CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020723
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Heterogeneous nuclear ribonucleoprotein M 
Protein Synonyms/Alias
 hnRNP M 
Gene Name
 Hnrnpm 
Gene Synonyms/Alias
 Hnrpm 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
68EPYSNPTKRYRAFITubiquitination[1]
82TNIPFDVKWQSLKDLubiquitination[1]
87DVKWQSLKDLVKEKVubiquitination[1]
380EILSNALKRGEIIAKubiquitination[1]
387KRGEIIAKQGGGGAGubiquitination[1]
671TWKMLKDKFNECGHVacetylation[2, 3]
691KMENGKSKGCGVVKFacetylation[2]
697SKGCGVVKFESPEVAacetylation[2, 3, 4]
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]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [4] 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
 Pre-mRNA binding protein in vivo, binds avidly to poly(G) and poly(U) RNA homopolymers in vitro. Involved in splicing. Acts as a receptor for carcinoembryonic antigen in Kupffer cells, may initiate a series of signaling events leading to tyrosine phosphorylation of proteins and induction of IL-1 alpha, IL-6, IL-10 and tumor necrosis factor alpha cytokines (By similarity). 
Sequence Annotation
 DOMAIN 70 148 RRM 1.
 DOMAIN 203 280 RRM 2.
 REPEAT 399 404 1.
 REPEAT 406 411 2.
 REPEAT 414 419 3.
 REPEAT 425 430 4.
 REPEAT 432 437 5.
 REPEAT 439 444 6.
 REPEAT 445 450 7.
 REPEAT 452 457 8.
 REPEAT 460 465 9.
 REPEAT 467 472 10.
 REPEAT 474 479 11.
 REPEAT 481 486 12.
 REPEAT 492 497 13.
 REPEAT 499 504 14.
 REPEAT 506 511 15.
 REPEAT 513 518 16.
 REPEAT 520 525 17.
 REPEAT 527 532 18.
 REPEAT 539 544 19.
 REPEAT 546 551 20.
 REPEAT 553 558 21.
 REPEAT 561 566 22.
 REPEAT 566 571 23.
 REPEAT 574 579 24.
 REPEAT 579 584 25.
 REPEAT 587 592 26.
 REPEAT 602 607 27.
 DOMAIN 652 728 RRM 3.
 REGION 399 607 27 X 6 AA repeats of [GEVSTPAN]-[ILMV]-
 MOD_RES 2 2 N-acetylalanine (By similarity).
 MOD_RES 29 29 Phosphoserine (By similarity).
 MOD_RES 276 276 N6-acetyllysine (By similarity).
 MOD_RES 431 431 Phosphoserine (By similarity).
 MOD_RES 451 451 Phosphoserine (By similarity).
 MOD_RES 467 467 Phosphoserine (By similarity).
 MOD_RES 480 480 Phosphoserine (By similarity).
 MOD_RES 527 527 Phosphoserine (By similarity).
 MOD_RES 539 539 Phosphoserine.
 MOD_RES 574 574 Phosphoserine (By similarity).
 MOD_RES 587 587 Phosphoserine (By similarity).
 MOD_RES 617 617 Phosphoserine.
 MOD_RES 632 632 Phosphoserine (By similarity).
 MOD_RES 636 636 Phosphoserine (By similarity).
 MOD_RES 697 697 N6-acetyllysine (By similarity).
 MOD_RES 700 700 Phosphoserine (By similarity).  
Keyword
 Acetylation; Alternative splicing; Complete proteome; Direct protein sequencing; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding; Spliceosome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 729 AA 
Protein Sequence
MAAGVEAAAE VAATEPKMEE ESGAPCVPSG NGAPGPKGEE RPTQNEKRKE KNIKRGGNRF 60
EPYSNPTKRY RAFITNIPFD VKWQSLKDLV KEKVGEVTYV ELLMDAEGKS RGCAVVEFKM 120
EESMKKAAEV LNKHSLSGRP LKVKEDPDGE HARRAMQKVM ATTGGMGMGP GGPGMINIPP 180
SILNNPNIPN EIIHALQAGR LGSTVFVANL DYKVGWKKLK EVFSMAGVVV RADILEDKDG 240
KSRGIGIVTF EQSIEAVQAI SMFNGQLLFD RPMHVKMDER ALPKGDFFPP ERPQQLPHGL 300
GGIGMGLGPG GQPIDANHLS KGIGMGNLGP AGMGMEGIGF GINKIGGMEG PFGGGMENMG 360
RFGSGMNMGR INEILSNALK RGEIIAKQGG GGAGGSVPGI ERMGPGIDRI SGAGMERMGA 420
GLGHGMDRVG SEIERMGLVM DRMGSVERMG SSIERMGPLG LDHMASSIER MGQTMERIGS 480
GVERMGAGMG FGLERMAAPI DRVGQTIERM GSGVERMGPA IERMGLSMDR MVPTGMGASL 540
ERMGPVMDRM ATGLERMGAN NLERMGLERM GANSLERMGL ERMGANSLER MGPAMGPALG 600
AGIERMGLAM GGAGGASFDR AIEMERGNFG GSFAGSFGGA GGHAPGVARK ACQIFVRNLP 660
FDFTWKMLKD KFNECGHVLY ADIKMENGKS KGCGVVKFES PEVAERACRM MNGMKLSGRE 720
IDVRIDRNA 729 
Gene Ontology
 GO:0071013; C:catalytic step 2 spliceosome; IEA:Compara.
 GO:0016363; C:nuclear matrix; IEA:Compara.
 GO:0042382; C:paraspeckles; IEA:Compara.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0000380; P:alternative mRNA splicing, via spliceosome; IEA:Compara. 
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