CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007637
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Matrin-3 
Protein Synonyms/Alias
  
Gene Name
 MATR3 
Gene Synonyms/Alias
 KIAA0723 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
3*****MSKSFQQSSLacetylation[1]
132LSRYPEDKITPENLPubiquitination[2, 3, 4]
146PQILLQLKRRRTEEGubiquitination[2, 4, 5]
473VRVHLSQKYKRIKKPacetylation[1]
491PDQKFDQKQELGRVIubiquitination[2, 6]
515YSDSAVLKLAEPYGKubiquitination[2, 4, 5]
522KLAEPYGKIKNYILMacetylation[1]
522KLAEPYGKIKNYILMubiquitination[2, 4, 5]
524AEPYGKIKNYILMRMubiquitination[2]
532NYILMRMKSQAFIEMubiquitination[2]
555MVDHCLKKALWFQGRubiquitination[2]
571VKVDLSEKYKKLVLRacetylation[1]
611SPSDKKSKTDGSQKTubiquitination[2]
625TESSTEGKEQEEKSGubiquitination[2]
770DGQSDENKDDYTIPDubiquitination[2, 4]
829SSLPHYQKLKKFLNKacetylation[1]
836KLKKFLNKLAEERRQacetylation[1]
836KLKKFLNKLAEERRQubiquitination[2, 4, 5]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] 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]
 [3] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [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] 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]
 [6] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572] 
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. 
Sequence Annotation
 DOMAIN 398 473 RRM 1.
 DOMAIN 496 571 RRM 2.
 ZN_FING 801 832 Matrin-type.
 MOTIF 710 718 Nuclear localization signal (Potential).
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 3 3 N6-acetyllysine.
 MOD_RES 4 4 Phosphoserine.
 MOD_RES 9 9 Phosphoserine.
 MOD_RES 14 14 Phosphoserine.
 MOD_RES 22 22 Phosphoserine.
 MOD_RES 41 41 Phosphoserine.
 MOD_RES 118 118 Phosphoserine.
 MOD_RES 188 188 Phosphoserine.
 MOD_RES 195 195 Phosphoserine.
 MOD_RES 206 206 Phosphoserine.
 MOD_RES 208 208 Phosphoserine.
 MOD_RES 219 219 Phosphotyrosine.
 MOD_RES 522 522 N6-acetyllysine.
 MOD_RES 533 533 Phosphoserine.
 MOD_RES 571 571 N6-acetyllysine.
 MOD_RES 596 596 Phosphoserine.
 MOD_RES 598 598 Phosphoserine.
 MOD_RES 604 604 Phosphoserine.
 MOD_RES 606 606 Phosphoserine.
 MOD_RES 741 741 Phosphothreonine.
 MOD_RES 747 747 Phosphoserine.
 MOD_RES 766 766 Phosphoserine.
 MOD_RES 836 836 N6-acetyllysine.  
Keyword
 Acetylation; Alternative splicing; Complete proteome; Direct protein sequencing; Disease mutation; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 847 AA 
Protein Sequence
MSKSFQQSSL SRDSQGHGRD LSAAGIGLLA AATQSLSMPA SLGRMNQGTA RLASLMNLGM 60
SSSLNQQGAH SALSSASTSS HNLQSIFNIG SRGPLPLSSQ HRGDADQASN 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 KTDGSQKTES STEGKEQEEK SGEDGEKDTK DDQTEQEPNM LLESEDELLV 660
DEEEAAALLE SGSSVGDETD LANLGDVASD GKKEPSDKAV KKDGSASAAA KKKLKKVDKI 720
EELDQENEAA LENGIKNEEN TEPGAESSEN ADDPNKDTSE NADGQSDENK DDYTIPDEYR 780
IGPYQPNVPV GIDYVIPKTG FYCKLCSLFY TNEEVAKNTH CSSLPHYQKL KKFLNKLAEE 840
RRQKKET 847 
Gene Ontology
 GO:0005637; C:nuclear inner membrane; TAS:ProtInc.
 GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0005198; F:structural molecule activity; TAS:ProtInc.
 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