CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012613
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Microtubule-associated protein RP/EB family member 1 
Protein Synonyms/Alias
 APC-binding protein EB1; End-binding protein 1; EB1 
Gene Name
 MAPRE1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
66KKVKFQAKLEHEYIQacetylation[1, 2]
66KKVKFQAKLEHEYIQubiquitination[3, 4]
76HEYIQNFKILQAGFKacetylation[2, 5]
76HEYIQNFKILQAGFKubiquitination[3, 4]
83KILQAGFKRMGVDKIacetylation[5]
83KILQAGFKRMGVDKIubiquitination[3, 4, 6, 7]
89FKRMGVDKIIPVDKLacetylation[2, 5]
95DKIIPVDKLVKGKFQubiquitination[4, 5]
98IPVDKLVKGKFQDNFubiquitination[7]
100VDKLVKGKFQDNFEFubiquitination[3]
113EFVQWFKKFFDANYDubiquitination[3, 4]
122FDANYDGKDYDPVAAubiquitination[5, 7]
148LVAPALNKPKKPLTSacetylation[2]
148LVAPALNKPKKPLTSubiquitination[3, 4, 5, 6, 7]
150APALNKPKKPLTSSSubiquitination[7]
151PALNKPKKPLTSSSAubiquitination[4]
174QRTAAAPKAGPGVVRubiquitination[4, 7]
182AGPGVVRKNPGVGNGubiquitination[7]
212LTVEDLEKERDFYFGubiquitination[3]
220ERDFYFGKLRNIELIubiquitination[4]
Reference
 [1] 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]
 [2] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [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] 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]
 [5] 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]
 [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] 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
Functional Description
 Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes cytoplasmic microtubule nucleation and elongation. May be involved in spindle function by stabilizing microtubules and anchoring them at centrosomes. May play a role in cell migration. 
Sequence Annotation
 DOMAIN 14 116 CH.
 DOMAIN 185 255 EB1 C-terminal.
 REGION 124 268 Interaction with MTUS2/TIP150.
 REGION 185 268 Interaction with CDK5RAP2.
 REGION 208 268 DCTN1-binding.
 REGION 220 242 APC-binding.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 124 124 Phosphotyrosine.  
Keyword
 3D-structure; Acetylation; Cell cycle; Cell division; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Microtubule; Mitosis; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 268 AA 
Protein Sequence
MAVNVYSTSV TSDNLSRHDM LAWINESLQL NLTKIEQLCS GAAYCQFMDM LFPGSIALKK 60
VKFQAKLEHE YIQNFKILQA GFKRMGVDKI IPVDKLVKGK FQDNFEFVQW FKKFFDANYD 120
GKDYDPVAAR QGQETAVAPS LVAPALNKPK KPLTSSSAAP QRPISTQRTA AAPKAGPGVV 180
RKNPGVGNGD DEAAELMQQV NVLKLTVEDL EKERDFYFGK LRNIELICQE NEGENDPVLQ 240
RIVDILYATD EGFVIPDEGG PQEEQEEY 268 
Gene Ontology
 GO:0031253; C:cell projection membrane; IEA:Compara.
 GO:0005813; C:centrosome; IDA:UniProtKB.
 GO:0030981; C:cortical microtubule cytoskeleton; IDA:UniProtKB.
 GO:0005881; C:cytoplasmic microtubule; IEA:Compara.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005794; C:Golgi apparatus; IEA:Compara.
 GO:0005874; C:microtubule; IDA:UniProtKB.
 GO:0035371; C:microtubule plus end; IEA:Compara.
 GO:0051010; F:microtubule plus-end binding; IDA:UniProtKB.
 GO:0008022; F:protein C-terminus binding; TAS:ProtInc.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0008283; P:cell proliferation; TAS:ProtInc.
 GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0031115; P:negative regulation of microtubule polymerization; IDA:UniProtKB.
 GO:0035372; P:protein localization to microtubule; IDA:UniProtKB. 
Interpro
 IPR001715; CH-domain.
 IPR004953; EB1_C.
 IPR027328; MAPRE. 
Pfam
 PF00307; CH
 PF03271; EB1 
SMART
  
PROSITE
 PS50021; CH
 PS51230; EB1_C 
PRINTS