CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014219
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 APOBEC1 complementation factor 
Protein Synonyms/Alias
 APOBEC1-stimulating protein 
Gene Name
 A1cf 
Gene Synonyms/Alias
 Acf; Asp 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
6**MESNHKSGDGLSGubiquitination[1]
62GCEIFIGKLPRDLFEubiquitination[1]
114QEAKNAIKQLNNYEIubiquitination[1]
249TSEEMIEKEFNSIKPubiquitination[1]
302PIEVTLAKPVDKDSYubiquitination[1]
440PMNTVSLKPQGIKLAubiquitination[1]
482QRQLFLYKVTIPALAubiquitination[1]
502IHPFIPPKLSAYVDEubiquitination[1]
511SAYVDEAKRYAAEHTubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
Functional Description
 Essential component of the apolipoprotein B mRNA editing enzyme complex which is responsible for the postranscriptional editing of a CAA codon for Gln to a UAA codon for stop in APOB mRNA. Binds to APOB mRNA and is probably responsible for docking the catalytic subunit, APOBEC1, to the mRNA to allow it to deaminate its target cytosine. The complex also seems to protect the edited APOB mRNA from nonsense-mediated decay (By similarity). 
Sequence Annotation
 DOMAIN 56 134 RRM 1.
 DOMAIN 136 218 RRM 2.
 DOMAIN 231 303 RRM 3.
 REGION 360 409 Required for nuclear localization (By  
Keyword
 Alternative splicing; Complete proteome; Cytoplasm; Endoplasmic reticulum; mRNA processing; Nucleus; Reference proteome; Repeat; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 595 AA 
Protein Sequence
MESNHKSGDG LSGTQKEAAL RALVQRTGYS LVQENGQRKY GGPPPGWDST PPERGCEIFI 60
GKLPRDLFED ELIPLCEKIG KIYEMRLMMD FNGNNRGYAF VTFSNKQEAK NAIKQLNNYE 120
IRTGRLLGVC ASVDNCRLFV GGIPKTKKRE EILSEMKKVT EGVVDVIVYP SAADKTKNRG 180
FAFVEYESHR AAAMARRRLL PGRIQLWGHP IAVDWAEPEV EVDEDTMSSV KILYVRNLML 240
STSEEMIEKE FNSIKPGAVE RVKKIRDYAF VHFSNREDAV EAMKALNGKV LDGSPIEVTL 300
AKPVDKDSYV RYTRGTGGRN TMLQGEYTYP LSHVYDPTTT YLGAPVFYTP QAYAAIPSLH 360
FPATKGHLSN RALIRTPSVR EIYMNVPVGA AGVRGLGGRG YLAYTGLGRG YHVKGDKRED 420
KLYDLLPGME LTPMNTVSLK PQGIKLAPQI LEEICQKNNW GQPVYQLHSA IGQDQRQLFL 480
YKVTIPALAS QNPAIHPFIP PKLSAYVDEA KRYAAEHTLQ TLGIPTEGGD AGTTAPTATS 540
ATVFPGYAVP SATAPVSTAQ LKQAVTLGQD LAAYTTYEVY PTFALTTRGD AYGTF 595 
Gene Ontology
 GO:0030895; C:apolipoprotein B mRNA editing enzyme complex; ISS:UniProtKB.
 GO:0005737; C:cytoplasm; ISS:UniProtKB.
 GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003727; F:single-stranded RNA binding; ISS:UniProtKB.
 GO:0016554; P:cytidine to uridine editing; TAS:HGNC.
 GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
 GO:0050821; P:protein stabilization; ISS:UniProtKB. 
Interpro
 IPR014720; dsRNA-bd-like_dom.
 IPR006535; HnRNP_R/Q_splicing_fac.
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 
Pfam
 PF00076; RRM_1 
SMART
 SM00360; RRM 
PROSITE
 PS50102; RRM 
PRINTS