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Q6PFW1 (VIP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1

EC=2.7.4.21
EC=2.7.4.24
Alternative name(s):
Diphosphoinositol pentakisphosphate kinase 1
Histidine acid phosphatase domain-containing protein 2A
IP6 kinase
Inositol pyrophosphate synthase 1
InsP6 and PP-IP5 kinase 1
VIP1 homolog
Short name=hsVIP1
Gene names
Name:PPIP5K1
Synonyms:HISPPD2A, IP6K, IPS1, KIAA0377, VIP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1433 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Activated when cells are exposed to hyperosmotic stress. Ref.7 Ref.8 Ref.9

Catalytic activity

ATP + 1D-myo-inositol hexakisphosphate = ADP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate. Ref.7 Ref.8 Ref.9 Ref.13 Ref.14

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. Ref.7 Ref.8 Ref.9 Ref.13 Ref.14

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. Ref.7 Ref.8 Ref.9 Ref.13 Ref.14

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

Subcellular location

Cytoplasmcytosol. Cell membrane. Note: Relocalizes to the plasma membrane upon activation of the PtdIns 3-kinase pathway. Ref.7 Ref.8 Ref.14

Tissue specificity

Widely expressed, with a higher expression in skeletal muscle, heart and brain. Ref.7

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.14). Ref.14

Sequence similarities

Belongs to the histidine acid phosphatase family. VIP1 subfamily.

Biophysicochemical properties

Kinetic parameters:

The catalytic efficiency is 80 folds higher for 5-PP-InsP5 (InsP7) compared to InsP6.

KM=0.12 µM for InsP6 Ref.7 Ref.8 Ref.14

KM=0.10 µM for InsP7

Vmax=0.03 nmol/min/mg enzyme with InsP6 as substrate

Vmax=0.13 nmol/min/mg enzyme with InsP7 as substrate

Sequence caution

The sequence BAA20831.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6PFW1-1)

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: Q6PFW1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     818-821: Missing.
     1082-1082: N → NG
Isoform 3 (identifier: Q6PFW1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     818-821: Missing.
     1062-1082: Missing.
Isoform 4 (identifier: Q6PFW1-4)

The sequence of this isoform differs from the canonical sequence as follows:
     653-653: Missing.
     818-821: Missing.
     1062-1082: Missing.
Isoform 5 (identifier: Q6PFW1-5)

The sequence of this isoform differs from the canonical sequence as follows:
     810-821: Missing.
     865-957: Missing.
     1107-1240: Missing.
Isoform 6 (identifier: Q6PFW1-6)

The sequence of this isoform differs from the canonical sequence as follows:
     818-1433: Missing.
Note: No experimental confirmation available.
Isoform 7 (identifier: Q6PFW1-7)

The sequence of this isoform differs from the canonical sequence as follows:
     818-821: Missing.
     1020-1082: Missing.
     1167-1167: Y → LETRFCHVGQAGLELLTSSDLPASASQSAGITGVSHRTQPD
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14331433Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1
PRO_0000315688

Regions

Nucleotide binding248 – 2514ATP By similarity
Nucleotide binding257 – 2593ATP By similarity
Nucleotide binding332 – 3343ATP By similarity
Region64 – 652Substrate binding By similarity
Region224 – 2252Substrate binding By similarity
Region337 – 3404Substrate binding By similarity
Region382 – 45372Polyphosphoinositide-binding domain

Sites

Binding site1451ATP By similarity
Binding site1981ATP By similarity
Binding site2051ATP By similarity
Binding site2241ATP By similarity
Binding site2591Substrate By similarity
Binding site2731Substrate By similarity
Binding site2751ATP By similarity
Binding site3201ATP By similarity

Amino acid modifications

Modified residue11521Phosphoserine Ref.10

Natural variations

Alternative sequence6531Missing in isoform 4.
VSP_030615
Alternative sequence810 – 82112Missing in isoform 5.
VSP_030616
Alternative sequence818 – 1433616Missing in isoform 6.
VSP_030617
Alternative sequence818 – 8214Missing in isoform 2, isoform 3, isoform 4 and isoform 7.
VSP_030618
Alternative sequence865 – 95793Missing in isoform 5.
VSP_030619
Alternative sequence1020 – 108263Missing in isoform 7.
VSP_030620
Alternative sequence1062 – 108221Missing in isoform 3 and isoform 4.
VSP_030621
Alternative sequence10821N → NG in isoform 2.
VSP_030622
Alternative sequence1107 – 1240134Missing in isoform 5.
VSP_030623
Alternative sequence11671Y → LETRFCHVGQAGLELLTSSD LPASASQSAGITGVSHRTQP D in isoform 7.
VSP_030624

Experimental info

Mutagenesis3991R → A: Decreases 8-fold the affinity for PtdIns(3,4,5)P3. Ref.14
Mutagenesis4171R → A: Decreases 16-fold the affinity for PtdIns(3,4,5)P3. Ref.14
Sequence conflict441D → G in CAD97968. Ref.4
Sequence conflict3041V → M in CAD97968. Ref.4
Sequence conflict3741E → V in CAD97968. Ref.4
Sequence conflict4231E → Q in AAP30843. Ref.1
Sequence conflict4231E → Q in AAP30845. Ref.1
Sequence conflict4231E → Q in AAN40768. Ref.1
Sequence conflict4731L → P in CAD97968. Ref.4
Sequence conflict4831F → S in AAP30845. Ref.1
Sequence conflict4831F → S in AAN40768. Ref.1
Sequence conflict4901V → E in CAD97968. Ref.4
Sequence conflict5481G → V in CAD97968. Ref.4
Sequence conflict7381I → L in AAP30845. Ref.1
Sequence conflict7381I → L in AAN40768. Ref.1
Sequence conflict7881V → A in AAP30845. Ref.1
Sequence conflict7881V → A in AAN40768. Ref.1
Sequence conflict9361E → G in CAI46011. Ref.4
Sequence conflict9851A → V in AAP30845. Ref.1
Sequence conflict9851A → V in AAN40768. Ref.1
Sequence conflict10201G → A in AAP30843. Ref.1
Sequence conflict10411L → P in AAP30845. Ref.1
Sequence conflict10411L → P in AAN40768. Ref.1
Sequence conflict10661V → L in AAP30842. Ref.1
Sequence conflict11261A → T in CAI46011. Ref.4
Sequence conflict11341M → V in CAI46011. Ref.4
Sequence conflict11981P → R in CAI46011. Ref.4
Sequence conflict12931H → M in AAP30845. Ref.1
Sequence conflict12931H → M in AAN40768. Ref.1
Sequence conflict12941D → T in AAP30845. Ref.1
Sequence conflict12941D → T in AAN40768. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: BA0DEFB2A71B1467

FASTA1,433159,521
        10         20         30         40         50         60 
MWSLTASEGE STTAHFFLGA GDEGLGTRGI GMRPEESDSE LLEDEEDEVP PEPQIIVGIC 

        70         80         90        100        110        120 
AMTKKSKSKP MTQILERLCR FDYLTVVILG EDVILNEPVE NWPSCHCLIS FHSKGFPLDK 

       130        140        150        160        170        180 
AVAYSKLRNP FLINDLAMQY YIQDRREVYR ILQEEGIDLP RYAVLNRDPA RPEECNLIEG 

       190        200        210        220        230        240 
EDQVEVNGAV FPKPFVEKPV SAEDHNVYIY YPSSAGGGSQ RLFRKIGSRS SVYSPESSVR 

       250        260        270        280        290        300 
KTGSYIYEEF MPTDGTDVKV YTVGPDYAHA EARKSPALDG KVERDSEGKE IRYPVMLTAM 

       310        320        330        340        350        360 
EKLVARKVCV AFKQTVCGFD LLRANGHSFV CDVNGFSFVK NSMKYYDDCA KILGNTIMRE 

       370        380        390        400        410        420 
LAPQFQIPWS IPTEAEDIPI VPTTSGTMME LRCVIAIIRH GDRTPKQKMK MEVKHPRFFA 

       430        440        450        460        470        480 
LFEKHGGYKT GKLKLKRPEQ LQEVLDITRL LLAELEKEPG GEIEEKTGKL EQLKSVLEMY 

       490        500        510        520        530        540 
GHFSGINRKV QLTYYPHGVK ASNEGQDPQR ETLAPSLLLV LKWGGELTPA GRVQAEELGR 

       550        560        570        580        590        600 
AFRCMYPGGQ GDYAGFPGCG LLRLHSTFRH DLKIYASDEG RVQMTAAAFA KGLLALEGEL 

       610        620        630        640        650        660 
TPILVQMVKS ANMNGLLDSD GDSLSSCQHR VKARLHHILQ QDAPFGPEDY DQLAPTRSTS 

       670        680        690        700        710        720 
LLNSMTIIQN PVKVCDQVFA LIENLTHQIR ERMQDPRSVD LQLYHSETLE LMLQRWSKLE 

       730        740        750        760        770        780 
RDFRQKSGRY DISKIPDIYD CVKYDVQHNG SLGLQGTAEL LRLSKALADV VIPQEYGISR 

       790        800        810        820        830        840 
EEKLEIAVGF CLPLLRKILL DLQRTHEDES VNKLHPLCYL RYSRGVLSPG RHVRTRLYFT 

       850        860        870        880        890        900 
SESHVHSLLS VFRYGGLLDE TQDAQWQRAL DYLSAISELN YMTQIVIMLY EDNTQDPLSE 

       910        920        930        940        950        960 
ERFHVELHFS PGVKGVEEEG SAPAGCGFRP ASSENEEMKT NQGSMENLCP GKASDEPDRA 

       970        980        990       1000       1010       1020 
LQTSPQPPEG PGLPRRSPLI RNRKAGSMEV LSETSSSRPG GYRLFSSSRP PTEMKQSGLG 

      1030       1040       1050       1060       1070       1080 
SQCTGLFSTT VLGGSSSAPN LQDYARSHGK KLPPASLKHR DELLFVPAVK RFSVSFAKHP 

      1090       1100       1110       1120       1130       1140 
TNGFEGCSMV PTIYPLETLH NALSLRQVSE FLSRVCQRHT DAQAQASAAL FDSMHSSQAS 

      1150       1160       1170       1180       1190       1200 
DNPFSPPRTL HSPPLQLQQR SEKPPWYSSG PSSTVSSAGP SSPTTVDGNS QFGFSDQPSL 

      1210       1220       1230       1240       1250       1260 
NSHVAEEHQG LGLLQETPGS GAQELSIEGE QELFEPNQSP QVPPMETSQP YEEVSQPCQE 

      1270       1280       1290       1300       1310       1320 
VPDISQPCQD ISEALSQPCQ KVPDISQQCQ ENHDNGNHTC QEVPHISQPC QKSSQLCQKV 

      1330       1340       1350       1360       1370       1380 
SEEVCQLCLE NSEEVSQPCQ GVSVEVGKLV HKFHVGVGSL VQETLVEVGS PAEEIPEEVI 

      1390       1400       1410       1420       1430 
QPYQEFSVEV GRLAQETSAI NLLSQGIPEI DKPSQEFPEE IDLQAQEVPE EIN 

« Hide

Isoform 2 [UniParc].

Checksum: 11E6EC888FB5703C
Show »

FASTA1,430159,042
Isoform 3 [UniParc].

Checksum: E88E96597599F5BA
Show »

FASTA1,408156,616
Isoform 4 [UniParc].

Checksum: 1DC5FCBF5A726F14
Show »

FASTA1,407156,502
Isoform 5 [UniParc].

Checksum: F29D866BFAD98841
Show »

FASTA1,194133,447
Isoform 6 [UniParc].

Checksum: 4DBCE9B366905530
Show »

FASTA81792,061
Isoform 7 [UniParc].

Checksum: 77C01F2E2AC7446D
Show »

FASTA1,406156,320

References

« Hide 'large scale' references
[1]"CATSPER2, a human autosomal nonsyndromic male infertility gene."
Avidan N., Tamary H., Dgany O., Cattan D., Pariente A., Thulliez M., Borot N., Moati L., Barthelme A., Shalmon L., Krasnov T., Ben-Asher E., Olender T., Khen M., Yaniv I., Zaizov R., Shalev H., Delaunay J. expand/collapse author list , Fellous M., Lancet D., Beckmann J.S.
Eur. J. Hum. Genet. 11:497-502(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 5).
Tissue: Bone marrow, Testis and Trachea.
[2]"Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
Tissue: Brain.
[3]Ohara O., Nagase T., Kikuno R., Nomura N.
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
Tissue: Endometrial adenocarcinoma.
[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] (ISOFORMS 1 AND 6).
Tissue: Eye and Uterus.
[6]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"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, TISSUE SPECIFICITY.
[8]"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, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
[9]"A conserved family of enzymes that phosphorylate inositol hexakisphosphate."
Mulugu S., Bai W., Fridy P.C., Bastidas R.J., Otto J.C., Dollins D.E., Haystead T.A., Ribeiro A.A., York J.D.
Science 316:106-109(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME ACTIVITY.
[10]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1152, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Structural analysis and detection of biological inositol pyrophosphates reveal that the family of VIP/diphosphoinositol pentakisphosphate kinases are 1/3-kinases."
Lin H., Fridy P.C., Ribeiro A.A., Choi J.H., Barma D.K., Vogel G., Falck J.R., Shears S.B., York J.D., Mayr G.W.
J. Biol. Chem. 284:1863-1872(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY.
[14]"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: BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, POLYPHOSPHOINOSITIDE-BINDING DOMAIN, MUTAGENESIS OF ARG-399 AND ARG-417.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF502586 mRNA. Translation: AAP30842.1.
AF502587 mRNA. Translation: AAP30843.1.
AF502588 mRNA. Translation: AAP30844.1.
AF502589 mRNA. Translation: AAP30845.1.
AF543190 mRNA. Translation: AAN40768.1.
AB002375 mRNA. Translation: BAA20831.2. Different initiation.
BX538022 mRNA. Translation: CAD97968.1.
BX647814 mRNA. Translation: CAI46011.1.
BC050263 mRNA. Translation: AAH50263.1.
BC057395 mRNA. Translation: AAH57395.1.
CCDSCCDS32215.1. [Q6PFW1-3]
CCDS45252.1. [Q6PFW1-1]
CCDS53937.1. [Q6PFW1-7]
RefSeqNP_001124330.1. NM_001130858.2. [Q6PFW1-1]
NP_001124331.1. NM_001130859.2. [Q6PFW1-3]
NP_001177143.1. NM_001190214.1. [Q6PFW1-7]
NP_055474.3. NM_014659.5. [Q6PFW1-3]
XP_005254861.1. XM_005254804.1. [Q6PFW1-3]
UniGeneHs.156814.
Hs.679911.

3D structure databases

ProteinModelPortalQ6PFW1.
SMRQ6PFW1. Positions 54-371.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115031. 11 interactions.
STRING9606.ENSP00000380129.

Chemistry

ChEMBLCHEMBL5046.

PTM databases

PhosphoSiteQ6PFW1.

Polymorphism databases

DMDM74758334.

Proteomic databases

MaxQBQ6PFW1.
PaxDbQ6PFW1.
PRIDEQ6PFW1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000334933; ENSP00000334779; ENSG00000168781. [Q6PFW1-3]
ENST00000348806; ENSP00000308773; ENSG00000168781. [Q6PFW1-7]
ENST00000360135; ENSP00000353253; ENSG00000168781. [Q6PFW1-7]
ENST00000360301; ENSP00000353446; ENSG00000168781. [Q6PFW1-3]
ENST00000396923; ENSP00000380129; ENSG00000168781. [Q6PFW1-1]
ENST00000420765; ENSP00000400887; ENSG00000168781. [Q6PFW1-1]
GeneID9677.
KEGGhsa:9677.
UCSCuc001zrw.3. human. [Q6PFW1-1]
uc001zrx.2. human. [Q6PFW1-7]
uc001zry.4. human. [Q6PFW1-3]
uc021sjz.1. human. [Q6PFW1-5]

Organism-specific databases

CTD9677.
GeneCardsGC15M043826.
H-InvDBHIX0012186.
HGNCHGNC:29023. PPIP5K1.
HPAHPA039380.
MIM610979. gene.
neXtProtNX_Q6PFW1.
PharmGKBPA165479401.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG245915.
HOVERGENHBG108657.
InParanoidQ6PFW1.
KOK13024.
OMAEEVSQPC.
PhylomeDBQ6PFW1.
TreeFamTF313594.

Enzyme and pathway databases

BioCycMetaCyc:HS09822-MONOMER.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ6PFW1.
BgeeQ6PFW1.
GenevestigatorQ6PFW1.

Family and domain databases

Gene3D3.40.50.1240. 4 hits.
InterProIPR000560. His_Pase_superF_clade-2.
IPR029033. His_PPase_superfam.
[Graphical view]
PfamPF00328. His_Phos_2. 1 hit.
[Graphical view]
SUPFAMSSF53254. SSF53254. 3 hits.
PROSITEPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPPIP5K1. human.
GenomeRNAi9677.
NextBio36337.
PROQ6PFW1.
SOURCESearch...

Entry information

Entry nameVIP1_HUMAN
AccessionPrimary (citable) accession number: Q6PFW1
Secondary accession number(s): O15082 expand/collapse secondary AC list , Q5HYF8, Q7Z3A7, Q86TE7, Q86UV3, Q86UV4, Q86XW8, Q8IZN0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM