CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012583
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Microtubule-associated protein RP/EB family member 2 
Protein Synonyms/Alias
 APC-binding protein EB2; End-binding protein 2; EB2 
Gene Name
 MAPRE2 
Gene Synonyms/Alias
 RP1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
119HEYIHNFKLLQASFKubiquitination[1]
126KLLQASFKRMNVDKVubiquitination[1, 2]
132FKRMNVDKVIPVEKLubiquitination[1]
138DKVIPVEKLVKGRFQubiquitination[1]
141IPVEKLVKGRFQDNLubiquitination[1]
155LDFIQWFKKFYDANYubiquitination[1, 2, 3, 4]
156DFIQWFKKFYDANYDubiquitination[1, 2]
165YDANYDGKEYDPVEAubiquitination[1, 2]
194QIFNLPKKSHHANSPubiquitination[1]
271ERDFYFGKLREIELLacetylation[5]
271ERDFYFGKLREIELLubiquitination[1, 3, 6, 7]
Reference
 [1] 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]
 [2] 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]
 [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] 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]
 [5] 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]
 [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] 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
Functional Description
 May be involved in microtubule polymerization, and spindle function by stabilizing microtubules and anchoring them at centrosomes. May play a role in cell migration (By similarity). 
Sequence Annotation
 DOMAIN 57 159 CH.
 DOMAIN 236 306 EB1 C-terminal.
 REGION 187 327 DCTN1-binding.
 REGION 259 302 APC-binding.
 MOD_RES 167 167 Phosphotyrosine.
 MOD_RES 219 219 Phosphoserine.  
Keyword
 Alternative splicing; Cell cycle; Cell division; Complete proteome; Cytoplasm; Cytoskeleton; Microtubule; Mitosis; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 327 AA 
Protein Sequence
MPGPTQTLSP NGENNNDIIQ DNNGTIIPFR KHTVRGERSY SWGMAVNVYS TSITQETMSR 60
HDIIAWVNDI VSLNYTKVEQ LCSGAAYCQF MDMLFPGCIS LKKVKFQAKL EHEYIHNFKL 120
LQASFKRMNV DKVIPVEKLV KGRFQDNLDF IQWFKKFYDA NYDGKEYDPV EARQGQDAIP 180
PPDPGEQIFN LPKKSHHANS PTAGAAKSSP AAKPGSTPSR PSSAKRASSS GSASKSDKDL 240
ETQVIQLNEQ VHSLKLALEG VEKERDFYFG KLREIELLCQ EHGQENDDLV QRLMDILYAS 300
EEHEGHTEEP EAEEQAHEQQ PPQQEEY 327 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
 GO:0005874; C:microtubule; IEA:UniProtKB-KW.
 GO:0015630; C:microtubule cytoskeleton; IDA:LIFEdb.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0008283; P:cell proliferation; TAS:ProtInc.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0007165; P:signal transduction; TAS:ProtInc. 
Interpro
 IPR001715; CH-domain.
 IPR004953; EB1_C.
 IPR027328; MAPRE. 
Pfam
 PF00307; CH
 PF03271; EB1 
SMART
  
PROSITE
 PS50021; CH
 PS51230; EB1_C 
PRINTS