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Purely Peptides
Research Catalog

Compound monograph

Humanin (HN)

Humanin is a 24-residue peptide encoded within the mitochondrial 16S ribosomal RNA gene, and the first-described member of the mitochondrial-derived peptide family.

Published: 2026-09-16Literature/identifier verification: 2026-09-15
Also known asHN
Mitochondrial-derived peptides

01

Identity & nomenclature

Humanin is a 24-residue peptide encoded within the mitochondrial 16S ribosomal RNA gene, and the first-described member of the mitochondrial-derived peptide family.

The humanin coding sequence lies within MT-RNR2, the mitochondrial 16S rRNA gene. A mitochondrial coding locus does not establish where translation occurs. This record specifies the 24-residue standard-code form; a mitochondrial-code prediction is a distinct sequence. Nuclear humanin-like loci further complicate assigning endogenous origin. HNG carries S14G, and HNGF6A carries F6A and S14G. N-formyl humanin is a distinct chemical form. MTRNR2L gene names denote nuclear loci and are not peptide aliases.

Canonical name: Humanin.

Declared aliases and development codes: HN.

02

Molecular properties

Molecular formulaC119H204N34O32S2
Molecular mass2687.3 Da
CAS Registry Number330936-69-1
PubChem CID16131438
UNIIH975EUX36G
One-letter sequenceMAPRGFSCLLLLTSEIDLPVKRRA
Terminal groupsFree N-terminus; Free C-terminal carboxyl

Twenty-four residues with free termini and one cysteine at position 8. This record specifies the standard-code form; it does not identify the mature product of mitochondrial translation.

03

Structural characteristics

Functional expression screening identified humanin cDNA, and the corresponding peptide was detected in culture medium. Humanin binds BAX, an intracellular partner, and limits its association with isolated mitochondria. Cell-binding and reconstituted-protein experiments implicate CNTFR-alpha, WSX-1 and gp130 in a separate cell-surface complex. A comparison of unmodified and N-formyl humanin measured receptor binding and activation; the chemical forms must be distinguished. Analysis of synonymous codon bias reports strong bias and conservation for humanin, consistent with amino-acid sequence constraint within the rRNA gene.

Terminal features: Free N-terminus, Free C-terminal carboxyl.

04

Molecular targets & mechanisms

05

Analytical considerations

Fragments spanning positions 14 and 16 and the C-terminal RRA segment distinguish the recorded sequence from related forms. A short shared fragment or immunoassay signal cannot identify the intact 24-mer or its transcript of origin. One cysteine permits an intermolecular disulfide but no intramolecular disulfide. Routine intact mass does not distinguish leucine from isoleucine or establish stereochemistry.

Disagreements and mix-ups

Points where sources disagree about this compound's identity, or where a name or form is easily confused with another, as noted in this record. The discrepancy register quotes the passage for each one.

What the studies reported

Each finding describes one cited study in its stated model. These observations are specific to that study and do not establish effects in other settings.

Cell and tissue studies

  • Bax and isolated-mitochondria binding assays

    Guo et al. reported that humanin blocked Bax association with isolated mitochondria and suppressed cytochrome c release in vitro.

    Reference [2]

  • Cellular Bax translocation assay

    Guo et al. observed that reducing humanin expression with small interfering RNAs sensitized cultured cells to Bax and increased Bax translocation to membranes.

    Reference [2]

  • Reconstituted CNTFR, WSX-1 and gp130 binding assay

    Hashimoto et al. observed humanin-induced hetero-oligomerization of CNTFR, WSX-1 and gp130 in reconstituted binding assays in vitro.

    Reference [3]

  • CHO cells expressing human FPRL1 or FPRL2

    Harada et al. reported that humanin suppressed forskolin-induced cAMP production in CHO cells expressing human FPRL1 or human FPRL2.

    Reference [4]

  • CHO cells expressing human FPRL1

    Harada et al. measured a humanin EC50 of 3.5 nM in CHO cells expressing human FPRL1.

    Reference [4]

Computational studies

  • Vertebrate humanin coding-sequence analysis

    Gruschus et al. found strong synonymous codon bias and sequence conservation for humanin in an analysis of vertebrate coding sequences.

    Reference [6]

06

Verified bibliography

Cited studies by type

The 7 papers this record cites, counted by the kind of work each reports. A count is the size of this record's selection, not of the research that exists, and says nothing about results, safety, effectiveness or approval.

A paper can report more than one kind of work. Each count opens those papers in the bibliography. Compare every record on the Evidence Map.

  1. Reference 1

    A rescue factor abolishing neuronal cell death by a wide spectrum of familial Alzheimer's disease genes and Abeta.

    Hashimoto Y, Niikura T, Tajima H, Yasukawa T, Sudo H, Ito Y, Kita Y, Kawasumi M, Kouyama K, Doyu M, Sobue G, Koide T, Tsuji S, Lang J, Kurokawa K, Nishimoto I

    Proceedings of the National Academy of Sciences of the United States of America · 2001-05-22 · Journal Article

    current
    PMID 11371646PMC33469DOI 10.1073/pnas.101133498Humanin (HN)

  2. Reference 2

    Humanin peptide suppresses apoptosis by interfering with Bax activation.

    Guo B, Zhai D, Cabezas E, Welsh K, Nouraini S, Satterthwait AC, Reed JC

    Nature · 2003-05-04 · Journal Article

    current
    PMID 12732850DOI 10.1038/nature01627Humanin (HN)

  3. Reference 3

    Humanin inhibits neuronal cell death by interacting with a cytokine receptor complex or complexes involving CNTF receptor alpha/WSX-1/gp130.

    Hashimoto Y, Kurita M, Aiso S, Nishimoto I, Matsuoka M

    Molecular biology of the cell · 2009-04-22 · Journal Article

    current
    PMID 19386761PMC2695794DOI 10.1091/mbc.e09-02-0168Humanin (HN)HNG ([Gly14]-Humanin)

  4. Reference 4

    N-Formylated humanin activates both formyl peptide receptor-like 1 and 2.

    Harada M, Habata Y, Hosoya M, Nishi K, Fujii R, Kobayashi M, Hinuma S

    Biochemical and biophysical research communications · 2004-11-05 · Journal Article

    current
    PMID 15465011DOI 10.1016/j.bbrc.2004.09.046Humanin (HN)

  5. Reference 5

    Evidence for potential functionality of nuclearly-encoded humanin isoforms.

    Bodzioch M, Lapicka-Bodzioch K, Zapala B, Kamysz W, Kiec-Wilk B, Dembinska-Kiec A

    Genomics · 2009-05-27 · Journal Article

    current
    PMID 19477263DOI 10.1016/j.ygeno.2009.05.006Humanin (HN)

  6. Reference 6

    Evidence of natural selection in the mitochondrial-derived peptides humanin and SHLP6.

    Gruschus JM, Morris DL, Tjandra N

    Scientific reports · 2023-08-29 · Journal Article

    current
    PMID 37644144PMC10465549DOI 10.1038/s41598-023-41053-0Humanin (HN)SHLP2SHLP3SHLP6

  7. Reference 7

    The mitochondrial-derived peptide MOTS-c promotes metabolic homeostasis and reduces obesity and insulin resistance.

    Lee C, Zeng J, Drew BG, Sallam T, Martin-Montalvo A, Wan J, Kim SJ, Mehta H, Hevener AL, de Cabo R, Cohen P

    Cell metabolism · 2015-03-03 · Journal Article

    current
    PMID 25738459PMC4350682DOI 10.1016/j.cmet.2015.02.009MOTS-cHumanin (HN)SHLP2SHLP3SHLP6AMP-activated protein kinase

Study models of these references

What kind of experiment each cited paper reports, taken from its abstract unless marked. Not a summary of results.

ReferenceStudy models
Hashimoto Y et al. 2001Study models reported: in vitro · from the abstractCorrection published: Proc Natl Acad Sci U S A 2001 Oct 23;98(22):12854
Guo B et al. 2003Study models reported: in vitro · from the abstract
Hashimoto Y et al. 2009Study models reported: in vitro · from the abstract
Harada M et al. 2004Study models reported: in vitro · from the abstract
Bodzioch M et al. 2009Study models reported: in vitro · from the abstract
Gruschus JM et al. 2023Computational analysis
Lee C et al. 2015Study models reported: in vitro; animal (mouse) · from the full text

Compare

Record history

Published 2026-09-16.

No changes to this record's content have been recorded since publication.

Each entry names the parts of this record that changed on that date. Changes to links between records and to catalogue links are not listed. This history covers the tracked record fields; study findings are not listed here.

Cite this record: Purely Peptides Research Library. Humanin (HN). Published 2026-09-16. https://purelypeptides.org/research/compounds/humanin/

10

Methodology & citation verification

Reference identity is checked against official PubMed metadata. Local deterministic receipts bind each normalized title and canonical metadata record to its verification date. Scientific values remain absent when an authoritative source has not been verified.

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