CPLM 1.0 - Compendium of Protein Lysine Modification| Tag | Content |
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| CPLM ID | CPLM-000686 | UniProt Accession | | Genbank Protein ID | | Genbank Nucleotide ID | | Protein Name | Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2 | Protein Synonyms/Alias | Diphosphoinositol pentakisphosphate kinase 2; Histidine acid phosphatase domain-containing protein 1; InsP6 and PP-IP5 kinase 2; VIP1 homolog 2; hsVIP2 | Gene Name | PPIP5K2 | Gene Synonyms/Alias | HISPPD1; KIAA0433; VIP2 | Created Date | July 27, 2013 | Organism | Homo sapiens (Human) | NCBI Taxa ID | 9606 | Lysine Modification | Position | Peptide | Type | References |
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| 115 | DKAVAYAKLRNPFVI | ubiquitination | [1] | | 248 | PTDGTDVKVYTVGPD | acetylation | [2] | | 270 | KSPALDGKVERDSEG | acetylation | [2] |
| 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] [2] Regulation of cellular metabolism by protein lysine acetylation. Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL. Science. 2010 Feb 19;327(5968):1000-4. [ PMID: 20167786] | 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. | Sequence Annotation | NP_BIND 237 240 ATP.
NP_BIND 246 248 ATP.
NP_BIND 321 323 ATP.
REGION 53 54 Substrate binding.
REGION 213 214 Substrate binding.
REGION 326 329 Substrate binding.
REGION 371 442 Polyphosphoinositide-binding domain.
BINDING 134 134 ATP.
BINDING 187 187 ATP.
BINDING 194 194 ATP.
BINDING 213 213 ATP.
BINDING 248 248 Substrate.
BINDING 262 262 Substrate.
BINDING 264 264 ATP.
BINDING 309 309 ATP.
MOD_RES 38 38 Phosphoserine.
MOD_RES 217 217 Phosphoserine (By similarity).
MOD_RES 220 220 Phosphoserine (By similarity).
MOD_RES 1006 1006 Phosphoserine.
MOD_RES 1016 1016 Phosphoserine.
MOD_RES 1172 1172 Phosphoserine.
MOD_RES 1180 1180 Phosphoserine (By similarity). | Keyword | 3D-structure; Alternative splicing; ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Transferase. | Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL | Protein Length | 1243 AA | Protein Sequence | MSEAPRFFVG PEDTEINPGN YRHFFHHADE DDEEEDDSPP ERQIVVGICS MAKKSKSKPM 60
KEILERISLF KYITVVVFEE EVILNEPVEN WPLCDCLISF HSKGFPLDKA VAYAKLRNPF 120
VINDLNMQYL IQDRREVYSI LQAEGILLPR YAILNRDPNN PKECNLIEGE DHVEVNGEVF 180
QKPFVEKPVS AEDHNVYIYY PTSAGGGSQR LFRKIGSRSS VYSPESNVRK TGSYIYEEFM 240
PTDGTDVKVY TVGPDYAHAE ARKSPALDGK VERDSEGKEV RYPVILNARE KLIAWKVCLA 300
FKQTVCGFDL LRANGQSYVC DVNGFSFVKN SMKYYDDCAK ILGNIVMREL APQFHIPWSI 360
PLEAEDIPIV PTTSGTMMEL RCVIAVIRHG DRTPKQKMKM EVRHQKFFDL FEKCDGYKSG 420
KLKLKKPKQL QEVLDIARQL LMELGQNNDS EIEENKPKLE QLKTVLEMYG HFSGINRKVQ 480
LTYLPHGCPK TSSEEEDSRR EEPSLLLVLK WGGELTPAGR VQAEELGRAF RCMYPGGQGD 540
YAGFPGCGLL RLHSTYRHDL KIYASDEGRV QMTAAAFAKG LLALEGELTP ILVQMVKSAN 600
MNGLLDSDSD SLSSCQQRVK ARLHEILQKD RDFTAEDYEK LTPSGSISLI KSMHLIKNPV 660
KTCDKVYSLI QSLTSQIRHR MEDPKSSDIQ LYHSETLELM LRRWSKLEKD FKTKNGRYDI 720
SKIPDIYDCI KYDVQHNGSL KLENTMELYR LSKALADIVI PQEYGITKAE KLEIAKGYCT 780
PLVRKIRSDL QRTQDDDTVN KLHPVYSRGV LSPERHVRTR LYFTSESHVH SLLSILRYGA 840
LCNESKDEQW KRAMDYLNVV NELNYMTQIV IMLYEDPNKD LSSEERFHVE LHFSPGAKGC 900
EEDKNLPSGY GYRPASRENE GRRPFKIDND DEPHTSKRDE VDRAVILFKP MVSEPIHIHR 960
KSPLPRSRKT ATNDEESPLS VSSPEGTGTW LHYTSGVGTG RRRRRSGEQI TSSPVSPKSL 1020
AFTSSIFGSW QQVVSENANY LRTPRTLVEQ KQNPTVGSHC AGLFSTSVLG GSSSAPNLQD 1080
YARTHRKKLT SSGCIDDATR GSAVKRFSIS FARHPTNGFE LYSMVPSICP LETLHNALSL 1140
KQVDEFLASI ASPSSDVPRK TAEISSTALR SSPIMRKKVS LNTYTPAKIL PTPPATLKST 1200
KASSKPATSG PSSAVVPNTS SRKKNITSKT ETHEHKKNTG KKK 1243 | Gene Ontology | GO:0005829; C:cytosol; ISS:UniProtKB. GO:0003993; F:acid phosphatase activity; IEA:InterPro. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0033857; F:diphosphoinositol-pentakisphosphate kinase activity; ISS: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; ISS:UniProtKB. GO:0000827; F:inositol-1,3,4,5,6-pentakisphosphate kinase activity; ISS:UniProtKB. GO:0016301; F:kinase activity; IEA:UniProtKB-KW. GO:0006020; P:inositol metabolic process; ISS:UniProtKB. GO:0043647; P:inositol phosphate metabolic process; TAS:Reactome. | Interpro | | Pfam | | SMART | | PROSITE | | PRINTS | |
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