| Tag | Content |
|---|
| CPLM ID | CPLM-012505 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-4 |
Protein Synonyms/Alias | Phosphoinositide phospholipase C-beta-4; Phospholipase C-beta-4; PLC-beta-4 |
Gene Name | PLCB4 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 113 | LFPFYDAKRAMQIIE | ubiquitination | [1] | | 869 | EIVAQHTKEWSEMIN | ubiquitination | [1] |
|
Reference | [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization. Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW. Nature. 2013 Apr 18;496(7445):372-6. [ PMID: 23503661] |
Functional Description | The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. This form has a role in retina signal transduction. |
Sequence Annotation | DOMAIN 313 463 PI-PLC X-box.
DOMAIN 565 681 PI-PLC Y-box.
DOMAIN 688 786 C2.
ACT_SITE 328 328 By similarity.
ACT_SITE 375 375 By similarity.
MOD_RES 2 2 N-acetylalanine.
MOD_RES 886 886 Phosphothreonine. |
Keyword | Acetylation; Alternative splicing; Calcium; Complete proteome; Direct protein sequencing; Disease mutation; Hydrolase; Lipid degradation; Lipid metabolism; Phosphoprotein; Polymorphism; Reference proteome; Transducer. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1175 AA |
Protein Sequence | MNNNWNVCFF LFCPSITRTF ASGKTEKVIF QALKELGLPS GKNDEIEPTA FSYEKFYELT 60
QKICPRTDIE DLFKKINGDK TDYLTVDQLV SFLNEHQRDP RLNEILFPFY DAKRAMQIIE 120
MYEPDEDLKK KGLISSDGFC RYLMSDENAP VFLDRLELYQ EMDHPLAHYF ISSSHNTYLT 180
GRQFGGKSSV EMYRQVLLAG CRCVELDCWD GKGEDQEPII THGKAMCTDI LFKDVIQAIK 240
ETAFVTSEYP VILSFENHCS KYQQYKMSKY CEDLFGDLLL KQALESHPLE PGRALPSPND 300
LKRKILIKNK RLKPEVEKKQ LEALRSMMEA GESASPANIL EDDNEEEIES ADQEEEAHPE 360
FKFGNELSAD DLGHKEAVAN SVKKGLVTVE DEQAWMASYK YVGATTNIHP YLSTMINYAQ 420
PVKFQGFHVA EERNIHYNMS SFNESVGLGY LKTHAIEFVN YNKRQMSRIY PKGGRVDSSN 480
YMPQIFWNAG CQMVSLNYQT PDLAMQLNQG KFEYNGSCGY LLKPDFMRRP DRTFDPFSET 540
PVDGVIAATC SVQVISGQFL SDKKIGTYVE VDMYGLPTDT IRKEFRTRMV MNNGLNPVYN 600
EESFVFRKVI LPDLAVLRIA VYDDNNKLIG QRILPLDGLQ AGYRHISLRN EGNKPLSLPT 660
IFCNIVLKTY VPDGFGDIVD ALSDPKKFLS ITEKRADQMR AMGIETSDIA DVPSDTSKND 720
KKGKANTAKA NVTPQSSSEL RPTTTAALAS GVEAKKGIEL IPQVRIEDLK QMKAYLKHLK 780
KQQKELNSLK KKHAKEHSTM QKLHCTQVDK IVAQYDKEKS THEKILEKAM KKKGGSNCLE 840
MKKETEIKIQ TLTSDHKSKV KEIVAQHTKE WSEMINTHSA EEQEIRDLHL SQQCELLKKL 900
LINAHEQQTQ QLKLSHDRES KEMRAHQAKI SMENSKAISQ DKSIKNKAER ERRVRELNSS 960
NTKKFLEERK RLAMKQSKEM DQLKKVQLEH LEFLEKQNEQ AKEMQQMVKL EAEMDRRPAT 1020
VV 1022 |
Gene Ontology | GO:0005829; C:cytosol; TAS:Reactome. GO:0005634; C:nucleus; IEA:Compara. GO:0014069; C:postsynaptic density; IEA:Compara. GO:0005790; C:smooth endoplasmic reticulum; IEA:Compara. GO:0005509; F:calcium ion binding; IEA:InterPro. GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:EC. GO:0004629; F:phospholipase C activity; TAS:ProtInc. GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW. GO:0043647; P:inositol phosphate metabolic process; TAS:Reactome. GO:0035556; P:intracellular signal transduction; IEA:InterPro. GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |