CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-031205
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tyrosine-protein phosphatase non-receptor type 23 
Protein Synonyms/Alias
 cDNA FLJ58078, highly similar to Tyrosine-protein phosphatase non-receptortype 23 (EC 3.1.3.48) 
Gene Name
 PTPN23 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
89AQVVDYYKEACRALEubiquitination[1, 2]
109SLLGRIQKDWKKLVQubiquitination[3]
153YFQSALDKLNEAIKLubiquitination[2, 3, 4, 5, 6, 7]
159DKLNEAIKLAKGQPDubiquitination[2, 5, 7]
162NEAIKLAKGQPDTVQubiquitination[2, 3, 5, 7]
182TMDVIGGKYNSAKKDubiquitination[2]
187GGKYNSAKKDNDFIYubiquitination[2]
188GKYNSAKKDNDFIYHubiquitination[2]
214VKGAPLVKPLPVNPTubiquitination[2, 3, 5]
482LFEEQLKKYDQLKVYmethylation[8]
487LKKYDQLKVYLEQNLmethylation[8]
1094IARCYSLKNRHQDVMubiquitination[2]
1509DPLWTLNKT******ubiquitination[2, 3]
Reference
 [1] 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]
 [2] 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]
 [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 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]
 [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]
 [6] 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]
 [7] 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]
 [8] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Hydrolase; Protein phosphatase; Receptor; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1510 AA 
Protein Sequence
MLGAMDKRVS EEGMKVSCTH FQCAAGAFAY LREHFPQAYS VDMSRQILTL NVNLMLGQAQ 60
ECLLEKSMLD NRKSFLVARI SAQVVDYYKE ACRALENPDT ASLLGRIQKD WKKLVQMKIY 120
YFAAVAHLHM GKQAEEQQKF GERVAYFQSA LDKLNEAIKL AKGQPDTVQD ALRFTMDVIG 180
GKYNSAKKDN DFIYHEAVPA LDTLQPVKGA PLVKPLPVNP TDPAVTGPDI FAKLVPMAAH 240
EASSLYSEEK AKLLREMMAK IEDKNEVLDQ FMDSMQLDPE TVDNLDAYSH IPPQLMEKCA 300
ALSVRPDTVR NLVQSMQVLS GVFTDVEASL KDIRDLLEED ELLEQKFQEA VGQAGAISIT 360
SKAELAEVRR EWAKYMEVHE KASFTNSELH RAMNLHVGNL RLLSGPLDQV RAALPTPALS 420
PEDKAVLQNL KRILAKVQEM RDQRVSLEQQ LRELIQKDDI TASLVTTDHS EMKKLFEEQL 480
KKYDQLKVYL EQNLAAQDRV LCALTEANVQ YAAVRRVLSD LDQKWNSTLQ TLVASYEAYE 540
DLMKKSQEGR DFYADLESKV AALLERTQST CQAREAARQQ LLDRELKKKP PPRPTAPKPL 600
LPRREESEAV EAGDPPEELR SLPPDMVAGP RLPDTFLGSA TPLHFPPSPF PSSTGPGPHY 660
LSGPLPPGTY SGPTQLIQPR APGPHAMPVA PGPALYPAPA YTPELGLVPR SSPQHGVVSS 720
PYVGVGPAPP VAGLPSAPPP QFSGPELAMA VRPATTTVDS IQAPIPSHTA PRPNPTPAPP 780
PPCFPVPPPQ PLPTPYTYPA GAKQPIPAQH HFSSGIPAGF PAPRIGPQPQ PHPQPHPSQA 840
FGPQPPQQPL PLQHPHLFPP QAPGLLPPQS PYPYAPQPGV LGQPPPPLHT QLYPGPAQDP 900
LPAHSGALPF PSPGPPQPPH PPLAYGPAPS TRPMGPQAAP LTIRGPSSAG QSTPSPHLVP 960
SPAPSPGPGP VPPRPPAAEP PPCLRRGAAA ADLLSSSPES QHGGTQSPGG GQPLLQPTKV 1020
DAAEGRRPQA LRLIERDPYE HPERLRQLQQ ELEAFRGQLG DVGALDTVWR ELQDAQEHDA 1080
RGRSIAIARC YSLKNRHQDV MPYDSNRVVL RSGKDDYINA SCVEGLSPYC PPLVATQAPL 1140
PGTAADFWLM VHEQKVSVIV MLVSEAEMEK QKVARYFPTE RGQPMVHGAL SLALSSVRST 1200
ETHVERVLSL QFRDQSLKRS LVHLHFPTWP ELGLPDSPSN LLRFIQEVHA HYLHQRPLHT 1260
PIIVHCSSGV GRTGAFALLY AAVQEVEAGN GIPELPQLVR RMRQQRKHML QEKLHLRFCY 1320
EAVVRHVEQV LQRHGVPPPC KPLASASISQ KNHLPQDSQD LVLGGDVPIS SIQATIAKLS 1380
IRPPGGLESP VASLPGPAEP PGLPPASLPE STPIPSSSPP PLSSPLPEAP QPKEEPPVPE 1440
APSSGPPSSS LELLASLTPE AFSLDSSLRG KQRMSKHNFL QAHNGQGLRA TRPSDDPLSL 1500
LDPLWTLNKT 1510 
Gene Ontology
 GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
 GO:0035335; P:peptidyl-tyrosine dephosphorylation; IEA:GOC. 
Interpro
 IPR025304; ALIX_V_dom.
 IPR004328; BRO1_dom.
 IPR000387; Tyr/Dual-sp_Pase.
 IPR016130; Tyr_Pase_AS.
 IPR000242; Tyr_Pase_rcpt/non-rcpt. 
Pfam
 PF13949; ALIX_LYPXL_bnd
 PF03097; BRO1
 PF00102; Y_phosphatase 
SMART
 SM01041; BRO1
 SM00194; PTPc 
PROSITE
 PS51180; BRO1
 PS00383; TYR_PHOSPHATASE_1
 PS50056; TYR_PHOSPHATASE_2
 PS50055; TYR_PHOSPHATASE_PTP 
PRINTS
 PR00700; PRTYPHPHTASE.