Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Transcription termination factor 3, mitochondrial

Gene

MTERF3

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

Functioni

Binds promoter DNA and regulates initiation of transcription. Required for normal mitochondrial transcription, and for normal assembly of mitochondrial respiratory complexes. Required for normal mitochondrial function (By similarity).By similarity1 Publication

GO - Molecular functioni

  • double-stranded DNA binding Source: InterPro
  • transcription regulatory region DNA binding Source: UniProtKB

GO - Biological processi

  • macroautophagy Source: Reactome
  • macromitophagy Source: Reactome
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-5205685. Pink/Parkin Mediated Mitophagy.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription termination factor 3, mitochondrial
Alternative name(s):
Mitochondrial transcription termination factor 3
Short name:
mTERF3
mTERF domain-containing protein 1, mitochondrial
Gene namesi
Name:MTERF3
Synonyms:MTERFD1
ORF Names:CGI-12
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:24258. MTERF3.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial outer membrane Source: Reactome
  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671309.

Polymorphism and mutation databases

BioMutaiMTERFD1.
DMDMi74731522.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6868MitochondrionAdd
BLAST
Chaini69 – 417349Transcription termination factor 3, mitochondrialPRO_0000255457Add
BLAST

Proteomic databases

EPDiQ96E29.
MaxQBiQ96E29.
PaxDbiQ96E29.
PRIDEiQ96E29.

PTM databases

iPTMnetiQ96E29.

Expressioni

Tissue specificityi

Highly expressed in heart, liver, kidney and testis. Detected at lower levels in brain, spleen and lung.1 Publication

Gene expression databases

BgeeiQ96E29.
CleanExiHS_MTERFD1.
ExpressionAtlasiQ96E29. baseline and differential.
GenevisibleiQ96E29. HS.

Organism-specific databases

HPAiHPA002966.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
AGTRAPQ6RW133EBI-7825321,EBI-741181
ARL6IP1Q150413EBI-7825321,EBI-714543
CMTM5Q96DZ93EBI-7825321,EBI-2548702
FUNDC1Q8IVP53EBI-7825321,EBI-3059266

Protein-protein interaction databases

BioGridi119209. 29 interactions.
IntActiQ96E29. 6 interactions.
MINTiMINT-3052237.
STRINGi9606.ENSP00000287025.

Structurei

Secondary structure

1
417
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi149 – 16113Combined sources
Helixi166 – 1694Combined sources
Helixi173 – 1808Combined sources
Helixi184 – 1874Combined sources
Helixi189 – 19810Combined sources
Helixi202 – 2043Combined sources
Helixi205 – 2117Combined sources
Helixi215 – 2173Combined sources
Helixi220 – 23213Combined sources
Helixi237 – 24610Combined sources
Helixi250 – 2523Combined sources
Helixi255 – 26915Combined sources
Helixi273 – 28210Combined sources
Helixi284 – 2874Combined sources
Helixi292 – 30312Combined sources
Helixi309 – 31810Combined sources
Helixi320 – 3234Combined sources
Helixi327 – 33812Combined sources
Helixi345 – 3506Combined sources
Helixi352 – 3565Combined sources
Helixi359 – 37113Combined sources
Beta strandi381 – 3833Combined sources
Helixi387 – 3926Combined sources
Helixi395 – 4017Combined sources
Helixi407 – 4148Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3M66X-ray1.60A148-417[»]
ProteinModelPortaliQ96E29.
SMRiQ96E29. Positions 148-417.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96E29.

Family & Domainsi

Domaini

Contains seven structural repeats of about 35 residues, where each repeat contains three helices. The repeats form a superhelical structure with a solenoid shape.1 Publication

Sequence similaritiesi

Belongs to the mTERF family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1267. Eukaryota.
ENOG410XT49. LUCA.
GeneTreeiENSGT00390000005801.
HOGENOMiHOG000044443.
HOVERGENiHBG062577.
InParanoidiQ96E29.
OMAiYFVRNVA.
PhylomeDBiQ96E29.
TreeFamiTF317943.

Family and domain databases

InterProiIPR003690. MTERF.
[Graphical view]
PfamiPF02536. mTERF. 1 hit.
[Graphical view]
SMARTiSM00733. Mterf. 6 hits.
[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: Q96E29-1) [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
MALSAQQIPR WFNSVKLRSL INAAQLTKRF TRPARTLLHG FSAQPQISSD
60 70 80 90 100
NCFLQWGFKT YRTSSLWNSS QSTSSSSQEN NSAQSSLLPS MNEQSQKTQN
110 120 130 140 150
ISSFDSELFL EELDELPPLS PMQPISEEEA IQIIADPPLP PASFTLRDYV
160 170 180 190 200
DHSETLQKLV LLGVDLSKIE KHPEAANLLL RLDFEKDIKQ MLLFLKDVGI
210 220 230 240 250
EDNQLGAFLT KNHAIFSEDL ENLKTRVAYL HSKNFSKADV AQMVRKAPFL
260 270 280 290 300
LNFSVERLDN RLGFFQKELE LSVKKTRDLV VRLPRLLTGS LEPVKENMKV
310 320 330 340 350
YRLELGFKHN EIQHMITRIP KMLTANKMKL TETFDFVHNV MSIPHHIIVK
360 370 380 390 400
FPQVFNTRLF KVKERHLFLT YLGRAQYDPA KPNYISLDKL VSIPDEIFCE
410
EIAKASVQDF EKFLKTL
Length:417
Mass (Da):47,971
Last modified:March 1, 2004 - v2
Checksum:i2062EFE902584696
GO
Isoform 2 (identifier: Q96E29-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-90: Missing.

Show »
Length:327
Mass (Da):37,907
Checksum:i3C396BD9DC336AE6
GO
Isoform 3 (identifier: Q96E29-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-121: Missing.

Note: No experimental confirmation available.
Show »
Length:296
Mass (Da):34,358
Checksum:i539D802B0FB47ABE
GO

Sequence cautioni

The sequence AAD27721.1 differs from that shown. Reason: Frameshift at positions 261 and 262. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti153 – 1531S → P in BAG50978 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti396 – 3961E → G.
Corresponds to variant rs7461970 [ dbSNP | Ensembl ].
VAR_053786

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 121121Missing in isoform 3. 1 PublicationVSP_053985Add
BLAST
Alternative sequencei1 – 9090Missing in isoform 2. 1 PublicationVSP_021292Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF132946 mRNA. Translation: AAD27721.1. Frameshift.
AK001801 mRNA. Translation: BAG50978.1.
AP003465 Genomic DNA. No translation available.
CH471060 Genomic DNA. Translation: EAW91752.1.
BC012995 mRNA. Translation: AAH12995.2.
CCDSiCCDS6270.1. [Q96E29-1]
RefSeqiNP_057026.3. NM_015942.4. [Q96E29-1]
XP_005250983.1. XM_005250926.3. [Q96E29-1]
XP_011515357.1. XM_011517055.1. [Q96E29-3]
UniGeneiHs.308613.

Genome annotation databases

EnsembliENST00000287025; ENSP00000287025; ENSG00000156469. [Q96E29-1]
ENST00000522822; ENSP00000430138; ENSG00000156469. [Q96E29-3]
GeneIDi51001.
UCSCiuc003yhr.3. human. [Q96E29-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF132946 mRNA. Translation: AAD27721.1. Frameshift.
AK001801 mRNA. Translation: BAG50978.1.
AP003465 Genomic DNA. No translation available.
CH471060 Genomic DNA. Translation: EAW91752.1.
BC012995 mRNA. Translation: AAH12995.2.
CCDSiCCDS6270.1. [Q96E29-1]
RefSeqiNP_057026.3. NM_015942.4. [Q96E29-1]
XP_005250983.1. XM_005250926.3. [Q96E29-1]
XP_011515357.1. XM_011517055.1. [Q96E29-3]
UniGeneiHs.308613.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3M66X-ray1.60A148-417[»]
ProteinModelPortaliQ96E29.
SMRiQ96E29. Positions 148-417.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119209. 29 interactions.
IntActiQ96E29. 6 interactions.
MINTiMINT-3052237.
STRINGi9606.ENSP00000287025.

PTM databases

iPTMnetiQ96E29.

Polymorphism and mutation databases

BioMutaiMTERFD1.
DMDMi74731522.

Proteomic databases

EPDiQ96E29.
MaxQBiQ96E29.
PaxDbiQ96E29.
PRIDEiQ96E29.

Protocols and materials databases

DNASUi51001.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000287025; ENSP00000287025; ENSG00000156469. [Q96E29-1]
ENST00000522822; ENSP00000430138; ENSG00000156469. [Q96E29-3]
GeneIDi51001.
UCSCiuc003yhr.3. human. [Q96E29-1]

Organism-specific databases

CTDi51001.
GeneCardsiMTERF3.
HGNCiHGNC:24258. MTERF3.
HPAiHPA002966.
neXtProtiNX_Q96E29.
PharmGKBiPA142671309.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1267. Eukaryota.
ENOG410XT49. LUCA.
GeneTreeiENSGT00390000005801.
HOGENOMiHOG000044443.
HOVERGENiHBG062577.
InParanoidiQ96E29.
OMAiYFVRNVA.
PhylomeDBiQ96E29.
TreeFamiTF317943.

Enzyme and pathway databases

ReactomeiR-HSA-5205685. Pink/Parkin Mediated Mitophagy.

Miscellaneous databases

EvolutionaryTraceiQ96E29.
GenomeRNAii51001.
NextBioi35468869.
PROiQ96E29.

Gene expression databases

BgeeiQ96E29.
CleanExiHS_MTERFD1.
ExpressionAtlasiQ96E29. baseline and differential.
GenevisibleiQ96E29. HS.

Family and domain databases

InterProiIPR003690. MTERF.
[Graphical view]
PfamiPF02536. mTERF. 1 hit.
[Graphical view]
SMARTiSM00733. Mterf. 6 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
    Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
    Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  2. "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 3).
    Tissue: Ovarian cancer.
  3. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 1).
    Tissue: Muscle.
  6. Cited for: FUNCTION, PARTIAL PROTEIN SEQUENCE, DNA-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Structure of mitochondrial transcription termination factor 3 reveals a novel nucleic acid-binding domain."
    Spaahr H., Samuelsson T., Haellberg B.M., Gustafsson C.M.
    Biochem. Biophys. Res. Commun. 397:386-390(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 148-417, DOMAIN, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiMTEF3_HUMAN
AccessioniPrimary (citable) accession number: Q96E29
Secondary accession number(s): B3KMG6, G3V130, Q9Y301
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: March 1, 2004
Last modified: May 11, 2016
This is version 113 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.