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Q9Y2I7

- FYV1_HUMAN

UniProt

Q9Y2I7 - FYV1_HUMAN

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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

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. phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity Source: Reactome
  5. zinc ion binding Source: Ensembl

GO - Biological processi

  1. cellular protein metabolic process Source: InterPro
  2. intracellular signal transduction Source: Ensembl
  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
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 2 Publications
Note: Mainly associated with membranes of the late endocytic pathway.

GO - Cellular componenti

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

BgeeiQ9Y2I7.
CleanExiHS_PIP5K3.
ExpressionAtlasiQ9Y2I7. baseline and differential.
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. 11 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.
GeneTreeiENSGT00750000117278.
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

        10         20         30         40         50
MATDDKTSPT LDSANDLPRS PTSPSHLTHF KPLTPDQDEP PFKSAYSSFV
60 70 80 90 100
NLFRFNKERA EGGQGEQQPL SGSWTSPQLP SRTQSVRSPT PYKKQLNEEL
110 120 130 140 150
QRRSSALDTR RKAEPTFGGH DPRTAVQLRS LSTVLKRLKE IMEGKSQDSD
160 170 180 190 200
LKQYWMPDSQ CKECYDCSEK FTTFRRRHHC RLCGQIFCSR CCNQEIPGKF
210 220 230 240 250
MGYTGDLRAC TYCRKIALSY AHSTDSNSIG EDLNALSDSA CSVSVLDPSE
260 270 280 290 300
PRTPVGSRKA SRNIFLEDDL AWQSLIHPDS SNTPLSTRLV SVQEDAGKSP
310 320 330 340 350
ARNRSASITN LSLDRSGSPM VPSYETSVSP QANRTYVRTE TTEDERKILL
360 370 380 390 400
DSVQLKDLWK KICHHSSGME 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 PADQKEYLIS
560 570 580 590 600
DTGGQQLSIS DAFIKESLFN RRVEEKSKEL PFTPLGWHHN NLELLREENG
610 620 630 640 650
EKQAMERLLS ANHNHMMALL QQLLHSDSLS SSWRDIIVSL VCQVVQTVRP
660 670 680 690 700
DVKNQDDDMD IRQFVHIKKI PGGKKFDSVV VNGFVCTKNI AHKKMSSCIK
710 720 730 740 750
NPKILLLKCS IEYLYREETK FTCIDPIVLQ EREFLKNYVQ RIVDVRPTLV
760 770 780 790 800
LVEKTVSRIA QDMLLEHGIT LVINVKSQVL ERISRMTQGD LVMSMDQLLT
810 820 830 840 850
KPHLGTCHKF YMQIFQLPNE QTKTLMFFEG CPQHLGCTIK LRGGSDYELA
860 870 880 890 900
RVKEILIFMI CVAYHSQLEI SFLMDEFAMP PTLMQNPSFH SLIEGRGHEG
910 920 930 940 950
AVQEQYGGGS IPWDPDIPPE SLPCDDSSLL ELRIVFEKGE QENKNLPQAV
960 970 980 990 1000
ASVKHQEHST TACPAGLPCA FFAPVPESLL PLPVDDQQDA LGSEQPETLQ
1010 1020 1030 1040 1050
QTVVLQDPKS QIRAFRDPLQ DDTGLYVTEE VTSSEDKRKT YSLAFKQELK
1060 1070 1080 1090 1100
DVILCISPVI TFREPFLLTE KGMRCSTRDY FAEQVYWSPL LNKEFKEMEN
1110 1120 1130 1140 1150
RRKKQLLRDL SGLQGMNGSI QAKSIQVLPS HELVSTRIAE HLGDSQSLGR
1160 1170 1180 1190 1200
MLADYRARGG RIQPKNSDPF AHSKDASSTS SGQSGSKNEG DEERGLILSD
1210 1220 1230 1240 1250
AVWSTKVDCL NPINHQRLCV LFSSSSAQSS NAPSACVSPW IVTMEFYGKN
1260 1270 1280 1290 1300
DLTLGIFLER YCFRPSYQCP SMFCDTPMVH HIRRFVHGQG CVQIILKELD
1310 1320 1330 1340 1350
SPVPGYQHTI LTYSWCRICK QVTPVVALSN ESWSMSFAKY LELRFYGHQY
1360 1370 1380 1390 1400
TRRANAEPCG HSIHHDYHQY FSYNQMVASF SYSPIRLLEV CVPLPKIFIK
1410 1420 1430 1440 1450
RQAPLKVSLL QDLKDFFQKV SQVYVAIDER LASLKTDTFS KTREEKMEDI
1460 1470 1480 1490 1500
FAQKEMEEGE FKNWIEKMQA RLMSSSVDTP QQLQSVFESL IAKKQSLCEV
1510 1520 1530 1540 1550
LQAWNNRLQD LFQQEKGRKR PSVPPSPGRL RQGEESKISA MDASPRNISP
1560 1570 1580 1590 1600
GLQNGEKEDR FLTTLSSQSS TSSTHLQLPT PPEVMSEQSV GGPPELDTAS
1610 1620 1630 1640 1650
SSEDVFDGHL LGSTDSQVKE KSTMKAIFAN LLPGNSYNPI PFPFDPDKHY
1660 1670 1680 1690 1700
LMYEHERVPI AVCEKEPSSI IAFALSCKEY RNALEELSKA TQWNSAEEGL
1710 1720 1730 1740 1750
PTNSTSDSRP KSSSPIRLPE MSGGQTNRTT ETEPQPTKKA SGMLSFFRGT
1760 1770 1780 1790 1800
AGKSPDLSSQ KRETLRGADS AYYQVGQTGK EGTENQGVEP QDEVDGGDTQ
1810 1820 1830 1840 1850
KKQLINPHVE LQFSDANAKF YCRLYYAGEF HKMREVILDS SEEDFIRSLS
1860 1870 1880 1890 1900
HSSPWQARGG KSGAAFYATE DDRFILKQMP RLEVQSFLDF APHYFNYITN
1910 1920 1930 1940 1950
AVQQKRPTAL AKILGVYRIG YKNSQNNTEK KLDLLVMENL FYGRKMAQVF
1960 1970 1980 1990 2000
DLKGSLRNRN VKTDTGKESC DVVLLDENLL KMVRDNPLYI RSHSKAVLRT
2010 2020 2030 2040 2050
SIHSDSHFLS SHLIIDYSLL VGRDDTSNEL VVGIIDYIRT FTWDKKLEMV
2060 2070 2080 2090
VKSTGILGGQ GKMPTVVSPE LYRTRFCEAM DKYFLMVPDH WTGLGLNC
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. 11 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.
GeneTreei ENSGT00750000117278.
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

Bgeei Q9Y2I7.
CleanExi HS_PIP5K3.
ExpressionAtlasi Q9Y2I7. baseline and differential.
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: October 29, 2014
This is version 143 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