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Q9Y2I7 (FYV1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
1-phosphatidylinositol 3-phosphate 5-kinase

Short name=Phosphatidylinositol 3-phosphate 5-kinase
EC=2.7.1.150
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 names
Name:PIKFYVE
Synonyms:KIAA0981, PIP5K3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2098 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10

Catalytic activity

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

Subunit structure

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. Ref.10 Ref.11

Subcellular location

Endosome membrane. Note: Mainly associated with membranes of the late endocytic pathway. Ref.7 Ref.10

Post-translational modification

Phosphorylated in response to insulin at Ser-318 in a protein kinase B (PKB)-dependent manner. Ref.15

Involvement in disease

Corneal dystrophy, fleck (CFD) [MIM:121850]: A form of stromal corneal dystrophy characterized by numerous small white flecks scattered in all levels of the stroma, with configurations varying from semicircular to wreath-like, curvilinear, or punctate. Although CFD may occasionally cause mild photophobia, patients are typically asymptomatic and have normal vision.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18

Sequence similarities

Contains 1 DEP domain.

Contains 1 FYVE-type zinc finger.

Contains 1 PIPK domain.

Sequence caution

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

Ontologies

Keywords
   Cellular componentEndosome
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCorneal dystrophy
Disease mutation
   DomainZinc-finger
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular protein metabolic process

Inferred from electronic annotation. Source: InterPro

intracellular signal transduction

Inferred from electronic annotation. Source: InterPro

myelin assembly

Inferred from electronic annotation. Source: Ensembl

phosphatidylinositol biosynthetic process

Traceable author statement. Source: Reactome

phosphatidylinositol phosphorylation

Traceable author statement PubMed 15046600. Source: GOC

phosphatidylinositol-3-phosphate biosynthetic process

Traceable author statement. Source: GOC

phospholipid metabolic process

Traceable author statement. Source: Reactome

protein localization to nucleus

Inferred from mutant phenotype PubMed 17909029. Source: UniProtKB

retrograde transport, endosome to Golgi

Inferred from mutant phenotype PubMed 14551253PubMed 16954148. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentGolgi membrane

Traceable author statement. Source: Reactome

cytoplasmic vesicle

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from electronic annotation. Source: Ensembl

early endosome membrane

Inferred from direct assay PubMed 16448788PubMed 16954148. Source: UniProtKB

endosome membrane

Inferred from direct assay Ref.10. Source: UniProtKB

late endosome membrane

Traceable author statement. Source: Reactome

membrane raft

Inferred from direct assay PubMed 15046600. Source: HGNC

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

   Molecular_function1-phosphatidylinositol-3-phosphate 5-kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

1-phosphatidylinositol-4-phosphate 5-kinase activity

Traceable author statement PubMed 15046600. Source: HGNC

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity

Traceable author statement. Source: Reactome

protein binding

Inferred from physical interaction Ref.10PubMed 17909029. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y2I7-1)

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.
Isoform 2 (identifier: Q9Y2I7-2)

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.
Isoform 3 (identifier: Q9Y2I7-3)

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.
Isoform 4 (identifier: Q9Y2I7-4)

The sequence of this isoform differs from the canonical sequence as follows:
     546-548: EYL → GRR
     549-2098: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.14
Chain2 – 209820971-phosphatidylinositol 3-phosphate 5-kinase
PRO_0000185452

Regions

Domain365 – 44076DEP
Domain1758 – 2084327PIPK
Zinc finger158 – 21861FYVE-type
Region1842 – 2098257Catalytic

Amino acid modifications

Modified residue21N-acetylalanine Ref.14 Ref.17
Modified residue2991Phosphoserine Ref.12 Ref.14
Modified residue3181Phosphoserine; by PKB/AKT1 or PKB/AKT2 Ref.15
Modified residue3291Phosphoserine Ref.13
Modified residue15441Phosphoserine Ref.12 Ref.14
Modified residue15491Phosphoserine Ref.14
Modified residue17541Phosphoserine Ref.14

Natural variations

Alternative sequence108 – 20497Missing in isoform 2.
VSP_040108
Alternative sequence109 – 20395TRRKA…KFMGY → NSLQHPQEN in isoform 3.
VSP_040109
Alternative sequence546 – 5483EYL → GRR in isoform 2, isoform 3 and isoform 4.
VSP_040110
Alternative sequence549 – 20981550Missing in isoform 2, isoform 3 and isoform 4.
VSP_040111
Natural variant6171M → V.
Corresponds to variant rs16840913 [ dbSNP | Ensembl ].
VAR_057097
Natural variant6961S → N. Ref.1 Ref.3
Corresponds to variant rs10932258 [ dbSNP | Ensembl ].
VAR_063406
Natural variant9321L → S. Ref.1 Ref.3
Corresponds to variant rs2363468 [ dbSNP | Ensembl ].
VAR_063407
Natural variant9951Q → L. Ref.1 Ref.3
Corresponds to variant rs893254 [ dbSNP | Ensembl ].
VAR_063408
Natural variant9981T → S. Ref.1 Ref.3
Corresponds to variant rs893253 [ dbSNP | Ensembl ].
VAR_063409
Natural variant10331S → A.
Corresponds to variant rs999890 [ dbSNP | Ensembl ].
VAR_057098
Natural variant11031K → R in CFD. Ref.18
VAR_025309
Natural variant11831Q → K. Ref.1 Ref.3 Ref.5
Corresponds to variant rs1529979 [ dbSNP | Ensembl ].
VAR_063410
Natural variant18581R → Q.
Corresponds to variant rs2289170 [ dbSNP | Ensembl ].
VAR_057099

Experimental info

Sequence conflict13351M → I in BAC03674. Ref.5
Sequence conflict20191L → S in BAC03674. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 13, 2010. Version 3.
Checksum: 390C43530D3B1E81

FASTA2,098237,136
        10         20         30         40         50         60 
MATDDKTSPT LDSANDLPRS PTSPSHLTHF KPLTPDQDEP PFKSAYSSFV NLFRFNKERA 

        70         80         90        100        110        120 
EGGQGEQQPL SGSWTSPQLP SRTQSVRSPT PYKKQLNEEL QRRSSALDTR RKAEPTFGGH 

       130        140        150        160        170        180 
DPRTAVQLRS LSTVLKRLKE IMEGKSQDSD LKQYWMPDSQ CKECYDCSEK FTTFRRRHHC 

       190        200        210        220        230        240 
RLCGQIFCSR CCNQEIPGKF MGYTGDLRAC TYCRKIALSY AHSTDSNSIG EDLNALSDSA 

       250        260        270        280        290        300 
CSVSVLDPSE PRTPVGSRKA SRNIFLEDDL AWQSLIHPDS SNTPLSTRLV SVQEDAGKSP 

       310        320        330        340        350        360 
ARNRSASITN LSLDRSGSPM VPSYETSVSP QANRTYVRTE TTEDERKILL DSVQLKDLWK 

       370        380        390        400        410        420 
KICHHSSGME FQDHRYWLRT HPNCIVGKEL VNWLIRNGHI ATRAQAIAIG QAMVDGRWLD 

       430        440        450        460        470        480 
CVSHHDQLFR DEYALYRPLQ STEFSETPSP DSDSVNSVEG HSEPSWFKDI KFDDSDTEQI 

       490        500        510        520        530        540 
AEEGDDNLAN SASPSKRTSV SSFQSTVDSD SAASISLNVE LDNVNFHIKK PSKYPHVPPH 

       550        560        570        580        590        600 
PADQKEYLIS DTGGQQLSIS DAFIKESLFN RRVEEKSKEL PFTPLGWHHN NLELLREENG 

       610        620        630        640        650        660 
EKQAMERLLS ANHNHMMALL QQLLHSDSLS SSWRDIIVSL VCQVVQTVRP DVKNQDDDMD 

       670        680        690        700        710        720 
IRQFVHIKKI PGGKKFDSVV VNGFVCTKNI AHKKMSSCIK NPKILLLKCS IEYLYREETK 

       730        740        750        760        770        780 
FTCIDPIVLQ EREFLKNYVQ RIVDVRPTLV LVEKTVSRIA QDMLLEHGIT LVINVKSQVL 

       790        800        810        820        830        840 
ERISRMTQGD LVMSMDQLLT KPHLGTCHKF YMQIFQLPNE QTKTLMFFEG CPQHLGCTIK 

       850        860        870        880        890        900 
LRGGSDYELA RVKEILIFMI CVAYHSQLEI SFLMDEFAMP PTLMQNPSFH SLIEGRGHEG 

       910        920        930        940        950        960 
AVQEQYGGGS IPWDPDIPPE SLPCDDSSLL ELRIVFEKGE QENKNLPQAV ASVKHQEHST 

       970        980        990       1000       1010       1020 
TACPAGLPCA FFAPVPESLL PLPVDDQQDA LGSEQPETLQ QTVVLQDPKS QIRAFRDPLQ 

      1030       1040       1050       1060       1070       1080 
DDTGLYVTEE VTSSEDKRKT YSLAFKQELK DVILCISPVI TFREPFLLTE KGMRCSTRDY 

      1090       1100       1110       1120       1130       1140 
FAEQVYWSPL LNKEFKEMEN RRKKQLLRDL SGLQGMNGSI QAKSIQVLPS HELVSTRIAE 

      1150       1160       1170       1180       1190       1200 
HLGDSQSLGR MLADYRARGG RIQPKNSDPF AHSKDASSTS SGQSGSKNEG DEERGLILSD 

      1210       1220       1230       1240       1250       1260 
AVWSTKVDCL NPINHQRLCV LFSSSSAQSS NAPSACVSPW IVTMEFYGKN DLTLGIFLER 

      1270       1280       1290       1300       1310       1320 
YCFRPSYQCP SMFCDTPMVH HIRRFVHGQG CVQIILKELD SPVPGYQHTI LTYSWCRICK 

      1330       1340       1350       1360       1370       1380 
QVTPVVALSN ESWSMSFAKY LELRFYGHQY TRRANAEPCG HSIHHDYHQY FSYNQMVASF 

      1390       1400       1410       1420       1430       1440 
SYSPIRLLEV CVPLPKIFIK RQAPLKVSLL QDLKDFFQKV SQVYVAIDER LASLKTDTFS 

      1450       1460       1470       1480       1490       1500 
KTREEKMEDI FAQKEMEEGE FKNWIEKMQA RLMSSSVDTP QQLQSVFESL IAKKQSLCEV 

      1510       1520       1530       1540       1550       1560 
LQAWNNRLQD LFQQEKGRKR PSVPPSPGRL RQGEESKISA MDASPRNISP GLQNGEKEDR 

      1570       1580       1590       1600       1610       1620 
FLTTLSSQSS TSSTHLQLPT PPEVMSEQSV GGPPELDTAS SSEDVFDGHL LGSTDSQVKE 

      1630       1640       1650       1660       1670       1680 
KSTMKAIFAN LLPGNSYNPI PFPFDPDKHY LMYEHERVPI AVCEKEPSSI IAFALSCKEY 

      1690       1700       1710       1720       1730       1740 
RNALEELSKA TQWNSAEEGL PTNSTSDSRP KSSSPIRLPE MSGGQTNRTT ETEPQPTKKA 

      1750       1760       1770       1780       1790       1800 
SGMLSFFRGT AGKSPDLSSQ KRETLRGADS AYYQVGQTGK EGTENQGVEP QDEVDGGDTQ 

      1810       1820       1830       1840       1850       1860 
KKQLINPHVE LQFSDANAKF YCRLYYAGEF HKMREVILDS SEEDFIRSLS HSSPWQARGG 

      1870       1880       1890       1900       1910       1920 
KSGAAFYATE DDRFILKQMP RLEVQSFLDF APHYFNYITN AVQQKRPTAL AKILGVYRIG 

      1930       1940       1950       1960       1970       1980 
YKNSQNNTEK KLDLLVMENL FYGRKMAQVF DLKGSLRNRN VKTDTGKESC DVVLLDENLL 

      1990       2000       2010       2020       2030       2040 
KMVRDNPLYI RSHSKAVLRT SIHSDSHFLS SHLIIDYSLL VGRDDTSNEL VVGIIDYIRT 

      2050       2060       2070       2080       2090 
FTWDKKLEMV VKSTGILGGQ GKMPTVVSPE LYRTRFCEAM DKYFLMVPDH WTGLGLNC 

« Hide

Isoform 2 [UniParc].

Checksum: E5C7D123475EA30E
Show »

FASTA45150,211
Isoform 3 [UniParc].

Checksum: 60E516304C47A038
Show »

FASTA46251,476
Isoform 4 [UniParc].

Checksum: 46091F5266458F67
Show »

FASTA54861,595

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS2382.1. [Q9Y2I7-1]
CCDS33368.1. [Q9Y2I7-2]
CCDS54431.1. [Q9Y2I7-4]
RefSeqNP_001171471.1. NM_001178000.1. [Q9Y2I7-4]
NP_055855.2. NM_015040.3. [Q9Y2I7-1]
NP_689884.1. NM_152671.3. [Q9Y2I7-2]
UniGeneHs.744997.

3D structure databases

ProteinModelPortalQ9Y2I7.
SMRQ9Y2I7. Positions 155-191, 540-872, 1819-2025.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid128336. 7 interactions.
IntActQ9Y2I7. 3 interactions.
MINTMINT-3084529.
STRING9606.ENSP00000264380.

Chemistry

ChEMBLCHEMBL1938222.

PTM databases

PhosphoSiteQ9Y2I7.

Polymorphism databases

DMDM300669693.

Proteomic databases

MaxQBQ9Y2I7.
PaxDbQ9Y2I7.
PRIDEQ9Y2I7.

Protocols and materials databases

DNASU200576.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264380; ENSP00000264380; ENSG00000115020. [Q9Y2I7-1]
ENST00000308862; ENSP00000308715; ENSG00000115020. [Q9Y2I7-3]
ENST00000392202; ENSP00000376038; ENSG00000115020. [Q9Y2I7-2]
ENST00000407449; ENSP00000384356; ENSG00000115020. [Q9Y2I7-4]
GeneID200576.
KEGGhsa:200576.
UCSCuc002vcv.3. human. [Q9Y2I7-2]
uc002vcw.3. human. [Q9Y2I7-4]
uc002vcx.3. human. [Q9Y2I7-3]
uc002vcz.3. human. [Q9Y2I7-1]

Organism-specific databases

CTD200576.
GeneCardsGC02P209130.
HGNCHGNC:23785. PIKFYVE.
HPAHPA042604.
MIM121850. phenotype.
609414. gene.
neXtProtNX_Q9Y2I7.
Orphanet98970. Fleck corneal dystrophy.
PharmGKBPA165697116.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0459.
HOGENOMHOG000059273.
HOVERGENHBG072055.
InParanoidQ9Y2I7.
KOK00921.
OMAWTEKMQA.
OrthoDBEOG757CWH.
PhylomeDBQ9Y2I7.
TreeFamTF321717.

Enzyme and pathway databases

BioCycMetaCyc:HS03825-MONOMER.
BRENDA2.7.1.68. 2681.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ9Y2I7.
BgeeQ9Y2I7.
CleanExHS_PIP5K3.
GenevestigatorQ9Y2I7.

Family and domain databases

Gene3D1.10.10.10. 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.
InterProIPR002423. 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]
PANTHERPTHR11353. PTHR11353. 1 hit.
PfamPF00118. Cpn60_TCP1. 1 hit.
PF00610. DEP. 1 hit.
PF01363. FYVE. 1 hit.
PF01504. PIP5K. 1 hit.
[Graphical view]
SMARTSM00049. DEP. 1 hit.
SM00064. FYVE. 1 hit.
SM00330. PIPKc. 1 hit.
[Graphical view]
SUPFAMSSF52029. SSF52029. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEPS50186. DEP. 1 hit.
PS51455. PIPK. 1 hit.
PS50178. ZF_FYVE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPIKFYVE. human.
GeneWikiPIKFYVE.
GenomeRNAi200576.
NextBio89946.
PROQ9Y2I7.
SOURCESearch...

Entry information

Entry nameFYV1_HUMAN
AccessionPrimary (citable) accession number: Q9Y2I7
Secondary accession number(s): Q08AR7 expand/collapse secondary AC list , Q08AR8, Q53ST3, Q53T36, Q8N5H0, Q8NB67
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 13, 2010
Last modified: July 9, 2014
This is version 140 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM