[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND CHARACTERIZATION. TISSUE=Adipose tissue; PubMed=9858586 [NCBI, ExPASy, EBI, Israel, Japan] Shisheva A., Sbrissa D., Ikonomov O.; "Cloning, characterization, and expression of a novel Zn2+-binding FYVE finger-containing phosphoinositide kinase in insulin-sensitive cells."; Mol. Cell. Biol. 19:623-634(1999).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). TISSUE=Pancreatic islet; DOI=10.1093/dnares/11.3.205; PubMed=15368895 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "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."; DNA Res. 11:205-218(2004).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). STRAIN=C57BL/6J; TISSUE=Cerebellum, Ovary, Spleen, and Uterus; DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The transcriptional landscape of the mammalian genome."; Science 309:1559-1563(2005).
[4]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND MASS SPECTROMETRY. TISSUE=Liver; DOI=10.1073/pnas.0609836104; PubMed=17242355 [NCBI, ExPASy, EBI, Israel, Japan] Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; "Large-scale phosphorylation analysis of mouse liver."; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).

Comments

FUNCTION: Supports the intracellular PIP pool and to a lesser extent, the PI 4,5-P(2) pool. It generates PIP from PI and, to a lesser extent, PI 4,5-P(2) from PI 4-P. There are indications that it phosphorylates the D-5 rather than the D-4 position. Has a role in endosome-related membrane trafficking.
CATALYTIC ACTIVITY: ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate.
SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Peripheral membrane protein. Note=Associated with vesicle structures. Displays a peripheral vesicular punctate pattern.

ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing.

Name	1
Synonyms	p235S
Isoform ID	Q9Z1T6-2
This is the isoform sequence displayed in this entry.

Name	2
Synonyms	p235L
Isoform ID	Q9Z1T6-1
Features which should be applied to build the isoform sequence: VSP_034953, VSP_034954.

Name	3
Isoform ID	Q9Z1T6-3
Features which should be applied to build the isoform sequence: VSP_034955, VSP_034956.

SIMILARITY: Contains 1 DEP domain.
SIMILARITY: Contains 1 FYVE-type zinc finger.
SIMILARITY: Contains 1 PI5K domain.
SEQUENCE CAUTION:
- Sequence=AAD10191.1; Type=Frameshift; Positions=Several;

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF102777; AAD10191.1; ALT_FRAME; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK173077; BAD32355.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK017186; BAB30626.3; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK139116; BAE23894.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK165350; BAE38145.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

T18290; T18290.

NP_035216.2; -.

3D structure databases

HSSP

P80318; 1GML. [HSSP ENTRY / PDB]

ModBase

Q9Z1T6.

PTM databases

PhosphoSite

Q9Z1T6; -.

2D gel databases

SWISS-2DPAGE

Q9Z1T6; -.

Organism-specific databases

MGI

MGI:1335106; Pip5k3.

Gene expression databases

ArrayExpress

Q9Z1T6; -.

GermOnline

ENSMUSG00000025949; Mus musculus.

Ontologies

GO:0030659;	Cellular component: cytoplasmic vesicle membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005829;	Cellular component: cytosol (inferred from direct assay from MGI).
GO:0016308;	Molecular function: 1-phosphatidylinositol-4-phosphate 5-kinase activity (inferred from direct assay from UniProtKB).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0008270;	Molecular function: zinc ion binding (inferred from direct assay from UniProtKB).
GO:0044267;	Biological process: cellular protein metabolic process (inferred from electronic annotation from InterPro).
GO:0007242;	Biological process: intracellular signaling cascade (inferred from direct assay from UniProtKB).
GO:0046488;	Biological process: phosphatidylinositol metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR002423; Cpn60/TCP-1.
IPR000591; DEP.
IPR002498; PIP5K_core.
IPR016034; PIP5K_core_sub.
IPR011991; Wing_hlx_DNA_bd.
IPR000306; Znf_FYVE.
IPR017455; Znf_FYVE-rel.
IPR013083; Znf_RING/FYVE/PHD.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.

PANTHER

PTHR11353; Cpn60/TCP-1; 1.

Pfam

PF00610; DEP; 1.
PF01363; FYVE; 1.
PF01504; PIP5K; 1.
Pfam graphical view of domain structure.

SMART

SM00049; DEP; 1.
SM00064; FYVE; 1.
SM00330; PIPKc; 1.
SMART graphical view of domain structure.

PROSITE

PS50186; DEP; 1.
PS50178; ZF_FYVE; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

Q9Z1T6.

Genome annotation databases

Ensembl

ENSMUSG00000025949; Mus musculus. [Contig view]

GeneID

18711; -.

KEGG

mmu:18711; -.

Phylogenomic databases

HOGENOM

Q9Z1T6; -.

HOVERGEN

Q9Z1T6; -.

Other

NextBio

294793; -.

SOURCE

Pip5k3; Mus musculus.

ROUGE

KIAA0981.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Alternative splicing; Cytoplasmic vesicle; Kinase; Membrane; Metal-binding; Phosphoprotein; Transferase; Zinc; Zinc-finger.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 2097`	`2097`	`FYVE finger-containing phosphoinositide kinase.`	`PRO_0000185453`
`DOMAIN`	`365 440`	`76`	`DEP.`
`DOMAIN`	`1846 2083`	`238`	`PI5K.`
`ZN_FING`	`158 218`	`61`	`FYVE-type.`
`REGION`	`1841 2097`	`257`	`Catalytic (By similarity).`
`COMPBIAS`	`1222 1225`	`4`	`Poly-Ser.`
`MOD_RES`	`46 46`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`307 307`		`Phosphoserine.`
`MOD_RES`	`318 318`		`Phosphoserine (By similarity).`
`MOD_RES`	`329 329`		`Phosphoserine (By similarity).`
`MOD_RES`	`1154 1154`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`1771 1771`		`Phosphotyrosine (By similarity).`
`VAR_SEQ`	`107 107`		`L -> LENTLPHPQEST (in isoform 2).`	`VSP_034953`
`VAR_SEQ`	`490 545`		`Missing (in isoform 2).`	`VSP_034954`
`VAR_SEQ`	`490 497`		`NSASPSKR -> SKFGFLML (in isoform 3).`	`VSP_034955`
`VAR_SEQ`	`498 2097`		`Missing (in isoform 3).`	`VSP_034956`
`CONFLICT`	`546 546`		`E -> K (in Ref. 1; AAD10191).`
`CONFLICT`	`944 944`		`Q -> K (in Ref. 1; AAD10191).`
`CONFLICT`	`994 995`		`QP -> HR (in Ref. 1; AAD10191).`
`CONFLICT`	`1107 1107`		`R -> T (in Ref. 3; BAB30626).`
`CONFLICT`	`1141 1141`		`L -> V (in Ref. 1; AAD10191).`
`CONFLICT`	`1264 1264`		`S -> Y (in Ref. 1; AAD10191).`
`CONFLICT`	`1996 1996`		`V -> E (in Ref. 1; AAD10191).`

Sequence information

Length: 2097 AA [This is the length of the unprocessed precursor]

Molecular weight: 236877 Da [This is the MW of the unprocessed precursor]

CRC64: 191A26607FD4A372 [This is a checksum on the sequence]

        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 LDNQSIPQAV 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

Q9Z1T6 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools