| Tag | Content |
|---|
| CPLM ID | CPLM-002660 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 |
Protein Synonyms/Alias | PLC-148; Phosphoinositide phospholipase C-gamma-1; Phospholipase C-II; PLC-II; Phospholipase C-gamma-1; PLC-gamma-1 |
Gene Name | PLCG1 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Bos taurus (Bovine) |
NCBI Taxa ID | 9913 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 389 | HTLTTKIKFSDVLHT | ubiquitination | [1] | | 941 | DARLTEGKMMERRKK | ubiquitination | [2] |
|
Reference | [1] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties. Chen Z, Zhou Y, Song J, Zhang Z. Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [ PMID: 23603789] [2] 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 | Mediates the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). Plays an important role in the regulation of intracellular signaling cascades. Becomes activated in response to ligand- mediated activation of receptor-type tyrosine kinases, such as PDGFRA, PDGFRB, FGFR1, FGFR2, FGFR3 and FGFR4. Plays a role in actin reorganization and cell migration (By similarity). |
Sequence Annotation | DOMAIN 27 142 PH 1.
DOMAIN 152 187 EF-hand.
DOMAIN 320 464 PI-PLC X-box.
DOMAIN 489 523 PH 2; first part.
DOMAIN 550 657 SH2 1.
DOMAIN 668 756 SH2 2.
DOMAIN 791 851 SH3.
DOMAIN 895 931 PH 2; second part.
DOMAIN 953 1070 PI-PLC Y-box.
DOMAIN 1075 1177 C2.
ACT_SITE 335 335 By similarity.
ACT_SITE 380 380 By similarity.
MOD_RES 2 2 N-acetylalanine (By similarity).
MOD_RES 379 379 Phosphotyrosine (By similarity).
MOD_RES 481 481 Phosphotyrosine (By similarity).
MOD_RES 506 506 Phosphotyrosine (By similarity).
MOD_RES 771 771 Phosphotyrosine; by SYK.
MOD_RES 775 775 Phosphotyrosine (By similarity).
MOD_RES 783 783 Phosphotyrosine; alternate.
MOD_RES 783 783 Phosphotyrosine; by ITK, SYK and TXK;
MOD_RES 977 977 Phosphotyrosine (By similarity).
MOD_RES 1222 1222 Phosphoserine (By similarity).
MOD_RES 1249 1249 Phosphoserine (By similarity).
MOD_RES 1254 1254 Phosphotyrosine.
MOD_RES 1264 1264 Phosphoserine (By similarity). |
Keyword | 3D-structure; Acetylation; Calcium; Cell projection; Complete proteome; Direct protein sequencing; Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding; Phosphoprotein; Reference proteome; Repeat; SH2 domain; SH3 domain; Transducer; Ubl conjugation. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1291 AA |
Protein Sequence | MAGAASPCAN GCGPSAPSDA EVVHLCRSLE VGTVMTLFYS KKSQRPERKT FQVKLETRQI 60
TWSRGADKIE GAIDIREIKE IRPGKTSRDF DRYQEDPAFR PDQSHCFVIL YGMEFRLKTL 120
SLQATSEDEV NMWIRGLTWL MEDTLQAATP LQIERWLRKQ FYSVDRNRED RISAKDLKNM 180
LSQVNYRVPN MRFLRERLTD LEQRTSDITY GQFAQLYRSL MYSAQKTMDL PFLEASALRA 240
GERPELCRVS LPEFQQFLLE YQGELWAVDR LQVQEFMLSF LRDPLREIEE PYFFLDEFVT 300
FLFSKENSIW NSQLDEVCPD TMNNPLSHYW ISSSHNTYLT GDQFSSESSL EAYARCLRMG 360
CRCIELDCWD GPDGMPVIYH GHTLTTKIKF SDVLHTIKEH AFVASEYPVI LSIEDHCSIA 420
QQRNMAQYFK KVLGDTLLTK PVDIAADGLP SPNQLKRKIL IKHKKLAEGS AYEEVPTSVM 480
YSENDISNSI KNGILYLEDP VNHEWYPHYF VLTSSKIYYS EETSSDQGNE DEEEPKEASG 540
STELHSNEKW FHGKLGAGRD GRHIAERLLT EYCIETGAPD GSFLVRESET FVGDYTLSFW 600
RNGKVQHCRI HSRQDAGTPK FFLTDNLVFD SLYDLITHYQ QVPLRCNEFE MRLSEPVPQT 660
NAHESKEWYH ASLTRAQAEH MLMRVPRDGA FLVRKRNEPN SYAISFRAEG KIKHCRVQQE 720
GQTVMLGNSE FDSLVDLISY YEKHPLYRKM KLRYPINEEA LEKIGTAEPD YGALYEGRNP 780
GFYVEANPMP TFKCAVKALF DYKAQREDEL TFTKSAIIQN VEKQEGGWWR GDYGGKKQLW 840
FPSNYVEEMV SPAALEPERE HLDENSPLGD LLRGVLDVPA CQIAVRPEGK NNRLFVFSIS 900
MASVAHWSLD VAADSQEELQ DWVKKIREVA QTADARLTEG KMMERRKKIA LELSELVVYC 960
RPVPFDEEKI GTERACYRDM SSFPETKAEK YVNKAKGKKF LQYNRLQLSR IYPKGQRLDS 1020
SNYDPLPMWI CGSQLVALNF QTPDKPMQMN QALFLAGGHC GYVLQPSVMR DEAFDPFDKS 1080
SLRGLEPCAI CIEVLGARHL PKNGRGIVCP FVEIEVAGAE YDSIKQKTEF VVDNGLNPVW 1140
PAKPFHFQIS NPEFAFLRFV VYEEDMFSDQ NFLAQATFPV KGLKTGYRAV PLKNNYSEGL 1200
ELASLLVKID VFPAKQENGD LSPFGGASLR ERSCDASGPL FHGRAREGSF EARYQQPFED 1260
FRISQEHLAD HFDGRDRRTP RRTRVNGDNR L 1291 |
Gene Ontology | GO:0030027; C:lamellipodium; ISS:UniProtKB. GO:0001726; C:ruffle; ISS:UniProtKB. GO:0008180; C:signalosome; ISS:UniProtKB. GO:0005509; F:calcium ion binding; IEA:InterPro. GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:EC. GO:0005543; F:phospholipid binding; IEA:InterPro. GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW. GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB. GO:0001701; P:in utero embryonic development; ISS:AgBase. GO:0035556; P:intracellular signal transduction; IEA:InterPro. GO:0009395; P:phospholipid catabolic process; IEA:InterPro. GO:0010634; P:positive regulation of epithelial cell migration; ISS:UniProtKB. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |