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Protein

Required for meiotic nuclear division protein 1 homolog

Gene

RMND1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for mitochondrial translation, possibly by coordinating the assembly or maintenance of the mitochondrial ribosome (PubMed:23022098, PubMed:25604853).2 Publications

GO - Biological processi

  • positive regulation of mitochondrial translation Source: UniProtKB
  • translation Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Protein biosynthesis

Names & Taxonomyi

Protein namesi
Recommended name:
Required for meiotic nuclear division protein 1 homolog
Gene namesi
Name:RMND1
Synonyms:C6orf96
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:21176. RMND1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Combined oxidative phosphorylation deficiency 11 (COXPD11)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA severe, multisystemic, autosomal recessive, disorder characterized by deficiencies of multiple mitochondrial respiratory enzymes leading to neonatal hypotonia and lactic acidosis. Affected individuals may have respiratory insufficiency, foot deformities, or seizures.
See also OMIM:614922
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti417 – 4171R → Q in COXPD11; alters homooligomeric formation of the protein; decreases the levels of mitochondrial protein synthesis. 3 Publications
VAR_069036

Keywords - Diseasei

Disease mutation

Organism-specific databases

MalaCardsiRMND1.
MIMi614922. phenotype.
Orphaneti324535. Combined oxidative phosphorylation defect type 11.
PharmGKBiPA162401372.

Polymorphism and mutation databases

DMDMi91208248.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1212MitochondrionSequence analysisAdd
BLAST
Chaini13 – 449437Required for meiotic nuclear division protein 1 homologPRO_0000229732Add
BLAST

Proteomic databases

EPDiQ9NWS8.
MaxQBiQ9NWS8.
PaxDbiQ9NWS8.
PRIDEiQ9NWS8.

PTM databases

iPTMnetiQ9NWS8.
PhosphoSiteiQ9NWS8.

Expressioni

Gene expression databases

BgeeiQ9NWS8.
CleanExiHS_RMND1.
ExpressionAtlasiQ9NWS8. baseline and differential.
GenevisibleiQ9NWS8. HS.

Organism-specific databases

HPAiHPA031397.
HPA031398.
HPA031399.

Interactioni

Subunit structurei

Homooligomer (PubMed:23022098, PubMed:25604853).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FAM9BQ8IZU03EBI-4401316,EBI-10175124

Protein-protein interaction databases

BioGridi120337. 31 interactions.
IntActiQ9NWS8. 2 interactions.
STRINGi9606.ENSP00000356272.

Structurei

3D structure databases

ProteinModelPortaliQ9NWS8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RMD1/sif2 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2861. Eukaryota.
COG1723. LUCA.
GeneTreeiENSGT00390000013337.
HOVERGENiHBG093175.
InParanoidiQ9NWS8.
OMAiMKHVMKV.
OrthoDBiEOG7BZVSP.
PhylomeDBiQ9NWS8.
TreeFamiTF105813.

Family and domain databases

InterProiIPR003734. DUF155.
[Graphical view]
PfamiPF02582. DUF155. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NWS8-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPATLLRAVA RSHHILSKAH QCRRIGHLML KPLKEFENTT CSTLTIRQSL
60 70 80 90 100
DLFLPDKTAS GLNKSQILEM NQKKSDTSML SPLNAARCQD EKAHLPTMKS
110 120 130 140 150
FGTHRRVTHK PNLLGSKWFI KILKRHFSSV STETFVPKQD FPQVKRPLKA
160 170 180 190 200
SRTRQPSRTN LPVLSVNEDL MHCTAFATAD EYHLGNLSQD LASHGYVEVT
210 220 230 240 250
SLPRDAANIL VMGVENSAKE GDPGTIFFFR EGAAVFWNVK DKTMKHVMKV
260 270 280 290 300
LEKHEIQPYE IALVHWENEE LNYIKIEGQS KLHRGEIKLN SELDLDDAIL
310 320 330 340 350
EKFAFSNALC LSVKLAIWEA SLDKFIESIQ SIPEALKAGK KVKLSHEEVM
360 370 380 390 400
QKIGELFALR HRINLSSDFL ITPDFYWDRE NLEGLYDKTC QFLSIGRRVK
410 420 430 440
VMNEKLQHCM ELTDLMRNHL NEKRALRLEW MIVILITIEV MFELGRVFF
Length:449
Mass (Da):51,604
Last modified:April 4, 2006 - v2
Checksum:iC4A7B8F6A397B385
GO
Isoform 2 (identifier: Q9NWS8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-211: Missing.

Note: No experimental confirmation available.
Show »
Length:238
Mass (Da):27,846
Checksum:iEC4E8714002497DC
GO
Isoform 3 (identifier: Q9NWS8-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     205-208: DAAN → GTSS
     209-449: Missing.

Note: No experimental confirmation available.
Show »
Length:208
Mass (Da):23,411
Checksum:i8A6E6A5F589C8065
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti170 – 1701L → P in BAA91299 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti42 – 421S → I.
Corresponds to variant rs11550103 [ dbSNP | Ensembl ].
VAR_051864
Natural varianti47 – 471R → H.
Corresponds to variant rs6934360 [ dbSNP | Ensembl ].
VAR_051865
Natural varianti132 – 1321T → M.2 Publications
Corresponds to variant rs3734800 [ dbSNP | Ensembl ].
VAR_025754
Natural varianti417 – 4171R → Q in COXPD11; alters homooligomeric formation of the protein; decreases the levels of mitochondrial protein synthesis. 3 Publications
VAR_069036

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 211211Missing in isoform 2. CuratedVSP_017735Add
BLAST
Alternative sequencei205 – 2084DAAN → GTSS in isoform 3. 1 PublicationVSP_017738
Alternative sequencei209 – 449241Missing in isoform 3. 1 PublicationVSP_017739Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000634 mRNA. Translation: BAA91299.1.
AK292339 mRNA. Translation: BAF85028.1.
AL590543, AL590413 Genomic DNA. Translation: CAI10940.1.
AL590413, AL590543 Genomic DNA. Translation: CAI13588.1.
AL590413 Genomic DNA. Translation: CAI13594.1.
CH471051 Genomic DNA. Translation: EAW47747.1.
BC012081 mRNA. Translation: AAH12081.1.
BC106065 mRNA. Translation: AAI06066.1.
BC119683 mRNA. Translation: AAI19684.1.
CCDSiCCDS5232.1. [Q9NWS8-1]
RefSeqiNP_001258866.1. NM_001271937.1.
NP_060379.2. NM_017909.3. [Q9NWS8-1]
XP_005267097.1. XM_005267040.2. [Q9NWS8-2]
UniGeneiHs.486835.
Hs.744622.

Genome annotation databases

EnsembliENST00000336451; ENSP00000336683; ENSG00000155906. [Q9NWS8-2]
ENST00000367303; ENSP00000356272; ENSG00000155906. [Q9NWS8-1]
GeneIDi55005.
KEGGihsa:55005.
UCSCiuc003qoi.4. human. [Q9NWS8-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000634 mRNA. Translation: BAA91299.1.
AK292339 mRNA. Translation: BAF85028.1.
AL590543, AL590413 Genomic DNA. Translation: CAI10940.1.
AL590413, AL590543 Genomic DNA. Translation: CAI13588.1.
AL590413 Genomic DNA. Translation: CAI13594.1.
CH471051 Genomic DNA. Translation: EAW47747.1.
BC012081 mRNA. Translation: AAH12081.1.
BC106065 mRNA. Translation: AAI06066.1.
BC119683 mRNA. Translation: AAI19684.1.
CCDSiCCDS5232.1. [Q9NWS8-1]
RefSeqiNP_001258866.1. NM_001271937.1.
NP_060379.2. NM_017909.3. [Q9NWS8-1]
XP_005267097.1. XM_005267040.2. [Q9NWS8-2]
UniGeneiHs.486835.
Hs.744622.

3D structure databases

ProteinModelPortaliQ9NWS8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120337. 31 interactions.
IntActiQ9NWS8. 2 interactions.
STRINGi9606.ENSP00000356272.

PTM databases

iPTMnetiQ9NWS8.
PhosphoSiteiQ9NWS8.

Polymorphism and mutation databases

DMDMi91208248.

Proteomic databases

EPDiQ9NWS8.
MaxQBiQ9NWS8.
PaxDbiQ9NWS8.
PRIDEiQ9NWS8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000336451; ENSP00000336683; ENSG00000155906. [Q9NWS8-2]
ENST00000367303; ENSP00000356272; ENSG00000155906. [Q9NWS8-1]
GeneIDi55005.
KEGGihsa:55005.
UCSCiuc003qoi.4. human. [Q9NWS8-1]

Organism-specific databases

CTDi55005.
GeneCardsiRMND1.
HGNCiHGNC:21176. RMND1.
HPAiHPA031397.
HPA031398.
HPA031399.
MalaCardsiRMND1.
MIMi614917. gene.
614922. phenotype.
neXtProtiNX_Q9NWS8.
Orphaneti324535. Combined oxidative phosphorylation defect type 11.
PharmGKBiPA162401372.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2861. Eukaryota.
COG1723. LUCA.
GeneTreeiENSGT00390000013337.
HOVERGENiHBG093175.
InParanoidiQ9NWS8.
OMAiMKHVMKV.
OrthoDBiEOG7BZVSP.
PhylomeDBiQ9NWS8.
TreeFamiTF105813.

Miscellaneous databases

GenomeRNAii55005.
PROiQ9NWS8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NWS8.
CleanExiHS_RMND1.
ExpressionAtlasiQ9NWS8. baseline and differential.
GenevisibleiQ9NWS8. HS.

Family and domain databases

InterProiIPR003734. DUF155.
[Graphical view]
PfamiPF02582. DUF155. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT MET-132.
    Tissue: Signet-ring cell carcinoma and Testis.
  2. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), VARIANT MET-132.
    Tissue: Kidney and Skin.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: INVOLVEMENT IN COXPD11, SUBCELLULAR LOCATION.
  7. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "RMND1 deficiency associated with neonatal lactic acidosis, infantile onset renal failure, deafness, and multiorgan involvement."
    Janer A., van Karnebeek C.D., Sasarman F., Antonicka H., Al Ghamdi M., Shyr C., Dunbar M., Stockler-Ispiroglu S., Ross C.J., Vallance H., Dionne J., Wasserman W.W., Shoubridge E.A.
    Eur. J. Hum. Genet. 23:1301-1307(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, CHARACTERIZATION VARIANT COXPD11 GLN-417.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "An RMND1 Mutation causes encephalopathy associated with multiple oxidative phosphorylation complex deficiencies and a mitochondrial translation defect."
    Janer A., Antonicka H., Lalonde E., Nishimura T., Sasarman F., Brown G.K., Brown R.M., Majewski J., Shoubridge E.A.
    Am. J. Hum. Genet. 91:737-743(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT COXPD11 GLN-417, FUNCTION, HOMOPOLYMERIZATION, SUBCELLULAR LOCATION.
  11. "Periventricular Calcification, Abnormal Pterins and Dry Thickened Skin: expanding the clinical spectrum of RMND1?"
    Casey J.P., Crushell E., Thompson K., Twomey E., He L., Ennis S., Philip R.K., Taylor R.W., King M.D., Lynch S.A.
    JIMD Rep. 0:0-0(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT COXPD11 GLN-417.

Entry informationi

Entry nameiRMND1_HUMAN
AccessioniPrimary (citable) accession number: Q9NWS8
Secondary accession number(s): A8K8H4
, Q0VDG6, Q5SZ48, Q5SZ83, Q6NSC5, Q96EN7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: April 4, 2006
Last modified: June 8, 2016
This is version 107 of the entry and version 2 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.