CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010972
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein hu-li tai shao 
Protein Synonyms/Alias
 Adducin-like protein 
Gene Name
 hts 
Gene Synonyms/Alias
 CG9325 
Created Date
 July 27, 2013 
Organism
 Drosophila melanogaster (Fruit fly) 
NCBI Taxa ID
 7227 
Lysine Modification
Position
Peptide
Type
References
114VESMGYAKGEKILRCacetylation[1]
117MGYAKGEKILRCKLAacetylation[1]
Reference
 [1] Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation.
 Weinert BT, Wagner SA, Horn H, Henriksen P, Liu WR, Olsen JV, Jensen LJ, Choudhary C.
 Sci Signal. 2011 Jul 26;4(183):ra48. [PMID: 21791702] 
Functional Description
 Required for assembling actin at ring canals in developing egg chambers. Probably interacts with other developmental proteins involved in nurse cell/oocyte transport through the ring canals. 
Sequence Annotation
 MOD_RES 478 478 Phosphoserine.
 MOD_RES 480 480 Phosphothreonine.
 MOD_RES 498 498 Phosphothreonine.
 MOD_RES 603 603 Phosphoserine.
 MOD_RES 608 608 Phosphotyrosine.
 MOD_RES 609 609 Phosphothreonine.
 MOD_RES 611 611 Phosphothreonine.
 MOD_RES 614 614 Phosphoserine.
 MOD_RES 627 627 Phosphotyrosine.
 MOD_RES 630 630 Phosphoserine.  
Keyword
 Actin-binding; Alternative splicing; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Developmental protein; Differentiation; Membrane; Oogenesis; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1156 AA 
Protein Sequence
MTEVEQPPQN GIDPTAGEDD DNSKARPADI EQDMREMERR KRVEAIMGSK LFREELERIV 60
DSARDGGAGA SGILQQLSDI VGVPVSRVGS VFKSSNCMVP INDIRGVESM GYAKGEKILR 120
CKLAATFRLL DLYGWTQGLG AQITARLKVD QEYFLVNPYG LLYHEITASA LNKVDMQGQI 180
VEQGTTNFGG NKSHFVLHSV VHAARPDIRC AIYIGCSPVV AISSLKTGLL PLTKDACVLG 240
EITTHAYTGL FDEEERNRLV RSLGPNSKVI LLTNHGALCC GETIEEAFFA ACHIVQACET 300
QLKLLPVGLD NLVLIPEESR KAIYEQSRRP PEDLEKKFAA VAAAEDGAAT AEKDAAEAVP 360
KVGSPPKWRV GGAEFEALMR MLDNAGYRTG YIYRHPLIKS DPPKPKNDVE LPPAVSSLGY 420
LLEEEELFRQ GIWKKGDIRK GGDRSRWLNS PNVYQKVEVL ETGTPDPKKI TKWVAEGSPT 480
HSTPVRIEDP LQFVPAGTNP REFKRVQQLI KDNRRADKIS AGPQSHILEG VTWDEASRLK 540
DATVSQAGDH VVMMGAASKG IIQRGFQHNA TVYKAPYAKN PFDNVTDDEL NEYKRTVERK 600
KKSVHGEYTD TDFSESEAVL QAGTKKYPQS EPETEHQVIE IQTQQAPVPR QAEVVLSDAL 660
VSQLAQKYAF LYSPGQYMYA CMKMAPLMHK VYVIHKVEPV SKHNYPPVND GNMSIHHNES 720
GAGFMAQESS VISSTPVRNA LASVSLPEER NHSILGLSST PYRTISHFGF NCPLITSPTI 780
LLHPEHRSIW QRVAEQREKV VSFIDLTTLS LDNRKLLNVV TSTHPTQCQS QSQSFISEKH 840
IQLEVTPPKR KQRVYSATIS SGLDDSLDEL DSLMSGLAIN MPRSREQDSG LYRSYTFLPS 900
NHALPKDTDA NNRDQTDRER PEAEQEESFH CAGDSGIGDS TGRRPRLATT SNDSSIQEAE 960
AYTQGKHVKL TLSSSPTPTA TQSPATIEIL INVSLRNAEC VQTVQTHEQE FRAKLERVID 1020
EEIHYISQQL AFKQRQAELH EQQTTSRAPI ATPSFTTMHP PAPASSSSMV HRSNSAPELC 1080
HTYSYVAVGD LSTKQDQASP QLPAEGEPLN DILSSLEKEL ERLLNSVVTA HMLHNKAIIH 1140
ECRARFSQLA DGIVSS 1156 
Gene Ontology
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0035183; C:female germline ring canal inner rim; TAS:FlyBase.
 GO:0045169; C:fusome; IDA:FlyBase.
 GO:0005811; C:lipid particle; IDA:FlyBase.
 GO:0005886; C:plasma membrane; IDA:FlyBase.
 GO:0045170; C:spectrosome; IDA:FlyBase.
 GO:0046872; F:metal ion binding; IEA:InterPro.
 GO:0007527; P:adult somatic muscle development; IMP:FlyBase.
 GO:0051297; P:centrosome organization; IMP:FlyBase.
 GO:0007282; P:cystoblast division; IMP:FlyBase.
 GO:0048135; P:female germ-line cyst formation; TAS:FlyBase.
 GO:0008302; P:female germline ring canal formation, actin assembly; IMP:FlyBase.
 GO:0007294; P:germarium-derived oocyte fate determination; TAS:FlyBase.
 GO:0000212; P:meiotic spindle organization; IMP:FlyBase.
 GO:0030723; P:ovarian fusome organization; IMP:FlyBase.
 GO:0072499; P:photoreceptor cell axon guidance; IMP:FlyBase.
 GO:0045214; P:sarcomere organization; IMP:FlyBase.
 GO:0030721; P:spectrosome organization; TAS:FlyBase.
 GO:0030724; P:testicular fusome organization; IMP:FlyBase. 
Interpro
 IPR001303; Aldolase_II/adducin_N. 
Pfam
 PF00596; Aldolase_II 
SMART
 SM01007; Aldolase_II 
PROSITE
  
PRINTS