CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004639
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Receptor-type tyrosine-protein phosphatase alpha 
Protein Synonyms/Alias
 Protein-tyrosine phosphatase alpha; R-PTP-alpha; LCA-related phosphatase; PTPTY-28 
Gene Name
 Ptpra 
Gene Synonyms/Alias
 Lrp; Ptpa 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
279AVSKDAVKALNKTTPacetylation[1]
334FINGYQEKNKFIAAQubiquitination[2]
409LVDYTVRKFCIQQVGacetylation[3]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [3] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441
Functional Description
  
Sequence Annotation
 DOMAIN 232 528 Tyrosine-protein phosphatase 1.
 DOMAIN 560 818 Tyrosine-protein phosphatase 2.
 REGION 469 475 Substrate binding (By similarity).
 ACT_SITE 469 469 Phosphocysteine intermediate (By
 ACT_SITE 759 759 Phosphocysteine intermediate (By
 BINDING 437 437 Substrate (By similarity).
 BINDING 513 513 Substrate (By similarity).
 MOD_RES 180 180 Phosphoserine.
 MOD_RES 204 204 Phosphoserine.
 MOD_RES 825 825 Phosphotyrosine.
 CARBOHYD 21 21 N-linked (GlcNAc...) (Potential).
 CARBOHYD 47 47 N-linked (GlcNAc...) (Potential).
 CARBOHYD 51 51 N-linked (GlcNAc...) (Potential).
 CARBOHYD 68 68 N-linked (GlcNAc...) (Potential).
 CARBOHYD 80 80 N-linked (GlcNAc...) (Potential).
 CARBOHYD 86 86 N-linked (GlcNAc...) (Potential).
 CARBOHYD 104 104 N-linked (GlcNAc...) (Potential).
 CARBOHYD 124 124 N-linked (GlcNAc...) (Potential).  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Direct protein sequencing; Glycoprotein; Hydrolase; Membrane; Phosphoprotein; Protein phosphatase; Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 829 AA 
Protein Sequence
MDSWFILVLF GSGLIHVSAN NATTVSPSLG TTRLIKTSTT ELAKEENKTS NSTSSVISLS 60
VAPTFSPNLT LEPTYVTTVN SSHSDNGTRR AASTESGGTT ISPNGSWLIE NQFTDAITEP 120
WEGNSSTAAT TPETFPPADE TPIIAVMVAL SSLLVIVFII IVLYMLRFKK YKQAGSHSNS 180
FRLSNGRTED VEPQSVPLLA RSPSTNRKYP PLPVDKLEEE INRRMADDNK LFREEFNALP 240
ACPIQATCEA ASKEENKEKN RYVNILPFLS LAVSKDAVKA LNKTTPLLER RFIGKSNSRG 300
CLSDDHSRVH LTPVEGVPDS DYINASFING YQEKNKFIAA QGPKEETVND FWRMIWEQNT 360
ATIVMVTNLK ERKECKCAQY WPDQGCWTYG NVRVSVEDVT VLVDYTVRKF CIQQVGDVTN 420
RKPQRLITQF HFTSWPDFGV PFTPIGMLKF LKKVKACNPQ YAGAIVVHCS AGVGRTGTFV 480
VIDAMLDMMH SERKVDVYGF VSRIRAQRCQ MVQTDMQYVF IYQALLEHYL YGDTELEVTS 540
LETHLQKIYN KIPGTSNNGL EEEFKKLTSI KIQNDKMRTG NLPANMKKNR VLQIIPYEFN 600
RVIIPVKRGE ENTDYVNASF IDGYRQKDSY IASQGPLLHT IEDFWRMIWE WKSCSIVMLT 660
ELEERGQEKC AQYWPSDGLV SYGDITVELK KEEECESYTV RDLLVTNTRE NKSRQIRQFH 720
FHGWPEVGIP SDGKGMINII AAVQKQQQQS GNHPITVHCS AGAGRTGTFC ALSTVLERVK 780
AEGILDVFQT VKSLRLQRPH MVQTLEQYEF CYKVVQEYID AFSDYANFK 829 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0004725; F:protein tyrosine phosphatase activity; IEA:EC.
 GO:0008286; P:insulin receptor signaling pathway; IMP:MGI.
 GO:0035335; P:peptidyl-tyrosine dephosphorylation; IEA:GOC.
 GO:0006468; P:protein phosphorylation; IDA:MGI. 
Interpro
 IPR000387; Tyr/Dual-sp_Pase.
 IPR016130; Tyr_Pase_AS.
 IPR000242; Tyr_Pase_rcpt/non-rcpt.
 IPR016336; Tyr_Pase_rcpt_a/e-type.
 IPR027262; Tyr_Pase_rcpt_alpha. 
Pfam
 PF00102; Y_phosphatase 
SMART
 SM00194; PTPc 
PROSITE
 PS00383; TYR_PHOSPHATASE_1
 PS50056; TYR_PHOSPHATASE_2
 PS50055; TYR_PHOSPHATASE_PTP 
PRINTS
 PR00700; PRTYPHPHTASE.