| Tag | Content |
|---|
| CPLM ID | CPLM-024366 |
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; InsP6 and PP-IP5 kinase 1; VIP1 homolog |
Gene Name | Ppip5k1 |
Gene Synonyms/Alias | Hisppd2a; Kiaa0377; Vip1 |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 241 | SPESSVRKTGSYIYE | ubiquitination | [1] | | 573 | STFRHDLKIYASDEG | ubiquitination | [1] | | 813 | HEDESVNKLHPLYSR | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
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 (By similarity). |
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 (By
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 1147 1147 Phosphoserine (By similarity). |
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 | 1436 AA |
Protein Sequence | MWSLTANEDE STTAHFFLGA GDEGLGTCGI GMRTEESDSE LLEDEEDEVP PEPQIIVGIC 60
AMTKKSKSKP MTQILERLCR FDYLTVVILG EDVILNEPVE NWPSCHCLIS FHSKGFPLDK 120
AVAYSKLRNP FLINDLAMQY YIQDRREVYR ILQEEGIDLP RYAVLNRDPA CPEECSLIEG 180
EDQVEVNGAV FPKPFVEKPV SAEDHNVYIY YPSSAGGGSQ RLFRKIGSRS SVYSPESSVR 240
KTGSYIYEEF MPTDGTDVKV YTVGPDYAHA EARKSPALDG KVERDSEGKE VRYPVMLTAM 300
EKLVARKVCV AFKQTVCGFD LLRANGHSFV CDVNGFSFVK NSMKYYDDCA KILGNTIMRE 360
LAPQFQIPWS IPTEAEDIPI VPTTSGTMME LRCVIAIIRH GDRTPKQKMK MEVTHPRFFA 420
LFEKHGGYKT GKLKLKRPEQ LQEVLDITRL LLAELEKEPE AEIEEKTGKL EQLKSVLEMY 480
GHFSGINRKV QLTYYPHGVK ASNEGQDLQR EPLAPSLLLV LKWGGELTPD GRVQAEELGR 540
AFRCMYPGGQ GDYAGFPGCG LLRLHSTFRH DLKIYASDEG RVQMTAAAFA KGLLALEGEL 600
TPILVQMVKS ANMNGLLDSD SDSLSSCQHR VKARLHHILQ QDAPFGPEDY DQLAPTGSTS 660
LLNSMSVIQN PVKVCDQVFA LIENLTHQIR ERMQDPSSVD LQLYHSETLE LMLQRWSKLE 720
RDFRQKSGRY DISKIPDIYD CVKYDVQHNG SLGLQGTAEL LRLSKALADV VIPQEYGISR 780
EEKVEIAVGF CLPLLRKILL DLQRTHEDES VNKLHPLYSR GVLSPGRHVR TRLYFTSESH 840
VHSLLSVFRY GGLLDETQDA QWQRALAYLS AISELNYMTQ IVIMLYEDNT RDPLSEERFH 900
VELHFSPGVK GVEEGSAPAG CGFRPASSEN EEMKTDPGSI ENLCPGKASD EPDRALQTSP 960
QPVEGTGLPR RSPLIRNRKA GSMEVLSETS SSRPGGYRLF SSSRPPTEMK QSGLGSQCTG 1020
LFSTTVLGGS SSAPNLQDYA RTHGKKLPPA SLKHRDELLF VPAVKRFSVS FAKHPTNGFE 1080
GCSMVPTIYP LETLHNALSL RQVSEFLTKV CQRHTDAHAQ ASAALFDSMH NHQASDSPFS 1140
PPRTLHSPPL QLRHRSEKPP WYSSGPSSTV SSAGPSSPTT VDGNSHFGFS DQSSVNIHMT 1200
EEKQGFGLLQ ETPGDGTREL HIERQQELVE PAQSPQELPV EICPSGSQGV TKVSQTCQEV 1260
PDIVQPCHNI HEEIGQPQQE VPDISQLLLK DHDTTTNTCH LCQASQLSQK VCEEICQLCQ 1320
DNHEESNQLC QEVSVKLGRM VHGFPVNVDS TAQETLMEIG RPTQEIPEDP YQEFSVKVGV 1380
LAQKAPAISE LSQDIPEADK PSQELSEETE LQAQEVSEEI DQESEVVDEL PPEAIS 1436 |
Gene Ontology | GO:0005829; C:cytosol; ISS:UniProtKB. GO:0005634; C:nucleus; IEA:Compara. 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; 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. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |