CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019779
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Heterogeneous nuclear ribonucleoprotein A/B 
Protein Synonyms/Alias
 hnRNP A/B; APOBEC1-binding protein 1; ABBP-1 
Gene Name
 HNRNPAB 
Gene Synonyms/Alias
 ABBP1; HNRPAB 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
83GLSWDTSKKDLKDYFubiquitination[1, 2, 3]
84LSWDTSKKDLKDYFTubiquitination[2]
92DLKDYFTKFGEVVDCubiquitination[1, 2]
102EVVDCTIKMDPNTGRubiquitination[2, 3]
119GFGFILFKDAASVEKubiquitination[2]
150KKAMAMKKDPVKKIFubiquitination[3]
169NPEATEEKIREYFGEubiquitination[2]
232EIKVAQPKEVYQQQQubiquitination[2]
Reference
 [1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661
Functional Description
 Binds single-stranded RNA. Has a high affinity for G- rich and U-rich regions of hnRNA. Also binds to APOB mRNA transcripts around the RNA editing site. 
Sequence Annotation
 DOMAIN 69 154 RRM 1.
 DOMAIN 153 233 RRM 2.
 MOD_RES 77 77 Phosphoserine (By similarity).
 MOD_RES 242 242 Phosphoserine.
 MOD_RES 245 245 Dimethylated arginine; alternate.
 MOD_RES 245 245 Omega-N-methylarginine; alternate.
 MOD_RES 322 322 Dimethylated arginine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; Methylation; Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 332 AA 
Protein Sequence
MSEAGEEQPM ETTGATENGH EAVPEGESPA GAGTGAAAGA GGATAAPPSG NQNGAEGDQI 60
NASKNEEDAG KMFVGGLSWD TSKKDLKDYF TKFGEVVDCT IKMDPNTGRS RGFGFILFKD 120
AASVEKVLDQ KEHRLDGRVI DPKKAMAMKK DPVKKIFVGG LNPEATEEKI REYFGEFGEI 180
EAIELPMDPK LNKRRGFVFI TFKEEEPVKK VLEKKFHTVS GSKCEIKVAQ PKEVYQQQQY 240
GSGGRGNRNR GNRGSGGGGG GGGQSQSWNQ GYGNYWNQGY GYQQGYGPGY GGYDYSPYGY 300
YGYGPGYDYS QGSTNYGKSQ RRGGHQNNYK PY 332 
Gene Ontology
 GO:0005737; C:cytoplasm; ISS:HGNC.
 GO:0005634; C:nucleus; ISS:HGNC.
 GO:0030529; C:ribonucleoprotein complex; IDA:UniProtKB.
 GO:0003729; F:mRNA binding; TAS:ProtInc.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0001837; P:epithelial to mesenchymal transition; ISS:HGNC.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; ISS:HGNC. 
Interpro
 IPR012956; CARG-binding_factor_N.
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 
Pfam
 PF08143; CBFNT
 PF00076; RRM_1 
SMART
 SM00360; RRM 
PROSITE
 PS50102; RRM 
PRINTS