CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-041893
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Solute carrier family 12 (Sodium/potassium/chloride transporters), member 2, isoform CRA_a 
Protein Synonyms/Alias
 Solute carrier family 12 member 2 
Gene Name
 SLC12A2 
Gene Synonyms/Alias
 hCG_27034 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
114AGAGAGAKQTPADGEubiquitination[1]
130SGESEPAKGSEEAKGubiquitination[1]
136AKGSEEAKGRFRVNFubiquitination[2]
237TAAQLGEKLLRPSLAubiquitination[2, 3]
252ELHDELEKEPFEDGFubiquitination[1, 2, 4]
280VTYTAESKGVVKFGWubiquitination[1, 2]
833GPRRQAMKEMSIDQAubiquitination[2, 5]
841EMSIDQAKYQRWLIKubiquitination[5]
923GVVVIRLKEGLDISHubiquitination[1, 2]
943ELLSSQEKSPGTKDVubiquitination[1, 2, 6]
948QEKSPGTKDVVVSVEubiquitination[1, 2, 4, 6]
958VVSVEYSKKSDLDTSubiquitination[1, 2, 4]
959VSVEYSKKSDLDTSKubiquitination[1, 2]
966KSDLDTSKPLSEKPIubiquitination[1, 2, 4]
971TSKPLSEKPITHKVEubiquitination[1, 2, 4]
976SEKPITHKVEEEDGKubiquitination[1, 2, 4]
983KVEEEDGKTATQPLLubiquitination[1, 2]
991TATQPLLKKESKGPIubiquitination[1, 2]
995PLLKKESKGPIVPLNubiquitination[1, 2, 5]
1007PLNVADQKLLEASTQubiquitination[1, 2, 3]
1017EASTQFQKKQGKNTIubiquitination[1, 2]
1061IRVFIGGKINRIDHDubiquitination[1, 2, 5, 7]
1078AMATLLSKFRIDFSDubiquitination[5]
1095VLGDINTKPKKENIIubiquitination[1, 2]
1098DINTKPKKENIIAFEubiquitination[1, 2, 6]
1118YRLHEDDKEQDIADKubiquitination[1, 2]
1125KEQDIADKMKEDEPWubiquitination[1]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [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] 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]
 [7] 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] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1150 AA 
Protein Sequence
MEPRPTAPSS GAPGLAGVGE TPSAAALAAA RVELPGTAVP SVPEDAAPAS RDGGGVRDEG 60
PAAAGDGLGR PLGPTPSQSR FQVDLVSENA GRAAAAAAAA AAAAAAAGAG AGAKQTPADG 120
EASGESEPAK GSEEAKGRFR VNFVDPAASS SAEDSLSDAA GVGVDGPNVS FQNGGDTVLS 180
EGSSLHSGGG GGSGHHQHYY YDTHTNTYYL RTFGHNTMDA VPRIDHYRHT AAQLGEKLLR 240
PSLAELHDEL EKEPFEDGFA NGEESTPTRD AVVTYTAESK GVVKFGWIKG VLVRCMLNIW 300
GVMLFIRLSW IVGQAGIGLS VLVIMMATVV TTITGLSTSA IATNGFVRGG GAYYLISRSL 360
GPEFGGAIGL IFAFANAVAV AMYVVGFAET VVELLKEHSI LMIDEINDIR IIGAITVVIL 420
LGISVAGMEW EAKAQIVLLV ILLLAIGDFV IGTFIPLESK KPKGFFGYKS EIFNENFGPD 480
FREEETFFSV FAIFFPAATG ILAGANISGD LADPQSAIPK GTLLAILITT LVYVGIAVSV 540
GSCVVRDATG NVNDTIVTEL TNCTSAACKL NFDFSSCESS PCSYGLMNNF QVMSMVSGFT 600
PLISAGIFSA TLSSALASLV SAPKIFQALC KDNIYPAFQM FAKGYGKNNE PLRGYILTFL 660
IALGFILIAE LNVIAPIISN FFLASYALIN FSVFHASLAK SPGWRPAFKY YNMWISLLGA 720
ILCCIVMFVI NWWAALLTYV IVLGLYIYVT YKKPDVNWGS STQALTYLNA LQHSIRLSGV 780
EDHVKNFRPQ CLVMTGAPNS RPALLHLVHD FTKNVGLMIC GHVHMGPRRQ AMKEMSIDQA 840
KYQRWLIKNK MKAFYAPVHA DDLREGAQYL MQAAGLGRMK PNTLVLGFKK DWLQADMRDV 900
DMYINLFHDA FDIQYGVVVI RLKEGLDISH LQGQEELLSS QEKSPGTKDV VVSVEYSKKS 960
DLDTSKPLSE KPITHKVEEE DGKTATQPLL KKESKGPIVP LNVADQKLLE ASTQFQKKQG 1020
KNTIDVWWLF DDGGLTLLIP YLLTTKKKWK DCKIRVFIGG KINRIDHDRR AMATLLSKFR 1080
IDFSDIMVLG DINTKPKKEN IIAFEEIIEP YRLHEDDKEQ DIADKMKEDE PWRITDNELE 1140
LYKTKFYEPC 1150 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:InterPro.
 GO:0015377; F:cation:chloride symporter activity; IEA:InterPro. 
Interpro
 IPR004841; AA-permease_dom.
 IPR013612; AA_permease_N.
 IPR002443; Na/K/Cl_cotranspt.
 IPR002444; Na/K/Cl_cotranspt1.
 IPR004842; Na/K/Cl_cotransptS. 
Pfam
 PF00324; AA_permease
 PF08403; AA_permease_N 
SMART
  
PROSITE
  
PRINTS
 PR01207; NAKCLTRNSPRT.
 PR01208; NAKCLTRSPRT1.