UniProt Accession

 TP4A1_HUMAN; Q93096; B2R6C8; O00648; Q49A54 

Genbank Protein ID

 U48296; AF051160; AK312526; CR749458; AL135905; CH471143; BC023975; BC045571; U69701 

Genbank Nucleotide ID

 AAB40597.1; AAC39836.1; BAG35425.1; CAH18292.1; CAC12761.1; EAW88494.1; AAH23975.1; AAH45571.1; AAB09080.1 

Protein Name

 Protein tyrosine phosphatase type IVA 1 

Protein Synonyms/Alias

 PTP(CAAXI); Protein-tyrosine phosphatase 4a1; Protein-tyrosine phosphatase of regenerating liver 1; PRL-1 

Gene Name

 PTP4A1 

Gene Synonyms/Alias

 PRL1; PTPCAAX1 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
15	APVEVTYKNMRFLIT	ubiquitination	[1, 2, 3]
32	PTNATLNKFIEELKK	ubiquitination	[1, 2, 3]
144	RRGAFNSKQLLYLEK	ubiquitination	[1, 2, 3, 4, 5, 6]
151	KQLLYLEKYRPKMRL	ubiquitination	[1, 2, 3]

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] 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]
 [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] 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]
 [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] 

Functional Description

 Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. May play a role in the development and maintenance of differentiating epithelial tissues. Enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. 

Sequence Annotation

 DOMAIN 82 148 Tyrosine-protein phosphatase.
 REGION 97 132 Interaction with ATF5 (By similarity).
 REGION 105 110 Phosphate binding.
 ACT_SITE 72 72 Proton donor (Probable).
 ACT_SITE 104 104 Phosphocysteine intermediate.
 BINDING 110 110 Substrate.
 MOD_RES 170 170 Cysteine methyl ester (Probable).
 LIPID 170 170 S-farnesyl cysteine.
 DISULFID 49 104  

Keyword

 3D-structure; Cell cycle; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Developmental protein; Disulfide bond; Endoplasmic reticulum; Endosome; Hydrolase; Lipoprotein; Membrane; Methylation; Prenylation; Protein phosphatase; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 173 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
 GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
 GO:0009898; C:internal side of plasma membrane; IDA:UniProtKB.
 GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
 GO:0004725; F:protein tyrosine phosphatase activity; NAS:UniProtKB.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
 GO:0030335; P:positive regulation of cell migration; IEA:Compara. 

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