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Entry version 113 (25 May 2022)
Sequence version 1 (01 Mar 2003)
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Protein

Humanin

Gene

MT-RNR2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Plays a role as a neuroprotective factor (PubMed:11371646, PubMed:11717357, PubMed:12860203, PubMed:19386761, PubMed:12787071, PubMed:12154011).

Protects against neuronal cell death induced by multiple different familial Alzheimer disease genes and amyloid-beta proteins in Alzheimer disease (PubMed:11371646, PubMed:11717357, PubMed:12860203, PubMed:19386761, PubMed:12787071, PubMed:12154011).

Mediates its neuroprotective effect by interacting with a receptor complex composed of IL6ST/GP130, IL27RA/WSX1 and CNTFR (PubMed:19386761).

Also acts as a ligand for G-protein coupled receptors FPR2/FPRL1 and FPR3/FPRL2 (PubMed:15465011).

Inhibits amyloid-beta protein 40 fibril formation (PubMed:27349871).

Also inhibits amyloid-beta protein 42 fibril formation (PubMed:28282805).

Suppresses apoptosis by binding to BAX and preventing the translocation of BAX from the cytosol to mitochondria (PubMed:12732850, PubMed:26990160).

Also suppresses apoptosis by binding to BID and inhibiting the interaction of BID with BAX and BAK which prevents oligomerization of BAX and BAK and suppresses release of apoptogenic proteins from mitochondria (PubMed:15661737).

Forms fibers with BAX and also with BID, inducing BAX and BID conformational changes and sequestering them into the fibers which prevents their activation (PubMed:31690630, PubMed:33106313).

Can also suppress apoptosis by interacting with BIM isoform BimEL, inhibiting BimEL-induced activation of BAX, blocking oligomerization of BAX and BAK, and preventing release of apoptogenic proteins from mitochondria (PubMed:15661735).

Plays a role in up-regulation of anti-apoptotic protein BIRC6/APOLLON, leading to inhibition of neuronal cell death (PubMed:25138702).

Binds to IGFBP3 and specifically blocks IGFBP3-induced cell death (PubMed:14561895, PubMed:26216267).

Competes with importin KPNB1 for binding to IGFBP3 which is likely to block IGFBP3 nuclear import (PubMed:26216267).

Induces chemotaxis of mononuclear phagocytes via FPR2/FPRL1 (PubMed:15153530).

Reduces aggregation and fibrillary formation by suppressing the effect of APP on mononuclear phagocytes and acts by competitively inhibiting the access of FPR2 to APP (PubMed:15153530).

Protects retinal pigment epithelium (RPE) cells against oxidative stress-induced and endoplasmic reticulum (ER) stress-induced apoptosis (PubMed:26990160, PubMed:27783653).

Promotes mitochondrial biogenesis in RPE cells following oxidative stress and promotes STAT3 phosphorylation which leads to inhibition of CASP3 release (PubMed:26990160).

Also reduces CASP4 levels in RPE cells, suppresses ER stress-induced mitochondrial superoxide production and plays a role in up-regulation of mitochondrial glutathione (PubMed:27783653).

Reduces testicular hormone deprivation-induced apoptosis of germ cells at the nonandrogen-sensitive stages of the seminiferous epithelium cycle (PubMed:19952275).

Protects endothelial cells against free fatty acid-induced inflammation by suppressing oxidative stress, reducing expression of TXNIP and inhibiting activation of the NLRP3 inflammasome which inhibits expression of pro-inflammatory cytokines IL1B and IL18 (PubMed:32923762).

Protects against high glucose-induced endothelial cell dysfunction by mediating activation of ERK5 which leads to increased expression of transcription factor KLF2 and prevents monocyte adhesion to endothelial cells (PubMed:30029058).

Inhibits the inflammatory response in astrocytes (PubMed:23277413).

Increases the expression of PPARGC1A/PGC1A in pancreatic beta cells which promotes mitochondrial biogenesis (PubMed:29432738).

Increases insulin sensitivity (PubMed:19623253).

26 Publications

Caution

The humanin peptide described here has been shown to be biologically active but is the product of a mitochondrial gene, MT-RNR2 (PubMed:12009529). If translation of the mRNA occurs in the mitochondrion rather than in the cytoplasm, then the usage of the mitochondrial genetic code would lead to the production of a shorter peptide lacking the last three C-terminal residues. The mechanisms allowing the production and the secretion of humanin remain unclear. The possibility exists that the physiologically active humanin peptide is encoded by one of the related genes present in the nuclear genome (PubMed:19477263).2 Publications

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processApoptosis

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

More...
PathwayCommonsi
Q8IVG9

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-416476, G alpha (q) signalling events
R-HSA-418594, G alpha (i) signalling events
R-HSA-444473, Formyl peptide receptors bind formyl peptides and many other ligands

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...
SignaLinki
Q8IVG9

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Humanin1 Publication
Alternative name(s):
Humanin mitochondrial1 Publication
Short name:
HNM1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:MT-RNR2Imported
Synonyms:HN1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates if the gene coding for the protein originates from the hydrogenosome, the mitochondrion, the nucleomorph, different plastids or a plasmid. The absence of this section means that the gene is located in one of the main chromosomal element(s).<p><a href='/help/encoded_on' target='_top'>More...</a></p>Encoded oniMitochondrion
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Mitochondrion

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:7471, MT-RNR2

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
606120, gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q8IVG9

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasm, Flagellum, Mitochondrion, Nucleus, Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi1 – 6Missing : No effect on binding to BAX. 1 Publication6
Mutagenesisi1 – 3Missing : Abolishes neuroprotective activity. 1 Publication3
Mutagenesisi1 – 2Missing : No effect on neuroprotective activity. 1 Publication2
Mutagenesisi3P → A: Abolishes neuroprotective activity. 2 Publications1
Mutagenesisi4 – 6RGF → AGA: Potentiates neuroprotective activity. 1 Publication3
Mutagenesisi6F → A: Abolishes binding to IGFBP3 and increases insulin sensitivity. 2 Publications1
Mutagenesisi7S → A: Abolishes neuroprotective activity and dimerization. No effect on insulin sensitivity. 3 Publications1
Mutagenesisi8C → A: Abolishes neuroprotective activity. Formation of short irregularly shaped fibers with BAX with fibers showing non-uniform diameters. Formation of thin irregularly kinked fibers with BID. 5 Publications1
Mutagenesisi8C → D, E, F, G, I, L, M, N, Q, S, T, V, W or Y: Abolishes neuroprotective activity. 2 Publications1
Mutagenesisi8C → H: Significantly reduces neuroprotective activity. 2 Publications1
Mutagenesisi8C → K or R: No effect on neuroprotective activity. 2 Publications1
Mutagenesisi8C → P: Abolishes neuroprotective activity and interaction with BAX and BID. Abolishes BID-induced caspase activation and mitochondrial release of SMAC. Greatly reduced interaction with BIM. Abolishes BIM-induced caspase activation and apoptosis. 4 Publications1
Mutagenesisi9L → A: Abolishes neuroprotective activity and dimerization. 3 Publications1
Mutagenesisi9L → R: Abolishes binding to BAX. Abolishes secretion. 4 Publications1
Mutagenesisi10L → D: Abolishes secretion. 1 Publication1
Mutagenesisi10L → R: Abolishes secretion. 1 Publication1
Mutagenesisi11L → R: Abolishes secretion. 1 Publication1
Mutagenesisi12L → A: Abolishes neuroprotective activity. 2 Publications1
Mutagenesisi13T → A: Abolishes neuroprotective activity. 2 Publications1
Mutagenesisi14S → A, R, W, E or P: Abolishes neuroprotective activity. 3 Publications1
Mutagenesisi14S → G: Potentiates neuroprotective activity. Increased inhibition of amyloid-beta protein 40 fibril formation. Reduced levels of amyloid-beta 42 protein. Affects fiber formation with BAX with fewer fibers running in parallel. Affects fiber formation with BID with formation of shorter fibers. No effect on binding to BID or on BID-induced caspase activation and mitochondrial release of SMAC. Does not affect interaction with FPR2 or FPR3. 7 Publications1
Mutagenesisi19 – 24Missing : Abolishes neuroprotective activity. 1 Publication6
Mutagenesisi19P → A: Abolishes neuroprotective activity. 2 Publications1
Mutagenesisi19P → R: Abolishes secretion. 1 Publication1
Mutagenesisi20 – 24Missing : No effect on neuroprotective activity. 1 Publication5
Mutagenesisi20V → R: Abolishes secretion. 1 Publication1

Organism-specific databases

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
155, NON RARE IN EUROPE: Familial isolated hypertrophic cardiomyopathy

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
Q8IVG9, Tdark

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
HGNC:7471

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000441461 – 24HumaninAdd BLAST24

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q8IVG9

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q8IVG9

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q8IVG9

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in testis, seminal plasma and sperm (at protein level) (PubMed:20542501, PubMed:30920769). Higher seminal plasma levels are associated with normospermia than with oligospermia, asthenospermia or oligoasthenospermia (at protein level) (PubMed:30920769). Higher sperm levels are associated with normospermia than with asthenospermia (at protein level) (PubMed:30920769). Expressed in retinal epithelial cells (at protein level) (PubMed:26990160). Expressed in the heart, skeletal muscle, kidney and liver. Lesser but significant expression is observed in the brain and the gastrointestinal tract. Expressed in the AD brain, where it is found in some of the large intact neurons of the occipital lobes and small and round reactive glial cells in the hippocampus.6 Publications

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Levels decline with increasing age.1 Publication

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Release is regulated by intracellular mechanism. The intracellular level is regulated by TRIM11 through proteasome-mediated degradation.1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (PubMed:12787071, PubMed:12860203).

Interacts with amyloid-beta protein 42 (Abeta42); the interaction prevents Abeta42 fibril formation (PubMed:28282805).

Interacts with BAX; forms fibers with BAX which results in BAX conformational changes and sequestering of BAX into the fibers, preventing BAX activation (PubMed:12732850, PubMed:31690630).

Interacts with both full-length BID and cleaved BID p15; forms fibers with BID which results in BID conformational changes and sequestering of BID into the fibers, preventing BID activation (PubMed:15661737, PubMed:33106313).

Interacts with BIM isoform BimEL but not with BIM isoforms BimL or BimS; the interaction prevents BIM-induced apoptosis (PubMed:15661735).

Interacts with IGFBP3; competes with importin KPNB1 for binding to IGFBP3, blocking IGFBP3 nuclear import (PubMed:14561895, PubMed:19623253, PubMed:26216267).

Interacts with TRIM11 (PubMed:12670303).

Interacts with MPP8 (PubMed:23532874).

13 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
Q8IVG9, 3 interactors

Molecular INTeraction database

More...
MINTi
Q8IVG9

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

124
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

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AlphaFoldDBi
Q8IVG9

Biological Magnetic Resonance Data Bank

More...
BMRBi
Q8IVG9

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q8IVG9

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q8IVG9

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 12Sufficient to interact with BID and BIM and to suppress BID and BIM activity2 PublicationsAdd BLAST12
Regioni3 – 19Sufficient for neuroprotective activityAdd BLAST17
Regioni5 – 12Sufficient to interact with MPP81 Publication8
Regioni9 – 11Required for secretion1 Publication3
Regioni19 – 20Required for secretion1 Publication2

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Largely unstructured in aqueous solution.1 Publication

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the humanin family.Curated

Phylogenomic databases

Database for complete collections of gene phylogenies

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PhylomeDBi
Q8IVG9

Family and domain databases

Conserved Domains Database

More...
CDDi
cd20245, humanin, 1 hit

Database of protein disorder

More...
DisProti
DP02267

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR028139, Humanin

The PANTHER Classification System

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PANTHERi
PTHR33895, PTHR33895, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF15040, Humanin, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q8IVG9-1 [UniParc]FASTAAdd to basket
« Hide
        10         20 
MAPRGFSCLL LLTSEIDLPV KRRA
Length:24
Mass (Da):2,687
Last modified:March 1, 2003 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i08B9A778EC13B971
GO

<p>This subsection of the 'Sequence' section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 2686.78 Da. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AY029066 mRNA Translation: AAK50430.1
BE899497 mRNA No translation available.

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY029066 mRNA Translation: AAK50430.1
BE899497 mRNA No translation available.

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Y32NMR-A1-24[»]
2GD3NMR-A1-24[»]
5GIWNMR-X1-24[»]
AlphaFoldDBiQ8IVG9
BMRBiQ8IVG9
SMRiQ8IVG9
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

IntActiQ8IVG9, 3 interactors
MINTiQ8IVG9

PTM databases

iPTMnetiQ8IVG9
PhosphoSitePlusiQ8IVG9

Genetic variation databases

BioMutaiHGNC:7471

Proteomic databases

PRIDEiQ8IVG9

Organism-specific databases

GeneCards: human genes, protein and diseases

More...
GeneCardsi
MT-RNR2
HGNCiHGNC:7471, MT-RNR2
MIMi606120, gene
neXtProtiNX_Q8IVG9
Orphaneti155, NON RARE IN EUROPE: Familial isolated hypertrophic cardiomyopathy

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

PhylomeDBiQ8IVG9

Enzyme and pathway databases

PathwayCommonsiQ8IVG9
ReactomeiR-HSA-416476, G alpha (q) signalling events
R-HSA-418594, G alpha (i) signalling events
R-HSA-444473, Formyl peptide receptors bind formyl peptides and many other ligands
SignaLinkiQ8IVG9

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
MT-RNR2, human
EvolutionaryTraceiQ8IVG9
PharosiQ8IVG9, Tdark

Protein Ontology

More...
PROi
PR:Q8IVG9

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Family and domain databases

CDDicd20245, humanin, 1 hit
DisProtiDP02267
InterProiView protein in InterPro
IPR028139, Humanin
PANTHERiPTHR33895, PTHR33895, 1 hit
PfamiView protein in Pfam
PF15040, Humanin, 1 hit

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiHUNIN_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q8IVG9
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: March 1, 2003
Last modified: May 25, 2022
This is version 113 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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