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Mitochondrial import receptor subunit TOM34 (hTom34) (Translocase of outer membrane 34 kDa subunit)

 TOM34_HUMAN             Reviewed;         309 AA.
Q15785; Q53GH9; Q6IBN7; Q9NTZ3;
19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
19-OCT-2002, sequence version 2.
18-JUL-2018, entry version 166.
RecName: Full=Mitochondrial import receptor subunit TOM34;
Short=hTom34;
AltName: Full=Translocase of outer membrane 34 kDa subunit;
Name=TOMM34; Synonyms=URCC3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
PubMed=9324309; DOI=10.1089/dna.1997.16.1067;
Nuttall S.D., Hanson B.J., Mori M., Hoogenraad N.J.;
"hTom34: a novel translocase for the import of proteins into human
mitochondria.";
DNA Cell Biol. 16:1067-1074(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=16820880;
Shimokawa T., Matsushima S., Tsunoda T., Tahara H., Nakamura Y.,
Furukawa Y.;
"Identification of TOMM34, which shows elevated expression in the
majority of human colon cancers, as a novel drug target.";
Int. J. Oncol. 29:381-386(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Muscle, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
INTERACTION WITH HSP90A.
PubMed=9660753; DOI=10.1074/jbc.273.29.18007;
Young J.C., Obermann W.M., Hartl F.U.;
"Specific binding of tetratricopeptide repeat proteins to the C-
terminal 12-kDa domain of hsp90.";
J. Biol. Chem. 273:18007-18010(1998).
[10]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10101285; DOI=10.1093/oxfordjournals.jbchem.a022342;
Chewawiwat N., Yano M., Terada K., Hoogenraad N.J., Mori M.;
"Characterization of the novel mitochondrial protein import component,
Tom34, in mammalian cells.";
J. Biochem. 125:721-727(1999).
[11]
FUNCTION.
PubMed=11913975; DOI=10.1006/abbi.2002.2777;
Mukhopadhyay A., Avramova L.V., Weiner H.;
"Tom34 unlike Tom20 does not interact with the leader sequences of
mitochondrial precursor proteins.";
Arch. Biochem. Biophys. 400:97-104(2002).
[12]
INTERACTION WITH VCP; ATP6M; KIAA0665; AMPK AND DMAP1.
PubMed=11913976; DOI=10.1006/abbi.2002.2778;
Yang C.-S., Weiner H.;
"Yeast two-hybrid screening identifies binding partners of human Tom34
that have ATPase activity and form a complex with Tom34 in the
cytosol.";
Arch. Biochem. Biophys. 400:105-110(2002).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160 AND SER-186, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[21]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-197, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Plays a role in the import of cytosolically synthesized
preproteins into mitochondria. Binds the mature portion of
precursor proteins. Interacts with cellular components, and
possesses weak ATPase activity. May be a chaperone-like protein
that helps to keep newly synthesized precursors in an unfolded
import compatible state. {ECO:0000269|PubMed:10101285,
ECO:0000269|PubMed:11913975, ECO:0000269|PubMed:9324309}.
-!- SUBUNIT: Interacts with HSP90A, VCP, ATP6M, KIAA0665, AMPK, and
DMAP1 through its TPR repeat. {ECO:0000269|PubMed:11913976,
ECO:0000269|PubMed:9660753}.
-!- INTERACTION:
Q9BSI4:TINF2; NbExp=2; IntAct=EBI-1054499, EBI-717399;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10101285}.
Mitochondrion outer membrane {ECO:0000269|PubMed:10101285};
Peripheral membrane protein {ECO:0000269|PubMed:10101285};
Cytoplasmic side {ECO:0000269|PubMed:10101285}.
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- SIMILARITY: Belongs to the Tom34 family. {ECO:0000305}.
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EMBL; U58970; AAC64484.1; -; mRNA.
EMBL; AB085681; BAF32949.1; -; mRNA.
EMBL; BT020008; AAV38811.1; -; mRNA.
EMBL; BT020009; AAV38812.1; -; mRNA.
EMBL; CR456765; CAG33046.1; -; mRNA.
EMBL; AK222952; BAD96672.1; -; mRNA.
EMBL; AL109839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471077; EAW75886.1; -; Genomic_DNA.
EMBL; BC007423; AAH07423.1; -; mRNA.
EMBL; BC001763; AAH01763.1; -; mRNA.
EMBL; BC014907; AAH14907.1; -; mRNA.
CCDS; CCDS13340.1; -.
RefSeq; NP_006800.2; NM_006809.4.
UniGene; Hs.517066; -.
ProteinModelPortal; Q15785; -.
SMR; Q15785; -.
BioGrid; 116153; 45.
IntAct; Q15785; 12.
STRING; 9606.ENSP00000361900; -.
iPTMnet; Q15785; -.
PhosphoSitePlus; Q15785; -.
SwissPalm; Q15785; -.
BioMuta; TOMM34; -.
DMDM; 24212065; -.
EPD; Q15785; -.
MaxQB; Q15785; -.
PaxDb; Q15785; -.
PeptideAtlas; Q15785; -.
PRIDE; Q15785; -.
ProteomicsDB; 60760; -.
DNASU; 10953; -.
Ensembl; ENST00000372813; ENSP00000361900; ENSG00000025772.
GeneID; 10953; -.
KEGG; hsa:10953; -.
UCSC; uc002xmy.4; human.
CTD; 10953; -.
DisGeNET; 10953; -.
EuPathDB; HostDB:ENSG00000025772.7; -.
GeneCards; TOMM34; -.
HGNC; HGNC:15746; TOMM34.
HPA; HPA018845; -.
HPA; HPA056875; -.
MIM; 616049; gene.
neXtProt; NX_Q15785; -.
OpenTargets; ENSG00000025772; -.
PharmGKB; PA38032; -.
eggNOG; KOG1124; Eukaryota.
eggNOG; COG0457; LUCA.
GeneTree; ENSGT00900000140844; -.
HOGENOM; HOG000070537; -.
HOVERGEN; HBG105545; -.
InParanoid; Q15785; -.
KO; K17766; -.
OMA; QSFRNGQ; -.
OrthoDB; EOG091G0FFR; -.
PhylomeDB; Q15785; -.
TreeFam; TF106202; -.
ChiTaRS; TOMM34; human.
GeneWiki; TOMM34; -.
GenomeRNAi; 10953; -.
PRO; PR:Q15785; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000025772; -.
CleanEx; HS_TOMM34; -.
Genevisible; Q15785; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; HDA:UniProtKB.
GO; GO:0031072; F:heat shock protein binding; IPI:UniProtKB.
GO; GO:0006626; P:protein targeting to mitochondrion; IMP:UniProtKB.
Gene3D; 1.25.40.10; -; 2.
InterPro; IPR013026; TPR-contain_dom.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR001440; TPR_1.
InterPro; IPR019734; TPR_repeat.
Pfam; PF00515; TPR_1; 1.
SMART; SM00028; TPR; 6.
SUPFAM; SSF48452; SSF48452; 2.
PROSITE; PS50005; TPR; 5.
PROSITE; PS50293; TPR_REGION; 2.
1: Evidence at protein level;
Chaperone; Complete proteome; Cytoplasm; Isopeptide bond; Membrane;
Mitochondrion; Mitochondrion outer membrane; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; TPR repeat; Ubl conjugation.
CHAIN 1 309 Mitochondrial import receptor subunit
TOM34.
/FTId=PRO_0000106334.
REPEAT 9 42 TPR 1.
REPEAT 51 84 TPR 2.
REPEAT 86 118 TPR 3.
REPEAT 193 226 TPR 4.
REPEAT 227 260 TPR 5.
REPEAT 262 294 TPR 6.
MOD_RES 8 8 Phosphoserine.
{ECO:0000250|UniProtKB:Q9CYG7}.
MOD_RES 160 160 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 186 186 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
CROSSLNK 197 197 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 293 293 R -> K (in dbSNP:rs6094061).
/FTId=VAR_059860.
CONFLICT 62 64 LKD -> WKN (in Ref. 1; AAC64484).
{ECO:0000305}.
CONFLICT 126 126 N -> S (in Ref. 5; BAD96672).
{ECO:0000305}.
CONFLICT 147 147 I -> F (in Ref. 1; AAC64484).
{ECO:0000305}.
CONFLICT 160 160 S -> F (in Ref. 1; AAC64484).
{ECO:0000305}.
SEQUENCE 309 AA; 34559 MW; A39D7987CC4A57E6 CRC64;
MAPKFPDSVE ELRAAGNESF RNGQYAEASA LYGRALRVLQ AQGSSDPEEE SVLYSNRAAC
HLKDGNCRDC IKDCTSALAL VPFSIKPLLR RASAYEALEK YPMAYVDYKT VLQIDDNVTS
AVEGINRMTR ALMDSLGPEW RLKLPSIPLV PVSAQKRWNS LPSENHKEMA KSKSKETTAT
KNRVPSAGDV EKARVLKEEG NELVKKGNHK KAIEKYSESL LCSNLESATY SNRALCYLVL
KQYTEAVKDC TEALKLDGKN VKAFYRRAQA HKALKDYKSS FADISNLLQI EPRNGPAQKL
RQEVKQNLH


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