THNSL2 threonine synthase like 2 [Homo sapiens (human)] - Gene

Summary

Official Symbol: THNSL2provided by HGNC
Official Full Name: threonine synthase like 2provided by HGNC
Primary source: HGNC:HGNC:25602
See related: Ensembl:ENSG00000144115 MIM:611261; AllianceGenome:HGNC:25602
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: THS2; TSH2; SOFAT
Summary: This gene encodes a threonine synthase-like protein. A similar enzyme in mouse can catalyze the degradation of O-phospho-homoserine to a-ketobutyrate, phosphate, and ammonia. This protein also has phospho-lyase activity on both gamma and beta phosphorylated substrates. In mouse an alternatively spliced form of this protein has been shown to act as a cytokine and can induce the production of the inflammatory cytokine IL6 in osteoblasts. Alternate splicing results in multiple transcript variants. [provided by RefSeq, Sep 2011]
Expression: Ubiquitous expression in kidney (RPKM 9.9), thyroid (RPKM 9.5) and 24 other tissues See more
Orthologs: mouse all
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Genomic context

Location:: 2p11.2

Exon count:: 9

Annotation release	Status	Assembly	Chr	Location
RS_2023_10	current	GRCh38.p14 (GCF_000001405.40)	2	NC_000002.12 (88170346..88186627)
RS_2023_10	current	T2T-CHM13v2.0 (GCF_009914755.1)	2	NC_060926.1 (88181454..88198653)
105.20220307	previous assembly	GRCh37.p13 (GCF_000001405.25)	2	NC_000002.11 (88469865..88486146)

Chromosome 2 - NC_000002.12 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

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Secreted Osteoclastogenic Factor of Activated T Cells (SOFAT) Is Associated With Rheumatoid Arthritis and Joint Pain: Initial Evidences of a New Pathway.
Title: Secreted Osteoclastogenic Factor of Activated T Cells (SOFAT) Is Associated With Rheumatoid Arthritis and Joint Pain: Initial Evidences of a New Pathway.
this study shows that SOFAT is a putative marker of osteoclasts in bone lesions
Title: SOFAT as a Putative Marker of Osteoclasts in Bone Lesions.
Our results provide evidence for new loci influencing abdominal visceral (BBS9, ADCY8, KCNK9) and subcutaneous (MLLT10/DNAJC1/EBLN1) fat, and confirmed a locus (THNSL2) previously reported to be associated with abdominal fat in women.
Title: Genome-wide association studies suggest sex-specific loci associated with abdominal and visceral fat.
These data support a putative role of SOFAT in the bone loss associated with chronic periodontal disease.
Title: Expression of SOFAT by T- and B-lineage cells may contribute to bone loss.
may exacerbate inflammation and support osteoclast formation and bone destruction
Title: In vitro evaluation of the biological effect of SOFAT on osteoblasts.
The present study demonstrated that SOFAT may play an important role in periodontitis.
Title: Secreted osteoclastogenic factor of activated T cells (SOFAT), a novel osteoclast activator, in chronic periodontitis.
THNSL2 was found to have bimodal expression in human skeletal muscle tissue.
Title: Bimodal distribution of RNA expression levels in human skeletal muscle tissue.
A cytokine named SOFAT (secreted osteoclastogenic factor of activated T cells) can induce osteoblastic IL-6 production and osteoclast formation in the absence of osteoblasts or RANKL. It is insensitive to RANKL inhibitor osteoprotegerin.
Title: A novel T cell cytokine, secreted osteoclastogenic factor of activated T cells, induces osteoclast formation in a RANKL-independent manner.

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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

EBI GWAS Catalog

Description
Genome-wide association for abdominal subcutaneous and visceral adipose reveals a novel locus for visceral fat in women. EBI GWAS Catalog EBI GWAS CatalogPubMed

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

HIV-1 interactions

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Replication interactions

Interaction	Pubs
Knockdown of threonine synthase-like 2 (THNSL2) by siRNA has both activating and inhibiting activities on HIV-1 replication in HeLa P4/R5 cells, suggesting a regulatory role in HIV replication	PubMed

Go to the HIV-1, Human Interaction Database

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

RH47580 (e-PCR)
- UniSTS:63546

D2S2610 (e-PCR)
- UniSTS:37791

RH103447 (e-PCR)
- UniSTS:97772

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables cytokine activity	IEA Inferred from Electronic Annotation more info
enables molecular_function	ND No biological Data available more info
enables pyridoxal phosphate binding	IBA Inferred from Biological aspect of Ancestor more info
enables pyridoxal phosphate binding	ISS Inferred from Sequence or Structural Similarity more info	PubMed
enables serine binding	ISS Inferred from Sequence or Structural Similarity more info	PubMed
NOT enables threonine synthase activity	IBA Inferred from Biological aspect of Ancestor more info

Process	Evidence Code	Pubs
involved_in 2-oxobutyrate biosynthetic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in 2-oxobutyrate biosynthetic process	ISS Inferred from Sequence or Structural Similarity more info	PubMed
involved_in biological_process	ND No biological Data available more info
involved_in dephosphorylation	IBA Inferred from Biological aspect of Ancestor more info
involved_in dephosphorylation	ISS Inferred from Sequence or Structural Similarity more info	PubMed
involved_in serine family amino acid catabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in serine family amino acid catabolic process	ISS Inferred from Sequence or Structural Similarity more info	PubMed
involved_in signal transduction	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
is_active_in cellular_component	ND No biological Data available more info
located_in extracellular space	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: threonine synthase-like 2

Names: secreted osteoclastogenic factor of activated T cells

NP_001231605.1

EC 4.2.3.-

NP_001231607.1

EC 4.2.3.-

NP_001371311.1

EC 4.2.3.-

NP_001371312.1

EC 4.2.3.-

NP_060741.3

EC 4.2.3.-

XP_005264458.1

EC 4.2.3.-

XP_005264459.1

EC 4.2.3.-

XP_006712104.1

EC 4.2.3.-

XP_006712105.1

EC 4.2.3.-

XP_006712106.1

EC 4.2.3.-

XP_006712107.1

EC 4.2.3.-

XP_011531255.1

EC 4.2.3.-

XP_011531256.1

EC 4.2.3.-

XP_011531257.1

EC 4.2.3.-

XP_024308743.1

EC 4.2.3.-

XP_047300852.1

EC 4.2.3.-

XP_047300854.1

EC 4.2.3.-

XP_047300855.1

EC 4.2.3.-

XP_047300856.1

EC 4.2.3.-

XP_047300857.1

EC 4.2.3.-

XP_047300858.1

EC 4.2.3.-

XP_054198756.1

EC 4.2.3.-

XP_054198757.1

EC 4.2.3.-

XP_054198758.1

EC 4.2.3.-

XP_054198759.1

EC 4.2.3.-

XP_054198760.1

EC 4.2.3.-

XP_054198761.1

EC 4.2.3.-

XP_054198762.1

EC 4.2.3.-

XP_054198763.1

EC 4.2.3.-

XP_054198764.1

EC 4.2.3.-

XP_054198765.1

EC 4.2.3.-

XP_054198766.1

EC 4.2.3.-

XP_054198767.1

EC 4.2.3.-

XP_054198768.1

EC 4.2.3.-

XP_054198769.1

EC 4.2.3.-

XP_054198770.1

EC 4.2.3.-

XP_054198771.1

EC 4.2.3.-

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.

Genomic

NG_030037.1 RefSeqGene

Range

5052..21333

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001244676.2 → NP_001231605.1 threonine synthase-like 2 isoform 2

See identical proteins and their annotated locations for NP_001231605.1

Status: REVIEWED

Description

Transcript Variant: This variant (2) has a longer 5' UTR and uses an alternate exon in the 3' coding region, which results in a frameshift, compared to variant 1. The resulting protein (isoform 2) has a distinct C-terminus, compared to isoform 1.

Source sequence(s)

AC092836, AI313402, BC064423

Consensus CDS

CCDS58718.1

UniProtKB/Swiss-Prot

Q86YJ6

Related

ENSP00000339563.4, ENST00000343544.8

Conserved Domains (1) summary

cd01560
Location:2 → 359

Thr-synth_2; Threonine synthase catalyzes the final step of threonine biosynthesis. The conversion of O-phosphohomoserine into threonine and inorganic phosphate is pyridoxal 5'-phosphate dependent. The Thr-synth_1 CD includes members from higher plants, cyanobacteria, ...
NM_001244678.2 → NP_001231607.1 threonine synthase-like 2 isoform 3

See identical proteins and their annotated locations for NP_001231607.1

Status: REVIEWED

Description

Transcript Variant: This variant (3) differs in the 5' UTR, 3' UTR, and has multiple coding region differences, compared to variant 1. The resulting protein (isoform 3) is shorter at the N-terminus and has a distinct C-terminus, compared to isoform 1.

Source sequence(s)

AC092836, AI313402, AK315831

Consensus CDS

CCDS74539.1

UniProtKB/TrEMBL

A8K0C1

Related

ENSP00000366464.4, ENST00000377254.7

Conserved Domains (1) summary

cl00342
Location:1 → 201

Trp-synth-beta_II; Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP)-dependent enzymes catalyzes beta-replacement and beta-elimination reactions. This CD corresponds to aminocyclopropane-1-carboxylate deaminase (ACCD), tryptophan ...
NM_001384382.1 → NP_001371311.1 threonine synthase-like 2 isoform 3

Status: REVIEWED

Source sequence(s)

AC092836

Consensus CDS

CCDS74539.1

UniProtKB/TrEMBL

A8K0C1

Conserved Domains (1) summary

cl00342
Location:1 → 201

Trp-synth-beta_II; Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP)-dependent enzymes catalyzes beta-replacement and beta-elimination reactions. This CD corresponds to aminocyclopropane-1-carboxylate deaminase (ACCD), tryptophan ...
NM_001384383.1 → NP_001371312.1 threonine synthase-like 2 isoform 5

Status: REVIEWED

Source sequence(s)

AC092836

Consensus CDS

CCDS92801.1

Related

ENST00000674282.1

Conserved Domains (1) summary

cd01560
Location:2 → 359

Thr-synth_2; Threonine synthase catalyzes the final step of threonine biosynthesis. The conversion of O-phosphohomoserine into threonine and inorganic phosphate is pyridoxal 5'-phosphate dependent. The Thr-synth_1 CD includes members from higher plants, cyanobacteria, ...
NM_018271.5 → NP_060741.3 threonine synthase-like 2 isoform 1

See identical proteins and their annotated locations for NP_060741.3

Status: REVIEWED

Description

Transcript Variant: This variant (1) encodes the longest isoform (1).

Source sequence(s)

AC092836

Consensus CDS

CCDS2002.2

UniProtKB/Swiss-Prot

B3KTB1, B5MDX8, B7WPF8, D9ZZB8, Q6P2M7, Q6PI27, Q86YJ6, Q9NV54

Related

ENSP00000501453.1, ENST00000674334.2

Conserved Domains (1) summary

cd01560
Location:2 → 464

Thr-synth_2; Threonine synthase catalyzes the final step of threonine biosynthesis. The conversion of O-phosphohomoserine into threonine and inorganic phosphate is pyridoxal 5'-phosphate dependent. The Thr-synth_1 CD includes members from higher plants, cyanobacteria, ...

RefSeqs of Annotated Genomes: GCF_000001405.40-RS_2023_10

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

Reference GRCh38.p14 Primary Assembly

Genomic

NC_000002.12 Reference GRCh38.p14 Primary Assembly

Range

88170346..88186627

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_006712041.4 → XP_006712104.1 threonine synthase-like 2 isoform X3

Conserved Domains (2) summary

cd01560
Location:2 → 408

Thr-synth_2; Threonine synthase catalyzes the final step of threonine biosynthesis. The conversion of O-phosphohomoserine into threonine and inorganic phosphate is pyridoxal 5'-phosphate dependent. The Thr-synth_1 CD includes members from higher plants, cyanobacteria, ...

PRK09225
Location:1 → 397

PRK09225; threonine synthase; Validated
XM_006712044.4 → XP_006712107.1 threonine synthase-like 2 isoform X13

UniProtKB/TrEMBL

C9JU10

Related

ENSP00000407553.1, ENST00000449349.5

Conserved Domains (1) summary

cl00342
Location:2 → 268

Trp-synth-beta_II; Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP)-dependent enzymes catalyzes beta-replacement and beta-elimination reactions. This CD corresponds to aminocyclopropane-1-carboxylate deaminase (ACCD), tryptophan ...
XM_011532954.3 → XP_011531256.1 threonine synthase-like 2 isoform X6

Conserved Domains (2) summary

cd01560
Location:2 → 399

Thr-synth_2; Threonine synthase catalyzes the final step of threonine biosynthesis. The conversion of O-phosphohomoserine into threonine and inorganic phosphate is pyridoxal 5'-phosphate dependent. The Thr-synth_1 CD includes members from higher plants, cyanobacteria, ...

PRK09225
Location:1 → 389

PRK09225; threonine synthase; Validated
XM_047444898.1 → XP_047300854.1 threonine synthase-like 2 isoform X8

Related

ENSP00000501447.1, ENST00000496844.6
XM_047444900.1 → XP_047300856.1 threonine synthase-like 2 isoform X10
XM_047444901.1 → XP_047300857.1 threonine synthase-like 2 isoform X12
XM_011532955.3 → XP_011531257.1 threonine synthase-like 2 isoform X11

Conserved Domains (1) summary

cl00342
Location:1 → 306

Trp-synth-beta_II; Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP)-dependent enzymes catalyzes beta-replacement and beta-elimination reactions. This CD corresponds to aminocyclopropane-1-carboxylate deaminase (ACCD), tryptophan ...
XM_047444902.1 → XP_047300858.1 threonine synthase-like 2 isoform X14
XM_024452975.2 → XP_024308743.1 threonine synthase-like 2 isoform X1

UniProtKB/Swiss-Prot

B3KTB1, B5MDX8, B7WPF8, D9ZZB8, Q6P2M7, Q6PI27, Q86YJ6, Q9NV54

Conserved Domains (1) summary

cd01560
Location:2 → 464

Thr-synth_2; Threonine synthase catalyzes the final step of threonine biosynthesis. The conversion of O-phosphohomoserine into threonine and inorganic phosphate is pyridoxal 5'-phosphate dependent. The Thr-synth_1 CD includes members from higher plants, cyanobacteria, ...
XM_006712043.3 → XP_006712106.1 threonine synthase-like 2 isoform X7

See identical proteins and their annotated locations for XP_006712106.1

UniProtKB/Swiss-Prot

Q86YJ6

Conserved Domains (1) summary

cd01560
Location:2 → 359

Thr-synth_2; Threonine synthase catalyzes the final step of threonine biosynthesis. The conversion of O-phosphohomoserine into threonine and inorganic phosphate is pyridoxal 5'-phosphate dependent. The Thr-synth_1 CD includes members from higher plants, cyanobacteria, ...
XM_047444899.1 → XP_047300855.1 threonine synthase-like 2 isoform X9
XM_011532953.3 → XP_011531255.1 threonine synthase-like 2 isoform X2

Conserved Domains (2) summary

cd01560
Location:2 → 408

Thr-synth_2; Threonine synthase catalyzes the final step of threonine biosynthesis. The conversion of O-phosphohomoserine into threonine and inorganic phosphate is pyridoxal 5'-phosphate dependent. The Thr-synth_1 CD includes members from higher plants, cyanobacteria, ...

PRK09225
Location:1 → 397

PRK09225; threonine synthase; Validated
XM_005264402.4 → XP_005264459.1 threonine synthase-like 2 isoform X4

Conserved Domains (2) summary

cd01560
Location:2 → 408

Thr-synth_2; Threonine synthase catalyzes the final step of threonine biosynthesis. The conversion of O-phosphohomoserine into threonine and inorganic phosphate is pyridoxal 5'-phosphate dependent. The Thr-synth_1 CD includes members from higher plants, cyanobacteria, ...

PRK09225
Location:1 → 397

PRK09225; threonine synthase; Validated
XM_006712042.4 → XP_006712105.1 threonine synthase-like 2 isoform X5

Conserved Domains (2) summary

cd01560
Location:2 → 408

Thr-synth_2; Threonine synthase catalyzes the final step of threonine biosynthesis. The conversion of O-phosphohomoserine into threonine and inorganic phosphate is pyridoxal 5'-phosphate dependent. The Thr-synth_1 CD includes members from higher plants, cyanobacteria, ...

PRK09225
Location:1 → 397

PRK09225; threonine synthase; Validated
XM_047444896.1 → XP_047300852.1 threonine synthase-like 2 isoform X1

UniProtKB/Swiss-Prot

B3KTB1, B5MDX8, B7WPF8, D9ZZB8, Q6P2M7, Q6PI27, Q86YJ6, Q9NV54

Related

ENSP00000327323.5, ENST00000324166.7
XM_005264401.6 → XP_005264458.1 threonine synthase-like 2 isoform X1

See identical proteins and their annotated locations for XP_005264458.1

UniProtKB/Swiss-Prot

B3KTB1, B5MDX8, B7WPF8, D9ZZB8, Q6P2M7, Q6PI27, Q86YJ6, Q9NV54

Conserved Domains (1) summary

cd01560
Location:2 → 464

Thr-synth_2; Threonine synthase catalyzes the final step of threonine biosynthesis. The conversion of O-phosphohomoserine into threonine and inorganic phosphate is pyridoxal 5'-phosphate dependent. The Thr-synth_1 CD includes members from higher plants, cyanobacteria, ...