| Tag | Content |
|---|
| CPLM ID | CPLM-023427 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | N-acetyltransferase eco |
Protein Synonyms/Alias | Establishment of cohesion 1 homolog; ECO1 homolog |
Gene Name | eco |
Gene Synonyms/Alias | CG8598 |
Created Date | July 27, 2013 |
Organism | Drosophila melanogaster (Fruit fly) |
NCBI Taxa ID | 7227 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 818 | RLQPVVQKSLRRRPD | acetylation | [1] | | 929 | DLIGVVDKELGYSSY | acetylation | [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 | Acetyltransferase required for the establishment of sister chromatid cohesion and couple the processes of cohesion and DNA replication to ensure that only sister chromatids become paired together. In contrast to the structural cohesins, the deposition and establishment factors are required only during S phase. |
Sequence Annotation | DOMAIN 906 1052 N-acetyltransferase.
ZN_FING 852 876 CCHH-type.
MOD_RES 176 176 Phosphoserine.
MOD_RES 177 177 Phosphoserine.
MOD_RES 310 310 Phosphoserine.
MOD_RES 312 312 Phosphoserine.
MOD_RES 314 314 Phosphoserine. |
Keyword | Acyltransferase; Cell cycle; Complete proteome; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transferase; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1052 AA |
Protein Sequence | METPTGSGRP SRMATPRLSE RKRQLFGSPR SRLRQINDDE DDADVDSLGV LPLKTHVAAN 60
RKGRSLFAAV PGKSSSSANS SPETNKENKK TRGGVMTATA EQLPQLFTAT MRLNSNSSSN 120
SRNSSPRQTR VQRKRADSSM SSPTSSSEGT PSSRARNSIR RSPRTFSAQK DPDAFSSPES 180
FQTRLSKVAA MLMKGQDSRS MLEKSKKKHN HSLKTTAQVH TTKPKKTSPA EESQSDDEKP 240
SSSKNSRKNT EVRETRSSQI ISPKTRNRRR PFTSADINCK TLKAAAHLHE NMRSYDEEKT 300
AAVKLENSRS RSKSPVEVFK SNDDAVKRNT GNTNNKTAKS SEVATAKRPE SPGSSMKIDV 360
EVPESDEEAS NHKPQKRQHP ETSTPVAPSA DADSGSPQSK MRKVTLSSSI PTMAFYSHSG 420
EAVTKSRRRP SISKNSLKQP TKISPTSRPL LGINKGVHHK IRKRHGFANR LPATDMDNIL 480
NSLSNERLKN LITTKREERA KVEEVHQILR NAKDPIKMAK PLSVIEADDA NNNNNLPATA 540
WQETSADFSD LSDVEDIDPI IEVEPIIPII RHEPVQKSPT AEPADLSKRK FFKSGRRSST 600
CMEVRITDNI RASVSQGKIE LVQTIRRKPR QVRVKSATIF SAEQATVDAI LKNLDDTVVD 660
EIVEANPVVQ ATPIDAEETT METESLPDII EYAPEANDVE IDPFAEFRQR LPYQTDDPNV 720
VEQQQILLEF LISNNICTEK NFEIFIANPD DYKDEANQIV DNLYMVVNSE EAAQLAQMET 780
VENTAVAIAP KQDAPAVEEV QPKLFPIFTQ RLQPVVQKSL RRRPDTSMRL LTAAGGSNQY 840
QIDAGQKAFG ARQCQQCGLV YTVHEPEEEL LHREYHNSIH VLRFKGWIDE DIVSVYPEWA 900
SDGRIIRINE RAPTARLDRL RDLIGVVDKE LGYSSYIVPK IFVAFIAVRK QQIVGFCLVQ 960
PLSQAHRFIQ VDGTDYFSEE SYPASCGVSR IWVSPLQRRS GIASKLLRVV QCHTVLGQEI 1020
ARECIAFSTP TDDGRALARQ FTGLDNFLTY DQ 1052 |
Gene Ontology | GO:0000790; C:nuclear chromatin; ISS:UniProtKB. GO:0016407; F:acetyltransferase activity; ISS:UniProtKB. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0008080; F:N-acetyltransferase activity; IEA:InterPro. GO:0007064; P:mitotic sister chromatid cohesion; IMP:FlyBase. GO:0007052; P:mitotic spindle organization; IMP:FlyBase. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |