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

Summary

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
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
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

Location:: 7q11.23

Exon count:: 12

Annotation release	Status	Assembly	Chr	Location
109.20211119	current	GRCh38.p13 (GCF_000001405.39)	7	NC_000007.14 (75995820..76049344, complement)
105.20201022	previous assembly	GRCh37.p13 (GCF_000001405.25)	7	NC_000007.13 (75625655..75677318, complement)

Chromosome 7 - NC_000007.14 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: 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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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

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.
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.
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.
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.
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.
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.
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.
MK-STYX regulates mitochondrial outer membrane permeabilization using a distinct mechanism.
Title: MK-STYX, a catalytically inactive phosphatase regulating mitochondrially dependent apoptosis.
Results illustrated a role for MK-STYX in regulating the ability of G3BP1 to integrate changes in growth-factor stimulation and environmental stress with the regulation of protein synthesis.
Title: The pseudophosphatase MK-STYX interacts with G3BP and decreases stress granule formation.

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Phenotypes

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Find tests for this gene in the NIH Genetic Testing Registry (GTR)

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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Homology

Homologs of the STYXL1 gene: The STYXL1 gene is conserved in chimpanzee, dog, cow, mouse, rat, chicken, zebrafish, and frog.
Orthologs from Annotation Pipeline: 408 organisms have orthologs with human gene STYXL1
Orthologs

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein phosphatase binding	IBA Inferred from Biological aspect of Ancestor more info	PubMed
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	PubMed
enables protein phosphatase inhibitor activity	IDA Inferred from Direct Assay more info	PubMed
enables protein tyrosine/serine/threonine phosphatase activity	IEA Inferred from Electronic Annotation more info
enables pseudophosphatase activity	IBA Inferred from Biological aspect of Ancestor more info	PubMed
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 phosphoprotein phosphatase activity	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of stress granule assembly	IBA Inferred from Biological aspect of Ancestor more info	PubMed
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	PubMed
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 protein dephosphorylation	IEA Inferred from Electronic Annotation more info
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	PubMed
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)

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

Q9Y6J8

UniProtKB/TrEMBL

A0A024R4L1

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 ...
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

Q9Y6J8

UniProtKB/TrEMBL

A0A024R4L1, Q7Z3H6

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 ...
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/Swiss-Prot

Q9Y6J8

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 ...
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 ...
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 ...
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

Q9Y6J8

UniProtKB/TrEMBL

A0A024R4L1

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

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
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: Homo sapiens Updated Annotation Release 109.20211119

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

Reference GRCh38.p13 Primary Assembly

Genomic

NC_000007.14 Reference GRCh38.p13 Primary Assembly

Range

75995820..76049344 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_017012298.2 → XP_016867787.1 serine/threonine/tyrosine-interacting-like protein 1 isoform X2

Conserved Domains (2) summary

pfam00581
Location:22 → 135

Rhodanese; Rhodanese-like domain

cl21483
Location:160 → 225

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 ...
XM_017012297.1 → XP_016867786.1 serine/threonine/tyrosine-interacting-like protein 1 isoform X2

Conserved Domains (2) summary

pfam00581
Location:22 → 135

Rhodanese; Rhodanese-like domain

cl21483
Location:160 → 225

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 ...
XM_011516292.3 → XP_011514594.1 serine/threonine/tyrosine-interacting-like protein 1 isoform X2

Conserved Domains (2) summary

pfam00581
Location:22 → 135

Rhodanese; Rhodanese-like domain

cl21483
Location:160 → 225

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 ...
XM_017012300.1 → XP_016867789.1 serine/threonine/tyrosine-interacting-like protein 1 isoform X5
XM_017012299.1 → XP_016867788.1 serine/threonine/tyrosine-interacting-like protein 1 isoform X4
XM_017012296.1 → XP_016867785.1 serine/threonine/tyrosine-interacting-like protein 1 isoform X1
XM_017012302.1 → XP_016867791.1 serine/threonine/tyrosine-interacting-like protein 1 isoform X6

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 ...
XM_011516293.3 → XP_011514595.1 serine/threonine/tyrosine-interacting-like protein 1 isoform X3

See identical proteins and their annotated locations for XP_011514595.1

UniProtKB/Swiss-Prot

Q9Y6J8

UniProtKB/TrEMBL

A0A024R4L1

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 ...
XM_017012301.2 → XP_016867790.1 serine/threonine/tyrosine-interacting-like protein 1 isoform X6

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 ...
XM_011516300.1 → XP_011514602.1 serine/threonine/tyrosine-interacting-like protein 1 isoform X6

See identical proteins and their annotated locations for XP_011514602.1

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 ...