CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-039740
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 4F2 cell-surface antigen heavy chain 
Protein Synonyms/Alias
  
Gene Name
 SLC3A2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
80QDTEVDMKEVELNELubiquitination[1, 2, 3]
91LNELEPEKQPMNAASubiquitination[1, 2, 3, 4]
109MSLAGAEKNGLVKIKubiquitination[1, 2, 3]
114AEKNGLVKIKVAEDEubiquitination[1, 2, 3]
116KNGLVKIKVAEDEAEubiquitination[1, 2, 3, 4, 5, 6, 7, 8, 9]
129AEAAAAAKFTGLSKEubiquitination[1, 2, 5, 6, 8, 9]
135AKFTGLSKEELLKVAubiquitination[1, 2, 6]
186CRELPAQKWWHTGALubiquitination[8]
214AGNLAGLKGRLDYLSubiquitination[1, 2, 3, 8]
224LDYLSSLKVKGLVLGubiquitination[2, 3, 8]
226YLSSLKVKGLVLGPIubiquitination[3, 8]
238GPIHKNQKDDVAQTDubiquitination[1, 3, 8]
256IDPNFGSKEDFDSLLubiquitination[1, 2, 3]
267DSLLQSAKKKSIRVIubiquitination[1]
298QVDTVATKVKDALEFubiquitination[1, 2, 3]
300DTVATKVKDALEFWLubiquitination[8]
323VRDIENLKDASSFLAubiquitination[1, 2, 3, 8]
337AEWQNITKGFSEDRLubiquitination[1, 2, 3]
385GSTGEHTKSLVTQYLubiquitination[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] 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]
 [3] 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]
 [4] A data set of human endogenous protein ubiquitination sites.
 Shi Y, Chan DW, Jung SY, Malovannaya A, Wang Y, Qin J.
 Mol Cell Proteomics. 2011 May;10(5):M110.002089. [PMID: 20972266]
 [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] 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] 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]
 [8] 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]
 [9] 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
 599 AA 
Protein Sequence
MELQPPEASI AVVSIPRQLP GSHSEAGVQG LSAGDDSETG SDCVTQAGLQ LLASSDPPAL 60
ASKNAEVTGT MSQDTEVDMK EVELNELEPE KQPMNAASGA AMSLAGAEKN GLVKIKVAED 120
EAEAAAAAKF TGLSKEELLK VAGSPGWVRT RWALLLLFWL GWLGMLAGAV VIIVRAPRCR 180
ELPAQKWWHT GALYRIGDLQ AFQGHGAGNL AGLKGRLDYL SSLKVKGLVL GPIHKNQKDD 240
VAQTDLLQID PNFGSKEDFD SLLQSAKKKS IRVILDLTPN YRGENSWFST QVDTVATKVK 300
DALEFWLQAG VDGFQVRDIE NLKDASSFLA EWQNITKGFS EDRLLIAGTN SSDLQQILSL 360
LESNKDLLLT SSYLSDSGST GEHTKSLVTQ YLNATGNRWC SWSLSQARLL TSFLPAQLLR 420
LYQLMLFTLP GTPVFSYGDE IGLDAAALPG QPMEAPVMLW DESSFPDIPG AVSANMTVKG 480
QSEDPGSLLS LFRRLSDQRS KERSLLHGDF HAFSAGPGLF SYIRHWDQNE RFLVVLNFGD 540
VGLSAGLQAS DLPASASLPA KADLLLSTQP GREEGSPLEL ERLKLEPHEG LLLRFPYAA 599 
Gene Ontology
 GO:0003824; F:catalytic activity; IEA:InterPro.
 GO:0043169; F:cation binding; IEA:InterPro.
 GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. 
Interpro
 IPR015902; Glyco_hydro_13.
 IPR013780; Glyco_hydro_13_b.
 IPR006047; Glyco_hydro_13_cat_dom.
 IPR013781; Glyco_hydro_catalytic_dom.
 IPR017853; Glycoside_hydrolase_SF. 
Pfam
 PF00128; Alpha-amylase 
SMART
  
PROSITE
  
PRINTS