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SPINT1 (serine peptidase inhibitor, Kunitz type 1)

Written2009-02Hiroaki Kataoka
Section of Oncopathology, Regenerative Biology, Faculty of Medicine, University of Miyazaki 5200 Kihara, Kiyotake, Miyazaki 889-1692, Japan

(Note : for Links provided by Atlas : click)


HGNC Alias symbHAI
HGNC Previous nameserine protease inhibitor, Kunitz type 1
LocusID (NCBI) 6692
Atlas_Id 44384
Location 15q15.1  [Link to chromosome band 15q15]
Location_base_pair Starts at 40844048 and ends at 40858207 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping SPINT1.png]
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
KRT19 (17q21.2)::SPINT1 (15q15.1)NCOA3 (20q13.12)::SPINT1 (15q15.1)PHB2 (12p13.31)::SPINT1 (15q15.1)
SPINT1 (15q15.1)::C7orf49 (7q33)SPINT1 (15q15.1)::CALM3 (19q13.32)SPINT1 (15q15.1)::DTWD2 (5q23.1)
SPINT1 (15q15.1)::HIF1A (14q23.2)SPINT1 (15q15.1)::SPINT2 (19q13.2)TIMM17B (Xp11.23)::SPINT1 (15q15.1)


  Structure of the human SPINT1 gene.
Description The human SPINT1 gene spans approximately 13.6 kb in length and consists of 11 exons separated by 10 introns. The size of the exons ranges from 26 bp (exon 6) to about 0.8kb (exon 11). The size of introns ranges from 83 bp to about 7 kb. The first exon encodes only a part of 5'-untranslated region (UTR) of the SPINT1 transcript. Exon 2 contains the remaining 5'-UTR and the putative signal sequence. Two Kunitz-type inhibitor domains (KD-1 and KD-2) are encoded by exons 5 and 9, respectively.
Transcription There are two major transcripts, isoform 1 (also known as HAI-1B) and isoform 2 (also known as HAI-1 or HAI-1A) produced by alternative splicing. Isoform 1 and isoform 2 mRNAs encode for 529 and 513 amino acids, respectively.


  Structures of SPINT1 protein isoform 1 (HAI-1B) and isoform 2 (HAI-1A). SP, signal peptide; MANSC, motif at N terminus with seven cysteines; KD-1, Kunitz domain-1; LDLa, low-density lipoprotein receptor domain class A; KD-2, Kunitz domain-2; TM, transmembrane domain. Isoform 1 (HAI-1B) contains an extra 16 amino acids adjacent to the C terminus of KD-1.
Description The protein encoded by this gene is a member of the Kunitz family of serine proteinase inhibitors. Shimomura et al. (1997) purified this protein from a conditioned medium of a gastric carcinoma cell line MKN45 as a potent inhibitor specific for hepatocyte growth factor activator (HGFAC), a serum serine proteinase that is thought to be involved in the proteolytic activation of hepatocyte growth factor (HGF) in injured tissues. For this reason, SPINT1 was initially designated as HGFAC inhibitor type 1 (HAI-1). The initially cloned cDNA of SPINT1 encoded a 513 amino acids protein (478-amino acid mature protein with a calculated molecular mass of 53.3 kD). SPINT1 is a transmembrane protein expressed on the cell surface. It is composed of an extracellular domain containing an N-terminal Kunitz domain (KD1), a low-density lipoprotein (LDL) receptor-like domain and a C-terminal Kunitz domain (KD2), followed by a transmembrane region and a short cytoplasmic domain. Later, a major transcript variant, also known as HAI-1B, was reported by Kirchhofer et al. (2003). This variant encodes the longer isoform consisting of an extra 16 amino acids adjacent to the C terminus of Kunitz domain-1 (KD1); however, there is no functional difference between HAI-1 (HAI-1A) and HAI-1B.
Previous studies demonstrated that SPINT1 potently inhibits the action of a variety of trypsin-like serine proteinases, some of which may be involved in carcinogenesis, invasion and metastasis. These proteinases include HGFAC, matriptase/ST14, hepsin/TMPRSS1 and human kallikrein 1-related peptidases such as KLK4 and KLK5. Among them, matriptase/ST14 and hepsin/TMPRSS1 belong to the type II transmembrane serine protease superfamily. Other possible target proteinases include prostasin/PRSS8 and trypsin. Evidence suggests that matriptase/ST14 is the most important cognate proteinase of SPINT1 on epithelial surface. KD-1 is responsible for the inhibition of two major target proteinases, matriptase/ST14 and HGFAC.
Expression SPINT1 protein is strongly expressed in the surface epithelium of gastrointestinal tracts, endocervical epithelium, ductal epithelia of biliary tracts and pancreas, prostatic glandular epithelium and renal tubular epithelium. It is also strongly expressed in hair cortex and cuticle cells, and to a lesser degree in epidermal keratinocytes. Mesothelial cells on the serous surface also express SPINT1. Weaker expression has been detected in the endothelial cells of capillaries, venules and lymphatics. Placental tissue shows very high level of SPINT1 mRNA, and villous cytotrophoblasts are mainly responsible for this expression.
Localisation SPINT1 is mainly located on the basolateral membrane of polarized epithelial cells.
Function To date, several proposed functions of SPINT1 have been reported.
  • Inhibition of serine proteinases: SPINT1 strongly inhibits HGFAC, trypsin, KLK4, KLK5, matriptase/ST14, prostasin/PRSS8 and hepsin/TMPRSS1.
  • Optimal regulation of pericellular proteinase activity: Evidence has suggested that SPINT1 is required for the trafficking of proforms of matriptase/ST14 to the cell surface and also for the activation of pro-matriptase/ST14 even though it can inhibit matriptase/ST14 activity. Therefore, without SPINT1, activation and proper localization of matriptase/ST14 appear to be significantly impaired. Such paradoxical effects of SPINT1 are also observed in the interaction with HGFAC. SPINT1 inhibits HGFAC, but paradoxically, serves as a reservoir of active HGFAC on the cell surface.
  • Regulation of pericellular HGF activation: Among target proteinases of SPINT1, HGFAC, matriptase/ST14 and hepsin/TMPRSS1 are known to activate precursor form of HGF (proHGF). Thus, SPINT1 is thought to regulate pericellular proHGF activation.
  • Function in the placenta development: SPINT1 is essential in the placental development, as SPINT1-deficient mouse embryos die during mid-gestation due to impaired formation of the placental labyrinth layer.
  • Function in the skin development: Rescue of the placental function results in successful delivery of SPINT-1-deficient neonates. However, they die within 16 days after delivery with significant skin abnormalities such as abnormal keratinization and impaired formation of hair cuticle. Therefore, SPINT1 is critical in the regulated keratinization of epidermis and formation of hair cuticle.
  • Tumor suppressor activity: Transgenic overexpression of matriptase/ST14 resulted in skin carcinogenesis. However, the development of skin cancer (squamous cell carcinoma) was suppressed when SPINT1 was co-expressed.
  • Homology SPINT-2 (also known as HAI-2 or placental bikunin) is also a membrane-bound Kunitz-type serine proteinase inhibitor consisting of two extracellular Kunitz domain. The amino acids identity between SPINT1 KD-1 and SPINT2 KD-1 is 54%, and between SPINT1 KD-2 and SPINT2 KD-2 is 36 %. However, SPINT2 lacks MANSC domain and LDL receptor-like domain.

    Implicated in

    Entity Various cancers
    Oncogenesis A possible tumor suppressor activity of SPINT1 has been reported in matriptase/ST14-induced skin carcinogenesis. Immunohistochemical studies suggest that the balance between SPINT1 and its target proteinase such as matriptase/ST14 may be important in the progression of breast cancer and prostate cancer. Downregulation of SPINT1 is also reported in part of the colon, renal cell and ovarian carcinoma cases. In vitro knockdown of SPINT1 results in an invasive phenotype of certain epithelial and carcinoma cells.


    Functional characterization of Kunitz domains in hepatocyte growth factor activator inhibitor type 1.
    Denda K, Shimomura T, Kawaguchi T, Miyazawa K, Kitamura N.
    J Biol Chem. 2002 Apr 19;277(16):14053-9. Epub 2002 Jan 22.
    PMID 11805118
    Hepatocyte growth factor activator inhibitor-1 (HAI-1) is essential for the integrity of basement membranes in the developing placental labyrinth.
    Fan B, Brennan J, Grant D, Peale F, Rangell L, Kirchhofer D.
    Dev Biol. 2007 Mar 1;303(1):222-30. Epub 2006 Nov 10.
    PMID 17174946
    Identification of hepatocyte growth factor activator inhibitor-1B as a potential physiological inhibitor of prostasin.
    Fan B, Wu TD, Li W, Kirchhofer D.
    J Biol Chem. 2005 Oct 14;280(41):34513-20. Epub 2005 Aug 15.
    PMID 16103126
    Hepatocyte growth factor activator inhibitor-1 has a complex subcellular itinerary.
    Godiksen S, Selzer-Plon J, Pedersen ED, Abell K, Rasmussen HB, Szabo R, Bugge TH, Vogel LK.
    Biochem J. 2008 Jul 15;413(2):251-9.
    PMID 18402552
    MANSC: a seven-cysteine-containing domain present in animal membrane and extracellular proteins.
    Guo J, Chen S, Huang C, Chen L, Studholme DJ, Zhao S, Yu L.
    Trends Biochem Sci. 2004 Apr;29(4):172-4.
    PMID 15124631
    Upregulation of HGF activator inhibitor type 1 but not type 2 along with regeneration of intestinal mucosa.
    Itoh H, Kataoka H, Tomita M, Hamasuna R, Nawa Y, Kitamura N, Koono M.
    Am J Physiol Gastrointest Liver Physiol. 2000 Apr;278(4):G635-43.
    PMID 10762618
    Genomic structure and chromosomal localization of the human hepatocyte growth factor activator inhibitor type 1 and 2 genes.
    Itoh H, Yamauchi M, Kataoka H, Hamasuna R, Kitamura N, Koono M.
    Eur J Biochem. 2000 Jun;267(11):3351-9.
    PMID 10824123
    Tissue microarray analysis of hepatocyte growth factor/Met pathway components reveals a role for Met, matriptase, and hepatocyte growth factor activator inhibitor 1 in the progression of node-negative breast cancer.
    Kang JY, Dolled-Filhart M, Ocal IT, Singh B, Lin CY, Dickson RB, Rimm DL, Camp RL.
    Cancer Res. 2003 Mar 1;63(5):1101-5.
    PMID 12615728
    Roles of hepatocyte growth factor (HGF) activator and HGF activator inhibitor in the pericellular activation of HGF/scatter factor.
    Kataoka H, Miyata S, Uchinokura S, Itoh H.
    Cancer Metastasis Rev. 2003 Jun-Sep;22(2-3):223-36. (REVIEW)
    PMID 12784998
    Hepatocyte growth factor activator inhibitor type 1 is a specific cell surface binding protein of hepatocyte growth factor activator (HGFA) and regulates HGFA activity in the pericellular microenvironment.
    Kataoka H, Shimomura T, Kawaguchi T, Hamasuna R, Itoh H, Kitamura N, Miyazawa K, Koono M.
    J Biol Chem. 2000 Dec 22;275(51):40453-62.
    PMID 11013244
    Hepsin activates pro-hepatocyte growth factor and is inhibited by hepatocyte growth factor activator inhibitor-1B (HAI-1B) and HAI-2.
    Kirchhofer D, Peek M, Lipari MT, Billeci K, Fan B, Moran P.
    FEBS Lett. 2005 Mar 28;579(9):1945-50.
    PMID 15792801
    Roles of functional and structural domains of hepatocyte growth factor activator inhibitor type 1 in the inhibition of matriptase.
    Kojima K, Tsuzuki S, Fushiki T, Inouye K.
    J Biol Chem. 2008 Feb 1;283(5):2478-87. Epub 2007 Nov 29.
    PMID 18048349
    Expression of hepatocyte growth factor activator inhibitor type 1 on the epithelial cell surface is regulated by hypoxic and oxidative stresses.
    Komaki W, Fukushima T, Tanaka H, Itoh H, Chosa E, Kataoka H.
    Virchows Arch. 2008 Oct;453(4):347-57. Epub 2008 Sep 4.
    PMID 18769935
    Simultaneous activation and hepatocyte growth factor activator inhibitor 1-mediated inhibition of matriptase induced at activation foci in human mammary epithelial cells.
    Lee MS, Kiyomiya K, Benaud C, Dickson RB, Lin CY.
    Am J Physiol Cell Physiol. 2005 Apr;288(4):C932-41. Epub 2004 Dec 8.
    PMID 15590895
    Purification and characterization of a complex containing matriptase and a Kunitz-type serine protease inhibitor from human milk.
    Lin CY, Anders J, Johnson M, Dickson RB.
    J Biol Chem. 1999 Jun 25;274(26):18237-42.
    PMID 10373425
    Deregulated matriptase causes ras-independent multistage carcinogenesis and promotes ras-mediated malignant transformation.
    List K, Szabo R, Molinolo A, Sriuranpong V, Redeye V, Murdock T, Burke B, Nielsen BS, Gutkind JS, Bugge TH.
    Genes Dev. 2005 Aug 15;19(16):1934-50.
    PMID 16103220
    Live imaging of chronic inflammation caused by mutation of zebrafish Hai1.
    Mathias JR, Dodd ME, Walters KB, Rhodes J, Kanki JP, Look AT, Huttenlocher A.
    J Cell Sci. 2007 Oct 1;120(Pt 19):3372-83.
    PMID 17881499
    Defect of hepatocyte growth factor activator inhibitor type 1/serine protease inhibitor, Kunitz type 1 (Hai-1/Spint1) leads to ichthyosis-like condition and abnormal hair development in mice.
    Nagaike K, Kawaguchi M, Takeda N, Fukushima T, Sawaguchi A, Kohama K, Setoyama M, Kataoka H..
    Am J Pathol. 2008 Nov;173(5):1464-75. Epub 2008 Oct 2.
    PMID 18832587
    Serum hepatocyte growth factor activator inhibitor type I (HAI-I) and type 2 (HAI-2) in prostate cancer.
    Nagakawa O, Yamagishi T, Akashi T, Nagaike K, Fuse H.
    Prostate. 2006 Apr 1;66(5):447-52.
    PMID 16353247
    Expression of hepatocyte growth factor activator inhibitors (HAI-1 and HAI-2) in ovarian cancer.
    Nakamura K, Abarzua F, Kodama J, Hongo A, Nasu Y, Kumon H, Hiramatsu Y.
    Int J Oncol. 2009 Feb;34(2):345-53.
    PMID 19148468
    Matriptase and HAI-1 are expressed by normal and malignant epithelial cells in vitro and in vivo.
    Oberst M, Anders J, Xie B, Singh B, Ossandon M, Johnson M, Dickson RB, Lin CY.
    Am J Pathol. 2001 Apr;158(4):1301-11.
    PMID 11290548
    HAI-1 regulates activation and expression of matriptase, a membrane-bound serine protease.
    Oberst MD, Chen LY, Kiyomiya K, Williams CA, Lee MS, Johnson MD, Dickson RB, Lin CY.
    Am J Physiol Cell Physiol. 2005 Aug;289(2):C462-70. Epub 2005 Mar 30.
    PMID 15800053
    Expression of the serine protease matriptase and its inhibitor HAI-1 in epithelial ovarian cancer: correlation with clinical outcome and tumor clinicopathological parameters.
    Oberst MD, Johnson MD, Dickson RB, Lin CY, Singh B, Stewart M, Williams A, al-Nafussi A, Smyth JF, Gabra H, Sellar GC.
    Clin Cancer Res. 2002 Apr;8(4):1101-7.
    PMID 11948120
    The activation of matriptase requires its noncatalytic domains, serine protease domain, and its cognate inhibitor.
    Oberst MD, Williams CA, Dickson RB, Johnson MD, Lin CY.
    J Biol Chem. 2003 Jul 18;278(29):26773-9. Epub 2003 May 8.
    PMID 12738778
    Hepatocyte growth factor activation inhibitors (HAI-1 and HAI-2) regulate HGF-induced invasion of human breast cancer cells.
    Parr C, Jiang WG.
    Int J Cancer. 2006 Sep 1;119(5):1176-83.
    PMID 16557597
    The hepatocyte growth factor regulatory factors in human breast cancer.
    Parr C, Watkins G, Mansel RE, Jiang WG.
    Clin Cancer Res. 2004 Jan 1;10(1 Pt 1):202-11.
    PMID 14734471
    A novel biomarker for staging human prostate adenocarcinoma: overexpression of matriptase with concomitant loss of its inhibitor, hepatocyte growth factor activator inhibitor-1.
    Saleem M, Adhami VM, Zhong W, Longley BJ, Lin CY, Dickson RB, Reagan-Shaw S, Jarrard DF, Mukhtar H.
    Cancer Epidemiol Biomarkers Prev. 2006 Feb;15(2):217-27.
    PMID 16492908
    Suppression of hepatocyte growth factor activator inhibitor-1 leads to a more aggressive phenotype of prostate cancer cells in vitro.
    Sanders AJ, Parr C, Mason MD, Jiang WG.
    Int J Mol Med. 2007 Oct;20(4):613-9.
    PMID 17786295
    Hepatocyte growth factor activator inhibitor, a novel Kunitz-type serine protease inhibitor.
    Shimomura T, Denda K, Kitamura A, Kawaguchi T, Kito M, Kondo J, Kagaya S, Qin L, Takata H, Miyazawa K, Kitamura N.
    J Biol Chem. 1997 Mar 7;272(10):6370-6.
    PMID 9045658
    Matriptase inhibition by hepatocyte growth factor activator inhibitor-1 is essential for placental development.
    Szabo R, Molinolo A, List K, Bugge TH.
    Oncogene. 2007 Mar 8;26(11):1546-56. Epub 2006 Sep 18.
    PMID 16983341
    Hepatocyte growth factor activator inhibitor type 1 (HAI-1) is required for branching morphogenesis in the chorioallantoic placenta.
    Tanaka H, Nagaike K, Takeda N, Itoh H, Kohama K, Fukushima T, Miyata S, Uchiyama S, Uchinokura S, Shimomura T, Miyazawa K, Kitamura N, Yamada G, Kataoka H.
    Mol Cell Biol. 2005 Jul;25(13):5687-98.
    PMID 15964823
    Hepatocyte growth factor activator inhibitor types 1 and 2 are expressed by tubular epithelium in kidney and down-regulated in renal cell carcinoma.
    Yamauchi M, Kataoka H, Itoh H, Seguchi T, Hasui Y, Osada Y.
    J Urol. 2004 Feb;171(2 Pt 1):890-6.
    PMID 14713848


    This paper should be referenced as such :
    Kataoka, H
    SPINT1 (serine peptidase inhibitor, Kunitz type 1)
    Atlas Genet Cytogenet Oncol Haematol. 2010;14(1):58-61.
    Free journal version : [ pdf ]   [ DOI ]

    External links


    HGNC (Hugo)SPINT1   11246
    Entrez_Gene (NCBI)SPINT1    serine peptidase inhibitor, Kunitz type 1
    AliasesHAI; HAI1; MANSC2
    GeneCards (Weizmann)SPINT1
    Ensembl hg19 (Hinxton)ENSG00000166145 [Gene_View]
    Ensembl hg38 (Hinxton)ENSG00000166145 [Gene_View]  ENSG00000166145 [Sequence]  chr15:40844048-40858207 [Contig_View]  SPINT1 [Vega]
    ICGC DataPortalENSG00000166145
    TCGA cBioPortalSPINT1
    AceView (NCBI)SPINT1
    Genatlas (Paris)SPINT1
    SOURCE (Princeton)SPINT1
    Genetics Home Reference (NIH)SPINT1
    Genomic and cartography
    GoldenPath hg38 (UCSC)SPINT1  -     chr15:40844048-40858207 +  15q15.1   [Description]    (hg38-Dec_2013)
    GoldenPath hg19 (UCSC)SPINT1  -     15q15.1   [Description]    (hg19-Feb_2009)
    GoldenPathSPINT1 - 15q15.1 [CytoView hg19]  SPINT1 - 15q15.1 [CytoView hg38]
    Genome Data Viewer NCBISPINT1 [Mapview hg19]  
    Gene and transcription
    Genbank (Entrez)AB000095 AI684245 AK300195 AK303899 AK314825
    RefSeq transcript (Entrez)NM_001032367 NM_001386873 NM_001386874 NM_001386875 NM_003710 NM_181642
    Consensus coding sequences : CCDS (NCBI)SPINT1
    Gene ExpressionSPINT1 [ NCBI-GEO ]   SPINT1 [ EBI - ARRAY_EXPRESS ]   SPINT1 [ SEEK ]   SPINT1 [ MEM ]
    Gene Expression Viewer (FireBrowse)SPINT1 [ Firebrowse - Broad ]
    GenevisibleExpression of SPINT1 in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
    BioGPS (Tissue expression)6692
    GTEX Portal (Tissue expression)SPINT1
    Human Protein AtlasENSG00000166145-SPINT1 [pathology]   [cell]   [tissue]
    Protein : pattern, domain, 3D structure
    UniProt/SwissProtO43278   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
    NextProtO43278  [Sequence]  [Exons]  [Medical]  [Publications]
    With graphics : InterProO43278
    Domaine pattern : Prosite (Expaxy)BPTI_KUNITZ_1 (PS00280)    BPTI_KUNITZ_2 (PS50279)    LDLRA_1 (PS01209)    LDLRA_2 (PS50068)    MANSC (PS50986)   
    Domains : Interpro (EBI)Ig-like_fold    Kunitz_BPTI    Kunitz_BPTI_sf    LDL_receptor-like_sf    LDLR_class-A_CS    LDrepeatLR_classA_rpt    MANSC_dom    MANSC_N    Prtase_inh_Kunz-CS    Spint1   
    Domain families : Pfam (Sanger)Kunitz_BPTI (PF00014)    Ldl_recept_a (PF00057)    MANEC (PF07502)   
    Domain families : Pfam (NCBI)pfam00014    pfam00057    pfam07502   
    Domain families : Smart (EMBL)KU (SM00131)  LDLa (SM00192)  MANEC (SM00765)  
    Conserved Domain (NCBI)SPINT1
    PDB (RSDB)1YC0    2MSX    4ISL    4ISN    4ISO    5EZD    5H7V   
    PDB Europe1YC0    2MSX    4ISL    4ISN    4ISO    5EZD    5H7V   
    PDB (PDBSum)1YC0    2MSX    4ISL    4ISN    4ISO    5EZD    5H7V   
    PDB (IMB)1YC0    2MSX    4ISL    4ISN    4ISO    5EZD    5H7V   
    Structural Biology KnowledgeBase1YC0    2MSX    4ISL    4ISN    4ISO    5EZD    5H7V   
    SCOP (Structural Classification of Proteins)1YC0    2MSX    4ISL    4ISN    4ISO    5EZD    5H7V   
    CATH (Classification of proteins structures)1YC0    2MSX    4ISL    4ISN    4ISO    5EZD    5H7V   
    AlphaFold pdb e-kbO43278   
    Human Protein Atlas [tissue]ENSG00000166145-SPINT1 [tissue]
    Protein Interaction databases
    DIP (DOE-UCLA)O43278
    IntAct (EBI)O43278
    Ontologies - Pathways
    Ontology : AmiGOneural tube closure  serine-type endopeptidase inhibitor activity  extracellular region  extracellular space  plasma membrane  negative regulation of endopeptidase activity  membrane  extracellular matrix organization  positive regulation of glial cell differentiation  branching involved in labyrinthine layer morphogenesis  placenta blood vessel development  extracellular exosome  cellular response to BMP stimulus  negative regulation of neural precursor cell proliferation  
    Ontology : EGO-EBIneural tube closure  serine-type endopeptidase inhibitor activity  extracellular region  extracellular space  plasma membrane  negative regulation of endopeptidase activity  membrane  extracellular matrix organization  positive regulation of glial cell differentiation  branching involved in labyrinthine layer morphogenesis  placenta blood vessel development  extracellular exosome  cellular response to BMP stimulus  negative regulation of neural precursor cell proliferation  
    Pathways : KEGGTranscriptional misregulation in cancer   
    REACTOMEO43278 [protein]
    REACTOME PathwaysR-HSA-8852405 [pathway]   
    NDEx NetworkSPINT1
    Atlas of Cancer Signalling NetworkSPINT1
    Wikipedia pathwaysSPINT1
    Orthology - Evolution
    GeneTree (enSembl)ENSG00000166145
    Phylogenetic Trees/Animal Genes : TreeFamSPINT1
    Homologs : HomoloGeneSPINT1
    Homology/Alignments : Family Browser (UCSC)SPINT1
    Gene fusions - Rearrangements
    Fusion : MitelmanNCOA3::SPINT1 [20q13.12/15q15.1]  
    Fusion : QuiverSPINT1
    Polymorphisms : SNP and Copy number variants
    NCBI Variation ViewerSPINT1 [hg38]
    dbSNP Single Nucleotide Polymorphism (NCBI)SPINT1
    Exome Variant ServerSPINT1
    GNOMAD BrowserENSG00000166145
    Varsome BrowserSPINT1
    ACMGSPINT1 variants
    Genomic Variants (DGV)SPINT1 [DGVbeta]
    DECIPHERSPINT1 [patients]   [syndromes]   [variants]   [genes]  
    CONAN: Copy Number AnalysisSPINT1 
    ICGC Data PortalSPINT1 
    TCGA Data PortalSPINT1 
    Broad Tumor PortalSPINT1
    OASIS PortalSPINT1 [ Somatic mutations - Copy number]
    Somatic Mutations in Cancer : COSMICSPINT1  [overview]  [genome browser]  [tissue]  [distribution]  
    Somatic Mutations in Cancer : COSMIC3DSPINT1
    Mutations and Diseases : HGMDSPINT1
    LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
    DgiDB (Drug Gene Interaction Database)SPINT1
    DoCM (Curated mutations)SPINT1
    CIViC (Clinical Interpretations of Variants in Cancer)SPINT1
    NCG (London)SPINT1
    Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
    Genetic Testing Registry SPINT1
    NextProtO43278 [Medical]
    Target ValidationSPINT1
    Huge Navigator SPINT1 [HugePedia]
    Clinical trials, drugs, therapy
    Protein Interactions : CTDSPINT1
    Pharm GKB GenePA36076
    Clinical trialSPINT1
    canSAR (ICR)SPINT1
    DataMed IndexSPINT1
    PubMed84 Pubmed reference(s) in Entrez
    GeneRIFsGene References Into Functions (Entrez)
    REVIEW articlesautomatic search in PubMed
    Last year publicationsautomatic search in PubMed

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