HAX1

HCLS1 associated protein X-1
Identifiers
Symbols	HAX1 ; HCLSBP1; HS1BP1; SCN3
External IDs	OMIM: 605998 MGI: 1346319 HomoloGene: 4463 GeneCards: HAX1 Gene
Gene ontology Molecular function • protein binding • interleukin-1 binding • protein N-terminus binding Cellular component • nuclear envelope • transcription factor complex • mitochondrion • mitochondrial outer membrane • mitochondrial intermembrane space • endoplasmic reticulum • actin cytoskeleton • cytoplasmic membrane-bounded vesicle • sarcoplasmic reticulum • lamellipodium • nuclear membrane Biological process • mitochondrion organization • positive regulation of phosphatidylinositol 3-kinase signaling • regulation of actin filament polymerization • positive regulation of granulocyte differentiation • positive regulation of peptidyl-serine phosphorylation • regulation of apoptotic process • negative regulation of apoptotic process • positive regulation of transcription from RNA polymerase II promoter • positive regulation of peptidyl-tyrosine phosphorylation • positive regulation of protein kinase B signaling • cellular response to cytokine stimulus • regulation of mitophagy • regulation of protein targeting to mitochondrion • positive regulation of actin cytoskeleton reorganization Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	10456	23897
Ensembl	ENSG00000143575	ENSMUSG00000027944
UniProt	O00165	O35387
RefSeq (mRNA)	NM_001018837	NM_001282032
RefSeq (protein)	NP_001018238	NP_001268961
Location (UCSC)	Chr 1: 154.27 – 154.28 Mb	Chr 3: 90 – 90 Mb
PubMed search

HCLS1-associated protein X-1 is a protein that in humans is encoded by the HAX1 gene.^[1][2][3]

The protein encoded by this gene is known to associate with HS1, a substrate of Src family tyrosine kinases. It also interacts with the product of PKD2 gene, mutations in which are associated with autosomal-dominant polycystic kidney disease, and with F-actin-binding protein, cortactin. It was earlier thought that this gene product is mainly localized in the mitochondria, however, recent studies indicate it to be localized in the cell body. Two transcript variants encoding different isoforms have been found for this gene.^[3]

Severe congenital neutropenia

Homozygous mutations in HAX1 are associated with autosomal recessive severe congenital neutropenia,^[4] also known as Kostmann syndrome.

Interactions

HAX1 has been shown to interact with IL1A.^[5]

References

1. Suzuki Y, Demoliere C, Kitamura D, Takeshita H, Deuschle U, Watanabe T (Apr 1997). "HAX-1, a novel intracellular protein, localized on mitochondria, directly associates with HS1, a substrate of Src family tyrosine kinases". J Immunol 158 (6): 2736–44. PMID 9058808.
2. Gallagher AR, Cedzich A, Gretz N, Somlo S, Witzgall R (May 2000). "The polycystic kidney disease protein PKD2 interacts with Hax-1, a protein associated with the actin cytoskeleton". Proc Natl Acad Sci U S A 97 (8): 4017–22. doi:10.1073/pnas.97.8.4017. PMC 18134. PMID 10760273.
3. "Entrez Gene: HAX1 HCLS1 associated protein X-1".
4. Klein C, Grudzien M, Appaswamy G, et al. (January 2007). "HAX1 deficiency causes autosomal recessive severe congenital neutropenia (Kostmann disease)". Nat. Genet. 39 (1): 86–92. doi:10.1038/ng1940. PMID 17187068.
5. Yin, H; Morioka H; Towle C A; Vidal M; Watanabe T; Weissbach L (Aug 2001). "Evidence that HAX-1 is an interleukin-1 alpha N-terminal binding protein". Cytokine (United States) 15 (3): 122–37. doi:10.1006/cyto.2001.0891. ISSN 1043-4666. PMID 11554782.

Further reading

• Modem S, Reddy TR (2007). "An anti-apoptotic protein, Hax-1, inhibits the HIV-1 rev function by altering its sub-cellular localization". J. Cell. Physiol. 214 (1): 14–9. doi:10.1002/jcp.21305. PMID 17929250.
• Klein C, Grudzien M, Appaswamy G, et al. (2007). "HAX1 deficiency causes autosomal recessive severe congenital neutropenia (Kostmann disease)". Nat. Genet. 39 (1): 86–92. doi:10.1038/ng1940. PMID 17187068.
• Kawaguchi Y, Nishimagi E, Tochimoto A, et al. (2006). "Intracellular IL-1α-binding proteins contribute to biological functions of endogenous IL-1α in systemic sclerosis fibroblasts". Proc. Natl. Acad. Sci. U.S.A. 103 (39): 14501–6. doi:10.1073/pnas.0603545103. PMC 1599989. PMID 16971486.
• Han Y, Chen YS, Liu Z, et al. (2006). "Overexpression of HAX-1 protects cardiac myocytes from apoptosis through caspase-9 inhibition". Circ. Res. 99 (4): 415–23. doi:10.1161/01.RES.0000237387.05259.a5. PMID 16857965.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Ortiz DF, Moseley J, Calderon G, et al. (2004). "Identification of HAX-1 as a protein that binds bile salt export protein and regulates its abundance in the apical membrane of Madin-Darby canine kidney cells". J. Biol. Chem. 279 (31): 32761–70. doi:10.1074/jbc.M404337200. PMID 15159385.
• Bouwmeester T, Bauch A, Ruffner H, et al. (2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nat. Cell Biol. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216.
• Mirmohammadsadegh A, Tartler U, Michel G, et al. (2003). "HAX-1, identified by differential display reverse transcription polymerase chain reaction, is overexpressed in lesional psoriasis". J. Invest. Dermatol. 120 (6): 1045–51. doi:10.1046/j.1523-1747.2003.12247.x. PMID 12787133.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Yin H, Morioka H, Towle CA, et al. (2001). "Evidence that HAX-1 is an interleukin-1 alpha N-terminal binding protein". Cytokine 15 (3): 122–37. doi:10.1006/cyto.2001.0891. PMID 11554782.