PRSS36 serine protease 36 [Homo sapiens (human)] - Gene

Summary

Official Symbol: PRSS36provided by HGNC
Official Full Name: serine protease 36provided by HGNC
Primary source: HGNC:HGNC:26906
See related: Ensembl:ENSG00000178226 MIM:610560; AllianceGenome:HGNC:26906
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
Summary: Enables serine-type endopeptidase activity. Predicted to be involved in proteolysis. Located in cytoplasm. [provided by Alliance of Genome Resources, Dec 2024]
Expression: Ubiquitous expression in placenta (RPKM 1.0), small intestine (RPKM 0.7) and 24 other tissues See more
Orthologs: mouse all
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Genomic context

Location:: 16p11.2

Exon count:: 15

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	16	NC_000016.10 (31138926..31150066, complement)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	16	NC_060940.1 (31526407..31537545, complement)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	16	NC_000016.9 (31150247..31161387, complement)

Chromosome 16 - NC_000016.10 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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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?

analysis of post-translational processing mechanisms of polyserase-2 revealed that this novel polyprotein is a secreted enzyme whose three protease domains remain as an integral part of a single polypeptide chain
Title: Human polyserase-2, a novel enzyme with three tandem serine protease domains in a single polypeptide chain.

Submit: New GeneRIF Correction

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)

General gene information

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Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables serine-type endopeptidase activity	IBA Inferred from Biological aspect of Ancestor more info
enables serine-type endopeptidase activity	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in proteolysis	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in extracellular region	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: polyserase-2

Names: polyserine protease-2; protease, serine 36

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_001258290.2 → NP_001245219.1 polyserase-2 isoform 2 precursor

See identical proteins and their annotated locations for NP_001245219.1

Status: VALIDATED

Description

Transcript Variant: This variant (2) uses an alternate splice site in the coding region, compared to variant 1. This results in a shorter protein (isoform 2), compared to isoform 1.

Source sequence(s)

AC009088, AI864473, AK290310, AK297997, BC144615

Consensus CDS

CCDS58453.1

UniProtKB/Swiss-Prot

Q5K4E3

UniProtKB/TrEMBL

B4DNP1

Related

ENSP00000454768.1, ENST00000569305.1

Conserved Domains (3) summary

smart00020
Location:46 → 286

Tryp_SPc; Trypsin-like serine protease

cd00190
Location:47 → 289

Tryp_SPc; Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad ...

cl21584
Location:596 → 778

Tryp_SPc; Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad ...
NM_001258291.2 → NP_001245220.1 polyserase-2 isoform 3 precursor

Status: VALIDATED

Description

Transcript Variant: This variant (3) lacks an alternate exon in the 3' coding region, compared to variant 1. This results in a shorter protein (isoform 3), compared to isoform 1.

Source sequence(s)

AC009088, AI864473, AK290310, AK297997, AK301409

Consensus CDS

CCDS58452.1

UniProtKB/Swiss-Prot

Q5K4E3

UniProtKB/TrEMBL

B4DNP1

Related

ENSP00000407160.2, ENST00000418068.6

Conserved Domains (3) summary

smart00020
Location:46 → 286

Tryp_SPc; Trypsin-like serine protease

cd00190
Location:47 → 289

Tryp_SPc; Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad ...

cl21584
Location:330 → 538

Tryp_SPc; Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad ...
NM_173502.5 → NP_775773.2 polyserase-2 isoform 1 precursor

See identical proteins and their annotated locations for NP_775773.2

Status: VALIDATED

Description

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

Source sequence(s)

AC009088, AI864473, AK290310, AK297997

Consensus CDS

CCDS32436.1

UniProtKB/Swiss-Prot

A8K2P5, B4DW80, B7ZMK8, E7EX56, Q5K4E3, Q8NBY4

Related

ENSP00000268281.4, ENST00000268281.9

Conserved Domains (3) summary

smart00020
Location:46 → 286

Tryp_SPc; Trypsin-like serine protease

cd00190
Location:47 → 289

Tryp_SPc; Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad ...

cl21584
Location:330 → 538

Tryp_SPc; Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad ...

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

NC_000016.10 Reference GRCh38.p14 Primary Assembly

Range

31138926..31150066 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_017022971.2 → XP_016878460.1 polyserase-2 isoform X2
XM_017022968.2 → XP_016878457.1 polyserase-2 isoform X1

Conserved Domains (2) summary

cd00190
Location:47 → 289

Tryp_SPc; Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad ...

cl21584
Location:330 → 538

Tryp_SPc; Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad ...