CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021662
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase MSL2 
Protein Synonyms/Alias
 Male-specific lethal 2-like 1; MSL2-like 1; Male-specific lethal-2 homolog; MSL-2; Male-specific lethal-2 homolog 1; RING finger protein 184 
Gene Name
 MSL2 
Gene Synonyms/Alias
 KIAA1585; MSL2L1; RNF184 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
26NYDPGDPKAFTEINRubiquitination[1, 2]
105ILVNCYKKLCEYITQubiquitination[1]
351RSESDSEKVQPLPISubiquitination[2]
375ASAPVTVKRESKISLubiquitination[2]
379VTVKRESKISLQPIAubiquitination[1, 2]
399GTTPKISKTVLLSTKubiquitination[1]
406KTVLLSTKSMKKSHEubiquitination[1]
488CPCYSNRKACLDCICubiquitination[1, 2]
508SYMANGEKKLEAFAVubiquitination[1]
509YMANGEKKLEAFAVPubiquitination[1, 2]
518EAFAVPEKALEQTRLubiquitination[1, 2]
Reference
 [1] 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]
 [2] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
Functional Description
 Component of histone acetyltransferase complex responsible for the majority of histone H4 acetylation at lysine 16 which is implicated in the formation of higher-order chromatin structure. Acts as an E3 ubiquitin ligase that promotes monoubiquitination of histone H2B at 'Lys-35' (H2BK34Ub), but not that of H2A. This activity is greatly enhanced by heterodimerization with MSL1. H2B ubiquitination in turn stimulates histine H3 methylation at 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) and leads to gene activation, including that of HOXA9 and MEIS1. 
Sequence Annotation
 ZN_FING 44 85 RING-type.  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Ligase; Metal-binding; Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 577 AA 
Protein Sequence
MNPVNATALY ISASRLVLNY DPGDPKAFTE INRLLPYFRQ SLSCCVCGHL LQDPIAPTNS 60
TCQHYVCKTC KGKKMMMKPS CSWCKDYEQF EENKQLSILV NCYKKLCEYI TQTTLARDII 120
EAVDCSSDIL ALLNDGSLFC EETEKPSDSS FTLCLTHSPL PSTSEPTTDP QASLSPMSES 180
TLSIAIGSSV INGLPTYNGL SIDRFGINIP SPEHSNTIDV CNTVDIKTED LSDSLPPVCD 240
TVATDLCSTG IDICSFSEDI KPGDSLLLSV EEVLRSLETV SNTEVCCPNL QPNLEATVSN 300
GPFLQLSSQS LSHNVFMSTS PALHGLSCTA ATPKIAKLNR KRSRSESDSE KVQPLPISTI 360
IRGPTLGASA PVTVKRESKI SLQPIATVPN GGTTPKISKT VLLSTKSMKK SHEHGSKKSH 420
SKTKPGILKK DKAVKEKIPS HHFMPGSPTK TVYKKPQEKK GCKCGRATQN PSVLTCRGQR 480
CPCYSNRKAC LDCICRGCQN SYMANGEKKL EAFAVPEKAL EQTRLTLGIN VTSIAVRNAS 540
TSTSVINVTG SPVTTFLAAS THDDKSLDEA IDMRFDC 577 
Gene Ontology
 GO:0072487; C:MSL complex; IDA:UniProtKB.
 GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0043984; P:histone H4-K16 acetylation; IDA:UniProtKB. 
Interpro
 IPR001841; Znf_RING. 
Pfam
  
SMART
  
PROSITE
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS