PASPSHLTHF KPLTPDQDEP PFKSAYSSFV
60 70 80 90 100
NLFRFNKERG EGGQGEQQSP SSSWASPQIP SRTQSVRSPV PYKKQLNEEL
110 120 130 140 150
HRRSSVLDSR RKAEPACGGH DPRTAVQLRS LSTVLKRLKE IMEGKSQDSD
160 170 180 190 200
LKQYWMPDSQ CKECYDCSEK FTTFRRRHHC RLCGQIFCSR CCNQEIPGKF
210 220 230 240 250
MGYTGDLRAC TYCRKIALSY AHSTDSNSIG EDLNALSDST CSVSILDPSE
260 270 280 290 300
PRTPVGSRKA SRNIFLEDDL AWQSLIHPDS SNSALSTRLV SVQEDAGKSP
310 320 330 340 350
ARNRSASITN LSLDRSGSPM VPSYETSVSP QANRNYIRTE TTEDERKILL
360 370 380 390 400
DSAQLKDLWK KICHHTSGME FQDHRYWLRT HPNCIVGKEL VNWLIRNGHI
410 420 430 440 450
ATRAQAIAIG QAMVDGRWLD CVSHHDQLFR DEYALYRPLQ STEFSETPSP
460 470 480 490 500
DSDSVNSVEG HSEPSWFKDI KFDDSDTEQI AEEGDDNLAN SASPSKRTSV
510 520 530 540 550
SSFQSTVDSD SAASISLNVE LDNVNFHIKK PSKYPHVPPH PADQKEYLVS
560 570 580 590 600
DTGGQQLSIS DAFIKESLFN RRVEEKSKEL PFTPLGWHHN NLELLREENE
610 620 630 640 650
EKQAMERLLS ANHNHMMALL QQLLQNESLS SSWRDIIVSL VCQVVQTVRP
660 670 680 690 700
DVKHQDDDMD IRQFVHIKKI PGGKKFDSVV VNGFVCTKNI AHKKMNSCIK
710 720 730 740 750
NPKILLLKCS IEYLYREETK FTCIDPIVLQ EREFLKNYVQ RIVDVRPTLV
760 770 780 790 800
LVEKTVSRIA QDMLLEHGIT LVINVKSQVL ERISRMTQGD LVVSMDQLLT
810 820 830 840 850
KPHLGTCHKF YMQIFQLPNE QTKTLMFFEG CPQHLGCTIK LRGGSDYELA
860 870 880 890 900
RVKEILIFMI CVAYHSQLEI SFLMDEFAMP PTLMQSPSFH LLTEGRGEEG
910 920 930 940 950
ASQEQVSGSS LPQDPECPRE ALSSEDSTLL ESRTVLEKGE LDNKSIPQAV
960 970 980 990 1000
ASLKHQDYTT PTCPAGIPCA LFALVPESLL PLHMDQQDAV GNEQPETSQQ
1010 1020 1030 1040 1050
TDEQQDPKSQ MKAFRDPLQD DTGMYVTEEV TSSEDQRKTY ALTFKQELKD
1060 1070 1080 1090 1100
VILCISPVIT FREPFLLTEK GMRCSTRDYF PEQIYWSPLL NKEVKEMESR
1110 1120 1130 1140 1150
RKKQLLRDLS GLQGMNGSVQ AKSIQVLPSH ELVSTRIAEH LGDSQTLGRM
1160 1170 1180 1190 1200
LADYRARGGR IQSKHLDPFV HSKDASCTSG GKSGNKTESD EERGLIPSDV
1210 1220 1230 1240 1250
IWPTKVDCLN PANHQRLCVL FSSSSAQSSN APSACVSPWI VTMEFYGKND
1260 1270 1280 1290 1300
LTLGIFLERY CFRSSYQCPS MFCDTPMVHH IRRFVHGQGC VQIILKELDS
1310 1320 1330 1340 1350
PVPGYQHTIL TYSWCRICKQ VTPVVALSNE SWSMSFAKYL ELRFYGHQYT
1360 1370 1380 1390 1400
RRANAEPCGH SIHHDYHQYF SYNQMVASFS YSPIRLLEVC VPLPKIFIKR
1410 1420 1430 1440 1450
QAPLKVSLLQ DLKDFFQKVS QVYLAVDERL ASLKTDTFSK TREEKMEDIF
1460 1470 1480 1490 1500
AQKEMEEGEF KNWTEKMQAR LMSSSVDTPQ QLQSIFESLI AKKQSLCEVL
1510 1520 1530 1540 1550
QAWNSRLQDL FQQEKGRKRP SVPPSPGRLR QGEESKINAM DTSPRNISPG
1560 1570 1580 1590 1600
LHNGEKEDRF LTTLSSQSST SSTHLQLPTP PEALAEQVVG GPTDLDSASG
1610 1620 1630 1640 1650
SEDVFDGHLL GSTDSQVKEK STMKAIFANL LPGNSYNPIP FPFDPDKHYL
1660 1670 1680 1690 1700
MYEHERVPIA VCEKEPSSII AFALSCKEYR NALEELSKAT LRNSAEEGLP
1710 1720 1730 1740 1750
ANSALDNRPK SSSPIRLPEI SGGQTNRTVE AEPQPTKKAS GMLSFFRGTA
1760 1770 1780 1790 1800
GKSPDLSSQK RETLRGADSA YYQVGQAGKE GLESQGLEPQ DEVDGGDTQK
1810 1820 1830 1840 1850
KQLTNPHVEL QFSDANAKFY CRLYYAGEFH KMREVILGSS EEEFIRSLSH
1860 1870 1880 1890 1900
SSPWQARGGK SGAAFYATED DRFILKQMPR LEVQSFLDFA PHYFNYITNA
1910 1920 1930 1940 1950
VQQKRPTALA KILGVYRIGY KNSQNNTEKK LDLLVMENLF YGRKMAQVFD
1960 1970 1980 1990 2000
LKGSLRNRNV KTDTGKESCD VVLLDENLLK MVRDNPLYIR SHSKSVLRTS
2010 2020 2030 2040 2050
IHSDAHFLSS HLIIDYSLLV GRDDTSNELV VGIIDYIRTF TWDKKLEMVV
2060 2070 2080 2090
KSTGILGGQG KMPTVVSPEL YRTRFCEAMD KYFLMVPDHW TGLDLNC
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. Curated
The sequence BAB30626.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAD32355.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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

MaxQBi Q9Z1T6.
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 ENSGT00770000120535.
HOGENOMi HOG000059273.
HOVERGENi HBG005775.
InParanoidi Q9Z1T6.
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

ChiTaRSi Pikfyve. mouse.
NextBioi 294793.
PROi Q9Z1T6.
SOURCEi Search...

Gene expression databases

Bgeei Q9Z1T6.
ExpressionAtlasi Q9Z1T6. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 135 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