Tag | Content |
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CPLM ID | CPLM-015284 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1 |
Protein Synonyms/Alias | 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; hsVIP1 |
Gene Name | PPIP5K1 |
Gene Synonyms/Alias | HISPPD2A; IP6K; IPS1; KIAA0377; VIP1 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
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126 | DKAVAYSKLRNPFLI | ubiquitination | [1] | 241 | SPESSVRKTGSYIYE | ubiquitination | [1] | 274 | YAHAEARKSPALDGK | ubiquitination | [1] | 344 | SFVKNSMKYYDDCAK | ubiquitination | [1] | 351 | KYYDDCAKILGNTIM | ubiquitination | [1] | 573 | STFRHDLKIYASDEG | ubiquitination | [1] | 765 | AELLRLSKALADVVI | ubiquitination | [1] | 813 | HEDESVNKLHPLYSR | ubiquitination | [1] |
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Reference | [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments. Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA. Mol Cell Proteomics. 2013 Mar;12(3):825-31. [ PMID: 23266961] |
Functional Description | 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. |
Sequence Annotation | NP_BIND 248 251 ATP (By similarity). NP_BIND 257 259 ATP (By similarity). NP_BIND 332 334 ATP (By similarity). REGION 64 65 Substrate binding (By similarity). REGION 224 225 Substrate binding (By similarity). REGION 337 340 Substrate binding (By similarity). REGION 382 453 Polyphosphoinositide-binding domain. BINDING 145 145 ATP (By similarity). BINDING 198 198 ATP (By similarity). BINDING 205 205 ATP (By similarity). BINDING 224 224 ATP (By similarity). BINDING 259 259 Substrate (By similarity). BINDING 273 273 Substrate (By similarity). BINDING 275 275 ATP (By similarity). BINDING 320 320 ATP (By similarity). MOD_RES 1152 1152 Phosphoserine. |
Keyword | Alternative splicing; ATP-binding; Cell membrane; Complete proteome; Cytoplasm; Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1433 AA |
Protein Sequence | MWSLTASEGE STTAHFFLGA GDEGLGTRGI GMRPEESDSE LLEDEEDEVP PEPQIIVGIC 60 AMTKKSKSKP MTQILERLCR FDYLTVVILG EDVILNEPVE NWPSCHCLIS FHSKGFPLDK 120 AVAYSKLRNP FLINDLAMQY YIQDRREVYR ILQEEGIDLP RYAVLNRDPA RPEECNLIEG 180 EDQVEVNGAV FPKPFVEKPV SAEDHNVYIY YPSSAGGGSQ RLFRKIGSRS SVYSPESSVR 240 KTGSYIYEEF MPTDGTDVKV YTVGPDYAHA EARKSPALDG KVERDSEGKE IRYPVMLTAM 300 EKLVARKVCV AFKQTVCGFD LLRANGHSFV CDVNGFSFVK NSMKYYDDCA KILGNTIMRE 360 LAPQFQIPWS IPTEAEDIPI VPTTSGTMME LRCVIAIIRH GDRTPKQKMK MEVKHPRFFA 420 LFEKHGGYKT GKLKLKRPEQ LQEVLDITRL LLAELEKEPG GEIEEKTGKL EQLKSVLEMY 480 GHFSGINRKV QLTYYPHGVK ASNEGQDPQR ETLAPSLLLV LKWGGELTPA GRVQAEELGR 540 AFRCMYPGGQ GDYAGFPGCG LLRLHSTFRH DLKIYASDEG RVQMTAAAFA KGLLALEGEL 600 TPILVQMVKS ANMNGLLDSD GDSLSSCQHR VKARLHHILQ QDAPFGPEDY DQLAPTRSTS 660 LLNSMTIIQN PVKVCDQVFA LIENLTHQIR ERMQDPRSVD LQLYHSETLE LMLQRWSKLE 720 RDFRQKSGRY DISKIPDIYD CVKYDVQHNG SLGLQGTAEL LRLSKALADV VIPQEYGISR 780 EEKLEIAVGF CLPLLRKILL DLQRTHEDES VNKLHPLYSR GVLSPGRHVR TRLYFTSESH 840 VHSLLSVFRY GGLLDETQDA QWQRALDYLS AISELNYMTQ IVIMLYEDNT QDPLSEERFH 900 VELHFSPGVK GVEEEGSAPA GCGFRPASSE NEEMKTNQGS MENLCPGKAS DEPDRALQTS 960 PQPPEGPGLP RRSPLIRNRK AGSMEVLSET SSSRPGGYRL FSSSRPPTEM KQSGLGSQCT 1020 GLFSTTVLGG SSSAPNLQDY ARSHGKKLPP ASLKHRDELL FVPAVKRFSV SFAKHPTNGG 1080 FEGCSMVPTI YPLETLHNAL SLRQVSEFLS RVCQRHTDAQ AQASAALFDS MHSSQASDNP 1140 FSPPRTLHSP PLQLQQRSEK PPWYSSGPSS TVSSAGPSSP TTVDGNSQFG FSDQPSLNSH 1200 VAEEHQGLGL LQETPGSGAQ ELSIEGEQEL FEPNQSPQVP PMETSQPYEE VSQPCQEVPD 1260 ISQPCQDISE ALSQPCQKVP DISQQCQENH DNGNHTCQEV PHISQPCQKS SQLCQKVSEE 1320 VCQLCLENSE EVSQPCQGVS VEVGKLVHKF HVGVGSLVQE TLVEVGSPAE EIPEEVIQPY 1380 QEFSVEVGRL AQETSAINLL SQGIPEIDKP SQEFPEEIDL QAQEVPEEIN 1430 |
Gene Ontology | GO:0005829; C:cytosol; IDA:UniProtKB. GO:0005634; C:nucleus; IDA:HPA. GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. GO:0003993; F:acid phosphatase activity; IEA:InterPro. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0033857; F:diphosphoinositol-pentakisphosphate kinase activity; IDA:UniProtKB. GO:0052723; F:inositol hexakisphosphate 1-kinase activity; IEA:EC. GO:0052724; F:inositol hexakisphosphate 3-kinase activity; IEA:EC. GO:0000832; F:inositol hexakisphosphate 5-kinase activity; IDA:UniProtKB. GO:0000827; F:inositol-1,3,4,5,6-pentakisphosphate kinase activity; IDA:UniProtKB. GO:0016301; F:kinase activity; IEA:UniProtKB-KW. GO:0006020; P:inositol metabolic process; IDA:UniProtKB. GO:0043647; P:inositol phosphate metabolic process; TAS:Reactome. |
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