CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017250
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Matrin-3 
Protein Synonyms/Alias
  
Gene Name
 Matr3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
3*****MSKSFQQSSLacetylation[1, 2]
146PQILLQLKRRRTEEGacetylation[1]
491PDQKFDQKQELGRVIacetylation[2]
491PDQKFDQKQELGRVIubiquitination[3]
515YSDSAVLKLAEPYGKacetylation[1]
515YSDSAVLKLAEPYGKubiquitination[3]
522KLAEPYGKIKNYILMacetylation[2]
522KLAEPYGKIKNYILMsuccinylation[2]
522KLAEPYGKIKNYILMubiquitination[3]
555MVDHCLKKALWFQGRubiquitination[3]
835KLKKFLNKLAEERRQacetylation[1, 2]
835KLKKFLNKLAEERRQubiquitination[3]
Reference
 [1] 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]
 [2] 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]
 [3] 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
 May play a role in transcription or may interact with other nuclear matrix proteins to form the internal fibrogranular network. In association with the SFPQ-NONO heteromer may play a role in nuclear retention of defective RNAs (By similarity). 
Sequence Annotation
 DOMAIN 398 473 RRM 1.
 DOMAIN 496 571 RRM 2.
 ZN_FING 800 831 Matrin-type.
 MOTIF 709 717 Nuclear localization signal (Potential).
 MOD_RES 2 2 N-acetylserine (By similarity).
 MOD_RES 3 3 N6-acetyllysine (By similarity).
 MOD_RES 4 4 Phosphoserine (By similarity).
 MOD_RES 9 9 Phosphoserine (By similarity).
 MOD_RES 14 14 Phosphoserine (By similarity).
 MOD_RES 22 22 Phosphoserine (By similarity).
 MOD_RES 41 41 Phosphoserine (By similarity).
 MOD_RES 118 118 Phosphoserine (By similarity).
 MOD_RES 188 188 Phosphoserine.
 MOD_RES 195 195 Phosphoserine (By similarity).
 MOD_RES 206 206 Phosphoserine (By similarity).
 MOD_RES 208 208 Phosphoserine (By similarity).
 MOD_RES 219 219 Phosphotyrosine (By similarity).
 MOD_RES 522 522 N6-acetyllysine (By similarity).
 MOD_RES 533 533 Phosphoserine (By similarity).
 MOD_RES 571 571 N6-acetyllysine (By similarity).
 MOD_RES 596 596 Phosphoserine (By similarity).
 MOD_RES 598 598 Phosphoserine.
 MOD_RES 604 604 Phosphoserine (By similarity).
 MOD_RES 606 606 Phosphoserine (By similarity).
 MOD_RES 740 740 Phosphothreonine (By similarity).
 MOD_RES 746 746 Phosphoserine (By similarity).
 MOD_RES 835 835 N6-acetyllysine (By similarity).  
Keyword
 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 846 AA 
Protein Sequence
MSKSFQQSSL GRDSQGHGRD LSAAGIGLLA AATQSLSMPA SLGRMNQGTA RLASLMNLGM 60
SSSLNQQGAH SALSSASTSS HNLQSIFNIG SRGPLPLSSQ HRGDTDQASN ILASFGLSAR 120
DLDELSRYPE DKITPENLPQ ILLQLKRRRT EEGPTLSYGR DGRSATREPP YRVPRDDWEE 180
KRHFRRDSFD DRGPSLNPVL DYDHGSRSQE SGYYDRMDYE DDRLRDGERC RDDSFFGETS 240
HNYHKFDSEY ERMGRGPGPL QERSLFEKKR GAPPSSNIED FHGLLPKGYP HLCSICDLPV 300
HSNKEWSQHI NGASHSRRCQ LLLEIYPEWN PDNDTGHTMG DPFMLQQSTN PAPGILGPPP 360
PSFHLGGPAV GPRGNLGAGN GNLQGPRHMQ KGRVETSRVV HIMDFQRGKN LRYQLLQLVE 420
PFGVISNHLI LNKINEAFIE MATTEDAQAA VDYYTTTPAL VFGKPVRVHL SQKYKRIKKP 480
EGKPDQKFDQ KQELGRVIHL SNLPHSGYSD SAVLKLAEPY GKIKNYILMR MKSQAFIEME 540
TREDAMAMVD HCLKKALWFQ GRCVKVDLSE KYKKLVLRIP NRGIDLLKKD KSRKRSYSPD 600
GKESPSDKKS KTDAQKTESP AEGKEQEEKS GEDGEKDTKD DQTEQEPSML LESEDELLVD 660
EEEAAALLES GSSVGDETDL ANLGDVSSDG KKEPSDKAVK KDPSASATSK KKLKKVDKIE 720
ELDQENEAAL ENGIKNEENT EPGAESAENA DDPNKDTSEN ADGQNDENKE DYTIPDEYRI 780
GPYQPNVPVG IDYVIPKTGF YCKLCSLFYT NEEVAKNTHC SSLPHYQKLK KFLNKLAEER 840
RQKKET 846 
Gene Ontology
 GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
Interpro
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom.
 IPR015880; Znf_C2H2-like.
 IPR000690; Znf_C2H2_matrin.
 IPR003604; Znf_U1. 
Pfam
  
SMART
 SM00360; RRM
 SM00355; ZnF_C2H2
 SM00451; ZnF_U1 
PROSITE
 PS50102; RRM
 PS50171; ZF_MATRIN 
PRINTS