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Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1 (EC 2.7.4.21) (EC 2.7.4.24) (Diphosphoinositol pentakisphosphate kinase 1) (Histidine acid phosphatase domain-containing protein 2A) (InsP6 and PP-IP5 kinase 1) (VIP1 homolog)

 VIP1_MOUSE              Reviewed;        1436 AA.
A2ARP1; A2ARP2; A2ARP3; A2ARP4; Q6P1C8; Q7TSP1; Q80U21; Q8BL16;
Q8BUN6; Q8BVG9;
15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
20-FEB-2007, sequence version 1.
10-MAY-2017, entry version 95.
RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1;
EC=2.7.4.21;
EC=2.7.4.24;
AltName: Full=Diphosphoinositol pentakisphosphate kinase 1;
AltName: Full=Histidine acid phosphatase domain-containing protein 2A;
AltName: Full=InsP6 and PP-IP5 kinase 1;
AltName: Full=VIP1 homolog;
Name=Ppip5k1; Synonyms=Hisppd2a, Kiaa0377, Vip1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=Swiss Webster; TISSUE=Brain;
Avidan N., Dgany O.D., Cattan D.C., Pariente A., Thulliez M.,
Borot N., Moati L., Alain B., Krasnov T., Olender T., Shalmon L.,
Ben-Asher E., Khen M., Shalev H., Fellous M., Delaunay J., Yaniv I.,
Zaizov R., Beckmann J.S., Lancet D., Tamary H.;
"A 60kb genomic deletion is associated with non-syndromic deafness and
sperm motility disorder but not with congenital dyserythropoietic
anemia type I.";
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=12693553; DOI=10.1093/dnares/10.1.35;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
Nakajima D., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
II. The complete nucleotide sequences of 400 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:35-48(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 6).
STRAIN=C57BL/6J;
TISSUE=Adipose tissue, Hippocampus, and Olfactory bulb;
PubMed=16141072; DOI=10.1126/science.1112014;
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
SPLICING.
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
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., 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.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
STRAIN=C57BL/6J; TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1140 AND SER-1147, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Kidney, and Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Bifunctional inositol kinase that acts in concert with
the IP6K kinases IP6K1, IP6K2 and IP6K3 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, regulate a
variety of cellular processes, including apoptosis, vesicle
trafficking, cytoskeletal dynamics, exocytosis, insulin signaling
and neutrophil activation. 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. Activated
when cells are exposed to hyperosmotic stress.
{ECO:0000250|UniProtKB:Q6PFW1}.
-!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol hexakisphosphate = ADP +
1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate.
-!- CATALYTIC ACTIVITY: 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.
-!- CATALYTIC ACTIVITY: 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.
-!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol hexakisphosphate = ADP +
1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000250|UniProtKB:Q6PFW1}. Cell membrane
{ECO:0000250|UniProtKB:Q6PFW1}. Note=Relocalizes to the plasma
membrane upon activation of the PtdIns 3-kinase pathway.
{ECO:0000250|UniProtKB:Q6PFW1}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1;
IsoId=A2ARP1-1; Sequence=Displayed;
Name=2;
IsoId=A2ARP1-2; Sequence=VSP_030631;
Note=No experimental confirmation available.;
Name=3;
IsoId=A2ARP1-3; Sequence=VSP_030634;
Note=No experimental confirmation available.;
Name=4;
IsoId=A2ARP1-5; Sequence=VSP_030625, VSP_030626;
Note=No experimental confirmation available.;
Name=5;
IsoId=A2ARP1-6; Sequence=VSP_030627, VSP_030628;
Note=No experimental confirmation available.;
Name=6;
IsoId=A2ARP1-7; Sequence=VSP_030629, VSP_030630;
Note=No experimental confirmation available.;
-!- DOMAIN: The C-terminal acid phosphatase-like domain binds
PtdIns(3,4,5)P3 and InsP6. Despite its similarity with the
phosphatase domain of histidine acid phosphatases, it has no
phosphatase activity. {ECO:0000250|UniProtKB:Q6PFW1}.
-!- SIMILARITY: Belongs to the histidine acid phosphatase family. VIP1
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC32838.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
Sequence=BAC37198.1; Type=Frameshift; Positions=42; Evidence={ECO:0000305};
Sequence=BAC65546.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AF502585; AAP46293.1; -; mRNA.
EMBL; AK122264; BAC65546.1; ALT_INIT; mRNA.
EMBL; AK046696; BAC32838.1; ALT_SEQ; mRNA.
EMBL; AK078268; BAC37198.1; ALT_FRAME; mRNA.
EMBL; AK083140; BAC38780.1; -; mRNA.
EMBL; AL845466; CAM24220.1; -; Genomic_DNA.
EMBL; AL845466; CAM24221.1; -; Genomic_DNA.
EMBL; AL845466; CAM24222.1; -; Genomic_DNA.
EMBL; BC065138; AAH65138.1; -; mRNA.
CCDS; CCDS16639.1; -. [A2ARP1-1]
RefSeq; NP_848910.3; NM_178795.4. [A2ARP1-1]
RefSeq; XP_006499804.1; XM_006499741.3. [A2ARP1-1]
RefSeq; XP_011237919.1; XM_011239617.2. [A2ARP1-3]
UniGene; Mm.386076; -.
ProteinModelPortal; A2ARP1; -.
SMR; A2ARP1; -.
STRING; 10090.ENSMUSP00000057632; -.
iPTMnet; A2ARP1; -.
PhosphoSitePlus; A2ARP1; -.
MaxQB; A2ARP1; -.
PaxDb; A2ARP1; -.
PeptideAtlas; A2ARP1; -.
PRIDE; A2ARP1; -.
Ensembl; ENSMUST00000052029; ENSMUSP00000057632; ENSMUSG00000033526. [A2ARP1-1]
Ensembl; ENSMUST00000110625; ENSMUSP00000106255; ENSMUSG00000033526. [A2ARP1-3]
Ensembl; ENSMUST00000110626; ENSMUSP00000106256; ENSMUSG00000033526. [A2ARP1-1]
Ensembl; ENSMUST00000110627; ENSMUSP00000106257; ENSMUSG00000033526. [A2ARP1-3]
Ensembl; ENSMUST00000110628; ENSMUSP00000106258; ENSMUSG00000033526. [A2ARP1-2]
GeneID; 327655; -.
KEGG; mmu:327655; -.
UCSC; uc008lyl.1; mouse. [A2ARP1-1]
UCSC; uc008lyq.1; mouse. [A2ARP1-7]
UCSC; uc008lyr.1; mouse. [A2ARP1-5]
UCSC; uc008lys.1; mouse. [A2ARP1-6]
CTD; 9677; -.
MGI; MGI:2443281; Ppip5k1.
eggNOG; KOG1057; Eukaryota.
eggNOG; ENOG410XNSN; LUCA.
GeneTree; ENSGT00390000009048; -.
HOVERGEN; HBG108657; -.
InParanoid; A2ARP1; -.
KO; K13024; -.
OMA; MHSNQAS; -.
OrthoDB; EOG091G00ZU; -.
PhylomeDB; A2ARP1; -.
TreeFam; TF313594; -.
Reactome; R-MMU-1855167; Synthesis of pyrophosphates in the cytosol.
PRO; PR:A2ARP1; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000033526; -.
CleanEx; MM_HISPPD2A; -.
ExpressionAtlas; A2ARP1; baseline and differential.
Genevisible; A2ARP1; MM.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0003993; F:acid phosphatase activity; IEA:InterPro.
GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
GO; GO:0033857; F:diphosphoinositol-pentakisphosphate kinase activity; ISS:UniProtKB.
GO; GO:0000829; F:inositol heptakisphosphate kinase activity; IBA:GO_Central.
GO; GO:0052723; F:inositol hexakisphosphate 1-kinase activity; IEA:UniProtKB-EC.
GO; GO:0052724; F:inositol hexakisphosphate 3-kinase activity; IEA:UniProtKB-EC.
GO; GO:0000832; F:inositol hexakisphosphate 5-kinase activity; ISS:UniProtKB.
GO; GO:0000828; F:inositol hexakisphosphate kinase activity; ISO:MGI.
GO; GO:0000827; F:inositol-1,3,4,5,6-pentakisphosphate kinase activity; ISS:UniProtKB.
GO; GO:0006020; P:inositol metabolic process; ISS:UniProtKB.
GO; GO:0032958; P:inositol phosphate biosynthetic process; IBA:GO_Central.
CDD; cd07061; HP_HAP_like; 1.
Gene3D; 3.40.50.1240; -; 1.
InterPro; IPR033379; Acid_Pase_AS.
InterPro; IPR000560; His_Pase_clade-2.
InterPro; IPR029033; His_PPase_superfam.
InterPro; IPR030138; PPIP5K1.
PANTHER; PTHR12750:SF15; PTHR12750:SF15; 1.
Pfam; PF00328; His_Phos_2; 1.
SUPFAM; SSF53254; SSF53254; 3.
PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Cell membrane; Complete proteome;
Cytoplasm; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
Reference proteome; Transferase.
CHAIN 1 1436 Inositol hexakisphosphate and
diphosphoinositol-pentakisphosphate
kinase 1.
/FTId=PRO_0000315689.
NP_BIND 248 251 ATP. {ECO:0000250|UniProtKB:O43314}.
NP_BIND 257 259 ATP. {ECO:0000250|UniProtKB:O43314}.
NP_BIND 332 334 ATP. {ECO:0000250|UniProtKB:O43314}.
REGION 64 65 Substrate binding.
{ECO:0000250|UniProtKB:O43314}.
REGION 224 225 Substrate binding.
{ECO:0000250|UniProtKB:O43314}.
REGION 337 340 Substrate binding.
{ECO:0000250|UniProtKB:O43314}.
REGION 382 453 Polyphosphoinositide-binding domain.
{ECO:0000250|UniProtKB:Q6PFW1}.
BINDING 145 145 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 198 198 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 205 205 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 224 224 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 259 259 Substrate.
{ECO:0000250|UniProtKB:O43314}.
BINDING 273 273 Substrate.
{ECO:0000250|UniProtKB:O43314}.
BINDING 275 275 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 320 320 ATP. {ECO:0000250|UniProtKB:O43314}.
MOD_RES 939 939 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PFW1}.
MOD_RES 982 982 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PFW1}.
MOD_RES 1032 1032 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PFW1}.
MOD_RES 1068 1068 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PFW1}.
MOD_RES 1140 1140 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1147 1147 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
VAR_SEQ 261 266 YTVGPD -> MVDAEI (in isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_030625.
VAR_SEQ 267 1436 Missing (in isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_030626.
VAR_SEQ 403 439 RTPKQKMKMEVTHPRFFALFEKHGGYKTGKLKLKRPE ->
HPSFVIEKLVPWRCCLKLHLQDLVATVCFHLHGHQQR (in
isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_030627.
VAR_SEQ 440 1436 Missing (in isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_030628.
VAR_SEQ 653 671 LAPTGSTSLLNSMSVIQNP -> VTLFSSPCSNYIATQFLK
F (in isoform 6).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_030629.
VAR_SEQ 672 1436 Missing (in isoform 6).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_030630.
VAR_SEQ 818 837 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_030631.
VAR_SEQ 1057 1077 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_030634.
CONFLICT 441 441 L -> I (in Ref. 3; BAC38780).
{ECO:0000305}.
CONFLICT 831 831 T -> A (in Ref. 3; BAC32838).
{ECO:0000305}.
CONFLICT 1049 1049 P -> S (in Ref. 2; BAC65546).
{ECO:0000305}.
CONFLICT 1180 1180 T -> A (in Ref. 1; AAP46293 and 2;
BAC65546). {ECO:0000305}.
SEQUENCE 1436 AA; 159923 MW; D160DDDA7F34B4F2 CRC64;
MWSLTANEDE STTAHFFLGA GDEGLGTCGI GMRTEESDSE LLEDEEDEVP PEPQIIVGIC
AMTKKSKSKP MTQILERLCR FDYLTVVILG EDVILNEPVE NWPSCHCLIS FHSKGFPLDK
AVAYSKLRNP FLINDLAMQY YIQDRREVYR ILQEEGIDLP RYAVLNRDPA CPEECSLIEG
EDQVEVNGAV FPKPFVEKPV SAEDHNVYIY YPSSAGGGSQ RLFRKIGSRS SVYSPESSVR
KTGSYIYEEF MPTDGTDVKV YTVGPDYAHA EARKSPALDG KVERDSEGKE VRYPVMLTAM
EKLVARKVCV AFKQTVCGFD LLRANGHSFV CDVNGFSFVK NSMKYYDDCA KILGNTIMRE
LAPQFQIPWS IPTEAEDIPI VPTTSGTMME LRCVIAIIRH GDRTPKQKMK MEVTHPRFFA
LFEKHGGYKT GKLKLKRPEQ LQEVLDITRL LLAELEKEPE AEIEEKTGKL EQLKSVLEMY
GHFSGINRKV QLTYYPHGVK ASNEGQDLQR EPLAPSLLLV LKWGGELTPD GRVQAEELGR
AFRCMYPGGQ GDYAGFPGCG LLRLHSTFRH DLKIYASDEG RVQMTAAAFA KGLLALEGEL
TPILVQMVKS ANMNGLLDSD SDSLSSCQHR VKARLHHILQ QDAPFGPEDY DQLAPTGSTS
LLNSMSVIQN PVKVCDQVFA LIENLTHQIR ERMQDPSSVD LQLYHSETLE LMLQRWSKLE
RDFRQKSGRY DISKIPDIYD CVKYDVQHNG SLGLQGTAEL LRLSKALADV VIPQEYGISR
EEKVEIAVGF CLPLLRKILL DLQRTHEDES VNKLHPLYSR GVLSPGRHVR TRLYFTSESH
VHSLLSVFRY GGLLDETQDA QWQRALAYLS AISELNYMTQ IVIMLYEDNT RDPLSEERFH
VELHFSPGVK GVEEGSAPAG CGFRPASSEN EEMKTDPGSI ENLCPGKASD EPDRALQTSP
QPVEGTGLPR RSPLIRNRKA GSMEVLSETS SSRPGGYRLF SSSRPPTEMK QSGLGSQCTG
LFSTTVLGGS SSAPNLQDYA RTHGKKLPPA SLKHRDELLF VPAVKRFSVS FAKHPTNGFE
GCSMVPTIYP LETLHNALSL RQVSEFLTKV CQRHTDAHAQ ASAALFDSMH NHQASDSPFS
PPRTLHSPPL QLRHRSEKPP WYSSGPSSTV SSAGPSSPTT VDGNSHFGFS DQSSVNIHMT
EEKQGFGLLQ ETPGDGTREL HIERQQELVE PAQSPQELPV EICPSGSQGV TKVSQTCQEV
PDIVQPCHNI HEEIGQPQQE VPDISQLLLK DHDTTTNTCH LCQASQLSQK VCEEICQLCQ
DNHEESNQLC QEVSVKLGRM VHGFPVNVDS TAQETLMEIG RPTQEIPEDP YQEFSVKVGV
LAQKAPAISE LSQDIPEADK PSQELSEETE LQAQEVSEEI DQESEVVDEL PPEAIS


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VIP2_MOUSE ELISA Kit FOR Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2; organism: Mouse; gene name: Ppip5k2 96T
PPL PPIP5K2 Gene diphosphoinositol pentakisphosphate kinase 2
E12626h Human Diphosphoinositol Pentakisphosphate Kinase 2 96T
E12625h Human Diphosphoinositol Pentakisphosphate Kinase 1 96T
PPKB PPIP5K1 Gene diphosphoinositol pentakisphosphate kinase 1
E15053h Rat ELISA Kit FOR Inositol-pentakisphosphate 2-kinase 96T
IQCA1 IPPK Gene inositol 1,3,4,5,6-pentakisphosphate 2-kinase
CSB-EL011783RA Rat Inositol-pentakisphosphate 2-kinase(IPPK) ELISA kit 96T
201-20-2827 IPPK{inositol 1,3,4,5,6-pentakisphosphate 2-kinase}rabbit.pAb 0.2ml
CSB-EL011783HU Human Inositol-pentakisphosphate 2-kinase(IPPK) ELISA kit 96T
CSB-EL011783MO Mouse Inositol-pentakisphosphate 2-kinase(IPPK) ELISA kit 96T
CSB-EL011783RA Rat Inositol-pentakisphosphate 2-kinase(IPPK) ELISA kit SpeciesRat 96T
CSB-EL011783HU Human Inositol-pentakisphosphate 2-kinase(IPPK) ELISA kit SpeciesHuman 96T
CSB-EL011783MO Mouse Inositol-pentakisphosphate 2-kinase(IPPK) ELISA kit SpeciesMouse 96T


 

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