Affinage

UBASH3B

Ubiquitin-associated and SH3 domain-containing protein B · UniProt Q8TF42

Length
649 aa
Mass
72.7 kDa
Annotated
2026-04-28
31 papers in source corpus 21 papers cited in narrative 21 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

UBASH3B (Sts-1/TULA-2) is a multi-domain tyrosine phosphatase of the histidine phosphatase superfamily that broadly attenuates receptor-proximal signaling by dephosphorylating activated tyrosine kinases and their substrates. Its PGM-like catalytic domain dephosphorylates Syk (at pY346, pY352, pY323, pY525/526) and ZAP-70 to negatively regulate TCR, GPVI, FcγRIIA, FcεRI, and CLEC-2 signaling, and knockout mice exhibit hyperresponsive T cells, hyperactive platelets with a prothrombotic phenotype, and increased osteoclast numbers with reduced bone volume (PMID:14738763, PMID:20585042, PMID:27609517, PMID:23149425). UBASH3B also dephosphorylates CBL ubiquitin ligase, stabilizing EGFR at the cell surface and promoting invasion in triple-negative breast cancer, and dephosphorylates MRPL12 to regulate mitochondrial transcription and oxidative phosphorylation (PMID:23784775, PMID:39343960). Beyond its phosphatase function, UBASH3B acts as a ubiquitin receptor through its UBA domain, binding ubiquitylated Aurora B kinase to direct its relocalization to mitotic microtubules and ensure chromosome segregation fidelity (PMID:26766443).

Mechanistic history

Synthesis pass · year-by-year structured walk · 12 steps
  1. 2004 High

    The foundational question of whether UBASH3B participates in immune signaling was answered when Sts-1/Sts-2 double-knockout mice revealed hyperresponsive T cells with elevated ZAP-70 phosphorylation, establishing UBASH3B as a negative regulator of TCR signaling.

    Evidence Double-knockout mice with phosphorylation assays and cytokine measurement in T cells

    PMID:14738763

    Open questions at the time
    • Individual Sts-1 versus Sts-2 contributions not fully separated
    • Mechanism of ZAP-70 dephosphorylation not yet identified
    • Whether phosphatase activity was direct was unknown
  2. 2004 High

    The domain architecture and non-immune functions were established when UBASH3B was shown to interact with Cbl via its SH3 domain and with mono-ubiquitin via its UBA domain, and to inhibit EGFR/PDGFR endocytosis, revealing a role in receptor trafficking beyond TCR signaling.

    Evidence Reciprocal co-immunoprecipitation with domain-deletion constructs, receptor internalization assays

    PMID:15159412

    Open questions at the time
    • Whether the effect on endocytosis was phosphatase-dependent was unknown
    • In vivo relevance of receptor trafficking regulation not tested
  3. 2007 High

    A critical mechanistic question — whether UBASH3B acts as a phosphatase or an adaptor — was resolved by crystal structure determination and in vitro reconstitution showing intrinsic phosphatase activity through a histidine-based PGM-like catalytic domain, with active-site mutations impairing both enzymatic activity and TCR signaling regulation.

    Evidence X-ray crystallography, in vitro phosphatase assays, active-site mutagenesis with T cell signaling readouts

    PMID:17348005 PMID:17679096

    Open questions at the time
    • Physiological substrates beyond ZAP-70 not yet defined
    • Substrate specificity determinants unknown
  4. 2010 High

    UBASH3B's role was extended beyond T cells when it was shown to associate with and dephosphorylate Syk in platelets, negatively regulating GPVI signaling, and systematic peptide library screening defined two substrate-specificity classes and identified Syk pY323 and pY352 as preferred target sites.

    Evidence TULA-2 KO mouse platelet assays, in vitro dephosphorylation, combinatorial phosphopeptide library screening with kinetic analysis

    PMID:20585042 PMID:20670933

    Open questions at the time
    • Which Syk phosphosite is the primary regulatory target in vivo was unresolved
    • Role in other ITAM/hemITAM receptor pathways not yet tested
  5. 2012 High

    The range of immune receptors regulated by UBASH3B expanded further with demonstration that it is recruited to phosphorylated Syk C-terminal tyrosines in mast cells after FcεRI activation and suppresses degranulation and NF-κB/NFAT activation, while in bone it was shown to regulate osteoclastogenesis through Syk dephosphorylation at Y352 and Y525/526.

    Evidence Phosphopeptide pulldown with MS, siRNA knockdown in mast cells; DKO mouse skeletal analysis with phosphatase-dead mutant in osteoclasts

    PMID:22267732 PMID:23149425

    Open questions at the time
    • How UBASH3B is recruited to distinct receptor complexes remained unclear
    • Relative importance of different Syk phosphosites across cell types unresolved
  6. 2013 High

    A direct phosphatase–substrate relationship was validated when substrate-trapping mutants (H380A, E490A) retained high-affinity binding to phospho-ZAP-70, and UBASH3B was shown to dephosphorylate CBL, inactivating its E3 ligase function and upregulating EGFR to promote breast cancer invasion and metastasis.

    Evidence Active-site substrate-trapping mutagenesis in T cells; siRNA/phosphatase-dead mutant rescue in TNBC cells with xenograft model

    PMID:23784775 PMID:24256567

    Open questions at the time
    • Full catalogue of UBASH3B substrates beyond ZAP-70, Syk, and CBL unknown
    • Whether CBL dephosphorylation occurs in normal physiology not addressed
  7. 2016 High

    The primary regulatory mechanism in platelets was pinpointed to dephosphorylation of Syk pY346, and UBASH3B's role was extended to FcγRIIA signaling where its loss worsened heparin-induced thrombocytopenia; concurrently, a non-phosphatase function was discovered in which UBASH3B's UBA domain binds ubiquitylated Aurora B to control its mitotic localization and chromosome segregation fidelity.

    Evidence In vitro kinetics with site-specific phosphopeptides and KO platelet analysis; FcγRIIA-transgenic/TULA-2-KO mice with in vivo HIT model; Co-IP of ubiquitylated Aurora B, live-cell imaging, LOF/GOF mitotic assays

    PMID:26766443 PMID:27609517 PMID:27765766

    Open questions at the time
    • Whether the UBA-mediated mitotic function requires phosphatase activity is unknown
    • Structural basis of Aurora B ubiquitin recognition not determined
    • Clinical relevance of UBASH3B in thrombotic disease not established
  8. 2017 High

    High-resolution crystal structures of the Sts-1 and Sts-2 histidine phosphatase domains explained the ~100-fold activity difference between paralogs and identified PHPS1 as a micromolar inhibitor, providing a structural framework for selective targeting.

    Evidence X-ray crystallography at 1.9–2.5 Å resolution, steady-state kinetics, inhibitor Ki determination

    PMID:28759203

    Open questions at the time
    • No co-crystal with a phosphotyrosine substrate exists
    • Selectivity of PHPS1 for UBASH3B over other histidine phosphatases not fully profiled
  9. 2018 High

    UBASH3B's role as a universal negative regulator of Syk-dependent signaling was consolidated when CLEC-2/hemITAM pathway activation was shown to be enhanced in TULA-2 KO platelets through failure to dephosphorylate Syk Y346.

    Evidence TULA-2 KO mouse platelets stimulated with CLEC-2 agonist, site-specific phosphorylation and functional aggregation assays

    PMID:31249969

    Open questions at the time
    • Whether UBASH3B regulation of CLEC-2 signaling is relevant in lymphatic development not tested
  10. 2020 Medium

    UBASH3B function was extended to endothelial biology when miR-25-3p–mediated suppression of TULA-2 was shown to increase Syk pY323 and VEGFR-2 pY1175 phosphorylation, promoting angiogenesis in vitro and in vivo.

    Evidence miR-25-3p overexpression/inhibition, Co-IP of TULA-2–Syk, VEGFR-2 phosphorylation analysis, hindlimb ischemia model

    PMID:33201836

    Open questions at the time
    • Direct dephosphorylation of VEGFR-2 by UBASH3B not demonstrated
    • Single-lab observation
    • Endogenous miR-25-3p regulation of UBASH3B in disease contexts not validated
  11. 2021 Medium

    The substrate repertoire was further broadened when UBASH3B was found to dephosphorylate PKCδ, promoting its proteasomal degradation in leukemia cells treated with TPA.

    Evidence RNAi knockdown with proteasome inhibitor treatment, PKCδ phosphorylation and stability analysis

    PMID:33556471

    Open questions at the time
    • Specific PKCδ phosphosite targeted by UBASH3B not identified
    • Not independently replicated
  12. 2024 Medium

    A mitochondrial function was uncovered when UBASH3B was shown to directly bind and dephosphorylate MRPL12 at Y60, disrupting the MRPL12–POLRMT interaction and downregulating mitochondrial oxidative phosphorylation to suppress lung adenocarcinoma progression.

    Evidence MS-identified phosphosite, Co-IP, Y60 phosphomutant studies in LUAD cell lines, xenografts, and organoids

    PMID:39343960

    Open questions at the time
    • Whether UBASH3B enters mitochondria or acts before import is unclear
    • Single-lab finding awaiting replication
    • In vivo relevance in normal mitochondrial physiology not tested

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key unresolved questions include how UBASH3B's phosphatase and ubiquitin-binding functions are coordinated, what determines substrate selectivity across diverse receptor systems, and whether UBASH3B can be therapeutically targeted to modulate thrombosis or anti-tumor immunity.
  • No co-crystal structure with a physiological phosphotyrosine substrate
  • Integration of UBA-mediated and phosphatase-mediated functions not mechanistically resolved
  • No selective high-potency inhibitor or activator reported

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140096 catalytic activity, acting on a protein 13 GO:0016787 hydrolase activity 4
Localization
GO:0005829 cytosol 2 GO:0005739 mitochondrion 1 GO:0005856 cytoskeleton 1
Pathway
R-HSA-168256 Immune System 5 R-HSA-162582 Signal Transduction 4 R-HSA-109582 Hemostasis 3 R-HSA-1430728 Metabolism 1 R-HSA-1640170 Cell Cycle 1
Partners
AURKBCBLEGFRMRPL12SHC1SYKZAP70

Evidence

Reading pass · 21 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2004 Sts-1 (UBASH3B) and Sts-2 negatively regulate TCR signaling by suppressing ZAP-70 phosphorylation and activation; knockout mice show hyperresponsive T cells with increased Zap-70 phosphorylation (including ubiquitylated forms), hyperactivation of downstream signaling proteins, and increased cytokine production. Genetic knockout (Sts-1/2 double knockout mice), phosphorylation assays, cytokine measurement, EAE autoimmunity model Immunity High 14738763
2004 Sts-1 (UBASH3B) interacts with Cbl via its SH3 domain, binds mono-ubiquitin via its UBA domain, is recruited into activated EGFR complexes, and inhibits EGFR and PDGFR endocytosis, thereby blocking receptor degradation and prolonging mitogenic signaling. Co-immunoprecipitation, domain-deletion constructs, receptor internalization assays, endocytic vesicle quantification, cell transformation assays The Journal of biological chemistry High 15159412
2007 Sts-1 (UBASH3B) possesses intrinsic phosphatase activity via a PGM/acid phosphatase-like catalytic domain; it can dephosphorylate Zap-70, and point mutations impairing phosphatase activity in vitro also impair TCR signaling regulation in T cells. X-ray crystallography, in vitro phosphatase assays, active-site mutagenesis, T cell signaling assays Molecular cell High 17679096
2007 Sts-1 (UBASH3B) catalyzes hydrolysis of ecdysteroid and steroid phosphates, demonstrating it is a member of the histidine phosphatase superfamily with phosphatase activity toward steroid substrates. Cloning, in vitro enzymatic assay with ecdysteroid/steroid phosphate substrates, structural homology modeling Proteins Medium 17348005
2010 TULA-2 (UBASH3B/Sts-1) associates with Syk and dephosphorylates it, negatively regulating GPVI-mediated platelet signaling; TULA-2 knockout mice show hyperphosphorylation of Syk and PLCγ2 and a prothrombotic phenotype with shortened bleeding times. Co-immunoprecipitation (TULA-2 with Syk), in vitro dephosphorylation assay, TULA-2 knockout mouse platelet functional assays, bleeding time measurement Blood High 20585042
2010 TULA-2 (UBASH3B) has defined substrate specificity for phosphotyrosyl peptides: class I substrates have Pro at pY-1, class II substrates have acidic residues at pY-1 to pY-3; TULA-2 is highly active toward Syk pY323 and pY352 sites, and TULA-2 KO increases Syk phosphorylation at Y323 and Y352 in platelets. Combinatorial phosphotyrosyl peptide library screening, in vitro kinetic analysis, TULA-2 knockout platelets with phosphorylation site-specific immunoblotting The Journal of biological chemistry High 20670933
2012 TULA-2 (UBASH3B) is recruited to phosphorylated C-terminal tyrosines of Syk in mast cells after FcεRI activation, and siRNA knockdown of TULA-2 increases Syk activation-loop phosphorylation, PLCγ2 phosphorylation, degranulation, and NF-κB/NFAT activation, establishing TULA-2 as a negative regulator of FcεRI signaling. Phosphopeptide pulldown with mass spectrometry identification, co-immunoprecipitation, far-Western blot, siRNA knockdown with functional degranulation assay The Journal of biological chemistry High 22267732
2012 TULA-2 (UBASH3B) is expressed in osteoclasts and negatively regulates osteoclast differentiation and function by dephosphorylating Syk at Y352 and Y525/526; phosphatase-dead TULA-2 mutant increases osteoclast function, and DKO mice show increased osteoclast numbers and decreased bone volume. Double knockout mouse skeletal analysis, in vitro osteoclast differentiation assay, phosphatase-dead mutant expression, site-specific Syk phosphorylation immunoblotting Cellular and molecular life sciences High 23149425
2013 UBASH3B (Sts-1) dephosphorylates CBL ubiquitin ligase, leading to CBL inactivation and EGFR upregulation in triple-negative breast cancer; this phosphatase activity is required for UBASH3B's oncogenic promotion of invasion and metastasis. siRNA knockdown, phosphatase-dead mutant rescue experiments, EGFR expression and signaling assays, in vitro invasion/metastasis assays, mouse xenograft model Proceedings of the National Academy of Sciences of the United States of America High 23784775
2013 Sts-1 (UBASH3B) substrate-trapping mutants (H380A and E490A active site mutations) retain high-affinity binding to tyrosine-phosphorylated Zap-70, validating Zap-70 as a direct substrate of the Sts-1 phosphatase active site; overexpression of these trapping mutants in T cells blocks TCR signaling. Active-site mutagenesis, substrate-trapping from T cell lysates, vanadate competition, T cell functional signaling assay The FEBS journal High 24256567
2015 UBASH3B/Sts-1 is upregulated by AML1-ETO and supports proliferation of AML1-ETO leukemic cells partly by inhibiting CBL function; UBASH3B depletion induces aberrant CBL phosphorylation and growth impairment that can be rescued by CBL mutants. shRNA knockdown, rescue with CBL mutants, CBL phosphorylation analysis, xenograft model Leukemia Medium 26449661
2015 STS-1 (UBASH3B) promotes IFN-α-induced autophagy in B cells by inhibiting CBL-mediated phosphorylation, thereby enhancing TYK2 phosphorylation and activating the JAK1-STAT1 signaling pathway. Overexpression and knockdown experiments, CBL phosphorylation assays, JAK1/STAT1 pathway activation measurement, autophagy assay, JAK/STAT inhibitor treatment European journal of immunology Medium 25959715
2016 UBASH3B acts as a ubiquitin receptor that binds ubiquitylated Aurora B kinase and controls Aurora B localization to mitotic microtubules prior to anaphase, which is necessary for proper timing and fidelity of chromosome segregation. Co-immunoprecipitation of ubiquitylated Aurora B with UBASH3B, live-cell imaging, loss-of-function and gain-of-function experiments, chromosome segregation assays Developmental cell High 26766443
2016 TULA-2 (UBASH3B) dephosphorylates Syk pY346 (a regulatory site phosphorylated early after receptor ligation) with high efficiency, and this dephosphorylation is the primary mechanism by which TULA-2 suppresses overall Syk activation downstream of GPVI-FcRγ in platelets. In vitro phosphatase assay with site-specific Syk phosphopeptides/proteins, TULA-2 KO platelet signaling analysis, site-specific phosphorylation immunoblotting The Journal of biological chemistry High 27609517
2016 TULA-2 (UBASH3B) negatively regulates FcγRIIA-mediated platelet signaling by dephosphorylating Syk; TULA-2 knockout enhances Syk, LAT, and PLCγ2 phosphorylation and augments platelet aggregation, granule secretion, and phosphatidylserine exposure, and worsens heparin-induced thrombocytopenia in vivo. TULA-2 knockout mouse crossed with FcγRIIA transgenic mouse, platelet signaling and functional assays, in vivo HIT model, bleeding time measurement Arteriosclerosis, thrombosis, and vascular biology High 27765766
2017 Crystal structures of the histidine phosphatase domains of human Sts-1 and Sts-2 were determined (Sts-1HP unliganded at 2.5 Å and with sulfate at 1.9 Å; Sts-2HP with sulfate at 2.4 Å); Sts-1HP has significantly higher phosphatase activity than Sts-2HP; full-length Sts-1 and Sts-1HP show similar kinetics; PHPS1 (SHP-1 inhibitor) inhibits Sts-1 with Ki = 1.05 μM; Sts-1 has robust phosphatase activity against Zap-70 in a cell-based assay. X-ray crystallography, steady-state kinetics, inhibitor assays, cell-based phosphatase assay Biochemistry High 28759203
2017 STS-1 (UBASH3B) is identified as a novel binding partner of ShcA; the interaction is mediated via phosphotyrosine-containing peptides and is regulated by EGF receptor activation. Phosphotyrosyl peptide pulldown, mass spectrometry identification, EGF stimulation-dependent interaction assay Biochemical and biophysical research communications Medium 28690151
2018 TULA-2 (UBASH3B) deficiency enhances CLEC-2-mediated platelet aggregation and secretion by failing to dephosphorylate Syk Y346, leading to enhanced PLCγ2 and SLP-76 phosphorylation, establishing TULA-2 as a negative regulator of CLEC-2/HemITAM signaling via Syk Y346 dephosphorylation. TULA-2 knockout mouse platelets, CLEC-2 agonist stimulation, site-specific phosphorylation immunoblotting, platelet aggregation and secretion assays TH open High 31249969
2020 TULA-2 (UBASH3B) negatively regulates Syk Y323 phosphorylation in endothelial cells; miR-25-3p suppresses TULA-2 expression, reducing TULA-2–Syk interaction and increasing Syk pY323, which elevates VEGFR-2 pY1175 and promotes angiogenesis. miR-25-3p overexpression/inhibition, TULA-2 protein expression analysis, Syk and VEGFR-2 phosphorylation immunoblotting, co-immunoprecipitation, in vitro angiogenesis assay, in vivo hindlimb ischemia model Aging Medium 33201836
2021 UBASH3B (Ubash3b) dephosphorylates PKCδ in leukemia cells treated with TPA, promoting PKCδ protein degradation via the proteasome; RNAi depletion of Ubash3b blocks TPA-induced PKCδ loss. RNAi knockdown, proteasome inhibitor treatment, PKCδ phosphorylation and protein level analysis, leukemia mouse model Biochimie Medium 33556471
2024 UBASH3B directly binds MRPL12 and dephosphorylates its tyrosine 60, which impedes MRPL12 binding to mitochondrial RNA polymerase POLRMT and downregulates mitochondrial oxidative phosphorylation, thereby inhibiting LUAD tumor progression. Mass spectrometry identification of phosphorylation site, co-immunoprecipitation (UBASH3B–MRPL12, MRPL12–POLRMT), Y60 phospho-mutant functional assays, in vitro/in vivo/organoid LUAD models Journal of experimental & clinical cancer research Medium 39343960

Source papers

Stage 0 corpus · 31 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2004 Regulation of ZAP-70 activation and TCR signaling by two related proteins, Sts-1 and Sts-2. Immunity 152 14738763
2004 Suppressors of T-cell receptor signaling Sts-1 and Sts-2 bind to Cbl and inhibit endocytosis of receptor tyrosine kinases. The Journal of biological chemistry 119 15159412
2007 A phosphatase activity of Sts-1 contributes to the suppression of TCR signaling. Molecular cell 100 17679096
2013 Protein tyrosine phosphatase UBASH3B is overexpressed in triple-negative breast cancer and promotes invasion and metastasis. Proceedings of the National Academy of Sciences of the United States of America 63 23784775
2010 A novel histidine tyrosine phosphatase, TULA-2, associates with Syk and negatively regulates GPVI signaling in platelets. Blood 61 20585042
2010 Determination of the substrate specificity of protein-tyrosine phosphatase TULA-2 and identification of Syk as a TULA-2 substrate. The Journal of biological chemistry 49 20670933
2015 UBASH3B/Sts-1-CBL axis regulates myeloid proliferation in human preleukemia induced by AML1-ETO. Leukemia 48 26449661
2012 Once phosphorylated, tyrosines in carboxyl terminus of protein-tyrosine kinase Syk interact with signaling proteins, including TULA-2, a negative regulator of mast cell degranulation. The Journal of biological chemistry 37 22267732
2016 Ubiquitin Receptor Protein UBASH3B Drives Aurora B Recruitment to Mitotic Microtubules. Developmental cell 35 26766443
2012 TULA-2, a novel histidine phosphatase, regulates bone remodeling by modulating osteoclast function. Cellular and molecular life sciences : CMLS 33 23149425
2015 STS-1 promotes IFN-α induced autophagy by activating the JAK1-STAT1 signaling pathway in B cells. European journal of immunology 31 25959715
1983 Medical results from STS 1-4: analysis of body fluids. Aviation, space, and environmental medicine 29 6661134
2016 TULA-2 Protein Phosphatase Suppresses Activation of Syk through the GPVI Platelet Receptor for Collagen by Dephosphorylating Tyr(P)346, a Regulatory Site of Syk. The Journal of biological chemistry 28 27609517
2013 Insights into the suppressor of T-cell receptor (TCR) signaling-1 (Sts-1)-mediated regulation of TCR signaling through the use of novel substrate-trapping Sts-1 phosphatase variants. The FEBS journal 21 24256567
2016 TULA-2 (T-Cell Ubiquitin Ligand-2) Inhibits the Platelet Fc Receptor for IgG IIA (FcγRIIA) Signaling Pathway and Heparin-Induced Thrombocytopenia in Mice. Arteriosclerosis, thrombosis, and vascular biology 20 27765766
2007 An unsuspected ecdysteroid/steroid phosphatase activity in the key T-cell regulator, Sts-1: surprising relationship to insect ecdysteroid phosphate phosphatase. Proteins 20 17348005
2020 miR-25-3p promotes endothelial cell angiogenesis in aging mice via TULA-2/SYK/VEGFR-2 downregulation. Aging 13 33201836
2017 Structural and Functional Characterization of the Histidine Phosphatase Domains of Human Sts-1 and Sts-2. Biochemistry 13 28759203
2024 UBASH3B-mediated MRPL12 Y60 dephosphorylation inhibits LUAD development by driving mitochondrial metabolism reprogramming. Journal of experimental & clinical cancer research : CR 12 39343960
2018 TULA-2 Deficiency Enhances Platelet Functional Responses to CLEC-2 Agonists. TH open : companion journal to thrombosis and haemostasis 12 31249969
2006 Crystallization and initial crystal characterization of the C-terminal phosphoglycerate mutase homology domain of Sts-1. Acta crystallographica. Section F, Structural biology and crystallization communications 12 16511305
2024 FLI1 induces erythroleukemia through opposing effects on UBASH3A and UBASH3B expression. BMC cancer 8 38461240
2017 Identification of STS-1 as a novel ShcA-binding protein. Biochemical and biophysical research communications 8 28690151
2017 UBASH3B-mediated silencing of the mitotic checkpoint: Therapeutic perspectives in cancer. Molecular & cellular oncology 8 29487893
2021 Ubash3b promotes TPA-mediated suppression of leukemogenesis through accelerated downregulation of PKCδ protein. Biochimie 7 33556471
2018 Ubiquitin Associated and SH3 Domain Containing B (UBASH3B) Gene Association with Behcet's Disease in Iranian Population. Current eye research 6 30289285
2017 UBASH3B promotes tamoxifen resistance and could be negatively regulated by ESR1. Oncotarget 6 29492198
2014 Enhanced response of T cells from murine gammaherpesvirus 68-infected mice lacking the suppressor of T cell receptor signaling molecules Sts-1 and Sts-2. PloS one 4 24587276
2023 STS-1 and STS-2, Multi-Enzyme Proteins Equipped to Mediate Protein-Protein Interactions. International journal of molecular sciences 3 37298164
1984 [Medical results from STS 1-4: analysis of body fluids]. Kosmicheskaia biologiia i aviakosmicheskaia meditsina 2 6700189
2025 Investigating the role of UBASH3B in cancer: structural relevance, physiological functions, and therapeutic possibilities. Journal of experimental & clinical cancer research : CR 0 40885971