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{{Infobox_gene}}
{{PBB_Controls
'''Growth hormone-inducible transmembrane protein''' (GHITM), also known as transmembrane BAX inhibitor motif containing protein 5 (TMBIM5), is a [[protein]] that in humans is encoded by the ''GHITM'' [[gene]] on chromosome 10.<ref name="pmid8619474">{{cite journal | vauthors = Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA | title = A "double adaptor" method for improved shotgun library construction | journal = Analytical Biochemistry | volume = 236 | issue = 1 | pages = 107–13 | date = Apr 1996 | pmid = 8619474 | pmc =  | doi = 10.1006/abio.1996.0138 }}</ref><ref name="pmid9110174">{{cite journal | vauthors = Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA | title = Large-scale concatenation cDNA sequencing | journal = Genome Research | volume = 7 | issue = 4 | pages = 353–8 | date = Apr 1997 | pmid = 9110174 | pmc = 139146 | doi = 10.1101/gr.7.4.353 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: GHITM growth hormone inducible transmembrane protein| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27069| accessdate = }}</ref> It is a member of the [[Bcl-2-associated X protein|BAX]] [[enzyme inhibitor|inhibitor]] motif containing (TMBIM) family and [[subcellular localization|localize]]s to the [[inner mitochondrial membrane]] (IMM), as well as the [[endoplasmic reticulum]] (ER), where it plays a role in [[apoptosis]] through mediating [[mitochondria]]l morphology and [[cytochrome c]] release.<ref name="pmid18417609">{{cite journal | vauthors = Oka T, Sayano T, Tamai S, Yokota S, Kato H, Fujii G, Mihara K | title = Identification of a novel protein MICS1 that is involved in maintenance of mitochondrial morphology and apoptotic release of cytochrome c | journal = Molecular Biology of the Cell | volume = 19 | issue = 6 | pages = 2597–608 | date = Jun 2008 | pmid = 18417609 | doi = 10.1091/mbc.E07-12-1205 | pmc=2397309}}</ref><ref name="pmid25764978">{{cite journal | vauthors = Lisak DA, Schacht T, Enders V, Habicht J, Kiviluoto S, Schneider J, Henke N, Bultynck G, Methner A | title = The transmembrane Bax inhibitor motif (TMBIM) containing protein family: Tissue expression, intracellular localization and effects on the ER CA(2+)-filling state | journal = Biochimica et Biophysica Acta | volume = 1853 | issue = 9 | pages = 2104–14 | date = Sep 2015 | pmid = 25764978 | doi = 10.1016/j.bbamcr.2015.03.002 }}</ref> Through its apoptotic function, GHITM may be involved in [[tumor]] [[metastasis]] and [[innate]] [[antiviral]] responses.<ref name="pmid18440869">{{cite journal | vauthors = Zhou J, Zhu T, Hu C, Li H, Chen G, Xu G, Wang S, Zhou J, Ma D | title = Comparative genomics and function analysis on BI1 family | journal = Computational Biology and Chemistry | volume = 32 | issue = 3 | pages = 159–62 | date = Jun 2008 | pmid = 18440869 | doi = 10.1016/j.compbiolchem.2008.01.002 }}</ref><ref name="pmid21903422">{{cite journal | vauthors = Li S, Wang L, Berman M, Kong YY, Dorf ME | title = Mapping a dynamic innate immunity protein interaction network regulating type I interferon production | journal = Immunity | volume = 35 | issue = 3 | pages = 426–40 | date = Sep 2011 | pmid = 21903422 | doi = 10.1016/j.immuni.2011.06.014 | pmc=3253658}}</ref>
| update_page = yes
| require_manual_inspection = no
| 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. -->
==Structure==
{{GNF_Protein_box
| image =
| image_source =
| PDB =  
| Name = Growth hormone inducible transmembrane protein
| HGNCid = 17281
| Symbol = GHITM
| AltSymbols =; DERP2; DKFZp566C0746; FLJ26584; HSPC282; My021; PTD010; TMBIM5
| OMIM = 
| ECnumber = 
| Homologene = 8667
| MGIid = 1913342
| GeneAtlas_image1 = PBB_GE_GHITM_209248_at_tn.png
| GeneAtlas_image2 = PBB_GE_GHITM_209249_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003674 |text = molecular_function}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0008150 |text = biological_process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 27069
    | Hs_Ensembl = ENSG00000165678
    | Hs_RefseqProtein = NP_055209
    | Hs_RefseqmRNA = NM_014394
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 10
    | Hs_GenLoc_start = 85889176
    | Hs_GenLoc_end = 85903291
    | Hs_Uniprot = Q9H3K2
    | Mm_EntrezGene = 66092
    | Mm_Ensembl = ENSMUSG00000041028
    | Mm_RefseqmRNA = NM_078478
    | Mm_RefseqProtein = NP_510963
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 14
    | Mm_GenLoc_start = 36032557
    | Mm_GenLoc_end = 36047038
    | Mm_Uniprot = 
  }}
}}
'''Growth hormone inducible transmembrane protein''', also known as '''GHITM''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GHITM growth hormone inducible transmembrane protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27069| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
This gene encodes a 37 kDa protein which putatively contains six to eight [[transmembrane]] [[domain (biology)|domains]]. As a member of the TMBIM family, GHITM shares a transmembrane BAX [[Enzyme inhibitor|inhibitor]] motif, a semi-hydrophobic transmembrane domain, and similar tertiary structure with the other five members. However, unlike the other members, GHITM possesses a unique [[acidic]] (D) instead of a [[basic (chemistry)|basic]] (H or R) residue near its second transmembrane domain, as well as an additional transmembrane domain that, after [[protein cleavage|cleavage]] behind [[amino acid|residue]] 57 (SREY|A), signals for localization to the IMM.<ref name="pmid18417609"/><ref name="pmid25764978"/><ref name="pmid18440869"/> Nonetheless, it is possible that cleavage at different sites (XXRR-like motif (LAAR) in the [[N-terminal]] and a KKXX-like motif (GNRK) in the [[C-terminal]]) or [[alternative splicing]] may account for the protein’s observed localization to the ER.<ref name="pmid25764978"/><ref name="pmid18440869"/>
{{PBB_Summary
| section_title =  
| summary_text =
}}


==References==
== Function ==
{{reflist|2}}
 
==Further reading==
GHITM is a mitochondrial protein and a member of the TMBIM family and BAX inhibitor-1 (BI1) superfamily.<ref name="pmid18417609"/><ref name="pmid25764978"/> It is ubiquitously expressed but is especially abundant in the [[brain]], [[heart]], [[liver]], [[kidney]], and [[skeletal muscle]] and scarce in the [[intestine]]s and [[thymus]].<ref name="pmid25764978"/> This protein localizes specifically to the IMM, where it regulates apoptosis through two separate processes: (1) the BAX-independent management of mitochondrial morphology and (2) the release of cytochrome c. In the first process, GHITM maintains [[cristae]] organization, and its downregulation results in mitochondrial [[fragmentation (cell biology)|fragmentation]], possibly through inducing fusing of the cristae structures, thus leading to the release of proapoptotic proteins such as cytochrome c, [[Second mitochondria-derived activator of caspases|Smac]], and [[HtrA serine peptidase 2|Htra2]]. Meanwhile, in the second process, GHITM is responsible for cross-linking cytochrome c to the IMM, and upregulation of GHITM is associated with delayed cytochrome c release, regardless of [[outer mitochondrial membrane]] [[semipermeable membrane|permeabilization]]. Thus, GHITM controls the release of [[cytochrome c]] from the mitochondria and can potentially interfere with the apoptotic process to promote cell survival.<ref name="pmid18417609"/><ref name="pmid25764978"/> Moreover, GHITM may further plays a role in apoptosis through maintaining [[calcium ion]] [[homeostasis]] in the ER. However, while overexpression of the other TMBIM proteins exhibit antiapoptotic effects by decreasing calcium ion concentrations, and thus preventing mitochondrial calcium ion overload, [[depolarization]], [[Adenosine triphosphate|ATP]] loss, [[reactive oxygen species]] production, cytochrome c release, and ultimately, cell death, overexpression of GHITM produces the opposite effect.<ref name="pmid25764978"/>
{{refbegin | 2}}
 
{{PBB_Further_reading
== Clinical significance ==
| 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=  }}
GHITM may be involved in tumor metastasis through its interactions with the [[Bcl-2]] family proteins to regulate apoptosis.<ref name="pmid18440869"/><ref name="pmid21903422"/> Its role as an apoptotic regulator may also associate it with innate antiviral responses.<ref name="pmid21903422"/> Overexpression of GHITM has also been observed to speed up the [[ageing]] process in [[HIV]] infected patients.<ref>{{cite journal | vauthors = Moni MA, Liò P | title = Network-based analysis of comorbidities risk during an infection: SARS and HIV case studies | journal = BMC Bioinformatics | volume = 15 | pages = 333 | date = 24 October 2014 | pmid = 25344230 | doi = 10.1186/1471-2105-15-333 | pmc=4363349}}</ref>
*{{cite journal | author=Andersson B, Wentland MA, Ricafrente JY, ''et al.'' |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107-13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 }}
 
*{{cite journal | author=Yu W, Andersson B, Worley KC, ''et al.'' |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353-8 |year= 1997 |pmid= 9110174 |doi= }}
== Interactions ==
*{{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= }}
 
*{{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= }}
GHITM has been shown to [[protein-protein interaction|interact]] with [[cytochrome c]].<ref name="pmid18417609"/>
*{{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 }}
 
*{{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 }}
== References ==
*{{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 }}
{{reflist|33em}}
*{{cite journal  | author=Clark HF, Gurney AL, Abaya E, ''et al.'' |title=The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. |journal=Genome Res. |volume=13 |issue= 10 |pages= 2265-70 |year= 2003 |pmid= 12975309 |doi= 10.1101/gr.1293003 }}
 
*{{cite journal  | author=Deloukas P, Earthrowl ME, Grafham DV, ''et al.'' |title=The DNA sequence and comparative analysis of human chromosome 10. |journal=Nature |volume=429 |issue= 6990 |pages= 375-81 |year= 2004 |pmid= 15164054 |doi= 10.1038/nature02462 }}
== Further reading ==
*{{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 }}
{{refbegin|33em}}
*{{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 = 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=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 = 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 | 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 = 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 }}
* {{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 = 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 }}
{{refend}}
{{refend}}


{{protein-stub}}
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Latest revision as of 08:44, 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
View/Edit Human

Growth hormone-inducible transmembrane protein (GHITM), also known as transmembrane BAX inhibitor motif containing protein 5 (TMBIM5), is a protein that in humans is encoded by the GHITM gene on chromosome 10.[1][2][3] It is a member of the BAX inhibitor motif containing (TMBIM) family and localizes to the inner mitochondrial membrane (IMM), as well as the endoplasmic reticulum (ER), where it plays a role in apoptosis through mediating mitochondrial morphology and cytochrome c release.[4][5] Through its apoptotic function, GHITM may be involved in tumor metastasis and innate antiviral responses.[6][7]

Structure

This gene encodes a 37 kDa protein which putatively contains six to eight transmembrane domains. As a member of the TMBIM family, GHITM shares a transmembrane BAX inhibitor motif, a semi-hydrophobic transmembrane domain, and similar tertiary structure with the other five members. However, unlike the other members, GHITM possesses a unique acidic (D) instead of a basic (H or R) residue near its second transmembrane domain, as well as an additional transmembrane domain that, after cleavage behind residue 57 (SREY|A), signals for localization to the IMM.[4][5][6] Nonetheless, it is possible that cleavage at different sites (XXRR-like motif (LAAR) in the N-terminal and a KKXX-like motif (GNRK) in the C-terminal) or alternative splicing may account for the protein’s observed localization to the ER.[5][6]

Function

GHITM is a mitochondrial protein and a member of the TMBIM family and BAX inhibitor-1 (BI1) superfamily.[4][5] It is ubiquitously expressed but is especially abundant in the brain, heart, liver, kidney, and skeletal muscle and scarce in the intestines and thymus.[5] This protein localizes specifically to the IMM, where it regulates apoptosis through two separate processes: (1) the BAX-independent management of mitochondrial morphology and (2) the release of cytochrome c. In the first process, GHITM maintains cristae organization, and its downregulation results in mitochondrial fragmentation, possibly through inducing fusing of the cristae structures, thus leading to the release of proapoptotic proteins such as cytochrome c, Smac, and Htra2. Meanwhile, in the second process, GHITM is responsible for cross-linking cytochrome c to the IMM, and upregulation of GHITM is associated with delayed cytochrome c release, regardless of outer mitochondrial membrane permeabilization. Thus, GHITM controls the release of cytochrome c from the mitochondria and can potentially interfere with the apoptotic process to promote cell survival.[4][5] Moreover, GHITM may further plays a role in apoptosis through maintaining calcium ion homeostasis in the ER. However, while overexpression of the other TMBIM proteins exhibit antiapoptotic effects by decreasing calcium ion concentrations, and thus preventing mitochondrial calcium ion overload, depolarization, ATP loss, reactive oxygen species production, cytochrome c release, and ultimately, cell death, overexpression of GHITM produces the opposite effect.[5]

Clinical significance

GHITM may be involved in tumor metastasis through its interactions with the Bcl-2 family proteins to regulate apoptosis.[6][7] Its role as an apoptotic regulator may also associate it with innate antiviral responses.[7] Overexpression of GHITM has also been observed to speed up the ageing process in HIV infected patients.[8]

Interactions

GHITM has been shown to interact with cytochrome c.[4]

References

  1. ↑ Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (Apr 1996). "A "double adaptor" method for improved shotgun library construction". Analytical Biochemistry. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
  2. ↑ Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA (Apr 1997). "Large-scale concatenation cDNA sequencing". Genome Research. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
  3. ↑ "Entrez Gene: GHITM growth hormone inducible transmembrane protein".
  4. ↑ 4.0 4.1 4.2 4.3 4.4 Oka T, Sayano T, Tamai S, Yokota S, Kato H, Fujii G, Mihara K (Jun 2008). "Identification of a novel protein MICS1 that is involved in maintenance of mitochondrial morphology and apoptotic release of cytochrome c". Molecular Biology of the Cell. 19 (6): 2597–608. doi:10.1091/mbc.E07-12-1205. PMC 2397309. PMID 18417609.
  5. ↑ 5.0 5.1 5.2 5.3 5.4 5.5 5.6 Lisak DA, Schacht T, Enders V, Habicht J, Kiviluoto S, Schneider J, Henke N, Bultynck G, Methner A (Sep 2015). "The transmembrane Bax inhibitor motif (TMBIM) containing protein family: Tissue expression, intracellular localization and effects on the ER CA(2+)-filling state". Biochimica et Biophysica Acta. 1853 (9): 2104–14. doi:10.1016/j.bbamcr.2015.03.002. PMID 25764978.
  6. ↑ 6.0 6.1 6.2 6.3 Zhou J, Zhu T, Hu C, Li H, Chen G, Xu G, Wang S, Zhou J, Ma D (Jun 2008). "Comparative genomics and function analysis on BI1 family". Computational Biology and Chemistry. 32 (3): 159–62. doi:10.1016/j.compbiolchem.2008.01.002. PMID 18440869.
  7. ↑ 7.0 7.1 7.2 Li S, Wang L, Berman M, Kong YY, Dorf ME (Sep 2011). "Mapping a dynamic innate immunity protein interaction network regulating type I interferon production". Immunity. 35 (3): 426–40. doi:10.1016/j.immuni.2011.06.014. PMC 3253658. PMID 21903422.
  8. ↑ Moni MA, Liò P (24 October 2014). "Network-based analysis of comorbidities risk during an infection: SARS and HIV case studies". BMC Bioinformatics. 15: 333. doi:10.1186/1471-2105-15-333. PMC 4363349. PMID 25344230.

Further reading

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