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    STYXL1 serine/threonine/tyrosine interacting like 1 [ Homo sapiens (human) ]

    Gene ID: 51657, updated on 14-Nov-2024

    Summary

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    Official Symbol
    STYXL1provided by HGNC
    Official Full Name
    serine/threonine/tyrosine interacting like 1provided by HGNC
    Primary source
    HGNC:HGNC:18165
    See related
    Ensembl:ENSG00000127952 MIM:616695; AllianceGenome:HGNC:18165
    Gene type
    protein coding
    RefSeq status
    VALIDATED
    Organism
    Homo sapiens
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
    Also known as
    DUSP24; MKSTYX; MK-STYX
    Summary
    Enables protein phosphatase binding activity; protein phosphatase inhibitor activity; and pseudophosphatase activity. Involved in negative regulation of stress granule assembly; positive regulation of intrinsic apoptotic signaling pathway; and positive regulation of neuron projection development. Located in mitochondrion. [provided by Alliance of Genome Resources, Nov 2024]
    Expression
    Ubiquitous expression in testis (RPKM 9.4), esophagus (RPKM 5.9) and 25 other tissues See more
    Orthologs
    mouse all
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    Genomic context

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    See STYXL1 in Genome Data Viewer
    Location:
    7q11.23
    Exon count:
    11
    Annotation release Status Assembly Chr Location
    RS_2024_08 current GRCh38.p14 (GCF_000001405.40) 7 NC_000007.14 (75996337..76048000, complement)
    RS_2024_08 current T2T-CHM13v2.0 (GCF_009914755.1) 7 NC_060931.1 (77283904..77335536, complement)
    RS_2024_09 previous assembly GRCh37.p13 (GCF_000001405.25) 7 NC_000007.13 (75625655..75677318, complement)

    Chromosome 7 - NC_000007.14Genomic Context describing neighboring genes Neighboring gene cytochrome p450 oxidoreductase Neighboring gene small nucleolar RNA, H/ACA box 14A Neighboring gene Sharpr-MPRA regulatory region 2709 Neighboring gene H3K27ac hESC enhancer GRCh37_chr7:75596037-75596916 Neighboring gene CDK7 strongly-dependent group 2 enhancer GRCh37_chr7:75612087-75613286 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 26185 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 26186 Neighboring gene Sharpr-MPRA regulatory region 3792 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 26187 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 18304 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 18303 Neighboring gene transmembrane protein 120A Neighboring gene H3K4me1 hESC enhancer GRCh37_chr7:75630123-75630623 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 26188 Neighboring gene H3K27ac hESC enhancer GRCh37_chr7:75648513-75649014 Neighboring gene NANOG-H3K27ac-H3K4me1 hESC enhancer GRCh37_chr7:75676791-75677573 Neighboring gene NANOG-H3K27ac-H3K4me1 hESC enhancer GRCh37_chr7:75677574-75678355 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 26191 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 26192 Neighboring gene malate dehydrogenase 2 Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr7:75700542-75701066 Neighboring gene RNA, U6 small nuclear 863, pseudogene

    Genomic regions, transcripts, and products

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    Go to nucleotide: Graphics FASTA GenBank

    Expression

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    • Project title: HPA RNA-seq normal tissues HPA RNA-seq normal tissues
    • Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
    • BioProject: PRJEB4337
    • Publication: PMID 24309898
    • Analysis date: Wed Apr 4 07:08:55 2018

    Bibliography

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    Related articles in PubMed

    1. Pseudophosphatase STYXL1 depletion enhances glucocerebrosidase trafficking to lysosomes via ER stress. Patel S, et al. Traffic, 2023 Jul. PMID 37198709
    2. Serine/threonine/tyrosine-interacting-like protein 1 (STYXL1), a pseudo phosphatase, promotes oncogenesis in glioma. Tomar VS, et al. Biochem Biophys Res Commun, 2019 Jul 12. PMID 31146910
    3. Pseudophosphatase MK-STYX Alters Histone Deacetylase 6 Cytoplasmic Localization, Decreases Its Phosphorylation, and Increases Detyrosination of Tubulin. Cao Y, et al. Int J Mol Sci, 2019 Mar 22. PMID 30909412, Free PMC Article
    4. A previously identified missense mutation in STYXL1 is likely benign. Hengel H, et al. Eur J Med Genet, 2019 Nov. PMID 30472486
    5. Homozygous missense mutation in STYXL1 associated with moderate intellectual disability, epilepsy and behavioural complexities. Isrie M, et al. Eur J Med Genet, 2015 Apr. PMID 25724587

    See all (34) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. The DUSP domain of pseudophosphatase MK-STYX interacts with G3BP1 to decrease stress granules.
      Title: The DUSP domain of pseudophosphatase MK-STYX interacts with G3BP1 to decrease stress granules.
    2. Pseudophosphatase STYXL1 depletion enhances glucocerebrosidase trafficking to lysosomes via ER stress.
      Title: Pseudophosphatase STYXL1 depletion enhances glucocerebrosidase trafficking to lysosomes via ER stress.
    3. STYXL1 promotes malignant progression of hepatocellular carcinoma via downregulating CELF2 through the PI3K/Akt pathway.
      Title: STYXL1 promotes malignant progression of hepatocellular carcinoma via downregulating CELF2 through the PI3K/Akt pathway.
    4. Silencing serine/threonine/tyrosine-interacting-like protein 1 (STYXL1) inhibited glioma cell growth, soft agar colony formation, migration, invasion, proliferation, and xenograft tumor growth [Review].
      Title: Serine/threonine/tyrosine-interacting-like protein 1 (STYXL1), a pseudo phosphatase, promotes oncogenesis in glioma.
    5. We have detected this variant via whole exome sequencing in a homozygous state in two families. Segregation analyses in our families and thorough validation in international genetic databases provides evidence that this variant is most likely benign. This is important information for genetic counselling. The role of STYXL1 variants in human disease needs to be established
      Title: A previously identified missense mutation in STYXL1 is likely benign.
    6. These findings show that MK-STYX decreases the number of HDAC6-containing aggregates and alters their localization, sustains microtubule acetylation, and increases detyrosination of microtubules, implicating MK-STYX as a signaling molecule in HDAC6 activity.
      Title: Pseudophosphatase MK-STYX Alters Histone Deacetylase 6 Cytoplasmic Localization, Decreases Its Phosphorylation, and Increases Detyrosination of Tubulin.
    7. this study revealed STYXL1 as a novel candidate gene for moderate intellectual disability, seizures and behavioral complexities.
      Title: Homozygous missense mutation in STYXL1 associated with moderate intellectual disability, epilepsy and behavioural complexities.
    8. our data support a model in which MK-STYX controls apoptosis by negatively regulating PTPMT1.
      Title: The pseudophosphatase MK-STYX physically and genetically interacts with the mitochondrial phosphatase PTPMT1.
    9. The pseudophosphatase MK-STYX plays a key role in the cellular response to stress.
      Title: The pseudophosphatase MK-STYX inhibits stress granule assembly independently of Ser149 phosphorylation of G3BP-1.
    10. MK-STYX regulates mitochondrial outer membrane permeabilization using a distinct mechanism.
      Title: MK-STYX, a catalytically inactive phosphatase regulating mitochondrially dependent apoptosis.
    Submit: New GeneRIF Correction See all GeneRIFs (11)

    Phenotypes

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    Review eQTL and phenotype association data in this region using PheGenI

    Variation

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    See variants in ClinVar

    See studies and variants in dbVar

    See Variation Viewer (GRCh37.p13)

    See Variation Viewer (GRCh38)

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Markers

    Homology

    Gene Ontology Provided by GOA

    Function Evidence Code Pubs
    enables phosphatase inhibitor activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables protein phosphatase binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables protein phosphatase binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables protein phosphatase inhibitor activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables pseudophosphatase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables pseudophosphatase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in intracellular signal transduction TAS
    Traceable Author Statement
    more info
    		 PubMed 
    involved_in negative regulation of stress granule assembly IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in negative regulation of stress granule assembly IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in positive regulation of intrinsic apoptotic signaling pathway IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in positive regulation of intrinsic apoptotic signaling pathway IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in positive regulation of neuron projection development IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in regulation of intrinsic apoptotic signaling pathway IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in mitochondrial matrix IEA
    Inferred from Electronic Annotation
    more info
    		  
    is_active_in mitochondrion IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in mitochondrion IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    serine/threonine/tyrosine-interacting-like protein 1
    Names
    dual specificity phosphatase 24 (putative)
    dual specificity phosphatase inhibitor MK-STYX
    dual specificity protein phosphatase 24
    inactive dual specificity protein phosphatase MK-STYX
    map kinase phosphatase-like protein MK-STYX

    NCBI Reference Sequences (RefSeq)

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    RefSeqs maintained independently of Annotated Genomes

    These reference sequences exist independently of genome builds. Explain

    These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

    mRNA and Protein(s)

    1. NM_001317785.2 → NP_001304714.1  serine/threonine/tyrosine-interacting-like protein 1 isoform a

      Status: VALIDATED

      Description
      Transcript Variant: This variant (2) differs in the 5' UTR compared to variant 1. Variants 1, 2, and 3 encode the same isoform (a).
      Source sequence(s)
      AC006330, AF069762, BC024035, BM824947, BM972220
      Consensus CDS
      CCDS5580.1
      UniProtKB/Swiss-Prot
      Q9UBP1, Q9UK06, Q9UK07, Q9UKG2, Q9UKG3, Q9Y6J8
      UniProtKB/TrEMBL
      C9J4H0
      Related
      ENSP00000352726.3, ENST00000359697.8
      Conserved Domains (2) summary
      pfam00581
      Location:22 → 135
      Rhodanese; Rhodanese-like domain
      cl21483
      Location:160 → 297
      PTPc; Protein tyrosine phosphatases (PTP) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr ...

    2. NM_001317786.2 → NP_001304715.1  serine/threonine/tyrosine-interacting-like protein 1 isoform a

      Status: VALIDATED

      Description
      Transcript Variant: This variant (3) differs in the 5' UTR compared to variant 1. Variants 1, 2, and 3 encode the same isoform (a).
      Source sequence(s)
      AC006330, AF069762, AL533027, BX537896
      Consensus CDS
      CCDS5580.1
      UniProtKB/Swiss-Prot
      Q9UBP1, Q9UK06, Q9UK07, Q9UKG2, Q9UKG3, Q9Y6J8
      UniProtKB/TrEMBL
      C9J4H0
      Related
      ENSP00000392221.1, ENST00000431581.5
      Conserved Domains (2) summary
      pfam00581
      Location:22 → 135
      Rhodanese; Rhodanese-like domain
      cl21483
      Location:160 → 297
      PTPc; Protein tyrosine phosphatases (PTP) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr ...

    3. NM_001317787.2 → NP_001304716.1  serine/threonine/tyrosine-interacting-like protein 1 isoform b

      Status: VALIDATED

      Description
      Transcript Variant: This variant (4) uses an alternate splice site in the 5' UTR, and lacks two consecutive in-frame exons in the 5' coding region, compared to variant 1. The encoded isoform (b) is shorter than isoform 1.
      Source sequence(s)
      AC006330, AF069762, BX537896
      Consensus CDS
      CCDS83193.1
      UniProtKB/TrEMBL
      Q7Z3H6
      Related
      ENSP00000343383.5, ENST00000340062.9
      Conserved Domains (2) summary
      cl00125
      Location:23 → 51
      RHOD; Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins ...
      cl21483
      Location:64 → 201
      PTPc; Protein tyrosine phosphatases (PTP) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr ...

    4. NM_001317788.2 → NP_001304717.1  serine/threonine/tyrosine-interacting-like protein 1 isoform c

      Status: VALIDATED

      Description
      Transcript Variant: This variant (5) lacks two exons in the 5' coding region, and uses an alternate splice site in the 3'coding region which results in a frameshift, compared to variant 1. The encoded isoform (c) is shorter and has a distinct C-terminus, compared to isoform 1.
      Source sequence(s)
      AC006330, AF069762, BM972220, BU859937
      UniProtKB/Swiss-Prot
      Q9Y6J8
      Conserved Domains (2) summary
      cl00125
      Location:23 → 51
      RHOD; Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins ...
      cl21483
      Location:64 → 129
      PTPc; Protein tyrosine phosphatases (PTP) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr ...

    5. NM_001317789.1 → NP_001304718.1  serine/threonine/tyrosine-interacting-like protein 1 isoform d

      Status: VALIDATED

      Description
      Transcript Variant: This variant (6) differs in its 5' UTR, lacks an exon in the 5' coding region, and uses an alternate downstream start codon which results in a frameshift, compared to variant 1. The encoded isoform (d) has a shorter and distinct N-terminus, compared to isoform 1.
      Source sequence(s)
      AF188204, BM126964, BM972220, BX537896
      UniProtKB/Swiss-Prot
      Q9Y6J8
      UniProtKB/TrEMBL
      Q7Z3H6
      Conserved Domains (1) summary
      cl21483
      Location:22 → 159
      PTPc; Protein tyrosine phosphatases (PTP) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr ...

    6. NM_016086.3 → NP_057170.1  serine/threonine/tyrosine-interacting-like protein 1 isoform a

      See identical proteins and their annotated locations for NP_057170.1

      Status: VALIDATED

      Description
      Transcript Variant: This variant (1) encodes isoform (a). Variants 1, 2, and 3 encode the same isoform (a).
      Source sequence(s)
      AA782050, AF069762, BC024035, BM824947
      Consensus CDS
      CCDS5580.1
      UniProtKB/Swiss-Prot
      Q9UBP1, Q9UK06, Q9UK07, Q9UKG2, Q9UKG3, Q9Y6J8
      UniProtKB/TrEMBL
      C9J4H0
      Related
      ENSP00000248600.1, ENST00000248600.5
      Conserved Domains (2) summary
      pfam00581
      Location:22 → 135
      Rhodanese; Rhodanese-like domain
      cl21483
      Location:160 → 297
      PTPc; Protein tyrosine phosphatases (PTP) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr ...

    RNA

    1. NR_134486.2 RNA Sequence

      Status: VALIDATED

      Description
      Transcript Variant: This variant (7) uses an alternate splice site in the 5'-terminal exon and lacks two internal exons, compared to variant 1. This variant is represented as non-coding because the predicted protein does not meet RefSeq quality criteria.
      Source sequence(s)
      AF069762, AY927581, BI772699, BM972220

    2. NR_134487.1 RNA Sequence

      Status: VALIDATED

      Description
      Transcript Variant: This variant (8) lacks two exons compared to variant 1. This variant is represented as non-coding because the predicted protein does not meet RefSeq quality criteria.
      Source sequence(s)
      AF188201, BM126964, BM972220

    RefSeqs of Annotated Genomes: GCF_000001405.40-RS_2024_08

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference GRCh38.p14 Primary Assembly

    Genomic

    1. NC_000007.14 Reference GRCh38.p14 Primary Assembly

      Range
      75996337..76048000 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_011516293.4 → XP_011514595.1  serine/threonine/tyrosine-interacting-like protein 1 isoform X1

      See identical proteins and their annotated locations for XP_011514595.1

      UniProtKB/Swiss-Prot
      Q9UBP1, Q9UK06, Q9UK07, Q9UKG2, Q9UKG3, Q9Y6J8
      UniProtKB/TrEMBL
      C9J4H0
      Related
      ENSP00000411812.1, ENST00000451157.1
      Conserved Domains (2) summary
      pfam00581
      Location:22 → 135
      Rhodanese; Rhodanese-like domain
      cl21483
      Location:160 → 297
      PTPc; Protein tyrosine phosphatases (PTP) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr ...

    2. XM_047420470.1 → XP_047276426.1  serine/threonine/tyrosine-interacting-like protein 1 isoform X2

    3. XM_047420466.1 → XP_047276422.1  serine/threonine/tyrosine-interacting-like protein 1 isoform X1

      UniProtKB/Swiss-Prot
      Q9UBP1, Q9UK06, Q9UK07, Q9UKG2, Q9UKG3, Q9Y6J8

    4. XM_047420468.1 → XP_047276424.1  serine/threonine/tyrosine-interacting-like protein 1 isoform X1

      UniProtKB/Swiss-Prot
      Q9UBP1, Q9UK06, Q9UK07, Q9UKG2, Q9UKG3, Q9Y6J8

    5. XM_047420467.1 → XP_047276423.1  serine/threonine/tyrosine-interacting-like protein 1 isoform X1

      UniProtKB/Swiss-Prot
      Q9UBP1, Q9UK06, Q9UK07, Q9UKG2, Q9UKG3, Q9Y6J8

    6. XM_047420469.1 → XP_047276425.1  serine/threonine/tyrosine-interacting-like protein 1 isoform X1

      UniProtKB/Swiss-Prot
      Q9UBP1, Q9UK06, Q9UK07, Q9UKG2, Q9UKG3, Q9Y6J8

    Alternate T2T-CHM13v2.0

    Genomic

    1. NC_060931.1 Alternate T2T-CHM13v2.0

      Range
      77283904..77335536 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_054358387.1 → XP_054214362.1  serine/threonine/tyrosine-interacting-like protein 1 isoform X3

    2. XM_054358382.1 → XP_054214357.1  serine/threonine/tyrosine-interacting-like protein 1 isoform X1

      UniProtKB/Swiss-Prot
      Q9UBP1, Q9UK06, Q9UK07, Q9UKG2, Q9UKG3, Q9Y6J8

    3. XM_054358388.1 → XP_054214363.1  serine/threonine/tyrosine-interacting-like protein 1 isoform X2

    4. XM_054358384.1 → XP_054214359.1  serine/threonine/tyrosine-interacting-like protein 1 isoform X1

      UniProtKB/Swiss-Prot
      Q9UBP1, Q9UK06, Q9UK07, Q9UKG2, Q9UKG3, Q9Y6J8

    5. XM_054358385.1 → XP_054214360.1  serine/threonine/tyrosine-interacting-like protein 1 isoform X1

      UniProtKB/Swiss-Prot
      Q9UBP1, Q9UK06, Q9UK07, Q9UKG2, Q9UKG3, Q9Y6J8

    6. XM_054358383.1 → XP_054214358.1  serine/threonine/tyrosine-interacting-like protein 1 isoform X1

      UniProtKB/Swiss-Prot
      Q9UBP1, Q9UK06, Q9UK07, Q9UKG2, Q9UKG3, Q9Y6J8

    7. XM_054358386.1 → XP_054214361.1  serine/threonine/tyrosine-interacting-like protein 1 isoform X1

      UniProtKB/Swiss-Prot
      Q9UBP1, Q9UK06, Q9UK07, Q9UKG2, Q9UKG3, Q9Y6J8
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    Q9Y6J8.1 GenPept UniProtKB/Swiss-Prot:Q9Y6J8

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

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