Pseudophosphatases (obsolete)
Contents
Human pseudophosphatases
PTPs
Second phosphatase domain (D2) in receptor PTPs
Most receptor PTPs have two tandem phosphatase domains. The 2nd phosphatase domain has no or negligible activity. The 2nd domain can interact with 1st domain in both intra- and intermolecular manners, therefore regulating receptor PTP stability, specificity, and dimerization [1, 2]. Because the first phosphatase domains are active, these receptor PTPs are active at protein level. These phosphatases include:
- Subfamily PTPRA: PTPRA and PTPRE
- Subfamily PTPRC: PTPRC
- Subfamily PTPRD: PTPRD, PTPRF and PTPRS
- Subfamily PTPRG: PTPRG and PTPRZ1
- Subfamily PTPRK: PTPRK, PTPRM, PTPRT and PTPRU
PTPN23 subfamily
The PTPN23 subfamily has a single member in human, PTPN23 (HD-PTP). Its catalytic activity is plausible. It has been reported to be catalytically inactive, - no phosphatase activity toward tyrosine or lipid. It was proposed that serine at position 1452 within Cx5R catalytic motif caused the inactivity. Replacing serine with alanine, which is found in catalytically active PTPs, can restore the phosphatase activity [3]. However, another study found SRC, E-cadherin, and beta-catenin are direct substrates of PTPN23 [4]. But, yet another study showed that PTPN23 did not modulate the levels of Src phosphorylation both in vitro and in vivo [5].
DSPs
STYX subfamily
The STYX subfamily has a single member in human, STYX. It binds to phosphorylated tyrosine to module signaling [6]. STYX localizes to the nucleus, competes with DUSP4 for binding to ERK, and acts as a nuclear anchor that regulates ERK nuclear export [7].
STYXL1 subfamily
The STYXL1 subfamily has a single member in human, STYXL1 (MK-STYX). STYXL1 binds to and modulate
One of the five of DSP3 subfamily: DUSP27
The function of DUSP27 is unknown, so is its catalytically inactive phosphatase domain.
PTEN-like phosphatases
Auxilin subfamily
There are two members of [[Phosphatase_Subfamily_Auxilin|auxilin subfamily] in human, GAK and DNAJC6. Both GAK and DNAJC6 phosphatase domains have been shown to bind to phospholipids [8, 9]. The phosphatase domains of both are predicted to be inactive due to arginine in catalytic motif Cx5R is replaced by alanine.
Tension subfamily
References
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