Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase

Gene

l(1)G0196

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Bifunctional inositol kinase that acts in concert with the IP6K kinases to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-InsP4, also respectively called InsP7 and InsP8, may regulate a variety of cellular processes, including apoptosis, vesicle trafficking, cytoskeletal dynamics, and exocytosis. Phosphorylates inositol hexakisphosphate (InsP6) at positions 1 or 3 to produce PP-InsP5 which is in turn phosphorylated by IP6Ks to produce (PP)2-InsP4. Alternatively, phosphorylates at position 1 or 3 PP-InsP5, produced by IP6Ks from InsP6, to produce (PP)2-InsP4 (By similarity).By similarity

Catalytic activityi

ATP + 1D-myo-inositol hexakisphosphate = ADP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate.
ATP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate = ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate.
ATP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate = ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate.
ATP + 1D-myo-inositol hexakisphosphate = ADP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei157 – 1571ATPBy similarity
Binding sitei210 – 2101ATPBy similarity
Binding sitei217 – 2171ATPBy similarity
Binding sitei236 – 2361ATPBy similarity
Binding sitei271 – 2711SubstrateBy similarity
Binding sitei285 – 2851SubstrateBy similarity
Binding sitei287 – 2871ATPBy similarity
Binding sitei332 – 3321ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi260 – 2634ATPBy similarity
Nucleotide bindingi269 – 2713ATPBy similarity
Nucleotide bindingi344 – 3463ATPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_302337. Synthesis of pyrophosphates in the cytosol.

Names & Taxonomyi

Protein namesi
Recommended name:
Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase (EC:2.7.4.21, EC:2.7.4.24)
Alternative name(s):
InsP6 and PP-IP5 kinase
Gene namesi
Name:l(1)G0196
ORF Names:CG14616
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0027279. l(1)G0196.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16961696Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinasePRO_0000315697Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei974 – 9741Phosphoserine1 Publication
Modified residuei1001 – 10011Phosphoserine1 Publication
Modified residuei1060 – 10601Phosphoserine1 Publication
Modified residuei1255 – 12551Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9VR59.
PRIDEiQ9VR59.

Expressioni

Gene expression databases

BgeeiQ9VR59.

Interactioni

Protein-protein interaction databases

BioGridi59411. 3 interactions.
DIPiDIP-21851N.
IntActiQ9VR59. 7 interactions.
MINTiMINT-1002676.
STRINGi7227.FBpp0288801.

Structurei

3D structure databases

ProteinModelPortaliQ9VR59.
SMRiQ9VR59. Positions 66-383.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni76 – 772Substrate bindingBy similarity
Regioni236 – 2372Substrate bindingBy similarity
Regioni349 – 3524Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG245915.
GeneTreeiENSGT00390000009048.
InParanoidiQ9VR59.
KOiK13024.
OMAiPRIHEGA.
OrthoDBiEOG77M8MT.
PhylomeDBiQ9VR59.

Family and domain databases

Gene3Di3.40.50.1240. 3 hits.
InterProiIPR000560. His_Pase_superF_clade-2.
IPR029033. His_PPase_superfam.
[Graphical view]
PfamiPF00328. His_Phos_2. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 3 hits.
PROSITEiPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform I (identifier: Q9VR59-1) [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
MSYTELESGY QDISQQHQQQ NPHQSQPQQR VGFYLGLQDG NGDTDFGDSN
60 70 80 90 100
DGMDSDTSTS SSNSKQVVVG ICAMAKKTQS KPMKEILTRL GEFEFIKLVT
110 120 130 140 150
FEENVILREP VQNWPTCDCL VSFHSKGFPL EKAIEYAQLR NPFVLNNLHM
160 170 180 190 200
QYDIQDRRRV YAILEKEGIE IPRYAVLDRD SPDPKHHELI ESEDHVEVNG
210 220 230 240 250
ITFNKPFVEK PVSAEDHNIY IYYPTSAGGG SQRLFRKIGS RSSVYSPESR
260 270 280 290 300
VRKTGSFIYE DFMPTDGTDV KVYTVGPDYA HAEARKSPAL DGKVERDSEG
310 320 330 340 350
KEIRYPVILN HSEKLISRKV CLAFKQTVCG FDLLRANGKS YVCDVNGFSF
360 370 380 390 400
VKNSNKYYDD CAKILGNMIL RELTPTLHIP WSVPFQLDDP PIVPTTFGKM
410 420 430 440 450
MELRCVVAVI RHGDRTPKQK MKVEVRHPKF FEIFEKYDGY KLGHVKLKRP
460 470 480 490 500
KQLQEILDIA RFLLSEIHTK AHAEIEEKES KLEQLKNVLE MYGHFSGINR
510 520 530 540 550
KVQMKYQPKG RPRGSSSDDT NLAADQPVEP SLVLILKWGG ELTPAGRIQA
560 570 580 590 600
EELGRIFRCM YPGGQGRSDY SGTQGLGLLR LHSTFRHDLK IYASDEGRVQ
610 620 630 640 650
MTAAAFAKGL LALEGELTPI LVQMVKSANT NGLLDNDCDS SKYQNLAKGR
660 670 680 690 700
LHELMQNDRE FSKEDRELIN PCNSKSITQA LDFVKNPVDC CHHVHLLIRE
710 720 730 740 750
LLHIISIKKD DPKTKDAILY HGETWDLMRC RWEKIEKDFS TKSKLFDISK
760 770 780 790 800
IPDIYDCIKY DLQHNQHTLQ YDQAEELYIY AKNLADIVIP QEYGLTPQEK
810 820 830 840 850
LAIGQGICSP LLRKIKGDLQ RNIDEVEDEF MNRLNPHYSH GVASPQRHVR
860 870 880 890 900
TRLYFTSESH VHSLLTVLRY GGLLNVVTDE QWRRAMDYIS MVSELNYMSQ
910 920 930 940 950
IVIMLYEDPT KDPTSEERFH VELHFSPGVN CCVQKNLPPG PGFRPHSHGD
960 970 980 990 1000
NACNVSLQSS DESNPARIEE ENDSNSGEER EGKKRGTSGQ RSTDRSAERI
1010 1020 1030 1040 1050
SPAFGFNRLE LRSKQFKSKP IPIGAHHTVS GHEAMDLAKR LNEELASHQQ
1060 1070 1080 1090 1100
QQNQQLRPIS PDIRAVTPDC EPRSRSFEQR PTSGVCAKEP DSQVSVSVSA
1110 1120 1130 1140 1150
SVSSANASTS SRRQRHSIAG QMSYMKMLGF GGFSKKMATS ANSLFSTAVI
1160 1170 1180 1190 1200
SGSSSAPNLR DMITVSSSGF GDVPPIRPLE TLHNALSLRK LDSFLQDMIL
1210 1220 1230 1240 1250
AQIFKTPTGS PPRGFSKNTL PAVSSMTLTA SNQTEVVEHE PISTTVTPTF
1260 1270 1280 1290 1300
DRRGSESGST ADAHLRLLSE SQCPNLDDSN TELRESLAGK MELWPQDIVK
1310 1320 1330 1340 1350
AAEDEELNLS ELETKPSLDL TMEIMERGVA GIASIQPMNR DSDETMGGGV
1360 1370 1380 1390 1400
FLSVCEEQGS GSTCLTPVSF GMDLDLSMVA NKGSITLSME GFDDDEDATL
1410 1420 1430 1440 1450
SAATTPSLLA DCEPRLESCY CCPSHAEAPP EVPSDDPRFG FALPVRVTQA
1460 1470 1480 1490 1500
SPEHARPVRR AHDPVSPRIQ KQISLFEGNA AMATGQEKTE SSGSVGGGAI
1510 1520 1530 1540 1550
LHASINLPAA GPHHLRQDAR LRKFENLTQS TSNSNFPFES NTLKRVPMQT
1560 1570 1580 1590 1600
TKDYDNVSHT QSCINLKSGS SGVLGGSPQR QRGSDGGGVG ASGVPAESRE
1610 1620 1630 1640 1650
PTRVHYGRMN STCCSASASP SPSPGALIVK ERFIEPPKRG VVRGYHGKTQ
1660 1670 1680 1690
SMDADFLFNE FLLLPAMAPA KISFDSSDID QASDDDSPSS SKQRHA

Note: No experimental confirmation available.

Length:1,696
Mass (Da):188,677
Last modified:June 16, 2009 - v2
Checksum:iBB013ECB582C96D3
GO
Isoform G (identifier: Q9VR59-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1293-1300: LWPQDIVK → QYPTEPSI
     1301-1696: Missing.

Note: No experimental confirmation available.

Show »
Length:1,300
Mass (Da):146,528
Checksum:i644A2123503DB726
GO
Isoform H (identifier: Q9VR59-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2-40: SYTELESGYQ...VGFYLGLQDG → EWTWFKDWWR...DDFCYCEVCM
     266-266: D → DVYFS
     1293-1305: LWPQDIVKAAEDE → RKCRKKSVVEWQC
     1306-1696: Missing.

Note: No experimental confirmation available.

Show »
Length:1,416
Mass (Da):159,831
Checksum:i95E98D85E6F735A6
GO
Isoform J (identifier: Q9VR59-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1090-1090: P → PATETAEDTS...PSCCTKTIAT
     1293-1300: LWPQDIVK → QYPTEPSI
     1301-1696: Missing.

Note: No experimental confirmation available.

Show »
Length:1,447
Mass (Da):162,288
Checksum:i33909E1FE36F5731
GO
Isoform K (identifier: Q9VR59-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1090-1090: P → PVSSPDFGDN...PSCCTKTIAT
     1293-1300: LWPQDIVK → QYPTEPSI
     1301-1696: Missing.

Note: No experimental confirmation available.

Show »
Length:1,846
Mass (Da):204,458
Checksum:i803BD74B91DAC0EE
GO

Sequence cautioni

The sequence ABN49448.1 differs from that shown. Reason: Frameshift at position 735. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti329 – 3291C → F in ABN49448 (Ref. 3) Curated
Sequence conflicti734 – 7341K → KN in ABN49448 (Ref. 3) Curated
Sequence conflicti906 – 9061Y → H in ABN49448 (Ref. 3) Curated
Sequence conflicti1092 – 10921S → G in AAT94524 (Ref. 3) Curated
Sequence conflicti1116 – 11161H → R in AAT94524 (Ref. 3) Curated
Sequence conflicti1124 – 11241Y → C in AAT94524 (Ref. 3) Curated
Sequence conflicti1124 – 11241Y → C in ABN49448 (Ref. 3) Curated

RNA editingi

Edited at positions 1093, 1117 and 1121.1 Publication
Partially edited. Target of Adar.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1093 – 10931Q → R in RNA edited version.
Natural varianti1117 – 11171S → G in RNA edited version.
Natural varianti1121 – 11211Q → R in RNA edited version.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2 – 4039SYTEL…GLQDG → EWTWFKDWWRLKKLRSRHQR HKKKLQATAASAEAAVTASA FLAGSGCAESGGSQDPQTNR LHSLDAVPSDGTLARRRHGS RDSLRRNRLLQRQRRSQSAA VRSHRSHDDDDDGEYGPFNV SDYEDYGPNHGSDEESDDFC YCEVCM in isoform H. 1 PublicationVSP_030640Add
BLAST
Alternative sequencei266 – 2661D → DVYFS in isoform H. 1 PublicationVSP_030641
Alternative sequencei1090 – 10901P → PATETAEDTSMDIQPKICIG KCAPGLLTPTVTTTDILKGI RDIAPTATQTSPPTFTPSTT TTTGAAAALFDNTATMSSNR PFTNQFQSIDPTSNDAPHQH HVHQHQYQHHRKTTTTIINN TLNENHTTATITNNTTTTPS CCTKTIAT in isoform J. CuratedVSP_030643
Alternative sequencei1090 – 10901P → PVSSPDFGDNSRTRSSEFGE TCHARVGTASNSDGGGSHPR ADHRTAFQIRVTNSLSFFKI DSSTNELPLSDIDFSLHPPT PQCGPLSHKRFHILTMRRME SCDDGAELEQVRHLPQISPM ATNERPLSSCNCSSSAAQAH SHSKSLMDLAQAVVMTSPQE TGPNSEQGCDPTTAADVSVS SFDDDFQLSSSAPAILMSAH FGNRPVVASLSSMVHVTTSP SASTLQLCRDKDKALASGTS SAHSKATSNSCGQLSMAGSA PVVTENPFRFTVSSLGSAAT NTACFVGSFEPIEEQITSIV EVDSKPLQPEPQVVYNLPTV LITGTASSSELSTKLNSNIL PTVTNAFSAIDTEINDEIGI SKEVGIGTIRITNTHTPCNK ATVTRPDTKIAITTDPQTVT ATETAEDTSMDIQPKICIGK CAPGLLTPTVTTTDILKGIR DIAPTATQTSPPTFTPSTTT TTGAAAALFDNTATMSSNRP FTNQFQSIDPTSNDAPHQHH VHQHQYQHHRKTTTTIINNT LNENHTTATITNNTTTTPSC CTKTIAT in isoform K. CuratedVSP_033593
Alternative sequencei1293 – 130513LWPQD…AAEDE → RKCRKKSVVEWQC in isoform H. 1 PublicationVSP_030648Add
BLAST
Alternative sequencei1293 – 13008LWPQDIVK → QYPTEPSI in isoform G, isoform J and isoform K. 1 PublicationVSP_030649
Alternative sequencei1301 – 1696396Missing in isoform G, isoform J and isoform K. 1 PublicationVSP_030650Add
BLAST
Alternative sequencei1306 – 1696391Missing in isoform H. 1 PublicationVSP_030651Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014298 Genomic DNA. Translation: AAN09569.2.
AE014298 Genomic DNA. Translation: AAN09570.3.
AE014298 Genomic DNA. Translation: AAN09571.2.
AE014298 Genomic DNA. Translation: AAN09573.2.
AE014298 Genomic DNA. Translation: ABW09458.2.
BT015295 mRNA. Translation: AAT94524.1.
BT030309 mRNA. Translation: ABN49448.1. Frameshift.
RefSeqiNP_001097041.2. NM_001103571.2. [Q9VR59-7]
NP_788950.2. NM_176777.2. [Q9VR59-1]
NP_788951.2. NM_176778.2. [Q9VR59-3]
NP_788952.2. NM_176779.3. [Q9VR59-6]
NP_788953.2. NM_176780.2. [Q9VR59-5]
UniGeneiDm.237.

Genome annotation databases

EnsemblMetazoaiFBtr0299524; FBpp0288799; FBgn0027279. [Q9VR59-1]
GeneIDi33137.
KEGGidme:Dmel_CG14616.

Keywords - Coding sequence diversityi

Alternative splicing, RNA editing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014298 Genomic DNA. Translation: AAN09569.2.
AE014298 Genomic DNA. Translation: AAN09570.3.
AE014298 Genomic DNA. Translation: AAN09571.2.
AE014298 Genomic DNA. Translation: AAN09573.2.
AE014298 Genomic DNA. Translation: ABW09458.2.
BT015295 mRNA. Translation: AAT94524.1.
BT030309 mRNA. Translation: ABN49448.1. Frameshift.
RefSeqiNP_001097041.2. NM_001103571.2. [Q9VR59-7]
NP_788950.2. NM_176777.2. [Q9VR59-1]
NP_788951.2. NM_176778.2. [Q9VR59-3]
NP_788952.2. NM_176779.3. [Q9VR59-6]
NP_788953.2. NM_176780.2. [Q9VR59-5]
UniGeneiDm.237.

3D structure databases

ProteinModelPortaliQ9VR59.
SMRiQ9VR59. Positions 66-383.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi59411. 3 interactions.
DIPiDIP-21851N.
IntActiQ9VR59. 7 interactions.
MINTiMINT-1002676.
STRINGi7227.FBpp0288801.

Proteomic databases

PaxDbiQ9VR59.
PRIDEiQ9VR59.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0299524; FBpp0288799; FBgn0027279. [Q9VR59-1]
GeneIDi33137.
KEGGidme:Dmel_CG14616.

Organism-specific databases

FlyBaseiFBgn0027279. l(1)G0196.

Phylogenomic databases

eggNOGiNOG245915.
GeneTreeiENSGT00390000009048.
InParanoidiQ9VR59.
KOiK13024.
OMAiPRIHEGA.
OrthoDBiEOG77M8MT.
PhylomeDBiQ9VR59.

Enzyme and pathway databases

ReactomeiREACT_302337. Synthesis of pyrophosphates in the cytosol.

Miscellaneous databases

GenomeRNAii33137.
NextBioi782108.
PROiQ9VR59.

Gene expression databases

BgeeiQ9VR59.

Family and domain databases

Gene3Di3.40.50.1240. 3 hits.
InterProiIPR000560. His_Pase_superF_clade-2.
IPR029033. His_PPase_superfam.
[Graphical view]
PfamiPF00328. His_Phos_2. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 3 hits.
PROSITEiPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  2. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS G AND H), RNA EDITING OF POSITIONS 1117 AND 1121.
    Strain: Berkeley.
    Tissue: Embryo and Head.
  4. "RNA editing in Drosophila melanogaster: new targets and functional consequences."
    Stapleton M., Carlson J.W., Celniker S.E.
    RNA 12:1922-1932(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: RNA EDITING OF POSITION 1093; 1117 AND 1121.
  5. "An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
    Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
    Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1060, IDENTIFICATION BY MASS SPECTROMETRY.
  6. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-974; SER-1001 AND SER-1255, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiVIP1_DROME
AccessioniPrimary (citable) accession number: Q9VR59
Secondary accession number(s): A2VEZ0
, A8JUU5, Q6AWF3, Q8IQ22, Q8IQ23, Q8IQ24
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 16, 2009
Last modified: April 1, 2015
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Caution

Although related to histidine acid phosphatases, it lacks the conserved active sites, suggesting that it has no phosphatase activity.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.