CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007439
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 1,3-beta-glucan synthase component GSC2 
Protein Synonyms/Alias
 1,3-beta-D-glucan-UDP glucosyltransferase; FK506 sensitivity protein 2; Glucan synthase of cerevisiae protein 2 
Gene Name
 GSC2 
Gene Synonyms/Alias
 FKS2; GLS2; YGR032W 
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
278KAKKKNKKAMQEASPubiquitination[1]
793LAIDHVQKLLYHQVPubiquitination[2]
806VPSEIEGKRTLRAPTubiquitination[2, 3, 4]
929NNEDEPEKEDALKSQubiquitination[1]
948PFYCIGFKSAAPEYTubiquitination[2]
1101NPILGDGKSDNQNHAubiquitination[2]
1566LVGDESEKSAGDASRubiquitination[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]
 [2] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047]
 [3] A proteomics approach to understanding protein ubiquitination.
 Peng J, Schwartz D, Elias JE, Thoreen CC, Cheng D, Marsischky G, Roelofs J, Finley D, Gygi SP.
 Nat Biotechnol. 2003 Aug;21(8):921-6. [PMID: 12872131]
 [4] Identification, analysis, and prediction of protein ubiquitination sites.
 Radivojac P, Vacic V, Haynes C, Cocklin RR, Mohan A, Heyen JW, Goebl MG, Iakoucheva LM.
 Proteins. 2010 Feb 1;78(2):365-80. [PMID: 19722269] 
Functional Description
 Alternate catalytic subunit of the 1,3-beta-glucan synthase (GS). Synthesizes 1,3-beta-glucan, a major structural component of the yeast cell wall. Required for spore wall assembly. Negative regulation of activity by SMK1 is important for spore wall deposition. Activity is positively regulated by RHO1. 
Sequence Annotation
 CROSSLNK 806 806 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Cell shape; Cell wall biogenesis/degradation; Complete proteome; Direct protein sequencing; Glycosyltransferase; Isopeptide bond; Membrane; Reference proteome; Sporulation; Transferase; Transmembrane; Transmembrane helix; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1895 AA 
Protein Sequence
MSYNDPNLNG QYYSNGDGTG DGNYPTYQVT QDQSAYDEYG QPIYTQNQLD DGYYDPNEQY 60
VDGTQFPQGQ DPSQDQGPYN NDASYYNQPP NMMNPSSQDG ENFSDFSSYG PPSGTYPNDQ 120
YTPSQMSYPD QDGSSGASTP YGNGVVNGNG QYYDPNAIEM ALPNDPYPAW TADPQSPLPI 180
EQIEDIFIDL TNKFGFQRDS MRNMFDHFMT LLDSRSSRMS PEQALLSLHA DYIGGDTANY 240
KKWYFAAQLD MDDEIGFRNM KLGKLSRKAR KAKKKNKKAM QEASPEDTEE TLNQIEGDNS 300
LEAADFRWKS KMNQLSPFEM VRQIALFLLC WGEANQVRFT PECLCFIYKC ASDYLDSAQC 360
QQRPDPLPEG DFLNRVITPL YRFIRSQVYE IVDGRYVKSE KDHNKVIGYD DVNQLFWYPE 420
GIAKIVMEDG TRLIDLPAEE RYLKLGEIPW DDVFFKTYKE TRSWLHLVTN FNRIWIMHIS 480
VYWMYCAYNA PTFYTHNYQQ LVDNQPLAAY KWATAALGGT VASLIQVAAT LCEWSFVPRK 540
WAGAQHLSRR FWFLCVIMGI NLGPVIFVFA YDKDTVYSTA AHVVGAVMFF VAVATLVFFS 600
VMPLGGLFTS YMKKSTRSYV ASQTFTASFA PLHGLDRWMS YLVWVTVFAA KYAESYFFLI 660
LSLRDPIRIL STTSMRCTGE YWWGNKICKV QPKIVLGLMI ATDFILFFLD TYLWYIVVNT 720
VFSVGKSFYL GISILTPWRN IFTRLPKRIY SKILATTDME IKYKPKVLIS QIWNAIIISM 780
YREHLLAIDH VQKLLYHQVP SEIEGKRTLR APTFFVSQDD NNFETEFFPR DSEAERRISF 840
FAQSLSTPIP EPLPVDNMPT FTVLTPHYAE RILLSLREII REDDQFSRVT LLEYLKQLHP 900
VEWDCFVKDT KILAEETAAY ENNEDEPEKE DALKSQIDDL PFYCIGFKSA APEYTLRTRI 960
WASLRSQTLY RTISGFMNYS RAIKLLYRVE NPEIVQMFGG NADGLERELE KMARRKFKFL 1020
VSMQRLAKFK PHELENAEFL LRAYPDLQIA YLDEEPPLNE GEEPRIYSAL IDGHCEILEN 1080
GRRRPKFRVQ LSGNPILGDG KSDNQNHALI FYRGEYIQLI DANQDNYLEE CLKIRSVLAE 1140
FEELGIEQIH PYTPGLKYED QSTNHPVAIV GAREYIFSEN SGVLGDVAAG KEQTFGTLFA 1200
RTLAQIGGKL HYGHPDFINA TFMTTRGGVS KAQKGLHLNE DIYAGMNAVL RGGRIKHCEY 1260
YQCGKGRDLG FGTILNFTTK IGAGMGEQML SREYYYLGTQ LPIDRFLTFY YAHPGFHLNN 1320
LFIQLSLQMF MLTLVNLHAL AHESILCVYD RDKPITDVLY PIGCYNFHPA IDWVRRYTLS 1380
IFIVFWIAFV PIVVQELIER GLWKATQRFF RHILSLSPMF EVFAGQIYSS ALLSDIAVGG 1440
ARYISTGRGF ATSRIPFSIL YSRFAGSAIY MGSRSMLMLL FGTVAHWQAP LLWFWASLSA 1500
LIFAPFIFNP HQFAWEDFFL DYRDYIRWLS RGNNKYHRNS WIGYVRMSRS RVTGFKRKLV 1560
GDESEKSAGD ASRAHRTNLI MAEIIPCAIY AAGCFIAFTF INAQTGVKTT DEDRVNSTLR 1620
IIICTLAPIV IDIGVLFFCM GLSCCSGPLL GMCCKKTGSV MAGIAHGIAV VVHIVFFIVM 1680
WVLEGFSFVR MLIGVVTCIQ CQRLIFHCMT VLLLTREFKN DHANTAFWTG KWYSTGLGYM 1740
AWTQPTRELT AKVIELSEFA ADFVLGHVIL IFQLPVICIP KIDKFHSIML FWLKPSRQIR 1800
PPIYSLKQAR LRKRMVRRYC SLYFLVLIIF AGCIVGPAVA SAHVPKDLGS GLTGTFHNLV 1860
QPRNVSNNDT GSQMSTYKSH YYTHTPSLKT WSTIK 1895 
Gene Ontology
 GO:0000148; C:1,3-beta-D-glucan synthase complex; IDA:SGD.
 GO:0030478; C:actin cap; TAS:SGD.
 GO:0016021; C:integral to membrane; ISM:SGD.
 GO:0005628; C:prospore membrane; IDA:SGD.
 GO:0003843; F:1,3-beta-D-glucan synthase activity; IDA:SGD.
 GO:0006075; P:(1->3)-beta-D-glucan biosynthetic process; IDA:SGD.
 GO:0030476; P:ascospore wall assembly; IMP:SGD.
 GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. 
Interpro
 IPR026899; FKS1-like_dom1.
 IPR003440; Glyco_trans_48. 
Pfam
 PF14288; FKS1_dom1
 PF02364; Glucan_synthase 
SMART
  
PROSITE
  
PRINTS