CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-045295
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Heterogeneous nuclear ribonucleoprotein M 
Protein Synonyms/Alias
  
Gene Name
 HNRNPM 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
37GNGAPGPKGEGERPAubiquitination[1, 2, 3, 4]
48ERPAQNEKRKEKNIKacetylation[5]
48ERPAQNEKRKEKNIKubiquitination[1, 4, 6]
69EPYANPTKRYRAFITubiquitination[1, 2, 3, 4, 5, 6, 7]
83TNIPFDVKWQSLKDLubiquitination[1, 2, 3, 4, 5, 6, 7]
88DVKWQSLKDLVKEKGubiquitination[1, 3, 4, 5, 6, 7]
92QSLKDLVKEKGIVVEubiquitination[3, 6]
94LKDLVKEKGIVVEFKubiquitination[3]
115KAAEVLNKHSLSGRPubiquitination[1, 3, 4, 5, 6]
126SGRPLKVKEDPDGEHubiquitination[1, 6]
140HARRAMQKAGRLGSTubiquitination[1]
156FVANLDYKVGWKKLKubiquitination[1]
163KVGWKKLKEVFSMAGubiquitination[1]
181RADILEDKDGKSRGIacetylation[5, 8, 9]
181RADILEDKDGKSRGIubiquitination[1, 2, 3, 4, 5, 6]
184ILEDKDGKSRGIGTVubiquitination[1, 2, 3, 4, 5]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [8] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [9] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 219 AA 
Protein Sequence
MAAGVEAAAE VAATEIKMEE ESGAPGVPSG NGAPGPKGEG ERPAQNEKRK EKNIKRGGNR 60
FEPYANPTKR YRAFITNIPF DVKWQSLKDL VKEKGIVVEF KMEESMKKAA EVLNKHSLSG 120
RPLKVKEDPD GEHARRAMQK AGRLGSTVFV ANLDYKVGWK KLKEVFSMAG VVVRADILED 180
KDGKSRGIGT VTFEQSIEAV QAISMFNGQL LFDRPMHVK 219 
Gene Ontology
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003723; F:RNA binding; IEA:InterPro.
 GO:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro. 
Interpro
 IPR024667; HnRNP_M.
 IPR024666; HnRNP_M_PY-NLS.
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 
Pfam
 PF11532; HnRNP_M
 PF00076; RRM_1 
SMART
 SM00360; RRM 
PROSITE
 PS50102; RRM 
PRINTS