CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-029511
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
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
3*****MSKSFQQSSLacetylation[1, 2]
3*****MSKSFQQSSLubiquitination[2, 3, 4, 5]
132LSRYPEDKITPENLPubiquitination[2, 3, 5, 6, 7, 8, 9]
146PQILLQLKRRRTEEGubiquitination[2, 3, 4, 5, 6, 9, 10, 11]
181PRDDWEEKRHFRRDSacetylation[2]
181PRDDWEEKRHFRRDSubiquitination[2, 3]
245ETSHNYHKFDSEYERubiquitination[5, 7]
304DLPVHSNKEWSQHINacetylation[2]
473VRVHLSQKYKRIKKPacetylation[12, 13]
473VRVHLSQKYKRIKKPubiquitination[5]
487PEGKPDQKFDQKQELubiquitination[7]
491PDQKFDQKQELGRVIacetylation[2]
491PDQKFDQKQELGRVIubiquitination[2, 3, 4, 5, 6]
515YSDSAVLKLAEPYGKubiquitination[2, 3, 4, 5, 6, 7, 9, 10, 11]
522KLAEPYGKIKNYILMacetylation[2, 12, 13]
522KLAEPYGKIKNYILMubiquitination[2, 3, 4, 5, 6, 7, 9, 10, 11]
524AEPYGKIKNYILMRMubiquitination[2, 5, 6]
532NYILMRMKSQAFIEMubiquitination[5, 6]
554AMVDHCLKKALWFQGubiquitination[5]
555MVDHCLKKALWFQGRubiquitination[2, 3, 4, 5, 6]
565WFQGRCVKVDLSEKYacetylation[2]
565WFQGRCVKVDLSEKYubiquitination[2, 5]
571VKVDLSEKYKKLVLRacetylation[13]
571VKVDLSEKYKKLVLRubiquitination[2, 3, 5]
589RGIDLLKKDKSRKRSubiquitination[3, 5]
591IDLLKKDKSRKRSYSubiquitination[5]
611SPSDKKSKTDGSQKTubiquitination[6]
617SKTDGSQKTESSTEGacetylation[2, 13]
625TESSTEGKEQEEKSGacetylation[2]
625TESSTEGKEQEEKSGubiquitination[6]
698GKKEPSDKAVKKDGSacetylation[2]
818DGQSDENKDDYTIPDubiquitination[6, 9]
846GIDYVIPKTGFYCKLubiquitination[5]
877SSLPHYQKLKKFLNKacetylation[2]
884KLKKFLNKLAEERRQacetylation[1, 2, 12, 13]
884KLKKFLNKLAEERRQubiquitination[2, 3, 4, 5, 6, 9, 10, 11]
Reference
 [1] 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]
 [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]
 [3] 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]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] 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]
 [11] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [12] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
 [13] 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
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Nucleus; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 895 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 KKKLKKRRFP 720
GSMEGFVTLD EVGDEEDSEL QKLRKSGMAF KSGDKNDDGL VEIKVDKIEE LDQENEAALE 780
NGIKNEENTE PGAESSENAD DPNKDTSENA DGQSDENKDD YTIPDEYRIG PYQPNVPVGI 840
DYVIPKTGFY CKLCSLFYTN EEVAKNTHCS SLPHYQKLKK FLNKLAEERR QKKET 895 
Gene Ontology
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0003676; F:nucleic acid binding; IEA:InterPro.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 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