CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011835
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Actin-like protein ARP8 
Protein Synonyms/Alias
  
Gene Name
 ARP8 
Gene Synonyms/Alias
 YOR141C; YOR3348C 
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
844NPALIIWKGASVLAQubiquitination[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
 Probably involved in transcription regulation via its interaction with the INO80 complex, a chromatin remodeling complex. Exhibits low basal ATPase activity, and unable to polymerize. Strongly prefer nucleosomes and H3-H4 tetramers over H2A-H2B dimers, suggesting it may act as a nucleosome recognition module within the complex. 
Sequence Annotation
 NP_BIND 502 505 ATP (By similarity).
 MOD_RES 65 65 Phosphoserine.
 MOD_RES 70 70 Phosphoserine.  
Keyword
 3D-structure; ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 881 AA 
Protein Sequence
MSQEEAESSI IYEEPIDIPL EDDDDEDELE EENSVPLSSQ ADQENAENES DDSVDNVVGS 60
ETPRSVTGLS VDPRDVADEE DEDEEGEDED EDEDDNDVDN EDENDNDNAN ENENELGSSR 120
DKRAPPAVQT SKRYKKYPKL DPAKAPPGKK VPLHLLEKRR LGRIKAAEEF AKTLKKIGIE 180
KVETTTLPAT GLFQPLMLIN QKNYSSDYLK KDDQIFALRD RKFLRNNNTS QISSTNTPDV 240
IDLKSLPHSE ASAAPLNDEI DLNDPTATIV IHPGSNSIKI GFPKDDHPVV VPNCVAVPKK 300
WLDLENSEHV ENVCLQREQS EEFNNIKSEM EKNFRERMRY YKRKVPGNAH EQVVSFNENS 360
KPEIISEKND PSPIEWIFDD SKLYYGSDAL RCVDEKFVIR KPFRGGSFNV KSPYYKSLAE 420
LISDVTKLLE HALNSETLNV KPTKFNQYKV VLVIPDIFKK SHVETFIRVL LTELQFQAVA 480
IIQESLATCY GAGISTSTCV VNIGAAETRI ACVDEGTVLE HSAITLDYGG DDITRLFALF 540
LLQSDFPLQD WKIDSKHGWL LAERLKKNFT TFQDADVAVQ LYNFMNRSPN QPTEKYEFKL 600
FDEVMLAPLA LFFPQIFKLI RTSSHKNSSL EFQLPESRDL FTNELNDWNS LSQFESKEGN 660
LYCDLNDDLK ILNRILDAHN IIDQLQDKPE NYGNTLKENF APLEKAIVQS IANASITADV 720
TRMNSFYSNI LIVGGSSKIP ALDFILTDRI NIWRPSLLSS ASFPQFYKKL TKEIKDLEGH 780
YVNAPDKTED ENKQILQAQI KEKIVEELEE QHQNIEHQNG NEHIFPVSII PPPRDMNPAL 840
IIWKGASVLA QIKLVEELFI TNSDWDVHGS RILQYKCIFT Y 881 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0031011; C:Ino80 complex; IPI:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003729; F:mRNA binding; IDA:SGD.
 GO:0006338; P:chromatin remodeling; IMP:SGD.
 GO:0006312; P:mitotic recombination; IMP:SGD.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006974; P:response to DNA damage stimulus; IMP:SGD.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR004000; Actin-related. 
Pfam
 PF00022; Actin 
SMART
 SM00268; ACTIN 
PROSITE
  
PRINTS