CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011514
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Seventh homolog of septin 1 
Protein Synonyms/Alias
 Septation protein 7 
Gene Name
 SHS1 
Gene Synonyms/Alias
 SEP7; YDL225W 
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
57PHKYQYGKSNASISSacetylation[1]
57PHKYQYGKSNASISSubiquitination[2]
82KVVSFNSKNGIPSYVacetylation[1]
204EVDVELMKSISKYTNacetylation[1]
321GSHLQEFKDTTQNLLubiquitination[2]
352EIGPNSTKRQSNAPSacetylation[1]
352EIGPNSTKRQSNAPSubiquitination[2]
426RQLGREIKQENENLIsumoylation[3, 4]
426RQLGREIKQENENLIubiquitination[2, 4]
437ENLIRSIKTESSPKFsumoylation[3, 4]
437ENLIRSIKTESSPKFubiquitination[4]
443IKTESSPKFLNSPDLacetylation[1]
478RILARQQKLEELEAQacetylation[1]
478RILARQQKLEELEAQubiquitination[2]
488ELEAQSAKELQKRIQacetylation[1, 5]
488ELEAQSAKELQKRIQubiquitination[2]
536STRSQIKKNDTYTDLacetylation[1]
536STRSQIKKNDTYTDLubiquitination[2]
Reference
 [1] Regulation of septin dynamics by the Saccharomyces cerevisiae lysine acetyltransferase NuA4.
 Mitchell L, Lau A, Lambert JP, Zhou H, Fong Y, Couture JF, Figeys D, Baetz K.
 PLoS One. 2011;6(10):e25336. [PMID: 21984913]
 [2] 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]
 [3] Sumoylation of topoisomerase I is involved in its partitioning between nucleoli and nucleoplasm and its clearing from nucleoli in response to camptothecin.
 Rallabhandi P, Hashimoto K, Mo YY, Beck WT, Moitra PK, D'Arpa P.
 J Biol Chem. 2002 Oct 18;277(42):40020-6. [PMID: 12149243]
 [4] Cytoplasmic sumoylation by PIAS-type Siz1-SUMO ligase.
 Takahashi Y, Iwase M, Strunnikov AV, Kikuchi Y.
 Cell Cycle. 2008 Jun 15;7(12):1738-44. [PMID: 18583943]
 [5] mChIP-KAT-MS, a method to map protein interactions and acetylation sites for lysine acetyltransferases.
 Mitchell L, Huard S, Cotrut M, Pourhanifeh-Lemeri R, Steunou AL, Hamza A, Lambert JP, Zhou H, Ning Z, Basu A, Côté J, Figeys DA, Baetz K.
 Proc Natl Acad Sci U S A. 2013 Apr 23;110(17):E1641-50. [PMID: 23572591
Functional Description
 Septins are GTPases involved in cytokinesis that assemble early in the cell cycle as a patch at the incipient bud site and form a ring approximate 15 min before bud emergence, which transforms into an hour-glass shaped collar of cortical filaments that spans both sides of the mother-bud neck. This collar persists until just before cytokinesis, when it splits into two rings that occupy opposite sides of the neck. The septins at the bud neck serve as a structural scaffold that recruits different components involved in diverse processes at specific stages during the cell cycle. Many proteins bind asymmetrically to the septin collar. The septin assembly is regulated by protein kinases GIN4 and/or CLA4. May act by recruiting MYO1 and HOF1, a protein involved in septation, to the site of cleavage. Septins are also involved in cell morphogenesis, bud site selection, chitin deposition, cell cycle regulation, cell compartmentalization and spore wall formation. 
Sequence Annotation
 NP_BIND 30 37 GTP (By similarity).
 NP_BIND 218 226 GTP (By similarity).
 BINDING 138 138 GTP; via amide nitrogen (By similarity).
 BINDING 288 288 GTP (By similarity).
 MOD_RES 400 400 Phosphotyrosine.
 MOD_RES 408 408 Phosphoserine.
 MOD_RES 416 416 Phosphoserine.
 MOD_RES 447 447 Phosphoserine.
 MOD_RES 460 460 Phosphoserine.
 MOD_RES 519 519 Phosphoserine.
 MOD_RES 520 520 Phosphoserine.
 MOD_RES 522 522 Phosphoserine.
 MOD_RES 525 525 Phosphoserine.
 MOD_RES 539 539 Phosphothreonine.
 MOD_RES 545 545 Phosphoserine.
 MOD_RES 548 548 Phosphoserine.
 CROSSLNK 426 426 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 437 437 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Cell cycle; Cell division; Coiled coil; Complete proteome; GTP-binding; Isopeptide bond; Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 551 AA 
Protein Sequence
MSTASTPPIN LFRRKKEHKR GITYTMLLCG PAGTGKTAFA NNLLETKIFP HKYQYGKSNA 60
SISSNPEVKV IAPTKVVSFN SKNGIPSYVS EFDPMRANLE PGITITSTSL ELGGNKDQGK 120
PEMNEDDTVF FNLIMTHGIG ENLDDSLCSE EVMSYLEQQF DIVLAEETRI KRNPRFEDTR 180
VHVALYFIEP TGHGLREVDV ELMKSISKYT NVLPIITRAD SFTKEELTQF RKNIMFDVER 240
YNVPIYKFEV DPEDDDLESM EENQALASLQ PFAIITSDTR DSEGRYVREY PWGIISIDDD 300
KISDLKVLKN VLFGSHLQEF KDTTQNLLYE NYRSEKLSSV ANAEEIGPNS TKRQSNAPSL 360
SNFASLISTG QFNSSQTLAN NLRADTPRNQ VSGNFKENEY EDNGEHDSAE NEQEMSPVRQ 420
LGREIKQENE NLIRSIKTES SPKFLNSPDL PERTKLRNIS ETVPYVLRHE RILARQQKLE 480
ELEAQSAKEL QKRIQELERK AHELKLREKL INQNKLNGSS SSINSLQQST RSQIKKNDTY 540
TDLASIASGR D 551 
Gene Ontology
 GO:0000144; C:cellular bud neck septin ring; IDA:SGD.
 GO:0043332; C:mating projection tip; IDA:SGD.
 GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
 GO:0031105; C:septin complex; IEA:InterPro.
 GO:0005525; F:GTP binding; IDA:SGD.
 GO:0000917; P:barrier septum assembly; IMP:SGD.
 GO:0032186; P:cellular bud neck septin ring organization; IMP:SGD.
 GO:0000915; P:cytokinesis, actomyosin contractile ring assembly; IMP:SGD.
 GO:0010458; P:exit from mitosis; IMP:SGD.
 GO:0000921; P:septin ring assembly; IGI:SGD. 
Interpro
 IPR000038; Cell_div_GTP-bd.
 IPR027417; P-loop_NTPase.
 IPR016491; Septin. 
Pfam
 PF00735; Septin 
SMART
  
PROSITE
  
PRINTS