CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022028
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Actin-binding protein anillin 
Protein Synonyms/Alias
  
Gene Name
 ANLN 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
371TPGGTGIKPFLERFGacetylation[1, 2]
491QSLPVTEKVTENQIPacetylation[2]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377
Functional Description
 Required for cytokinesis. Essential for the structural integrity of the cleavage furrow and for completion of cleavage furrow ingression. 
Sequence Annotation
 DOMAIN 983 1107 PH.
 REGION 1 230 Nuclear localization.
 REGION 1 155 Interaction with CD2AP.
 REGION 1 45 Required for ubiquitination.
 REGION 231 676 Interaction with F-actin.
 REGION 730 1124 Localization to the cleavage furrow.
 MOD_RES 54 54 Phosphoserine.
 MOD_RES 72 72 Phosphoserine.
 MOD_RES 102 102 Phosphoserine.
 MOD_RES 172 172 Phosphoserine.
 MOD_RES 182 182 Phosphoserine.
 MOD_RES 194 194 Phosphothreonine.
 MOD_RES 320 320 Phosphothreonine.
 MOD_RES 323 323 Phosphoserine.
 MOD_RES 364 364 Phosphothreonine.
 MOD_RES 371 371 N6-acetyllysine.
 MOD_RES 397 397 Phosphothreonine.
 MOD_RES 401 401 Phosphothreonine.
 MOD_RES 449 449 Phosphoserine.
 MOD_RES 485 485 Phosphoserine.
 MOD_RES 515 515 Phosphothreonine (By similarity).
 MOD_RES 518 518 Phosphoserine.
 MOD_RES 553 553 Phosphoserine.
 MOD_RES 561 561 Phosphoserine.
 MOD_RES 642 642 Phosphoserine.
 MOD_RES 658 658 Phosphoserine.
 MOD_RES 661 661 Phosphoserine.
 MOD_RES 664 664 Phosphoserine.
 MOD_RES 792 792 Phosphoserine.
 MOD_RES 927 927 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Actin-binding; Alternative splicing; Cell cycle; Cell division; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Mitosis; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1124 AA 
Protein Sequence
MDPFTEKLLE RTRARRENLQ RKMAERPTAA PRSMTHAKRA RQPLSEASNQ QPLSGGEEKS 60
CTKPSPSKKR CSDNTEVEVS NLENKQPVES TSAKSCSPSP VSPQVQPQAA DTISDSVAVP 120
ASLLGMRRGL NSRLEATAAS SVKTRMQKLA EQRRRWDNDD MTDDIPESSL FSPMPSEEKA 180
ASPPRPLLSN ASATPVGRRG RLANLAATIC SWEDDVNHSF AKQNSVQEQP GTACLSKFSS 240
ASGASARINS SSVKQEATFC SQRDGDASLN KALSSSADDA SLVNASISSS VKATSPVKST 300
TSITDAKSCE GQNPELLPKT PISPLKTGVS KPIVKSTLSQ TVPSKGELSR EICLQSQSKD 360
KSTTPGGTGI KPFLERFGER CQEHSKESPA RSTPHRTPII TPNTKAIQER LFKQDTSSST 420
THLAQQLKQE RQKELACLRG RFDKGNIWSA EKGGNSKSKQ LETKQETHCQ STPLKKHQGV 480
SKTQSLPVTE KVTENQIPAK NSSTEPKGFT ECEMTKSSPL KITLFLEEDK SLKVTSDPKV 540
EQKIEVIREI EMSVDDDDIN SSKVINDLFS DVLEEGELDM EKSQEEMDQA LAESSEEQED 600
ALNISSMSLL APLAQTVGVV SPESLVSTPR LELKDTSRSD ESPKPGKFQR TRVPRAESGD 660
SLGSEDRDLL YSIDAYRSQR FKETERPSIK QVIVRKEDVT SKLDEKNNAF PCQVNIKQKM 720
QELNNEINMQ QTVIYQASQA LNCCVDEEHG KGSLEEAEAE RLLLIATGKR TLLIDELNKL 780
KNEGPQRKNK ASPQSEFMPS KGSVTLSEIR LPLKADFVCS TVQKPDAANY YYLIILKAGA 840
ENMVATPLAS TSNSLNGDAL TFTTTFTLQD VSNDFEINIE VYSLVQKKDP SGLDKKKKTS 900
KSKAITPKRL LTSITTKSNI HSSVMASPGG LSAVRTSNFA LVGSYTLSLS SVGNTKFVLD 960
KVPFLSSLEG HIYLKIKCQV NSSVEERGFL TIFEDVSGFG AWHRRWCVLS GNCISYWTYP 1020
DDEKRKNPIG RINLANCTSR QIEPANREFC ARRNTFELIT VRPQREDDRE TLVSQCRDTL 1080
CVTKNWLSAD TKEERDLWMQ KLNQVLVDIR LWQPDACYKP IGKP 1124 
Gene Ontology
 GO:0005826; C:actomyosin contractile ring; IDA:MGI.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0003779; F:actin binding; IDA:MGI.
 GO:0005543; F:phospholipid binding; IEA:InterPro.
 GO:0000910; P:cytokinesis; IDA:MGI.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0007096; P:regulation of exit from mitosis; TAS:ProtInc.
 GO:0000921; P:septin ring assembly; TAS:ProtInc. 
Interpro
 IPR012966; DUF1709.
 IPR011993; PH_like_dom.
 IPR001849; Pleckstrin_homology. 
Pfam
 PF08174; Anillin
 PF00169; PH 
SMART
 SM00233; PH 
PROSITE
 PS50003; PH_DOMAIN 
PRINTS