SubmitCancel

Skip Header

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

O43314

- VIP2_HUMAN

UniProt

O43314 - VIP2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2

Gene
PPIP5K2, HISPPD1, KIAA0433, VIP2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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-InsP4.2 Publications

Catalytic activityi

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

Kineticsi

  1. KM=0.13 µM for InsP61 Publication
  2. 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei134 – 1341ATP
Binding sitei187 – 1871ATP
Binding sitei194 – 1941ATP
Binding sitei213 – 2131ATP
Binding sitei248 – 2481Substrate
Binding sitei262 – 2621Substrate
Binding sitei264 – 2641ATP
Binding sitei309 – 3091ATP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi237 – 2404ATP
Nucleotide bindingi246 – 2483ATP
Nucleotide bindingi321 – 3233ATP

GO - Molecular functioni

  1. acid phosphatase activity Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  3. diphosphoinositol-pentakisphosphate kinase activity Source: UniProtKB
  4. inositol-1,3,4,5,6-pentakisphosphate kinase activity Source: UniProtKB
  5. inositol hexakisphosphate 1-kinase activity Source: UniProtKB-EC
  6. inositol hexakisphosphate 3-kinase activity Source: UniProtKB-EC
  7. inositol hexakisphosphate 5-kinase activity Source: UniProtKB

GO - Biological processi

  1. inositol metabolic process Source: UniProtKB
  2. inositol phosphate metabolic process Source: Reactome
  3. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_150188. Synthesis of pyrophosphates in the cytosol.

Names & Taxonomyi

Protein namesi
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 namesi
Name:PPIP5K2
Synonyms:HISPPD1, KIAA0433, VIP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:29035. PPIP5K2.

Subcellular locationi

Cytoplasmcytosol 1 Publication

GO - Cellular componenti

  1. cytosol Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi213 – 2131R → A or K: Reduces enzyme activity by about 99%. 1 Publication
Mutagenesisi248 – 2481K → A: Loss of enzyme activity. 1 Publication
Mutagenesisi262 – 2621R → A: Reduces enzyme activity by about 99%. 1 Publication

Organism-specific databases

PharmGKBiPA165660454.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12431243Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2PRO_0000315692Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei38 – 381Phosphoserine1 Publication
Modified residuei1006 – 10061Phosphoserine1 Publication
Modified residuei1016 – 10161Phosphoserine1 Publication
Modified residuei1172 – 11721Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO43314.
PaxDbiO43314.
PRIDEiO43314.

PTM databases

PhosphoSiteiO43314.

Expressioni

Gene expression databases

ArrayExpressiO43314.
BgeeiO43314.
CleanExiHS_HISPPD1.
GenevestigatoriO43314.

Organism-specific databases

HPAiHPA038442.

Interactioni

Protein-protein interaction databases

BioGridi116864. 8 interactions.
IntActiO43314. 1 interaction.

Structurei

Secondary structure

1
1243
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi44 – 507
Helixi52 – 554
Helixi58 – 6710
Beta strandi73 – 775
Helixi80 – 856
Helixi88 – 903
Beta strandi95 – 995
Helixi107 – 11711
Beta strandi120 – 1234
Helixi127 – 1315
Helixi134 – 14310
Beta strandi151 – 1544
Beta strandi158 – 1603
Helixi161 – 1633
Beta strandi164 – 1685
Beta strandi170 – 1756
Beta strandi178 – 19013
Beta strandi197 – 1993
Helixi202 – 2043
Beta strandi208 – 2158
Beta strandi218 – 2247
Beta strandi230 – 2323
Beta strandi234 – 2385
Beta strandi243 – 25311
Beta strandi257 – 2637
Beta strandi265 – 2673
Beta strandi275 – 2795
Helixi288 – 30013
Beta strandi303 – 31311
Beta strandi316 – 32510
Helixi332 – 35423

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3T54X-ray1.90A37-366[»]
3T7AX-ray1.70A41-366[»]
3T99X-ray2.10A37-366[»]
3T9AX-ray1.80A41-366[»]
3T9BX-ray1.85A41-366[»]
3T9CX-ray1.90A41-366[»]
3T9DX-ray1.85A41-366[»]
3T9EX-ray1.90A41-366[»]
3T9FX-ray2.00A41-366[»]
4HN2X-ray1.90A41-366[»]
4NZMX-ray2.00A41-366[»]
4NZNX-ray1.75A41-366[»]
4NZOX-ray1.90A41-366[»]
ProteinModelPortaliO43314.
SMRiO43314. Positions 42-360.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni53 – 542Substrate binding
Regioni213 – 2142Substrate binding
Regioni326 – 3294Substrate binding
Regioni371 – 44272Polyphosphoinositide-binding domainAdd
BLAST

Domaini

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.1 Publication

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG245915.
HOGENOMiHOG000177917.
HOVERGENiHBG108657.
InParanoidiO43314.
KOiK13024.
OMAiYPINILA.
PhylomeDBiO43314.
TreeFamiTF313594.

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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O43314-1) [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

MSEAPRFFVG PEDTEINPGN YRHFFHHADE DDEEEDDSPP ERQIVVGICS     50
MAKKSKSKPM KEILERISLF KYITVVVFEE EVILNEPVEN WPLCDCLISF 100
HSKGFPLDKA VAYAKLRNPF VINDLNMQYL IQDRREVYSI LQAEGILLPR 150
YAILNRDPNN PKECNLIEGE DHVEVNGEVF QKPFVEKPVS AEDHNVYIYY 200
PTSAGGGSQR LFRKIGSRSS VYSPESNVRK TGSYIYEEFM PTDGTDVKVY 250
TVGPDYAHAE ARKSPALDGK VERDSEGKEV RYPVILNARE KLIAWKVCLA 300
FKQTVCGFDL LRANGQSYVC DVNGFSFVKN SMKYYDDCAK ILGNIVMREL 350
APQFHIPWSI PLEAEDIPIV PTTSGTMMEL RCVIAVIRHG DRTPKQKMKM 400
EVRHQKFFDL FEKCDGYKSG KLKLKKPKQL QEVLDIARQL LMELGQNNDS 450
EIEENKPKLE QLKTVLEMYG HFSGINRKVQ LTYLPHGCPK TSSEEEDSRR 500
EEPSLLLVLK WGGELTPAGR VQAEELGRAF RCMYPGGQGD YAGFPGCGLL 550
RLHSTYRHDL KIYASDEGRV QMTAAAFAKG LLALEGELTP ILVQMVKSAN 600
MNGLLDSDSD SLSSCQQRVK ARLHEILQKD RDFTAEDYEK LTPSGSISLI 650
KSMHLIKNPV KTCDKVYSLI QSLTSQIRHR MEDPKSSDIQ LYHSETLELM 700
LRRWSKLEKD FKTKNGRYDI SKIPDIYDCI KYDVQHNGSL KLENTMELYR 750
LSKALADIVI PQEYGITKAE KLEIAKGYCT PLVRKIRSDL QRTQDDDTVN 800
KLHPVYSRGV LSPERHVRTR LYFTSESHVH SLLSILRYGA LCNESKDEQW 850
KRAMDYLNVV NELNYMTQIV IMLYEDPNKD LSSEERFHVE LHFSPGAKGC 900
EEDKNLPSGY GYRPASRENE GRRPFKIDND DEPHTSKRDE VDRAVILFKP 950
MVSEPIHIHR KSPLPRSRKT ATNDEESPLS VSSPEGTGTW LHYTSGVGTG 1000
RRRRRSGEQI TSSPVSPKSL AFTSSIFGSW QQVVSENANY LRTPRTLVEQ 1050
KQNPTVGSHC AGLFSTSVLG GSSSAPNLQD YARTHRKKLT SSGCIDDATR 1100
GSAVKRFSIS FARHPTNGFE LYSMVPSICP LETLHNALSL KQVDEFLASI 1150
ASPSSDVPRK TAEISSTALR SSPIMRKKVS LNTYTPAKIL PTPPATLKST 1200
KASSKPATSG PSSAVVPNTS SRKKNITSKT ETHEHKKNTG KKK 1243
Length:1,243
Mass (Da):140,407
Last modified:January 15, 2008 - v3
Checksum:iA8831DDDAB9B2E6E
GO
Isoform 2 (identifier: O43314-2) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:1,222
Mass (Da):138,106
Checksum:iC61F832FE77F87F3
GO

Sequence cautioni

The sequence BAA24863.2 differs from that shown. Reason: Erroneous initiation.
The sequence EAW49076.1 differs from that shown. Reason: Erroneous gene model prediction.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti944 – 9441A → G.
Corresponds to variant rs17155115 [ dbSNP | Ensembl ].
VAR_038276
Natural varianti985 – 9851E → K.
Corresponds to variant rs12519525 [ dbSNP | Ensembl ].
VAR_038277
Natural varianti1003 – 10031R → K.
Corresponds to variant rs12520040 [ dbSNP | Ensembl ].
VAR_038278
Natural varianti1206 – 12061P → Q.
Corresponds to variant rs17155138 [ dbSNP | Ensembl ].
VAR_038279
Natural varianti1232 – 12321T → M.
Corresponds to variant rs17155147 [ dbSNP | Ensembl ].
VAR_038280

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1097 – 111721Missing in isoform 2. VSP_030636Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS34207.1. [O43314-2]
CCDS64212.1. [O43314-1]
RefSeqiNP_001263206.1. NM_001276277.1. [O43314-1]
NP_001268400.1. NM_001281471.1.
NP_056031.2. NM_015216.3. [O43314-2]
XP_005271992.1. XM_005271935.1. [O43314-2]
UniGeneiHs.212046.

Genome annotation databases

EnsembliENST00000321521; ENSP00000313070; ENSG00000145725. [O43314-2]
ENST00000358359; ENSP00000351126; ENSG00000145725. [O43314-1]
ENST00000414217; ENSP00000416016; ENSG00000145725. [O43314-2]
ENST00000570566; ENSP00000459756; ENSG00000262234. [O43314-1]
ENST00000576175; ENSP00000458792; ENSG00000262234. [O43314-2]
GeneIDi23262.
KEGGihsa:23262.
UCSCiuc003kod.5. human. [O43314-1]
uc003koe.4. human. [O43314-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS34207.1. [O43314-2 ]
CCDS64212.1. [O43314-1 ]
RefSeqi NP_001263206.1. NM_001276277.1. [O43314-1 ]
NP_001268400.1. NM_001281471.1.
NP_056031.2. NM_015216.3. [O43314-2 ]
XP_005271992.1. XM_005271935.1. [O43314-2 ]
UniGenei Hs.212046.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
4NZM X-ray 2.00 A 41-366 [» ]
4NZN X-ray 1.75 A 41-366 [» ]
4NZO X-ray 1.90 A 41-366 [» ]
ProteinModelPortali O43314.
SMRi O43314. Positions 42-360.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116864. 8 interactions.
IntActi O43314. 1 interaction.

PTM databases

PhosphoSitei O43314.

Proteomic databases

MaxQBi O43314.
PaxDbi O43314.
PRIDEi O43314.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000321521 ; ENSP00000313070 ; ENSG00000145725 . [O43314-2 ]
ENST00000358359 ; ENSP00000351126 ; ENSG00000145725 . [O43314-1 ]
ENST00000414217 ; ENSP00000416016 ; ENSG00000145725 . [O43314-2 ]
ENST00000570566 ; ENSP00000459756 ; ENSG00000262234 . [O43314-1 ]
ENST00000576175 ; ENSP00000458792 ; ENSG00000262234 . [O43314-2 ]
GeneIDi 23262.
KEGGi hsa:23262.
UCSCi uc003kod.5. human. [O43314-1 ]
uc003koe.4. human. [O43314-2 ]

Organism-specific databases

CTDi 23262.
GeneCardsi GC05P102455.
H-InvDB HIX0005068.
HIX0029534.
HGNCi HGNC:29035. PPIP5K2.
HPAi HPA038442.
MIMi 611648. gene.
neXtProti NX_O43314.
PharmGKBi PA165660454.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG245915.
HOGENOMi HOG000177917.
HOVERGENi HBG108657.
InParanoidi O43314.
KOi K13024.
OMAi YPINILA.
PhylomeDBi O43314.
TreeFami TF313594.

Enzyme and pathway databases

Reactomei REACT_150188. Synthesis of pyrophosphates in the cytosol.

Miscellaneous databases

GenomeRNAii 23262.
NextBioi 45000.
PROi O43314.
SOURCEi Search...

Gene expression databases

ArrayExpressi O43314.
Bgeei O43314.
CleanExi HS_HISPPD1.
Genevestigatori O43314.

Family and domain databases

Gene3Di 3.40.50.1240. 3 hits.
InterProi IPR000560. His_Pase_superF_clade-2.
IPR029033. His_PPase_superfam.
[Graphical view ]
Pfami PF00328. His_Phos_2. 1 hit.
[Graphical view ]
SUPFAMi SSF53254. SSF53254. 3 hits.
PROSITEi PS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1006; SER-1016 AND SER-1172, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. 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.

Entry informationi

Entry nameiVIP2_HUMAN
AccessioniPrimary (citable) accession number: O43314
Secondary accession number(s): A1NI53, A6NGS8, Q8TB50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: September 3, 2014
This is version 103 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi