CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000355
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 U2 snRNP-associated SURP motif-containing protein 
Protein Synonyms/Alias
 140 kDa Ser/Arg-rich domain protein; U2-associated protein SR140 
Gene Name
 U2SURP 
Gene Synonyms/Alias
 KIAA0332; SR140 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
80SRPLLENKLKAFSIGacetylation[1]
82PLLENKLKAFSIGKMubiquitination[2]
88LKAFSIGKMSTAKRTubiquitination[2]
98TAKRTLSKKEQEELKacetylation[3]
105KKEQEELKKKEDEKAacetylation[3]
153EEHETDEKRGKIYKPubiquitination[2]
168SSRFADQKNPPNQSSubiquitination[2]
392AQPRERLKNPNAPMLubiquitination[2]
410KNKEDFEKTLSQAIVubiquitination[2]
476AHVYYRWKLYSILQGubiquitination[4, 5]
488LQGDSPTKWRTEDFRubiquitination[2, 4, 5, 6]
535PSKKGALKEEQRDKLubiquitination[6]
541LKEEQRDKLEEILRGubiquitination[2, 4, 5]
608VLYNSSAKVANASYYubiquitination[2, 6]
622YRKFFETKLCQIFSDubiquitination[2]
647HLQSENFKQRVMTCFubiquitination[2, 6]
755KKNEPIFKVAPSKWEubiquitination[6]
760IFKVAPSKWEAVDESacetylation[3]
760IFKVAPSKWEAVDESubiquitination[6]
902RERDKKDKEKLESRSacetylation[7]
910EKLESRSKDKKEKDEacetylation[7]
912LESRSKDKKEKDECTacetylation[7]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [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] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786
Functional Description
  
Sequence Annotation
 DOMAIN 274 355 RRM.
 REPEAT 430 473 SURP motif.
 DOMAIN 534 679 CID.
 MOD_RES 202 202 Phosphoserine.
 MOD_RES 485 485 Phosphoserine.
 MOD_RES 760 760 N6-acetyllysine.
 MOD_RES 788 788 Phosphoserine.
 MOD_RES 800 800 Phosphoserine.
 MOD_RES 811 811 Phosphoserine.
 MOD_RES 931 931 Phosphothreonine.
 MOD_RES 946 946 Phosphoserine.
 MOD_RES 948 948 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; Coiled coil; Complete proteome; Nucleus; Phosphoprotein; Reference proteome; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1029 AA 
Protein Sequence
MADKTPGGSQ KASSKTRSSD VHSSGSSDAH MDASGPSDSD MPSRTRPKSP RKHNYRNESA 60
RESLCDSPHQ NLSRPLLENK LKAFSIGKMS TAKRTLSKKE QEELKKKEDE KAAAEIYEEF 120
LAAFEGSDGN KVKTFVRGGV VNAAKEEHET DEKRGKIYKP SSRFADQKNP PNQSSNERPP 180
SLLVIETKKP PLKKGEKEKK KSNLELFKEE LKQIQEERDE RHKTKGRLSR FEPPQSDSDG 240
QRRSMDAPSR RNRSSGVLDD YAPGSHDVGD PSTTNLYLGN INPQMNEEML CQEFGRFGPL 300
ASVKIMWPRT DEERARERNC GFVAFMNRRD AERALKNLNG KMIMSFEMKL GWGKAVPIPP 360
HPIYIPPSMM EHTLPPPPSG LPFNAQPRER LKNPNAPMLP PPKNKEDFEK TLSQAIVKVV 420
IPTERNLLAL IHRMIEFVVR EGPMFEAMIM NREINNPMFR FLFENQTPAH VYYRWKLYSI 480
LQGDSPTKWR TEDFRMFKNG SFWRPPPLNP YLHGMSEEQE TEAFVEEPSK KGALKEEQRD 540
KLEEILRGLT PRKNDIGDAM VFCLNNAEAA EEIVDCITES LSILKTPLPK KIARLYLVSD 600
VLYNSSAKVA NASYYRKFFE TKLCQIFSDL NATYRTIQGH LQSENFKQRV MTCFRAWEDW 660
AIYPEPFLIK LQNIFLGLVN IIEEKETEDV PDDLDGAPIE EELDGAPLED VDGIPIDATP 720
IDDLDGVPIK SLDDDLDGVP LDATEDSKKN EPIFKVAPSK WEAVDESELE AQAVTTSKWE 780
LFDQHEESEE EENQNQEEES EDEEDTQSSK SEEHHLYSNP IKEEMTESKF SKYSEMSEEK 840
RAKLREIELK VMKFQDELES GKRPKKPGQS FQEQVEHYRD KLLQREKEKE LERERERDKK 900
DKEKLESRSK DKKEKDECTP TRKERKRRHS TSPSPSRSSS GRRVKSPSPK SERSERSERS 960
HKESSRSRSS HKDSPRDVSK KAKRSPSGSR TPKRSRRSRS RSPKKSGKKS RSQSRSPHRS 1020
HKKSKKNKH 1029 
Gene Ontology
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0006396; P:RNA processing; IEA:InterPro. 
Interpro
 IPR006569; CID_dom.
 IPR008942; ENTH_VHS.
 IPR013170; mRNA_splic_Cwf21.
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom.
 IPR000061; Surp. 
Pfam
 PF08312; cwf21
 PF00076; RRM_1
 PF01805; Surp 
SMART
 SM00582; RPR
 SM00360; RRM
 SM00648; SWAP 
PROSITE
 PS51391; CID
 PS50102; RRM
 PS50128; SURP 
PRINTS