O43314 (VIP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2
EC=2.7.4.21
EC=2.7.4.24

Alternative name(s):
Diphosphoinositol pentakisphosphate kinase 2
Histidine acid phosphatase domain-containing protein 1
InsP6 and PP-IP5 kinase 2
VIP1 homolog 2
Short name=hsVIP2

Gene names

Name:	PPIP5K2
Synonyms:	HISPPD1, KIAA0433, VIP2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1243 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.6 Ref.7
Catalytic activity	ATP + 1D-myo-inositol hexakisphosphate = ADP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate. Ref.6 Ref.7 Ref.11 ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate = ADP + 1D-myo-inositol diphosphate tetrakisphosphate (isomeric configuration unknown). Ref.6 Ref.7 Ref.11 ATP + 1D-myo-inositol 5-diphosphate pentakisphosphate = ADP + 1D-myo-inositol bisdiphosphate tetrakisphosphate (isomeric configuration unknown). Ref.6 Ref.7 Ref.11
Subcellular location	Cytoplasm › cytosol Ref.6.
Domain	The polyphosphoinositide-binding domain mediates binding of PtdIns(3,4,5)P3 and InsP6. Despite its similarity with the phosphatase domain of histidine acid phosphatases, it has no phosphatase activity. Ref.11
Sequence similarities	Belongs to the histidine acid phosphatase family. VIP1 subfamily.
Biophysicochemical properties	Kinetic parameters: KM=0.13 µM for InsP6 Ref.6 KM=0.19 µM for InsP7 Vmax=0.39 nmol/min/mg enzyme with InsP6 as substrate Vmax=1.38 nmol/min/mg enzyme with InsP7 as substrate
Sequence caution	The sequence BAA24863.2 differs from that shown. Reason: Erroneous initiation. The sequence EAW49076.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	inositol metabolic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytosol Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acid phosphatase activity Inferred from electronic annotation. Source: InterPro diphosphoinositol-pentakisphosphate kinase activity Inferred from sequence or structural similarity. Source: UniProtKB inositol hexakisphosphate 1-kinase activity Inferred from electronic annotation. Source: EC inositol hexakisphosphate 3-kinase activity Inferred from electronic annotation. Source: EC inositol hexakisphosphate 5-kinase activity Inferred from sequence or structural similarity. Source: UniProtKB inositol-1,3,4,5,6-pentakisphosphate kinase activity Inferred from sequence or structural similarity. Source: UniProtKB kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O43314-1)

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: O43314-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1097-1117: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1243

1243

Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2

PRO_0000315692

Regions

Nucleotide binding

237 – 240

4

ATP

Nucleotide binding

246 – 248

3

ATP

Nucleotide binding

321 – 323

3

ATP

Region

53 – 54

2

Substrate binding

Region

213 – 214

2

Substrate binding

Region

326 – 329

4

Substrate binding

Region

371 – 442

72

Polyphosphoinositide-binding domain

Sites

Binding site

134

1

ATP

Binding site

187

1

ATP

Binding site

194

1

ATP

Binding site

213

1

ATP

Binding site

248

1

Substrate

Binding site

262

1

Substrate

Binding site

264

1

ATP

Binding site

309

1

ATP

Amino acid modifications

Modified residue

38

1

Phosphoserine Ref.9

Modified residue

217

1

Phosphoserine By similarity

Modified residue

220

1

Phosphoserine By similarity

Modified residue

1006

1

Phosphoserine Ref.8

Modified residue

1016

1

Phosphoserine Ref.8

Modified residue

1172

1

Phosphoserine Ref.8

Modified residue

1180

1

Phosphoserine By similarity

Natural variations

Alternative sequence

1097 – 1117

21

Missing in isoform 2.

VSP_030636

Natural variant

944

1

A → G.
Corresponds to variant rs17155115 [ dbSNP | Ensembl ].

VAR_038276

Natural variant

985

1

E → K.
Corresponds to variant rs12519525 [ dbSNP | Ensembl ].

VAR_038277

Natural variant

1003

1

R → K.
Corresponds to variant rs12520040 [ dbSNP | Ensembl ].

VAR_038278

Natural variant

1206

1

P → Q.
Corresponds to variant rs17155138 [ dbSNP | Ensembl ].

VAR_038279

Natural variant

1232

1

T → M.
Corresponds to variant rs17155147 [ dbSNP | Ensembl ].

VAR_038280

Experimental info

Mutagenesis

213

1

R → A or K: Reduces enzyme activity by about 99%. Ref.12

Mutagenesis

248

1

K → A: Loss of enzyme activity. Ref.12

Mutagenesis

262

1

R → A: Reduces enzyme activity by about 99%. Ref.12

Secondary structure

1

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1243

Helix Strand Turn

Details...

Beta strand

44 – 50

7

Helix

52 – 55

4

Helix

58 – 67

10

Beta strand

73 – 77

5

Helix

80 – 85

6

Helix

88 – 90

3

Beta strand

95 – 99

5

Helix

107 – 117

11

Beta strand

120 – 123

4

Helix

127 – 131

5

Helix

134 – 143

10

Beta strand

151 – 154

4

Beta strand

158 – 160

3

Helix

161 – 163

3

Beta strand

164 – 168

5

Beta strand

170 – 175

6

Beta strand

178 – 190

13

Beta strand

197 – 199

3

Helix

202 – 204

3

Beta strand

208 – 215

8

Beta strand

218 – 224

7

Beta strand

230 – 232

3

Beta strand

234 – 238

5

Beta strand

243 – 253

11

Beta strand

257 – 263

7

Beta strand

265 – 267

3

Beta strand

275 – 279

5

Helix

288 – 300

13

Beta strand

303 – 313

11

Beta strand

316 – 325

10

Helix

332 – 354

23

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 15, 2008. Version 3. Checksum: A8831DDDAB9B2E6E	FASTA	1,243	140,407
	10 20 30 40 50 60 MSEAPRFFVG PEDTEINPGN YRHFFHHADE DDEEEDDSPP ERQIVVGICS MAKKSKSKPM 70 80 90 100 110 120 KEILERISLF KYITVVVFEE EVILNEPVEN WPLCDCLISF HSKGFPLDKA VAYAKLRNPF 130 140 150 160 170 180 VINDLNMQYL IQDRREVYSI LQAEGILLPR YAILNRDPNN PKECNLIEGE DHVEVNGEVF 190 200 210 220 230 240 QKPFVEKPVS AEDHNVYIYY PTSAGGGSQR LFRKIGSRSS VYSPESNVRK TGSYIYEEFM 250 260 270 280 290 300 PTDGTDVKVY TVGPDYAHAE ARKSPALDGK VERDSEGKEV RYPVILNARE KLIAWKVCLA 310 320 330 340 350 360 FKQTVCGFDL LRANGQSYVC DVNGFSFVKN SMKYYDDCAK ILGNIVMREL APQFHIPWSI 370 380 390 400 410 420 PLEAEDIPIV PTTSGTMMEL RCVIAVIRHG DRTPKQKMKM EVRHQKFFDL FEKCDGYKSG 430 440 450 460 470 480 KLKLKKPKQL QEVLDIARQL LMELGQNNDS EIEENKPKLE QLKTVLEMYG HFSGINRKVQ 490 500 510 520 530 540 LTYLPHGCPK TSSEEEDSRR EEPSLLLVLK WGGELTPAGR VQAEELGRAF RCMYPGGQGD 550 560 570 580 590 600 YAGFPGCGLL RLHSTYRHDL KIYASDEGRV QMTAAAFAKG LLALEGELTP ILVQMVKSAN 610 620 630 640 650 660 MNGLLDSDSD SLSSCQQRVK ARLHEILQKD RDFTAEDYEK LTPSGSISLI KSMHLIKNPV 670 680 690 700 710 720 KTCDKVYSLI QSLTSQIRHR MEDPKSSDIQ LYHSETLELM LRRWSKLEKD FKTKNGRYDI 730 740 750 760 770 780 SKIPDIYDCI KYDVQHNGSL KLENTMELYR LSKALADIVI PQEYGITKAE KLEIAKGYCT 790 800 810 820 830 840 PLVRKIRSDL QRTQDDDTVN KLHPVYSRGV LSPERHVRTR LYFTSESHVH SLLSILRYGA 850 860 870 880 890 900 LCNESKDEQW KRAMDYLNVV NELNYMTQIV IMLYEDPNKD LSSEERFHVE LHFSPGAKGC 910 920 930 940 950 960 EEDKNLPSGY GYRPASRENE GRRPFKIDND DEPHTSKRDE VDRAVILFKP MVSEPIHIHR 970 980 990 1000 1010 1020 KSPLPRSRKT ATNDEESPLS VSSPEGTGTW LHYTSGVGTG RRRRRSGEQI TSSPVSPKSL 1030 1040 1050 1060 1070 1080 AFTSSIFGSW QQVVSENANY LRTPRTLVEQ KQNPTVGSHC AGLFSTSVLG GSSSAPNLQD 1090 1100 1110 1120 1130 1140 YARTHRKKLT SSGCIDDATR GSAVKRFSIS FARHPTNGFE LYSMVPSICP LETLHNALSL 1150 1160 1170 1180 1190 1200 KQVDEFLASI ASPSSDVPRK TAEISSTALR SSPIMRKKVS LNTYTPAKIL PTPPATLKST 1210 1220 1230 1240 KASSKPATSG PSSAVVPNTS SRKKNITSKT ETHEHKKNTG KKK
	Isoform 2 [UniParc]. Checksum: C61F832FE77F87F3	FASTA	1,222	138,106
	10 20 30 40 50 60 MSEAPRFFVG PEDTEINPGN YRHFFHHADE DDEEEDDSPP ERQIVVGICS MAKKSKSKPM 70 80 90 100 110 120 KEILERISLF KYITVVVFEE EVILNEPVEN WPLCDCLISF HSKGFPLDKA VAYAKLRNPF 130 140 150 160 170 180 VINDLNMQYL IQDRREVYSI LQAEGILLPR YAILNRDPNN PKECNLIEGE DHVEVNGEVF 190 200 210 220 230 240 QKPFVEKPVS AEDHNVYIYY PTSAGGGSQR LFRKIGSRSS VYSPESNVRK TGSYIYEEFM 250 260 270 280 290 300 PTDGTDVKVY TVGPDYAHAE ARKSPALDGK VERDSEGKEV RYPVILNARE KLIAWKVCLA 310 320 330 340 350 360 FKQTVCGFDL LRANGQSYVC DVNGFSFVKN SMKYYDDCAK ILGNIVMREL APQFHIPWSI 370 380 390 400 410 420 PLEAEDIPIV PTTSGTMMEL RCVIAVIRHG DRTPKQKMKM EVRHQKFFDL FEKCDGYKSG 430 440 450 460 470 480 KLKLKKPKQL QEVLDIARQL LMELGQNNDS EIEENKPKLE QLKTVLEMYG HFSGINRKVQ 490 500 510 520 530 540 LTYLPHGCPK TSSEEEDSRR EEPSLLLVLK WGGELTPAGR VQAEELGRAF RCMYPGGQGD 550 560 570 580 590 600 YAGFPGCGLL RLHSTYRHDL KIYASDEGRV QMTAAAFAKG LLALEGELTP ILVQMVKSAN 610 620 630 640 650 660 MNGLLDSDSD SLSSCQQRVK ARLHEILQKD RDFTAEDYEK LTPSGSISLI KSMHLIKNPV 670 680 690 700 710 720 KTCDKVYSLI QSLTSQIRHR MEDPKSSDIQ LYHSETLELM LRRWSKLEKD FKTKNGRYDI 730 740 750 760 770 780 SKIPDIYDCI KYDVQHNGSL KLENTMELYR LSKALADIVI PQEYGITKAE KLEIAKGYCT 790 800 810 820 830 840 PLVRKIRSDL QRTQDDDTVN KLHPVYSRGV LSPERHVRTR LYFTSESHVH SLLSILRYGA 850 860 870 880 890 900 LCNESKDEQW KRAMDYLNVV NELNYMTQIV IMLYEDPNKD LSSEERFHVE LHFSPGAKGC 910 920 930 940 950 960 EEDKNLPSGY GYRPASRENE GRRPFKIDND DEPHTSKRDE VDRAVILFKP MVSEPIHIHR 970 980 990 1000 1010 1020 KSPLPRSRKT ATNDEESPLS VSSPEGTGTW LHYTSGVGTG RRRRRSGEQI TSSPVSPKSL 1030 1040 1050 1060 1070 1080 AFTSSIFGSW QQVVSENANY LRTPRTLVEQ KQNPTVGSHC AGLFSTSVLG GSSSAPNLQD 1090 1100 1110 1120 1130 1140 YARTHRKKLT SSGCIDGFEL YSMVPSICPL ETLHNALSLK QVDEFLASIA SPSSDVPRKT 1150 1160 1170 1180 1190 1200 AEISSTALRS SPIMRKKVSL NTYTPAKILP TPPATLKSTK ASSKPATSGP SSAVVPNTSS 1210 1220 RKKNITSKTE THEHKKNTGK KK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro." Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 4:307-313(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[2]	"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones." Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T. DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION.
[3]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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. , 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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] (ISOFORM 2). Tissue: Uterus.
[6]	"Cloning and characterization of two human VIP1-like inositol hexakisphosphate and diphosphoinositol pentakisphosphate kinases." Fridy P.C., Otto J.C., Dollins D.E., York J.D. J. Biol. Chem. 282:30754-30762(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
[7]	"Purification, sequencing, and molecular identification of a mammalian PP-InsP5 kinase that is activated when cells are exposed to hyperosmotic stress." Choi J.H., Williams J., Cho J., Falck J.R., Shears S.B. J. Biol. Chem. 282:30763-30775(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ENZYME ACTIVITY.
[8]	"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-1006; SER-1016 AND SER-1172, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[10]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]	"Receptor-dependent compartmentalization of PPIP5K1, a kinase with a cryptic polyphosphoinositide binding domain." Gokhale N.A., Zaremba A., Shears S.B. Biochem. J. 434:415-426(2011) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, POLYPHOSPHOINOSITIDE-BINDING DOMAIN.
[12]	"Structural basis for an inositol pyrophosphate kinase surmounting phosphate crowding." Wang H., Falck J.R., Hall T.M., Shears S.B. Nat. Chem. Biol. 8:111-116(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 41-366 IN COMPLEXES WITH ATP; SUBSTRATE AND TRANSITION STATE ANALOG, MUTAGENESIS OF ARG-213; LYS-248 AND ARG-262.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB007893 mRNA. Translation: BAA24863.2. Different initiation.
AC011362 Genomic DNA. No translation available.
CH471086 Genomic DNA. Translation: EAW49076.1. Sequence problems.
BC024591 mRNA. Translation: AAH24591.1.

IPI

IPI00178375.
IPI00784254.

RefSeq

NP_001263206.1. NM_001276277.1.
NP_056031.2. NM_015216.3.

UniGene

Hs.212046.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3T54	X-ray	1.90	A	37-366	[»]
3T7A	X-ray	1.70	A	41-366	[»]
3T99	X-ray	2.10	A	37-366	[»]
3T9A	X-ray	1.80	A	41-366	[»]
3T9B	X-ray	1.85	A	41-366	[»]
3T9C	X-ray	1.90	A	41-366	[»]
3T9D	X-ray	1.85	A	41-366	[»]
3T9E	X-ray	1.90	A	41-366	[»]
3T9F	X-ray	2.00	A	41-366	[»]
4HN2	X-ray	1.90	A	41-366	[»]

ProteinModelPortal

O43314.

ModBase

Search...

Protein-protein interaction databases

IntAct

O43314. 1 interaction.

PTM databases

PhosphoSite

O43314.

Proteomic databases

PaxDb

O43314.

PRIDE

O43314.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000321521; ENSP00000313070; ENSG00000145725.
ENST00000358359; ENSP00000351126; ENSG00000145725.
ENST00000414217; ENSP00000416016; ENSG00000145725.
ENST00000570566; ENSP00000459756; ENSG00000262234.
ENST00000576175; ENSP00000458792; ENSG00000262234.

GeneID

23262.

KEGG

hsa:23262.

UCSC

uc003kod.4. human.
uc003koe.3. human.

Organism-specific databases

CTD

23262.

GeneCards

GC05P102455.

H-InvDB

HIX0005068.
HIX0029534.

HGNC

HGNC:29035. PPIP5K2.

HPA

HPA038442.

MIM

611648. gene.

neXtProt

NX_O43314.

PharmGKB

PA165660454.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG245915.

HOGENOM

HOG000177917.

HOVERGEN

HBG108657.

InParanoid

O43314.

KO

K13024.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

O43314.

Bgee

O43314.

CleanEx

HS_HISPPD1.

Genevestigator

O43314.

Family and domain databases

InterPro

IPR000560. His_Pase_superF_clade-2.
[Graphical view]

Pfam

PF00328. His_Phos_2. 1 hit.
[Graphical view]

PROSITE

PS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
PS00778. HIS_ACID_PHOSPHAT_2. False negative.
[Graphical view]

ProtoNet

Search...

Other

GenomeRNAi

23262.

NextBio

45000.

SOURCE

Search...

Entry information

Entry name

VIP2_HUMAN

Accession

Primary (citable) accession number: O43314
Secondary accession number(s): A1NI53, A6NGS8, Q8TB50

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	January 15, 2008
Last modified:	May 1, 2013
This is version 89 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.