SERPINB13 serpin family B member 13 [Homo sapiens (human)] - Gene

Summary

Official Symbol: SERPINB13provided by HGNC
Official Full Name: serpin family B member 13provided by HGNC
Primary source: HGNC:HGNC:8944
See related: Ensembl:ENSG00000197641 MIM:604445; AllianceGenome:HGNC:8944
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: HUR7; PI13; headpin; HSHUR7SEQ
Summary: The protein encoded by this gene is a member of the serpin family of serine protease inhibitors. The encoded protein inhibits the activity of cathepsin K and is itself transcriptionally repressed by RUNX1. This gene is downregulated in many types of cancer. [provided by RefSeq, Jan 2017]
Expression: Restricted expression toward esophagus (RPKM 94.0) See more
Orthologs: mouse all
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Genomic context

Location:: 18q21.33

Exon count:: 9

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	18	NC_000018.10 (63587343..63599192)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	18	NC_060942.1 (63792453..63804288)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	18	NC_000018.9 (61254577..61266426)

Chromosome 18 - NC_000018.10 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?

clade B serpins help to maintain homeostasis by inducing protective humoral immunity
Title: Enhanced anti-serpin antibody activity inhibits autoimmune inflammation in type 1 diabetes.
These data demonstrate that RUNX1 is an important regulator of SERPINB13 and cathepsin K activity.
Title: SERPINB13 is a novel RUNX1 target gene.
Observational study of gene-disease association. (HuGE Navigator)
Title: Genetic analysis of diabetic nephropathy on chromosome 18 in African Americans: linkage analysis and dense SNP mapping.
Downregulation of SERPINB13 protein expression in HNSCC is positively associated with poor clinical outcome. Therefore, SERPINB13 seems to act as an important protease inhibitor involved in the progression of HNSCC.
Title: Downregulation of SERPINB13 expression in head and neck squamous cell carcinomas associates with poor clinical outcome.
Down-regulation of SERPINB13 is associated with head and neck squamous cell carcinoma
Title: Headpin: a serpin with endogenous and exogenous suppression of angiogenesis.
Hurpin is a selective inhibitor of lysosomal cathepsin L and protects keratinocytes from ultraviolet-induced apoptosis.
Title: Hurpin is a selective inhibitor of lysosomal cathepsin L and protects keratinocytes from ultraviolet-induced apoptosis.
A novel member of the serine proteinase inhibitor (Serpin) gene family that was originally cloned from a keratinocyte cDNA library. It has specificity for inhibiting lysosomal cysteine proteinases.
Title: Inhibition of the cysteine proteinases cathepsins K and L by the serpin headpin (SERPINB13): a kinetic analysis.
hurpin is expressed in skin and has a possible role in inflammatory processes or the regulation of endogenous or pathogen-derived proteinase activity
Title: Expression of hurpin, a serine proteinase inhibitor, in normal and pathological skin: overexpression and redistribution in psoriasis and cutaneous carcinomas.
the expression of hurpin was confined mainly to the basal layer in normal skin samples, whereas hurpin was overexpressed and redistributed in diseased skin
Title: Expression of cathepsin L and its inhibitor hurpin in inflammatory and neoplastic skin diseases.

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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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Markers

ECD00529 (e-PCR)
- UniSTS:281640

NoName (e-PCR)
- UniSTS:481105

RH47046 (e-PCR)
- UniSTS:73380

REN10471 (e-PCR)
- UniSTS:335271

REN10472 (e-PCR)
- UniSTS:335272

REN10473 (e-PCR)
- UniSTS:335273

REN10474 (e-PCR)
- UniSTS:335274

REN10475 (e-PCR)
- UniSTS:335275

REN10476 (e-PCR)
- UniSTS:335276

ECD17912 (e-PCR)
- UniSTS:298924

REN10477 (e-PCR)
- UniSTS:335277

REN10478 (e-PCR)
- UniSTS:335278

REN10479 (e-PCR)
- UniSTS:335279

REN10480 (e-PCR)
- UniSTS:335280

REN10481 (e-PCR)
- UniSTS:335281

REN10482 (e-PCR)
- UniSTS:335282

REN10483 (e-PCR)
- UniSTS:335283

REN10484 (e-PCR)
- UniSTS:335284

REN10485 (e-PCR)
- UniSTS:335285

SHGC-142006 (e-PCR)
- UniSTS:171189

REN10486 (e-PCR)
- UniSTS:335286

REN10487 (e-PCR)
- UniSTS:335287

REN10488 (e-PCR)
- UniSTS:335288

REN10489 (e-PCR)
- UniSTS:335289

REN10490 (e-PCR)
- UniSTS:335290

REN10491 (e-PCR)
- UniSTS:335291

REN10492 (e-PCR)
- UniSTS:335292

REN10493 (e-PCR)
- UniSTS:335293

REN10494 (e-PCR)
- UniSTS:335294

REN10495 (e-PCR)
- UniSTS:335295

stSG619327 (e-PCR)
- UniSTS:453311

NoName (e-PCR)
- UniSTS:485575

ECD01217 (e-PCR)
- UniSTS:282324

ECD05624 (e-PCR)
- UniSTS:286687

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables cysteine-type endopeptidase inhibitor activity	IDA Inferred from Direct Assay more info	PubMed
enables cysteine-type endopeptidase inhibitor activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables protease binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
NOT enables serine-type endopeptidase inhibitor activity	IDA Inferred from Direct Assay more info	PubMed
enables serine-type endopeptidase inhibitor activity	NAS Non-traceable Author Statement more info	PubMed

Process	Evidence Code	Pubs
involved_in negative regulation of endopeptidase activity	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of keratinocyte apoptotic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in regulation of proteolysis	NAS Non-traceable Author Statement more info	PubMed
involved_in response to UV	TAS Traceable Author Statement more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytosol	IDA Inferred from Direct Assay more info
located_in extracellular exosome	HDA more info	PubMed
is_active_in extracellular space	IBA Inferred from Biological aspect of Ancestor more info
located_in lysosomal lumen	TAS Traceable Author Statement more info
located_in nuclear speck	IDA Inferred from Direct Assay more info
NOT located_in nucleolus	IDA Inferred from Direct Assay more info	PubMed
located_in nucleoplasm	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: serpin B13

Names: HURPIN; PI-13; UV-B repressed sequence, HUR 7; haCaT UV-repressible serpin; peptidase inhibitor 13; protease inhibitor 13 (hurpin, headpin); proteinase inhibitor 13; serine (or cysteine) proteinase inhibitor, clade B (ovalbumin), member 13; serpin peptidase inhibitor, clade B (ovalbumin), member 13

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_052858.1 RefSeqGene

Range

5142..16991

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001307923.2 → NP_001294852.1 serpin B13 isoform 1

See identical proteins and their annotated locations for NP_001294852.1

Status: REVIEWED

Description

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

Source sequence(s)

AJ001696, AK296797, AL050177

Consensus CDS

CCDS77195.1

UniProtKB/TrEMBL

A0A0A0MQW3, B7ZKV6

Related

ENSP00000269489.6, ENST00000269489.9

Conserved Domains (1) summary

cl00137
Location:4 → 400

SERPIN; SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate ...
NM_001348267.2 → NP_001335196.1 serpin B13 isoform 3

Status: REVIEWED

Description

Transcript Variant: This variant (3), as well as variant 4, encodes isoform 3.

Source sequence(s)

AC090307

UniProtKB/TrEMBL

B7Z4X7

Conserved Domains (1) summary

cl00137
Location:22 → 255

SERPIN; SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate ...
NM_001348268.2 → NP_001335197.1 serpin B13 isoform 3

Status: REVIEWED

Description

Transcript Variant: This variant (4), as well as variant 3, encodes isoform 3.

Source sequence(s)

AC090307

UniProtKB/TrEMBL

B7Z4X7

Conserved Domains (1) summary

cl00137
Location:22 → 255

SERPIN; SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate ...
NM_001348269.2 → NP_001335198.1 serpin B13 isoform 4

Status: REVIEWED

Description

Transcript Variant: This variant (5), as well as variant 6, encodes isoform 4.

Source sequence(s)

AC090307

UniProtKB/TrEMBL

B7Z4X7

Conserved Domains (1) summary

cl00137
Location:2 → 212

SERPIN; SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate ...
NM_001348270.2 → NP_001335199.1 serpin B13 isoform 4

Status: REVIEWED

Description

Transcript Variant: This variant (6), as well as variant 5, encodes isoform 4.

Source sequence(s)

AC090307

UniProtKB/TrEMBL

B7Z4X7

Conserved Domains (1) summary

cl00137
Location:2 → 212

SERPIN; SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate ...
NM_012397.4 → NP_036529.1 serpin B13 isoform 2

See identical proteins and their annotated locations for NP_036529.1

Status: REVIEWED

Description

Transcript Variant: This variant (2) uses an alternate in-frame splice site in the 5' coding region compared to variant 1. The encoded isoform (2) is shorter than isoform 1.

Source sequence(s)

AJ001696, AL050177, BC101821, DC346089

Consensus CDS

CCDS11985.1

UniProtKB/Swiss-Prot

A8K2Q8, Q3MII2, Q9HCX1, Q9UBW1, Q9UIV8, Q9UKG0

UniProtKB/TrEMBL

B7ZKV6

Related

ENSP00000341584.6, ENST00000344731.10

Conserved Domains (1) summary

cl00137
Location:4 → 391

SERPIN; SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate ...

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_000018.10 Reference GRCh38.p14 Primary Assembly

Range

63587343..63599192

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_011526029.4 → XP_011524331.1 serpin B13 isoform X1

UniProtKB/TrEMBL

B7ZKV6

Conserved Domains (1) summary

cl00137
Location:4 → 390

SERPIN; SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate ...