CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012297
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Src substrate cortactin 
Protein Synonyms/Alias
 Amplaxin; Oncogene EMS1 
Gene Name
 CTTN 
Gene Synonyms/Alias
 EMS1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
87ASHGYGGKFGVEQDRubiquitination[1, 2]
124SVRGFGGKFGVQMDRubiquitination[1, 2, 3]
144VGFEYQGKTEKHASQubiquitination[1, 2]
161YSSGFGGKYGVQADRubiquitination[1, 2]
171VQADRVDKSAVGFDYubiquitination[1, 2]
181VGFDYQGKTEKHESQubiquitination[1, 2]
198YSKGFGGKYGIDKDKubiquitination[1, 2]
208IDKDKVDKSAVGFEYubiquitination[1, 2]
235YVKGFGGKFGVQTDRacetylation[4]
235YVKGFGGKFGVQTDRubiquitination[1, 2, 3]
272YKTGFGGKFGVQSERacetylation[4]
272YKTGFGGKFGVQSERubiquitination[1, 2]
309YSKGFGGKYGVQKDRacetylation[4]
336QVSSAYQKTVPVEAVubiquitination[5]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [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] 
Functional Description
 Contributes to the organization of the actin cytoskeleton and cell structure. In complex with ABL1 and MYLK regulates cortical actin-based cytoskeletal rearrangement critical to sphingosine 1-phosphate (S1P)-mediated endothelial cell (EC) barrier enhancement. Plays a role in the regulation of cell migration. Plays a role in the invasiveness of cancer cells, and the formation of metastases. 
Sequence Annotation
 REPEAT 80 116 Cortactin 1.
 REPEAT 117 153 Cortactin 2.
 REPEAT 154 190 Cortactin 3.
 REPEAT 191 227 Cortactin 4.
 REPEAT 228 264 Cortactin 5.
 REPEAT 265 301 Cortactin 6.
 REPEAT 302 324 Cortactin 7; truncated.
 DOMAIN 492 550 SH3.
 MOD_RES 87 87 N6-acetyllysine.
 MOD_RES 198 198 N6-acetyllysine.
 MOD_RES 235 235 N6-acetyllysine.
 MOD_RES 272 272 N6-acetyllysine.
 MOD_RES 304 304 N6-acetyllysine.
 MOD_RES 309 309 N6-acetyllysine.
 MOD_RES 399 399 Phosphothreonine.
 MOD_RES 401 401 Phosphothreonine.
 MOD_RES 405 405 Phosphoserine.
 MOD_RES 411 411 Phosphothreonine.
 MOD_RES 417 417 Phosphoserine.
 MOD_RES 418 418 Phosphoserine.
 MOD_RES 421 421 Phosphotyrosine; by SRC.
 MOD_RES 446 446 Phosphotyrosine.
 MOD_RES 453 453 Phosphotyrosine.
 MOD_RES 486 486 Phosphotyrosine; by SRC.
 MOD_RES 489 489 Phosphotyrosine; by SRC.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Cell projection; Complete proteome; Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome; Repeat; SH3 domain. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 550 AA 
Protein Sequence
MWKASAGHAV SIAQDDAGAD DWETDPDFVN DVSEKEQRWG AKTVQGSGHQ EHINIHKLRE 60
NVFQEHQTLK EKELETGPKA SHGYGGKFGV EQDRMDKSAV GHEYQSKLSK HCSQVDSVRG 120
FGGKFGVQMD RVDQSAVGFE YQGKTEKHAS QKDYSSGFGG KYGVQADRVD KSAVGFDYQG 180
KTEKHESQRD YSKGFGGKYG IDKDKVDKSA VGFEYQGKTE KHESQKDYVK GFGGKFGVQT 240
DRQDKCALGW DHQEKLQLHE SQKDYKTGFG GKFGVQSERQ DSAAVGFDYK EKLAKHESQQ 300
DYSKGFGGKY GVQKDRMDKN ASTFEDVTQV SSAYQKTVPV EAVTSKTSNI RANFENLAKE 360
KEQEDRRKAE AERAQRMAKE RQEQEEARRK LEEQARAKTQ TPPVSPAPQP TEERLPSSPV 420
YEDAASFKAE LSYRGPVSGT EPEPVYSMEA ADYREASSQQ GLAYATEAVY ESAEAPGHYP 480
AEDSTYDEYE NDLGITAVAL YDYQAAGDDE ISFDPDDIIT NIEMIDDGWW RGVCKGRYGL 540
FPANYVELRQ 550 
Gene Ontology
 GO:0005938; C:cell cortex; ISS:UniProtKB.
 GO:0005856; C:cytoskeleton; TAS:ProtInc.
 GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
 GO:0030027; C:lamellipodium; ISS:UniProtKB.
 GO:0001726; C:ruffle; ISS:UniProtKB. 
Interpro
 IPR015503; Cortactin.
 IPR003134; Hs1_Cortactin.
 IPR000108; p67phox.
 IPR001452; SH3_domain. 
Pfam
 PF02218; HS1_rep
 PF00018; SH3_1 
SMART
 SM00326; SH3 
PROSITE
 PS51090; CORTACTIN
 PS50002; SH3 
PRINTS
 PR00499; P67PHOX.
 PR00452; SH3DOMAIN.