O74429 (VIP1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Cortical actin cytoskeleton protein asp1
InsP6 and PP-IP5 kinase

Gene names

Name:	asp1
Synonyms:	vip1
ORF Names:	SPCC1672.06c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	920 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 to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4. 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. Required for maintaining cellular integrity, normal growth and interactions with the ARP complex. Acts as a regulator of the PHO80-PHO85 cyclin/cyclin-dependent kinase (CDK) complex, thereby regulating signaling of phosphate availability By similarity. Required for the function of the cortical actin cytoskeleton, possibly by participating in correct F-actin localization and ensuring polarized growth. Ref.2
Catalytic activity	ATP + 1D-myo-inositol hexakisphosphate = ADP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate. ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate = ADP + 1D-myo-inositol diphosphate tetrakisphosphate (isomeric configuration unknown). ATP + 1D-myo-inositol 5-diphosphate pentakisphosphate = ADP + 1D-myo-inositol bisdiphosphate tetrakisphosphate (isomeric configuration unknown).
Subcellular location	Cytoplasm. Nucleus. Cytoplasm › cytoskeleton Ref.2 Ref.3.
Sequence similarities	Belongs to the histidine acid phosphatase family. VIP1 subfamily.
Caution	Although related to histidine acid phosphatase proteins, it lacks the conserved active sites, suggesting that it has no phosphatase activity.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cortical actin cytoskeleton organization Inferred from mutant phenotype Ref.2. Source: PomBase establishment or maintenance of actin cytoskeleton polarity Inferred from mutant phenotype Ref.2. Source: PomBase inositol phosphate biosynthetic process Inferred from sequence orthology. Source: PomBase
Cellular_component	cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from direct assay Ref.3. Source: PomBase nucleus Inferred from direct assay Ref.3. Source: PomBase
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 electronic annotation. Source: EC inositol heptakisphosphate kinase activity Inferred from sequence orthology. Source: PomBase 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 electronic annotation. Source: EC inositol hexakisphosphate kinase activity Inferred from sequence orthology. Source: PomBase kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 920	920	Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase		PRO_0000270923
Regions
	Nucleotide binding	248 – 251	4	ATP By similarity
	Nucleotide binding	258 – 260	3	ATP By similarity
	Nucleotide binding	333 – 335	3	ATP By similarity
	Region	42 – 43	2	Substrate binding By similarity
	Region	223 – 224	2	Substrate binding By similarity
	Region	338 – 341	4	Substrate binding By similarity
Sites
	Binding site	123	1	ATP By similarity
	Binding site	197	1	ATP By similarity
	Binding site	204	1	ATP By similarity
	Binding site	223	1	ATP By similarity
	Binding site	260	1	Substrate By similarity
	Binding site	274	1	Substrate By similarity
	Binding site	276	1	ATP By similarity
	Binding site	321	1	ATP By similarity
Amino acid modifications
	Modified residue	19	1	Phosphothreonine Ref.4
	Modified residue	21	1	Phosphoserine Ref.4
	Modified residue	706	1	Phosphoserine Ref.4
	Modified residue	720	1	Phosphoserine Ref.4

Sequences

	Sequence		Length	Mass (Da)
	O74429 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 507872D240110C0A	FASTA	920	105,680
	10 20 30 40 50 60 MIQNASHLTS IDTESSTRTA SPVSSIVTPT KRNVVGICAM DAKARSKPCR NILNRIIAEG 70 80 90 100 110 120 EFEAIVFGDN MILDEAVENW PACDYLICFY SSGFPLKKAE KYVELRKPFC VNDVVFQELL 130 140 150 160 170 180 WDRRLVLNIL DAIRVSTPQR LICSRDGGPK INKVLEEKLR RKFGIEITEV PTPEVKMLDE 190 200 210 220 230 240 DTLSVDGKII KKPYVEKPVY GEDHNIYIYF PKSVGGGGRK LFRKVANKSS DYDPDLCAPR 250 260 270 280 290 300 TEGSFIYEEF MNVDNAEDVK VYTVGPHYSH AETRKSPVVD GIVRRNPHGK EIRFITNLSE 310 320 330 340 350 360 EEKNMASKIS IAFEQPVCGF DLLRVSGQSY VIDVNGWSFV KDNNDYYDNA ARILKQMFHV 370 380 390 400 410 420 AERHRRNRVP SVQEVLNPPP RESEAWRLKS LVGVLRHADR TPKQKFKFSF TSDPFVKLLQ 430 440 450 460 470 480 GHTEEVILRN EQLNSVLAAT NLATELKCED INKLKQLRLA LETKKDLPGT KVQLKPAYSP 490 500 510 520 530 540 EGKLLKLQLI IKWGGEFTHS ARYQSKDLGE QFHKDLYIMN RDCLKDVEIY TSSERRVSAS 550 560 570 580 590 600 AEIFAMAFLE QETIPSDLLK VRKDLLDDSN AAKDTMDKVK KHLKSLLRVG DTARKEFTWP 610 620 630 640 650 660 ENMPKPCEVM QQVVQLMKYH RAVMRENFII LGPEVEQVQS RWCCNENPAL FRERWEKLFS 670 680 690 700 710 720 EFCDSEKADP SKVSELYDTL KYDALHNRQF LERIFTPYQY LKLPQSPSLI AKEPPQRTDS 730 740 750 760 770 780 NGNLVGMTGA NTNHTERPLE KLYELYDLAK VLFDFVSPQE YGIEPKEKLE IGLLTSVPLL 790 800 810 820 830 840 RQIIHDIKEA RDSDHASTRM YFTKESHIYT LLNCILESGL PMKLPRNQIP ELDYLTQICF 850 860 870 880 890 900 ELFERTNPSG NKEFSVRITL SPGCYAQCPL DMNLDAKHCI SVSPRRSLTR HLDLQQFITK 910 920 TEDLCNSVHL PKRFIPVNIN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
[2]	"Identification and characterization of Schizosaccharomyces pombe asp1(+), a gene that interacts with mutations in the Arp2/3 complex and actin." Feoktistova A., McCollum D., Ohi R., Gould K.L. Genetics 152:895-908(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[3]	"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[4]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-21; SER-706 AND SER-720, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329672 Genomic DNA. Translation: CAA20444.1.
PIR	T41050.
RefSeq	NP_587877.1. NM_001022869.2.
3D structure databases
ProteinModelPortal	O74429.
ModBase	Search...
Protein-protein interaction databases
STRING	4896.SPCC1672.06c-1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPCC1672.06c.1; SPCC1672.06c.1:pep; SPCC1672.06c.
GeneID	2539244.
KEGG	spo:SPCC1672.06c.
Organism-specific databases
PomBase	SPCC1672.06c.
Phylogenomic databases
eggNOG	NOG245915.
HOGENOM	HOG000177917.
OMA	LTDCQQK.
OrthoDB	EOG403119.
Family and domain databases
InterPro	IPR013651. ATP-grasp_RimK-type. IPR000560. His_Pase_superF_clade-2. [Graphical view]
Pfam	PF00328. His_Phos_2. 1 hit. PF08443. RimK. 1 hit. [Graphical view]
PROSITE	PS00616. HIS_ACID_PHOSPHAT_1. False negative. PS00778. HIS_ACID_PHOSPHAT_2. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	20800414.

Entry information

Entry name

VIP1_SCHPO

Accession

Primary (citable) accession number: O74429

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	November 1, 1998
Last modified:	May 1, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program