Tag | Content |
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CPLM ID | CPLM-023284 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Inactive phospholipase C-like protein 2 |
Protein Synonyms/Alias | PLC-L(2); PLC-L2; Phospholipase C-L2; Phospholipase C-epsilon-2; PLC-epsilon-2 |
Gene Name | PLCL2 |
Gene Synonyms/Alias | KIAA1092; PLCE2 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
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131 | FSSMPTEKKISSASD | acetylation | [1] | 132 | SSMPTEKKISSASDC | acetylation | [1] | 150 | MVEGSELKKVRSNSR | acetylation | [1] |
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Reference | [1] 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 | May play an role in the regulation of Ins(1,4,5)P3 around the endoplasmic reticulum (By similarity). |
Sequence Annotation | DOMAIN 141 251 PH. DOMAIN 426 570 PI-PLC X-box. DOMAIN 618 734 PI-PLC Y-box. DOMAIN 741 846 C2. MOD_RES 2 2 N-acetylalanine. MOD_RES 17 17 Phosphoserine. MOD_RES 584 584 Phosphothreonine. MOD_RES 1113 1113 Phosphoserine. |
Keyword | Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Phosphoprotein; Polymorphism; Reference proteome; Transducer. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1127 AA |
Protein Sequence | MAECGRGGAA GGALPTSPGP ALGAKGALKA GVGEGGGGGG RLGHGRARYD SGGVSNGDCS 60 LGVSGDEARA SPTRGPRGVA LAPTPSAVVC TLPRESKPGG LPRRSSIIKD GTKQKRERKK 120 TVSFSSMPTE KKISSASDCI NSMVEGSELK KVRSNSRIYH RYFLLDADMQ SLRWEPSKKD 180 SEKAKIDIKS IKEVRTGKNT DIFRSNGISD QISEDCAFSV IYGENYESLD LVANSADVAN 240 IWVTGLRYLI SYGKHTLDML ESSQDNMRTS WVSQMFSEID VDNLGHITLC NAVQCIRNLN 300 PGLKTSKIEL KFKELHKSKD KAGTEVTKEE FIEVFHELCT RPEIYFLLVQ FSSNKEFLDT 360 KDLMMFLEAE QGVAHINEEI SLEIIHKYEP SKEGQEKGWL SIDGFTNYLM SPDCYIFDPE 420 HKKVCQDMKQ PLSHYFINSS HNTYLIEDQF RGPSDITGYI RALKMGCRSV ELDVWDGPDN 480 EPVIYTGHTM TSQIVFRSVI DIINKYAFFA SEYPLILCLE NHCSIKQQKV MVQHMKKLLG 540 DKLYTTSPNV EESYLPSPDV LKGKILIKAK KLSSNCSGVE GDVTDEDEGA EMSQRMGKEN 600 MEQPNNVPVK RFQLCKELSE LVSICKSVQF KEFQVSFQVQ KYWEVCSFNE VLASKYANEN 660 PGDFVNYNKR FLARVFPSPM RIDSSNMNPQ DFWKCGCQIV AMNFQTPGLM MDLNIGWFRQ 720 NGNCGYVLRP AIMREEVSFF SANTKDSVPG VSPQLLHIKI ISGQNFPKPK GSGAKGDVVD 780 PYVYVEIHGI PADCAEQRTK TVHQNGDAPI FDESFEFQIN LPELAMVRFV VLDDDYIGDE 840 FIGQYTIPFE CLQTGYRHVP LQSLTGEVLA HASLFVHVAI TNRRGGGKPH KRGLSVRKGK 900 KSREYASLRT LWIKTVDEVF KNAQPPIRDA TDLRENMQNA VVSFKELCGL SSVANLMQCM 960 LAVSPRFLGP DNTPLVVLNL SEQYPTMELQ GIVPEVLKKI VTTYDMMIQS LKALIENADA 1020 VYEKIVHCQK AAMEFHEHLH SIGTKEGLKE RKLQKAVESF TWNITILKGQ ADLLKYAKNE 1080 TLENLKQIHF AAVSCGLNKP GTENADVQKP RRSLEVIPEK ANDETGE 1127 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0005509; F:calcium ion binding; IEA:InterPro. GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:InterPro. GO:0005543; F:phospholipid binding; IEA:InterPro. GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW. GO:0035556; P:intracellular signal transduction; IEA:InterPro. GO:0006629; P:lipid metabolic process; IEA:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |