CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018825
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Symplekin 
Protein Synonyms/Alias
  
Gene Name
 SYMPK 
Gene Synonyms/Alias
 SPK 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
358DDSDSTLKKMKLEPNacetylation[1]
361DSTLKKMKLEPNLGEsumoylation[2, 3]
483PKEEKVVKTESVLIKsumoylation[2]
483PKEEKVVKTESVLIKubiquitination[4]
520EEEAPQAKRRPEPIIubiquitination[5]
551FRLSDVLKPLTDAQVubiquitination[4, 5, 6, 7]
656LLSGLQEKPDQKDGIubiquitination[5]
705TLRDLIFKRPSRQFQubiquitination[4]
901VLNGLEKKEVIQALPubiquitination[4]
909EVIQALPKLIKLNPIubiquitination[6, 7]
912QALPKLIKLNPIVVKubiquitination[4]
919KLNPIVVKEVFNRLLubiquitination[4, 6, 7]
964CDMKSIIKATNLCFAubiquitination[4]
1040KVWEGFIKCCQRTKPubiquitination[4, 6, 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] Sumoylation modulates the assembly and activity of the pre-mRNA 3' processing complex.
 Vethantham V, Rao N, Manley JL.
 Mol Cell Biol. 2007 Dec;27(24):8848-58. [PMID: 17923699]
 [3] Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif.
 Matic I, Schimmel J, Hendriks IA, van Santen MA, van de Rijke F, van Dam H, Gnad F, Mann M, Vertegaal AC.
 Mol Cell. 2010 Aug 27;39(4):641-52. [PMID: 20797634]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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] 
Functional Description
 Scaffold protein that functions as a component of a multimolecular complex involved in histone mRNA 3'-end processing. Specific component of the tight junction (TJ) plaque, but might not be an exclusively junctional component. May have a house- keeping rule. Is involved in pre-mRNA polyadenylation. Enhances SSU72 phosphatase activity. 
Sequence Annotation
 REPEAT 31 64 HEAT 1.
 REPEAT 67 101 HEAT 2.
 REPEAT 104 146 HEAT 3.
 REPEAT 153 192 HEAT 4.
 REPEAT 227 266 HEAT 5.
 REGION 1 124 Interaction with HSF1.
 MOTIF 345 360 Nuclear localization signal (Potential).
 MOD_RES 494 494 Phosphoserine.
 MOD_RES 1243 1243 Phosphoserine.
 MOD_RES 1257 1257 Phosphothreonine.
 MOD_RES 1259 1259 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Cell adhesion; Cell junction; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Membrane; mRNA processing; Nucleus; Phosphoprotein; Reference proteome; Repeat; Tight junction. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1274 AA 
Protein Sequence
MASGSGDSVT RRSVASQFFT QEEGPGIDGM TTSERVVDLL NQAALITNDS KITVLKQVQE 60
LIINKDPTLL DNFLDEIIAF QADKSIEVRK FVIGFIEEAC KRDIELLLKL IANLNMLLRD 120
ENVNVVKKAI LTMTQLYKVA LQWMVKSRVI SELQEACWDM VSAMAGDIIL LLDSDNDGIR 180
THAIKFVEGL IVTLSPRMAD SEIPRRQEHD ISLDRIPRDH PYIQYNVLWE EGKAALEQLL 240
KFMVHPAISS INLTTALGSL ANIARQRPMF MSEVIQAYET LHANLPPTLA KSQVSSVRKN 300
LKLHLLSVLK HPASLEFQAQ ITTLLVDLGT PQAEIARNMP SSKDTRKRPR DDSDSTLKKM 360
KLEPNLGEDD EDKDLEPGPS GTSKASAQIS GQSDTDITAE FLQPLLTPDN VANLVLISMV 420
YLPEAMPASF QAIYTPVESA GTEAQIKHLA RLMATQMTAA GLGPGVEQTK QCKEEPKEEK 480
VVKTESVLIK RRLSAQGQAI SVVGSLSSMS PLEEEAPQAK RRPEPIIPVT QPRLAGAGGR 540
KKIFRLSDVL KPLTDAQVEA MKLGAVKRIL RAEKAVACSG AAQVRIKILA SLVTQFNSGL 600
KAEVLSFILE DVRARLDLAF AWLYQEYNAY LAAGASGSLD KYEDCLIRLL SGLQEKPDQK 660
DGIFTKVVLE APLITESALE VVRKYCEDES RTYLGMSTLR DLIFKRPSRQ FQYLHVLLDL 720
SSHEKDKVRS QALLFIKRMY EKEQLREYVE KFALNYLQLL VHPNPPSVLF GADKDTEVAA 780
PWTEETVKQC LYLYLALLPQ NHKLIHELAA VYTEAIADIK RTVLRVIEQP IRGMGMNSPE 840
LLLLVENCPK GAETLVTRCL HSLTDKVPPS PELVKRVRDL YHKRLPDVRF LIPVLNGLEK 900
KEVIQALPKL IKLNPIVVKE VFNRLLGTQH GEGNSALSPL NPGELLIALH NIDSVKCDMK 960
SIIKATNLCF AERNVYTSEV LAVVMQQLME QSPLPMLLMR TVIQSLTMYP RLGGFVMNIL 1020
SRLIMKQVWK YPKVWEGFIK CCQRTKPQSF QVILQLPPQQ LGAVFDKCPE LREPLLAHVR 1080
SFTPHQQAHI PNSIMTILEA SGKQEPEAKE APAGPLEEDD LEPLTLAPAP APRPPQDLIG 1140
LRLAQEKALK RQLEEEQKLK PGGVGAPSSS SPSPSPSARP GPPPSEEAMD FREEGPECET 1200
PGIFISMDDD SGLTEAALLD SSLEGPLPKE TAAGGLTLKE ERSPQTLAPV GEDAMKTPSP 1260
AAEDAREPEA KGNS 1274 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0005654; C:nucleoplasm; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0005923; C:tight junction; IEA:UniProtKB-SubCell.
 GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
 GO:0006378; P:mRNA polyadenylation; IMP:UniProtKB.
 GO:0035307; P:positive regulation of protein dephosphorylation; IDA:UniProtKB. 
Interpro
 IPR011989; ARM-like.
 IPR016024; ARM-type_fold.
 IPR021850; DUF3453.
 IPR022075; Symplekin_C. 
Pfam
 PF11935; DUF3453
 PF12295; Symplekin_C 
SMART
  
PROSITE
 PS50077; HEAT_REPEAT 
PRINTS