| Tag | Content |
|---|
| CPLM ID | CPLM-006526 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Rho-GTPase-activating protein LRG1 |
Protein Synonyms/Alias | LIM-RhoGAP protein 1 |
Gene Name | LRG1 |
Gene Synonyms/Alias | YDL240W |
Created Date | July 27, 2013 |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
NCBI Taxa ID | 559292 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 582 | PTKQGDSKNLVIQTD | ubiquitination | [1] | | 998 | DYSECDIKTPVTVKD | ubiquitination | [1] |
|
Reference | [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J. Nat Methods. 2013 Jul;10(7):676-82. [ PMID: 23749301] |
Functional Description | Acts in signal transduction. Activates CDC42, RHO1 and RHO2. Negatively regulates 1,3-beta-glucan synthesis. May be responsible for the down-regulation of CDC42 during mating. |
Sequence Annotation | DOMAIN 28 88 LIM zinc-binding 1.
DOMAIN 98 148 LIM zinc-binding 2.
DOMAIN 155 184 LIM zinc-binding 3; truncated.
DOMAIN 419 474 LIM zinc-binding 4.
DOMAIN 730 953 Rho-GAP.
MOD_RES 562 562 Phosphoserine. |
Keyword | Complete proteome; Cytoplasm; GTPase activation; LIM domain; Metal-binding; Phosphoprotein; Reference proteome; Repeat; Sporulation; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1017 AA |
Protein Sequence | MIQNSAGYRS LNTASPMTVQ VKNQKKICAR CNKLVIPDSQ RTKTTLKALG KYYHESCFTC 60
QDCQKPLKPK YFPYQVDKTS ESILLCQYDY FRRHNLLCHV CDTPLRGLYY TAFGYRYDEE 120
HFSCTICATP CGVKKCFMYG NQLYCKYHFL KYFSKRCKGC EFPISDQYIE FPKGEEIHCW 180
HPECYGIHKY WHVNLAAETV GLQYLPKLEY NPNSGDKDIN PTAYELDKQM QAFNFILSKT 240
WSVLYRFEEE AASCISDMFQ YLTSNDQLKG IESTGLLVLK IDCLFRGLDT LNLSTNKSMP 300
VNSDQECIEN NAMAASKYSK FPKNLSTKIM IYLQLLRKLG TENKNETITI SSFMSVITGL 360
AHFLKLLTRF GLYTALENNK LTHSVNPLLR FLREVEKNEL FENNPFQYIK TPVNATDSCA 420
GCNKYIQEEC IQFYEHRWHI ACFTCSSCHK NINPRSLTDP TFNKEKKKIL CSHCSIDDPA 480
SVPGFKFVTK LAQLIFLLKI ALVKSRTVML KSKASNKVGR NSLQSTMLKE QTYIRTLNDI 540
KRLRSRRESV RVTHNKQQAR KSVILETAET DLNDPTKQGD SKNLVIQTDD PSSSQQVSTR 600
ENVFSNTKTL TLDDISRIVA AEQARELRPN AFAHFKKLKE TDDETSNVVP KKSGVYYSEL 660
STMELSMIRA ISLSLLAGKQ LISKTDPNYT SLVSMVFSNE KQVTGSFWNR MKIMMSMEPK 720
KPITKTVFGA PLDVLCEKWG VDSDLGVGPV KIRIPIIIDE LISSLRQMDM SVEGIFRKNG 780
NIRRLRELTA NIDSNPTEAP DFSKENAIQL SALLKKFIRE LPQPILSTDL YELWIKAAKI 840
DLEDEKQRVI LLIYSLLPTY NRNLLEALLS FLHWTSSFSY IENEMGSKMD IHNLSTVITP 900
NILYLRHKEI SNDNVPDEPE SGLVDSFAQN KGENYFLAIE IVDYLITHNE EMAMVPKFLM 960
NLLKDVQLQK LDNYESINHF ISTVMQSKTI DYSECDIKTP VTVKDSTTTV IQGEINK 1017 |
Gene Ontology | GO:0005935; C:cellular bud neck; IDA:SGD. GO:0005739; C:mitochondrion; IDA:SGD. GO:0005100; F:Rho GTPase activator activity; IDA:SGD. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0009272; P:fungal-type cell wall biogenesis; IGI:SGD. GO:0007264; P:small GTPase mediated signal transduction; IPI:SGD. GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |