CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011961
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein tyrosine phosphatase type IVA 2 
Protein Synonyms/Alias
 HU-PP-1; OV-1; PTP(CAAXII); Protein-tyrosine phosphatase 4a2; Protein-tyrosine phosphatase of regenerating liver 2; PRL-2 
Gene Name
 PTP4A2 
Gene Synonyms/Alias
 PRL2; PTPCAAX2; BM-008 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
29PTNATLNKFTEELKKubiquitination[1, 2, 3]
36KFTEELKKYGVTTLVubiquitination[1, 2, 3]
141RRGAFNSKQLLYLEKubiquitination[1, 2, 3, 4, 5, 6, 7]
148KQLLYLEKYRPKMRLubiquitination[1, 2, 7]
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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [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
Functional Description
 Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. Promotes tumors. Inhibits geranylgeranyl transferase type II activity by blocking the association between RABGGTA and RABGGTB. 
Sequence Annotation
 DOMAIN 79 145 Tyrosine-protein phosphatase.
 REGION 102 107 Phosphate binding (By similarity).
 ACT_SITE 69 69 Proton donor (By similarity).
 ACT_SITE 101 101 Phosphocysteine intermediate.
 BINDING 107 107 Substrate (By similarity).
 MOD_RES 164 164 Cysteine methyl ester (Probable).
 LIPID 164 164 S-farnesyl cysteine.
 DISULFID 46 101 By similarity.  
Keyword
 Alternative splicing; Cell membrane; Complete proteome; Cytoplasm; Disulfide bond; Endosome; Hydrolase; Lipoprotein; Membrane; Methylation; Prenylation; Protein phosphatase; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 167 AA 
Protein Sequence
MNRPAPVEIS YENMRFLITH NPTNATLNKF TEELKKYGVT TLVRVCDATY DKAPVEKEGI 60
HVLDWPFDDG APPPNQIVDD WLNLLKTKFR EEPGCCVAVH CVAGLGRAPV LVALALIECG 120
MKYEDAVQFI RQKRRGAFNS KQLLYLEKYR PKMRLRFRDT NGHCCVQ 167 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0004727; F:prenylated protein tyrosine phosphatase activity; TAS:ProtInc. 
Interpro
 IPR000387; Tyr/Dual-sp_Pase.
 IPR000242; Tyr_Pase_rcpt/non-rcpt. 
Pfam
 PF00102; Y_phosphatase 
SMART
  
PROSITE
 PS00383; TYR_PHOSPHATASE_1
 PS50056; TYR_PHOSPHATASE_2
 PS50055; TYR_PHOSPHATASE_PTP 
PRINTS