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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''HIG1 domain family member 1A''' (HIGD1A), also known as hypoglycemia/hypoxia inducible mitochondrial protein1-a (HIMP1-a) and hypoxia induced gene 1 (HIG1),  is a [[protein]] that in humans is encoded by the ''HIGD1A'' [[gene]] on chromosome 3.<ref name="pmid11042152">{{cite journal | vauthors = Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z | title = Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells | journal = Genome Research | volume = 10 | issue = 10 | pages = 1546–60 | date = Oct 2000 | pmid = 11042152 | pmc = 310934 | doi = 10.1101/gr.140200 }}</ref><ref name="pmid11230166">{{cite journal | vauthors = Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Böcher M, Blöcker H, Bauersachs S, Blum H, Lauber J, Düsterhöft A, Beyer A, Köhrer K, Strack N, Mewes HW, Ottenwälder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A | title = Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs | journal = Genome Research | volume = 11 | issue = 3 | pages = 422–35 | date = Mar 2001 | pmid = 11230166 | pmc = 311072 | doi = 10.1101/gr.GR1547R }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: HIGD1A HIG1 domain family, member 1A| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=25994| accessdate = }}</ref><ref name="pmid23878241">{{cite journal | vauthors = An HJ, Cho G, Lee JO, Paik SG, Kim YS, Lee H | title = Higd-1a interacts with Opa1 and is required for the morphological and functional integrity of mitochondria | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 110 | issue = 32 | pages = 13014–9 | date = Aug 2013 | pmid = 23878241 | doi = 10.1073/pnas.1307170110 | pmc=3740888}}</ref> This protein promotes [[mitochondria]]l [[homeostasis]] and survival of [[cell (biology)|cells]] under stress and is involved in [[inflammation|inflammatory]] and [[hypoxia (medical)|hypoxia]]-related [[disease]]s, including [[atherosclerosis]], [[ischemia|ischemic]] [[heart disease]], and [[Alzheimer’s disease]], as well as [[cancer]].<ref name="pmid23878241"/><ref name="pmid21856340">{{cite journal | vauthors = An HJ, Shin H, Jo SG, Kim YJ, Lee JO, Paik SG, Lee H | title = The survival effect of mitochondrial Higd-1a is associated with suppression of cytochrome C release and prevention of caspase activation | journal = Biochimica et Biophysica Acta | volume = 1813 | issue = 12 | pages = 2088–98 | date = Dec 2011 | pmid = 21856340 | doi = 10.1016/j.bbamcr.2011.07.017 }}</ref><ref name="pmid23646141">{{cite journal | vauthors = Ameri K, Rajah AM, Nguyen V, Sanders TA, Jahangiri A, Delay M, Donne M, Choi HJ, Tormos KV, Yeghiazarians Y, Jeffrey SS, Rinaudo PF, Rowitch DH, Aghi M, Maltepe E | title = Nuclear localization of the mitochondrial factor HIGD1A during metabolic stress | journal = PLOS ONE | volume = 8 | issue = 4 | pages = e62758 | date = 2013 | pmid = 23646141 | doi = 10.1371/journal.pone.0062758 | pmc=3639984}}</ref><ref name="pmid22355194">{{cite journal | vauthors = Hayashi H, Nakagami H, Takeichi M, Shimamura M, Koibuchi N, Oiki E, Sato N, Koriyama H, Mori M, Gerardo Araujo R, Maeda A, Morishita R, Tamai K, Kaneda Y | title = HIG1, a novel regulator of mitochondrial γ-secretase, maintains normal mitochondrial function | journal = FASEB Journal | volume = 26 | issue = 6 | pages = 2306–17 | date = Jun 2012 | pmid = 22355194 | doi = 10.1096/fj.11-196063 }}</ref>
| update_page = yes
| require_manual_inspection = no
== Structure ==
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The protein encoded by this gene is 10.4 kDa [[inner mitochondrial membrane|mitochondrial inner membrane]] protein with two [[transmembrane]] domains at the N- and C-terminals.<ref name="pmid21856340"/><ref name="pmid23646141"/> These two domains are arranged such that the N- and C-terminals face outward into the [[intermembrane space]] while the rest of the protein loops inside the [[mitochondrial matrix|matrix]]. Though the N-terminal domain is not necessary to direct the localization of HIGD1A, it is required for the survival of the protein.
{{GNF_Protein_box
   
| image =
The gene ''HIGD1A'' is an [[isoform]] of ''HIMP1-b'' via [[alternative splicing]].<ref name="pmid21856340"/>
| image_source = 
| PDB =
| Name = HIG1 domain family, member 1A
| HGNCid = 29527
| Symbol = HIGD1A
| AltSymbols =; DKFZP564K247; HIG1
| OMIM = 
| ECnumber = 
| Homologene = 40919
| MGIid = 1930666
| GeneAtlas_image1 = PBB_GE_HIGD1A_217845_x_at_tn.png
  | GeneAtlas_image2 = PBB_GE_HIGD1A_221896_s_at_tn.png
| Function =
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0043234 |text = protein complex}}
| Process =
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 25994
    | Hs_Ensembl = ENSG00000181061
    | Hs_RefseqProtein = NP_054775
    | Hs_RefseqmRNA = NM_014056
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 3
    | Hs_GenLoc_start = 42800799
    | Hs_GenLoc_end = 42820997
    | Hs_Uniprot = Q9Y241
    | Mm_EntrezGene = 56295
    | Mm_Ensembl = ENSMUSG00000044330
    | Mm_RefseqmRNA = NM_019814
    | Mm_RefseqProtein = NP_062788
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 3
    | Mm_GenLoc_start = 86001710
    | Mm_GenLoc_end = 86001997
    | Mm_Uniprot = Q1XG81
  }}
}}
'''HIG1 domain family, member 1A''', also known as '''HIGD1A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HIGD1A HIG1 domain family, member 1A| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=25994| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
== Function ==
{{PBB_Summary
HIGD1A primarily functions in mitochondrial [[homeostasis]] and, thus, cell survival when under conditions of stress, such as [[hypoxia (medical)|hypoxia]] and [[glucose]] deprivation. For instance, HIGD1A promotes survival of [[pancreas|pancreatic]] α and β cells under stress.<ref name="pmid23878241"/><ref name="pmid21856340"/> HIGD1A has also been found in other parts of the [[brain]], [[heart]], [[liver]], and [[kidney]], where it enhances the survival of these organs.<ref name="pmid23878241"/><ref name="pmid22355194"/> In macrophages, HIGD1A prevents apoptosis by inhibiting [[cytochrome C]] release and [[caspase]] activity.<ref name="pmid21856340"/><ref name="pmid23646141"/>
| section_title =  
| summary_text =  
HIGD1A is also involved in [[mitochondrial fusion]] by regulating [[OPA1]] activity. Its inhibition of the cleavage of OPA1 preserves mitochondrial [[membrane potential]], protects against [[apoptosis]], and maintains [[Adenosine triphosphate|ATP]] levels. Its role in mitochondrial fusion also influences downstream processes such as mtDNA synthesis, cell growth, and [[cristae]] organization.<ref name="pmid23878241"/>
}}
In addition, HIGD1A helps preserve mitochondrial function by regulating mitochondrial [[gamma secretase|γ-secretase]] activity under hypoxic conditions.<ref name="pmid23878241"/><ref name="pmid22355194"/> In the absence of HIGD1A, γ-secretase contributes to the accumulation of [[amyloid beta]] in the mitochondria, leading to increased ROS production, mitochondrial dysfunction, and eventually, [[apoptosis|cell death]].<ref name="pmid22355194"/>
While HIGD1A predominantly contributes to cell survival, it can also promote apoptosis in neurons during the early developmental stages of the [[central nervous system]].<ref name="pmid23646141"/>


==References==
== Clinical significance ==
{{reflist|2}}
 
==Further reading==
Since HIGD1A promotes cell survival under hypoxia, the protein protects organs like the heart and brain from hypoxia-related diseases.<ref name="pmid21856340"/> In particular, HIGD1A localization to the nucleus correlates with the severity of stress in [[ischemia|ischemic]] heart disease, hypoxic-ischemic [[encephalopathy]], and cancer, and thus may serve as a biomarker for these diseases.<ref name="pmid23646141"/> Moreover, HIGD1A is involved in inflammatory diseases, such as [[atherosclerosis]] and [[rheumatoid arthritis]], through its role in macrophage survival.<ref name="pmid21856340"/> Similarly, HIGD1A could become a key target for treating Alzheimer’s disease by inhibiting γ-secretase, and by extension, amyloid beta production. Notably, HIGD1A inhibits γ-secretase without interfering with [[Notch proteins|Notch]] cleavage, thus minimizing detrimental side effects from targeting this protein.<ref name="pmid22355194"/>
{{refbegin | 2}}
{{PBB_Further_reading
== Interactions ==
| citations =
 
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
HIGD1A is known to [[protein interaction|interact]] with:
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
* [[AIFM1|AIF]],<ref name="pmid23646141"/>
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
* [[gamma secretase|γ-secretase]]<ref name="pmid22355194"/> and
*{{cite journal | author=Denko N, Schindler C, Koong A, ''et al.'' |title=Epigenetic regulation of gene expression in cervical cancer cells by the tumor microenvironment. |journal=Clin. Cancer Res. |volume=6 |issue= 2 |pages= 480-7 |year= 2000 |pmid= 10690527 |doi=  }}
* [[OPA1]].<ref name="pmid23878241"/>
*{{cite journal | author=Zhang QH, Ye M, Wu XY, ''et al.'' |title=Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. |journal=Genome Res. |volume=10 |issue= 10 |pages= 1546-60 |year= 2001 |pmid= 11042152 |doi=  }}
 
*{{cite journal  | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi= }}
== References ==
*{{cite journal  | author=Wiemann S, Weil B, Wellenreuther R, ''et al.'' |title=Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. |journal=Genome Res. |volume=11 |issue= 3 |pages= 422-35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.154701 }}
{{reflist|33em}}
*{{cite journal | author=Simpson JC, Wellenreuther R, Poustka A, ''et al.'' |title=Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing. |journal=EMBO Rep. |volume=1 |issue= 3 |pages= 287-92 |year= 2001 |pmid= 11256614 |doi= 10.1093/embo-reports/kvd058 }}
 
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
== Further reading ==
*{{cite journal  | author=Suzuki Y, Yamashita R, Shirota M, ''et al.'' |title=Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions. |journal=Genome Res. |volume=14 |issue= 9 |pages= 1711-8 |year= 2004 |pmid= 15342556 |doi= 10.1101/gr.2435604 }}
{{refbegin|33em}}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
* {{cite journal | vauthors = Maruyama K, Sugano S | title = Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides | journal = Gene | volume = 138 | issue = 1–2 | pages = 171–4 | date = Jan 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }}
*{{cite journal | author=Wiemann S, Arlt D, Huber W, ''et al.'' |title=From ORFeome to biology: a functional genomics pipeline. |journal=Genome Res. |volume=14 |issue= 10B |pages= 2136-44 |year= 2004 |pmid= 15489336 |doi= 10.1101/gr.2576704 }}
* {{cite journal | vauthors = Bonaldo MF, Lennon G, Soares MB | title = Normalization and subtraction: two approaches to facilitate gene discovery | journal = Genome Research | volume = 6 | issue = 9 | pages = 791–806 | date = Sep 1996 | pmid = 8889548 | doi = 10.1101/gr.6.9.791 }}
*{{cite journal  | author=Kimura K, Wakamatsu A, Suzuki Y, ''et al.'' |title=Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. |journal=Genome Res. |volume=16 |issue= 1 |pages= 55-65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406 }}
* {{cite journal | vauthors = Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S | title = Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library | journal = Gene | volume = 200 | issue = 1–2 | pages = 149–56 | date = Oct 1997 | pmid = 9373149 | doi = 10.1016/S0378-1119(97)00411-3 }}
*{{cite journal | author=Mehrle A, Rosenfelder H, Schupp I, ''et al.'' |title=The LIFEdb database in 2006. |journal=Nucleic Acids Res. |volume=34 |issue= Database issue |pages= D415-8 |year= 2006 |pmid= 16381901 |doi= 10.1093/nar/gkj139 }}
* {{cite journal | vauthors = Denko N, Schindler C, Koong A, Laderoute K, Green C, Giaccia A | title = Epigenetic regulation of gene expression in cervical cancer cells by the tumor microenvironment | journal = Clinical Cancer Research | volume = 6 | issue = 2 | pages = 480–7 | date = Feb 2000 | pmid = 10690527 | doi =  }}
*{{cite journal | author=Ewing RM, Chu P, Elisma F, ''et al.'' |title=Large-scale mapping of human protein-protein interactions by mass spectrometry. |journal=Mol. Syst. Biol. |volume=3 |issue= |pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 }}
* {{cite journal | vauthors = Hartley JL, Temple GF, Brasch MA | title = DNA cloning using in vitro site-specific recombination | journal = Genome Research | volume = 10 | issue = 11 | pages = 1788–95 | date = Nov 2000 | pmid = 11076863 | pmc = 310948 | doi = 10.1101/gr.143000 }}
}}
* {{cite journal | vauthors = Simpson JC, Wellenreuther R, Poustka A, Pepperkok R, Wiemann S | title = Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing | journal = EMBO Reports | volume = 1 | issue = 3 | pages = 287–92 | date = Sep 2000 | pmid = 11256614 | pmc = 1083732 | doi = 10.1093/embo-reports/kvd058 }}
* {{cite journal | vauthors = Suzuki Y, Yamashita R, Shirota M, Sakakibara Y, Chiba J, Mizushima-Sugano J, Nakai K, Sugano S | title = Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions | journal = Genome Research | volume = 14 | issue = 9 | pages = 1711–8 | date = Sep 2004 | pmid = 15342556 | pmc = 515316 | doi = 10.1101/gr.2435604 }}
* {{cite journal | vauthors = Wiemann S, Arlt D, Huber W, Wellenreuther R, Schleeger S, Mehrle A, Bechtel S, Sauermann M, Korf U, Pepperkok R, Sültmann H, Poustka A | title = From ORFeome to biology: a functional genomics pipeline | journal = Genome Research | volume = 14 | issue = 10B | pages = 2136–44 | date = Oct 2004 | pmid = 15489336 | pmc = 528930 | doi = 10.1101/gr.2576704 }}
* {{cite journal | vauthors = Mehrle A, Rosenfelder H, Schupp I, del Val C, Arlt D, Hahne F, Bechtel S, Simpson J, Hofmann O, Hide W, Glatting KH, Huber W, Pepperkok R, Poustka A, Wiemann S | title = The LIFEdb database in 2006 | journal = Nucleic Acids Research | volume = 34 | issue = Database issue | pages = D415-8 | date = Jan 2006 | pmid = 16381901 | pmc = 1347501 | doi = 10.1093/nar/gkj139 }}
* {{cite journal | vauthors = Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D | title = Large-scale mapping of human protein-protein interactions by mass spectrometry | journal = Molecular Systems Biology | volume = 3 | issue = 1 | pages = 89 | year = 2007 | pmid = 17353931 | pmc = 1847948 | doi = 10.1038/msb4100134 }}
{{refend}}
{{refend}}


{{protein-stub}}
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Latest revision as of 13:36, 31 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
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HIG1 domain family member 1A (HIGD1A), also known as hypoglycemia/hypoxia inducible mitochondrial protein1-a (HIMP1-a) and hypoxia induced gene 1 (HIG1), is a protein that in humans is encoded by the HIGD1A gene on chromosome 3.[1][2][3][4] This protein promotes mitochondrial homeostasis and survival of cells under stress and is involved in inflammatory and hypoxia-related diseases, including atherosclerosis, ischemic heart disease, and Alzheimer’s disease, as well as cancer.[4][5][6][7]

Structure

The protein encoded by this gene is 10.4 kDa mitochondrial inner membrane protein with two transmembrane domains at the N- and C-terminals.[5][6] These two domains are arranged such that the N- and C-terminals face outward into the intermembrane space while the rest of the protein loops inside the matrix. Though the N-terminal domain is not necessary to direct the localization of HIGD1A, it is required for the survival of the protein.

The gene HIGD1A is an isoform of HIMP1-b via alternative splicing.[5]

Function

HIGD1A primarily functions in mitochondrial homeostasis and, thus, cell survival when under conditions of stress, such as hypoxia and glucose deprivation. For instance, HIGD1A promotes survival of pancreatic α and β cells under stress.[4][5] HIGD1A has also been found in other parts of the brain, heart, liver, and kidney, where it enhances the survival of these organs.[4][7] In macrophages, HIGD1A prevents apoptosis by inhibiting cytochrome C release and caspase activity.[5][6]

HIGD1A is also involved in mitochondrial fusion by regulating OPA1 activity. Its inhibition of the cleavage of OPA1 preserves mitochondrial membrane potential, protects against apoptosis, and maintains ATP levels. Its role in mitochondrial fusion also influences downstream processes such as mtDNA synthesis, cell growth, and cristae organization.[4]

In addition, HIGD1A helps preserve mitochondrial function by regulating mitochondrial γ-secretase activity under hypoxic conditions.[4][7] In the absence of HIGD1A, γ-secretase contributes to the accumulation of amyloid beta in the mitochondria, leading to increased ROS production, mitochondrial dysfunction, and eventually, cell death.[7]

While HIGD1A predominantly contributes to cell survival, it can also promote apoptosis in neurons during the early developmental stages of the central nervous system.[6]

Clinical significance

Since HIGD1A promotes cell survival under hypoxia, the protein protects organs like the heart and brain from hypoxia-related diseases.[5] In particular, HIGD1A localization to the nucleus correlates with the severity of stress in ischemic heart disease, hypoxic-ischemic encephalopathy, and cancer, and thus may serve as a biomarker for these diseases.[6] Moreover, HIGD1A is involved in inflammatory diseases, such as atherosclerosis and rheumatoid arthritis, through its role in macrophage survival.[5] Similarly, HIGD1A could become a key target for treating Alzheimer’s disease by inhibiting γ-secretase, and by extension, amyloid beta production. Notably, HIGD1A inhibits γ-secretase without interfering with Notch cleavage, thus minimizing detrimental side effects from targeting this protein.[7]

Interactions

HIGD1A is known to interact with:

References

  1. ↑ Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z (Oct 2000). "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells". Genome Research. 10 (10): 1546–60. doi:10.1101/gr.140200. PMC 310934. PMID 11042152.
  2. ↑ Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Böcher M, Blöcker H, Bauersachs S, Blum H, Lauber J, Düsterhöft A, Beyer A, Köhrer K, Strack N, Mewes HW, Ottenwälder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A (Mar 2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Research. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
  3. ↑ "Entrez Gene: HIGD1A HIG1 domain family, member 1A".
  4. ↑ 4.0 4.1 4.2 4.3 4.4 4.5 4.6 An HJ, Cho G, Lee JO, Paik SG, Kim YS, Lee H (Aug 2013). "Higd-1a interacts with Opa1 and is required for the morphological and functional integrity of mitochondria". Proceedings of the National Academy of Sciences of the United States of America. 110 (32): 13014–9. doi:10.1073/pnas.1307170110. PMC 3740888. PMID 23878241.
  5. ↑ 5.0 5.1 5.2 5.3 5.4 5.5 5.6 An HJ, Shin H, Jo SG, Kim YJ, Lee JO, Paik SG, Lee H (Dec 2011). "The survival effect of mitochondrial Higd-1a is associated with suppression of cytochrome C release and prevention of caspase activation". Biochimica et Biophysica Acta. 1813 (12): 2088–98. doi:10.1016/j.bbamcr.2011.07.017. PMID 21856340.
  6. ↑ 6.0 6.1 6.2 6.3 6.4 6.5 Ameri K, Rajah AM, Nguyen V, Sanders TA, Jahangiri A, Delay M, Donne M, Choi HJ, Tormos KV, Yeghiazarians Y, Jeffrey SS, Rinaudo PF, Rowitch DH, Aghi M, Maltepe E (2013). "Nuclear localization of the mitochondrial factor HIGD1A during metabolic stress". PLOS ONE. 8 (4): e62758. doi:10.1371/journal.pone.0062758. PMC 3639984. PMID 23646141.
  7. ↑ 7.0 7.1 7.2 7.3 7.4 7.5 Hayashi H, Nakagami H, Takeichi M, Shimamura M, Koibuchi N, Oiki E, Sato N, Koriyama H, Mori M, Gerardo Araujo R, Maeda A, Morishita R, Tamai K, Kaneda Y (Jun 2012). "HIG1, a novel regulator of mitochondrial γ-secretase, maintains normal mitochondrial function". FASEB Journal. 26 (6): 2306–17. doi:10.1096/fj.11-196063. PMID 22355194.

Further reading

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