Seroatlas · Human Serome Atlas

THNSL2

Threonine synthase-like 2

Also known as: FLJ10916, SOFAT, THNS2_HUMAN, TSH2

Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene

Protein identityUniProt · HPA

UniProt accession: Q86YJ6
Gene: THNSL2
Ensembl: ENSG00000144115
Chromosome: 2
Canonical length: 484 aa
Protein class: Predicted intracellular proteins, Predicted secreted proteins
Secretome location: Secreted - unknown location

OverviewNCBI Gene

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]

Canonical amino-acid sequenceUniProt

484 residues, UniProt reviewed canonical sequence.

>Q86YJ6|THNSL2
     1  MWYVSTRGVA PRVNFEGALF SGYAPDGGLF MPEELPQLDR GTLCQWSTLS YPGLVKELCA
    61  LFIGSELLPK DELNDLIDRA FSRFRHREVV HLSRLRNGLN VLELWHGVTY AFKDLSLSCT
   121  TQFLQYFLEK REKHVTVVVG TSGDTGSAAI ESVQGAKNMD IIVLLPKGHC TKIQELQMTT
   181  VLKQNVHVFG VEGNSDELDE PIKTVFADVA FVKKHNLMSL NSINWSRVLV QMAHHFFAYF
   241  QCTPSLDTHP LPLVEVVVPT GAAGNLAAGY IAQKIGLPIR LVVAVNRNDI IHRTVQQGDF
   301  SLSEAVKSTL ASAMDIQVPY NMERVFWLLS GSDSQVTRAL MEQFERTQSV NLPKELHSKL
   361  SEAVTSVSVS DEAITQTMGR CWDENQYLLC PHSAVAVNYH YQQIDRQQPS TPRCCLAPAS
   421  AAKFPEAVLA AGLTPETPAE IVALEHKETR CTLMRRGDNW MLMLRDTIED LSRQWRSHAL
   481  NTSQ

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against THNSL2 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability: Secreted
Secreted: Yes
Transmembrane segments: 0
Mean surface accessibility (rSASA): 0.2
Highest tissue expression: 55 nTPM

Expression across tissuesHPA

Tissue

skeletal muscle: 55 nTPM
liver: 43 nTPM
tongue: 34 nTPM
parathyroid gland: 30 nTPM
kidney: 28 nTPM
pituitary gland: 28 nTPM

Single-cell type

hepatocytes: 64 nCPM
cytotrophoblasts: 53 nCPM
sertoli cells: 46 nCPM
migrating cytotrophoblasts: 43 nCPM
medullary thymic epithelial cells: 43 nCPM
breast lactating cells: 40 nCPM

Immune cell

naive B-cell: 0.7 nTPM
intermediate monocyte: 0.4 nTPM
memory B-cell: 0.4 nTPM
myeloid DC: 0.4 nTPM
eosinophil: 0.3 nTPM
gdT-cell: 0.3 nTPM

Brain region

hypothalamus: 17 nTPM
medulla oblongata: 13 nTPM
basal ganglia: 12 nTPM
midbrain: 12 nTPM
white matter: 11 nTPM
spinal cord: 11 nTPM

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance): 1.02
gnomAD pLI: 0
gnomAD missense Z: 0.09
DepMap mean gene effect: -0.06
DepMap dependency class: selective

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 5% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

2-oxobutyrate biosynthetic process
serine family amino acid catabolic process

Molecular functions

Cellular components

extracellular space

Protein domainsUniProt · Pfam · InterPro

KeywordsUniProt

Antibody and autoantibody relevanceSeroatlas analysis

Seroatlas reads THNSL2 as an antibody target. Whether an autoantibody or antibody against THNSL2 could matter depends on whether native THNSL2 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.

THNSL2 is annotated as secreted, so native THNSL2 circulates and is directly accessible to antibodies. Secreted and cell-surface proteins are the autoantibody targets most likely to act like drugs, blocking or depleting the native protein.

Annotation status

The present source text does not explicitly label THNSL2 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.

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