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Q9Z1T6 (FYV1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
p235
Gene names
Name:Pikfyve
Synonyms:Kiaa0981, Pip5k3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2097 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. 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. Ref.8

Catalytic activity

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

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.8

Subcellular location

Cytoplasmic vesicle membrane; Peripheral membrane protein. 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. Ref.8

Tissue specificity

Ubiquitous. Ref.7

Sequence similarities

Contains 1 DEP domain.

Contains 1 FYVE-type zinc finger.

Contains 1 PIPK domain.

Sequence caution

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.

Ontologies

Keywords
   Cellular componentCytoplasmic vesicle
Endosome
Membrane
   Coding sequence diversityAlternative splicing
   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 direct assay Ref.1. Source: UniProtKB

myelin assembly

Inferred from genetic interaction PubMed 22028665. Source: MGI

phosphatidylinositol phosphorylation

Inferred from direct assay Ref.1. Source: GOC

   Cellular_componentGolgi membrane

Traceable author statement. Source: Reactome

cytoplasmic vesicle

Inferred from direct assay PubMed 11112776. Source: MGI

cytoplasmic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from direct assay PubMed 11112776. Source: MGI

early endosome membrane

Traceable author statement. Source: Reactome

late endosome membrane

Traceable author statement. Source: Reactome

perinuclear region of cytoplasm

Inferred from direct assay PubMed 19056739. Source: MGI

vesicle membrane

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_function1-phosphatidylinositol-3-phosphate 5-kinase activity

Traceable author statement. Source: Reactome

1-phosphatidylinositol-4-phosphate 5-kinase activity

Inferred from direct assay Ref.1. Source: UniProtKB

1-phosphatidylinositol-5-kinase activity

Traceable author statement. Source: Reactome

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

zinc ion binding

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Z1T6-2)

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.
Isoform 2 (identifier: Q9Z1T6-1)

Also known as: p235L;

The sequence of this isoform differs from the canonical sequence as follows:
     107-107: L → LENTLPHPQEST
     490-545: Missing.
Isoform 3 (identifier: Q9Z1T6-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 209720961-phosphatidylinositol 3-phosphate 5-kinase
PRO_0000185453

Regions

Domain365 – 44076DEP
Domain1757 – 2083327PIPK
Zinc finger158 – 21861FYVE-type
Region1841 – 2097257Catalytic By similarity
Compositional bias1222 – 12254Poly-Ser

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue2991Phosphoserine By similarity
Modified residue3181Phosphoserine; by PKB/AKT1 or PKB/AKT2 By similarity
Modified residue3291Phosphoserine By similarity
Modified residue15431Phosphoserine By similarity
Modified residue15481Phosphoserine By similarity
Modified residue17531Phosphoserine By similarity

Natural variations

Alternative sequence1071L → LENTLPHPQEST in isoform 2.
VSP_034953
Alternative sequence490 – 54556Missing in isoform 2.
VSP_034954
Alternative sequence490 – 4978NSASPSKR → SKFGFLML in isoform 3.
VSP_034955
Alternative sequence498 – 20971600Missing in isoform 3.
VSP_034956

Experimental info

Sequence conflict5461E → K in AAD10191. Ref.1
Sequence conflict9441K → Q in BAD32355. Ref.2
Sequence conflict994 – 9952QP → HR in AAD10191. Ref.1
Sequence conflict11071R → T in BAB30626. Ref.3
Sequence conflict11411L → V in AAD10191. Ref.1
Sequence conflict12641S → Y in AAD10191. Ref.1
Sequence conflict19961V → E in AAD10191. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (p235S) [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 8C529E86FBEED8E6

FASTA2,097236,877
        10         20         30         40         50         60 
MATDDKSSPT LDSANDLPRS PASPSHLTHF KPLTPDQDEP PFKSAYSSFV NLFRFNKERG 

        70         80         90        100        110        120 
EGGQGEQQSP SSSWASPQIP SRTQSVRSPV PYKKQLNEEL HRRSSVLDSR RKAEPACGGH 

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

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

       250        260        270        280        290        300 
CSVSILDPSE PRTPVGSRKA SRNIFLEDDL AWQSLIHPDS SNSALSTRLV SVQEDAGKSP 

       310        320        330        340        350        360 
ARNRSASITN LSLDRSGSPM VPSYETSVSP QANRNYIRTE TTEDERKILL DSAQLKDLWK 

       370        380        390        400        410        420 
KICHHTSGME 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 
PADQKEYLVS DTGGQQLSIS DAFIKESLFN RRVEEKSKEL PFTPLGWHHN NLELLREENE 

       610        620        630        640        650        660 
EKQAMERLLS ANHNHMMALL QQLLQNESLS SSWRDIIVSL VCQVVQTVRP DVKHQDDDMD 

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

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

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

       850        860        870        880        890        900 
LRGGSDYELA RVKEILIFMI CVAYHSQLEI SFLMDEFAMP PTLMQSPSFH LLTEGRGEEG 

       910        920        930        940        950        960 
ASQEQVSGSS LPQDPECPRE ALSSEDSTLL ESRTVLEKGE LDNKSIPQAV ASLKHQDYTT 

       970        980        990       1000       1010       1020 
PTCPAGIPCA LFALVPESLL PLHMDQQDAV GNEQPETSQQ TDEQQDPKSQ MKAFRDPLQD 

      1030       1040       1050       1060       1070       1080 
DTGMYVTEEV TSSEDQRKTY ALTFKQELKD VILCISPVIT FREPFLLTEK GMRCSTRDYF 

      1090       1100       1110       1120       1130       1140 
PEQIYWSPLL NKEVKEMESR RKKQLLRDLS GLQGMNGSVQ AKSIQVLPSH ELVSTRIAEH 

      1150       1160       1170       1180       1190       1200 
LGDSQTLGRM LADYRARGGR IQSKHLDPFV HSKDASCTSG GKSGNKTESD EERGLIPSDV 

      1210       1220       1230       1240       1250       1260 
IWPTKVDCLN PANHQRLCVL FSSSSAQSSN APSACVSPWI VTMEFYGKND LTLGIFLERY 

      1270       1280       1290       1300       1310       1320 
CFRSSYQCPS MFCDTPMVHH IRRFVHGQGC VQIILKELDS PVPGYQHTIL TYSWCRICKQ 

      1330       1340       1350       1360       1370       1380 
VTPVVALSNE SWSMSFAKYL ELRFYGHQYT RRANAEPCGH SIHHDYHQYF SYNQMVASFS 

      1390       1400       1410       1420       1430       1440 
YSPIRLLEVC VPLPKIFIKR QAPLKVSLLQ DLKDFFQKVS QVYLAVDERL ASLKTDTFSK 

      1450       1460       1470       1480       1490       1500 
TREEKMEDIF AQKEMEEGEF KNWTEKMQAR LMSSSVDTPQ QLQSIFESLI AKKQSLCEVL 

      1510       1520       1530       1540       1550       1560 
QAWNSRLQDL FQQEKGRKRP SVPPSPGRLR QGEESKINAM DTSPRNISPG LHNGEKEDRF 

      1570       1580       1590       1600       1610       1620 
LTTLSSQSST SSTHLQLPTP PEALAEQVVG GPTDLDSASG SEDVFDGHLL GSTDSQVKEK 

      1630       1640       1650       1660       1670       1680 
STMKAIFANL LPGNSYNPIP FPFDPDKHYL MYEHERVPIA VCEKEPSSII AFALSCKEYR 

      1690       1700       1710       1720       1730       1740 
NALEELSKAT LRNSAEEGLP ANSALDNRPK SSSPIRLPEI SGGQTNRTVE AEPQPTKKAS 

      1750       1760       1770       1780       1790       1800 
GMLSFFRGTA GKSPDLSSQK RETLRGADSA YYQVGQAGKE GLESQGLEPQ DEVDGGDTQK 

      1810       1820       1830       1840       1850       1860 
KQLTNPHVEL QFSDANAKFY CRLYYAGEFH KMREVILGSS EEEFIRSLSH SSPWQARGGK 

      1870       1880       1890       1900       1910       1920 
SGAAFYATED DRFILKQMPR LEVQSFLDFA PHYFNYITNA VQQKRPTALA KILGVYRIGY 

      1930       1940       1950       1960       1970       1980 
KNSQNNTEKK LDLLVMENLF YGRKMAQVFD LKGSLRNRNV KTDTGKESCD VVLLDENLLK 

      1990       2000       2010       2020       2030       2040 
MVRDNPLYIR SHSKSVLRTS IHSDAHFLSS HLIIDYSLLV GRDDTSNELV VGIIDYIRTF 

      2050       2060       2070       2080       2090 
TWDKKLEMVV KSTGILGGQG KMPTVVSPEL YRTRFCEAMD KYFLMVPDHW TGLDLNC 

« Hide

Isoform 2 (p235L) [UniParc].

Checksum: C7FA5897A3319DA0
Show »

FASTA2,052232,081
Isoform 3 [UniParc].

Checksum: 5BB1E9BE48047A7A
Show »

FASTA49755,999

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT18290.
RefSeqNP_035216.2. NM_011086.2.
XP_006495843.1. XM_006495780.1.
XP_006495844.1. XM_006495781.1.
UniGeneMm.38370.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202165. 2 interactions.
IntActQ9Z1T6. 1 interaction.
STRING10090.ENSMUSP00000109676.

Chemistry

ChEMBLCHEMBL2176842.

PTM databases

PhosphoSiteQ9Z1T6.

2D gel databases

SWISS-2DPAGEQ9Z1T6.

Proteomic databases

PaxDbQ9Z1T6.
PRIDEQ9Z1T6.

Protocols and materials databases

DNASU18711.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000097707; ENSMUSP00000095314; ENSMUSG00000025949. [Q9Z1T6-2]
GeneID18711.
KEGGmmu:18711.
UCSCuc007bho.1. mouse. [Q9Z1T6-3]
uc007bht.1. mouse. [Q9Z1T6-2]

Organism-specific databases

CTD200576.
MGIMGI:1335106. Pikfyve.
RougeSearch...

Phylogenomic databases

eggNOGCOG0459.
GeneTreeENSGT00750000117278.
HOGENOMHOG000059273.
HOVERGENHBG005775.
KOK00921.
OMAKAEPTFG.
OrthoDBEOG757CWH.
TreeFamTF321717.

Enzyme and pathway databases

ReactomeREACT_188937. Metabolism.

Gene expression databases

BgeeQ9Z1T6.
GenevestigatorQ9Z1T6.

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

NextBio294793.
PROQ9Z1T6.
SOURCESearch...

Entry information

Entry nameFYV1_MOUSE
AccessionPrimary (citable) accession number: Q9Z1T6
Secondary accession number(s): E9QL40 expand/collapse secondary AC list , Q3TNE4, Q3UTT6, Q69ZU1, Q9CU94
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 128 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot