CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017154
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tensin-4 
Protein Synonyms/Alias
 C-terminal tensin-like protein 
Gene Name
 TNS4 
Gene Synonyms/Alias
 CTEN; PP14434 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
75QAPQVEAKATCFLPSubiquitination[1, 2]
140STMSMRKKEESEALDubiquitination[3]
518FLIESSAKGVHLKGAubiquitination[3]
577DSPASCQKKSAGCHTubiquitination[1, 3]
Reference
 [1] 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]
 [2] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [3] 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
 May be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton (By similarity). May promote apoptosis, via its cleavage by caspase-3. 
Sequence Annotation
 DOMAIN 449 556 SH2.
 DOMAIN 548 714 Phosphatase tensin-type.
 MOD_RES 82 82 Phosphoserine.
 MOD_RES 248 248 Phosphoserine.  
Keyword
 Actin-binding; Apoptosis; Cell junction; Complete proteome; Cytoplasm; Cytoskeleton; Phosphoprotein; Polymorphism; Reference proteome; SH2 domain; Signal. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 715 AA 
Protein Sequence
MSQVMSSPLL AGGHAVSLAP CDEPRRTLHP APSPSLPPQC SYYTTEGWGA QALMAPVPCM 60
GPPGRLQQAP QVEAKATCFL PSPGEKALGT PEDLDSYIDF SLESLNQMIL ELDPTFQLLP 120
PGTGGSQAEL AQSTMSMRKK EESEALDIKY IEVTSARSRC HDGPQHCSSP SVTPPFGSLR 180
SGGLLLSRDV PRETRSSSES LIFSGNQGRG HQRPLPPSEG LSPRPPNSPS ISIPCMGSKA 240
SSPHGLGSPL VASPRLEKRL GGLAPQRGSR ISVLSASPVS DVSYMFGSSQ SLLHSSNSSH 300
QSSSRSLESP ANSSSSLHSL GSVSLCTRPS DFQAPRNPTL TMGQPRTPHS PPLAKEHASS 360
CPPSITNSMV DIPIVLINGC PEPGSSPPQR TPGHQNSVQP GAASPSNPCP ATRSNSQTLS 420
DAPFTTCPEG PARDMQPTMK FVMDTSKYWF KPNITREQAI ELLRKEEPGA FVIRDSSSYR 480
GSFGLALKVQ EVPASAQSRP GEDSNDLIRH FLIESSAKGV HLKGADEEPY FGSLSAFVCQ 540
HSIMALALPC KLTIPQRELG GADGASDSTD SPASCQKKSA GCHTLYLSSV SVETLTGALA 600
VQKAISTTFE RDILPTPTVV HFKVTEQGIT LTDVQRKVFF RRHYPLTTLR FCGMDPEQRK 660
WQKYCKPSWI FGFVAKSQTE PQENVCHLFA EYDMVQPASQ VIGLVTALLQ DAERM 715 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0005925; C:focal adhesion; IDA:UniProtKB.
 GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
 GO:0008104; P:protein localization; IDA:UniProtKB. 
Interpro
 IPR011993; PH_like_dom.
 IPR013625; PTB.
 IPR000980; SH2. 
Pfam
 PF08416; PTB
 PF00017; SH2 
SMART
 SM00252; SH2 
PROSITE
 PS51181; PPASE_TENSIN
 PS50001; SH2 
PRINTS