CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006182
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Fimbrin 
Protein Synonyms/Alias
 ABP67 
Gene Name
 SAC6 
Gene Synonyms/Alias
 YDR129C; YD9302.04C 
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
47QALEAVSKDGDATYDacetylation[1]
47QALEAVSKDGDATYDubiquitination[2]
61DEARETLKHVGVDASacetylation[1]
184RDGLVLSKLINDSVPubiquitination[2]
363AEKLDCRKYLTPSSLubiquitination[2]
458MPGAVDFKHVNKRPAacetylation[1]
474GAEISRFKALENTNYubiquitination[2]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [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] 
Functional Description
 Binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. 
Sequence Annotation
 DOMAIN 16 50 EF-hand 1.
 DOMAIN 51 86 EF-hand 2.
 DOMAIN 125 394 Actin-binding 1.
 DOMAIN 139 259 CH 1.
 DOMAIN 287 390 CH 2.
 DOMAIN 395 642 Actin-binding 2.
 DOMAIN 411 521 CH 3.
 DOMAIN 534 642 CH 4.  
Keyword
 Actin-binding; Calcium; Complete proteome; Metal-binding; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 642 AA 
Protein Sequence
MNIVKLQRKF PILTQEDLFS TIEKFRAIDL DDKGWVEKQQ ALEAVSKDGD ATYDEARETL 60
KHVGVDASGR VELDDYVGLV AKLRESKTGA APQTTFNVAP NSTPIVSTAA TGLQHKGKGT 120
QAKIIVAGSQ TGTTHTINEE ERREFTKHIN SVLAGDQDIG DLLPFPTDTF QLFDECRDGL 180
VLSKLINDSV PDTIDTRVLN WPKKGKELNN FQASENANIV INSAKAIGCV VVNVHSEDII 240
EGREHLILGL IWQIIRRGLL SKIDIKLHPE LYRLLEDDET LEQFLRLPPE QILLRWFNYH 300
LKQANWNRRV TNFSKDVSDG ENYTILLNQL DPALCSKAPL QTTDLMERAE QVLQNAEKLD 360
CRKYLTPSSL VAGNPKLNLA FVAHLFNTHP GLEPIQEEEK PEIEEFDAEG EREARVFTLW 420
LNSLDVDPPV ISLFDDLKDG LILLQAYEKV MPGAVDFKHV NKRPASGAEI SRFKALENTN 480
YAVDLGRAKG FSLVGIEGSD IVDGNKLLTL GLVWQLMRRN ISITMKTLSS SGRDMSDSQI 540
LKWAQDQVTK GGKNSTIRSF KDQALSNAHF LLDVLNGIAP GYVDYDLVTP GNTEEERYAN 600
ARLAISIARK LGALIWLVPE DINEVRARLI ITFIASLMTL NK 642 
Gene Ontology
 GO:0030479; C:actin cortical patch; IDA:SGD.
 GO:0032432; C:actin filament bundle; IDA:SGD.
 GO:0005934; C:cellular bud tip; IDA:SGD.
 GO:0043332; C:mating projection tip; IDA:SGD.
 GO:0005886; C:plasma membrane; IDA:SGD.
 GO:0051015; F:actin filament binding; IDA:SGD.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0030674; F:protein binding, bridging; IDA:SGD.
 GO:0007015; P:actin filament organization; IMP:SGD.
 GO:0007121; P:bipolar cellular bud site selection; TAS:SGD.
 GO:0006897; P:endocytosis; TAS:SGD.
 GO:0006970; P:response to osmotic stress; TAS:SGD. 
Interpro
 IPR001589; Actinin_actin-bd_CS.
 IPR001715; CH-domain.
 IPR011992; EF-hand-like_dom. 
Pfam
 PF00307; CH 
SMART
 SM00033; CH 
PROSITE
 PS00019; ACTININ_1
 PS00020; ACTININ_2
 PS50021; CH
 PS50222; EF_HAND_2 
PRINTS