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

Gene ID: 51657, updated on 5-Jul-2020

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

Genomic context

See STYXL1 in Genome Data Viewer
Location:
7q11.23
Exon count:
12
Annotation release Status Assembly Chr Location
109.20200522 current GRCh38.p13 (GCF_000001405.39) 7 NC_000007.14 (75995820..76049344, complement)
105 previous assembly GRCh37.p13 (GCF_000001405.25) 7 NC_000007.13 (75625610..75677321, 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 transmembrane protein 120A Neighboring gene malate dehydrogenase 2 Neighboring gene RNA, U6 small nuclear 863, pseudogene Neighboring gene general transcription factor IIi pseudogene 7

Genomic regions, transcripts, and products

Expression

  • 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

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

Markers

Homology

Gene Ontology Provided by GOA

Function Evidence Code Pubs
protein binding IPI
Inferred from Physical Interaction
more info
PubMed 
protein phosphatase binding IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
protein phosphatase binding IPI
Inferred from Physical Interaction
more info
PubMed 
protein phosphatase inhibitor activity IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
protein phosphatase inhibitor activity IDA
Inferred from Direct Assay
more info
PubMed 
protein tyrosine/serine/threonine phosphatase activity IEA
Inferred from Electronic Annotation
more info
 
pseudophosphatase activity IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
pseudophosphatase activity IMP
Inferred from Mutant Phenotype
more info
PubMed 
Component Evidence Code Pubs
mitochondrial matrix IEA
Inferred from Electronic Annotation
more info
 
mitochondrion IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
mitochondrion IDA
Inferred from Direct Assay
more info
PubMed 

General protein information

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)

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_001317785.2NP_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:22135
    Rhodanese; Rhodanese-like domain
    cl21483
    Location:160297
    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_001317786.2NP_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:22135
    Rhodanese; Rhodanese-like domain
    cl21483
    Location:160297
    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_001317787.2NP_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:2351
    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:64201
    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_001317788.2NP_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:2351
    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:64129
    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_001317789.1NP_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:22159
    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_016086.2NP_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, AI676056, BC024035, BM824947, W58723
    Consensus CDS
    CCDS5580.1
    UniProtKB/Swiss-Prot
    Q9Y6J8
    UniProtKB/TrEMBL
    A0A024R4L1
    Related
    ENSP00000248600.1, ENST00000248600.5
    Conserved Domains (2) summary
    pfam00581
    Location:22135
    Rhodanese; Rhodanese-like domain
    cl21483
    Location:160297
    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: Homo sapiens Updated Annotation Release 109.

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

Reference GRCh38.p13 Primary Assembly

Genomic

  1. NC_000007.14 Reference GRCh38.p13 Primary Assembly

    Range
    75995820..76049344 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

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

    Conserved Domains (2) summary
    pfam00581
    Location:22135
    Rhodanese; Rhodanese-like domain
    cl21483
    Location:160225
    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_017012297.1XP_016867786.1  serine/threonine/tyrosine-interacting-like protein 1 isoform X2

    Conserved Domains (2) summary
    pfam00581
    Location:22135
    Rhodanese; Rhodanese-like domain
    cl21483
    Location:160225
    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. XM_011516292.3XP_011514594.1  serine/threonine/tyrosine-interacting-like protein 1 isoform X2

    Conserved Domains (2) summary
    pfam00581
    Location:22135
    Rhodanese; Rhodanese-like domain
    cl21483
    Location:160225
    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. XM_017012300.1XP_016867789.1  serine/threonine/tyrosine-interacting-like protein 1 isoform X5

  5. XM_017012299.1XP_016867788.1  serine/threonine/tyrosine-interacting-like protein 1 isoform X4

  6. XM_017012296.1XP_016867785.1  serine/threonine/tyrosine-interacting-like protein 1 isoform X1

  7. XM_017012302.1XP_016867791.1  serine/threonine/tyrosine-interacting-like protein 1 isoform X6

    Conserved Domains (1) summary
    cl21483
    Location:22159
    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 ...
  8. XM_011516293.3XP_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:22135
    Rhodanese; Rhodanese-like domain
    cl21483
    Location:160297
    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 ...
  9. XM_017012301.2XP_016867790.1  serine/threonine/tyrosine-interacting-like protein 1 isoform X6

    Conserved Domains (1) summary
    cl21483
    Location:22159
    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 ...
  10. XM_011516300.1XP_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:22159
    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 ...
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