TOM34_HUMAN
ID TOM34_HUMAN Reviewed; 309 AA.
AC Q15785; Q53GH9; Q6IBN7; Q9NTZ3;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Mitochondrial import receptor subunit TOM34;
DE Short=hTom34;
DE AltName: Full=Translocase of outer membrane 34 kDa subunit;
GN Name=TOMM34; Synonyms=URCC3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=9324309; DOI=10.1089/dna.1997.16.1067;
RA Nuttall S.D., Hanson B.J., Mori M., Hoogenraad N.J.;
RT "hTom34: a novel translocase for the import of proteins into human
RT mitochondria.";
RL DNA Cell Biol. 16:1067-1074(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16820880;
RA Shimokawa T., Matsushima S., Tsunoda T., Tahara H., Nakamura Y.,
RA Furukawa Y.;
RT "Identification of TOMM34, which shows elevated expression in the majority
RT of human colon cancers, as a novel drug target.";
RL Int. J. Oncol. 29:381-386(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP INTERACTION WITH HSP90A.
RX PubMed=9660753; DOI=10.1074/jbc.273.29.18007;
RA Young J.C., Obermann W.M., Hartl F.U.;
RT "Specific binding of tetratricopeptide repeat proteins to the C-terminal
RT 12-kDa domain of hsp90.";
RL J. Biol. Chem. 273:18007-18010(1998).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10101285; DOI=10.1093/oxfordjournals.jbchem.a022342;
RA Chewawiwat N., Yano M., Terada K., Hoogenraad N.J., Mori M.;
RT "Characterization of the novel mitochondrial protein import component,
RT Tom34, in mammalian cells.";
RL J. Biochem. 125:721-727(1999).
RN [11]
RP FUNCTION.
RX PubMed=11913975; DOI=10.1006/abbi.2002.2777;
RA Mukhopadhyay A., Avramova L.V., Weiner H.;
RT "Tom34 unlike Tom20 does not interact with the leader sequences of
RT mitochondrial precursor proteins.";
RL Arch. Biochem. Biophys. 400:97-104(2002).
RN [12]
RP INTERACTION WITH VCP; ATP6V1D; KIAA0665; AMPK AND DMAP1.
RX PubMed=11913976; DOI=10.1006/abbi.2002.2778;
RA Yang C.-S., Weiner H.;
RT "Yeast two-hybrid screening identifies binding partners of human Tom34 that
RT have ATPase activity and form a complex with Tom34 in the cytosol.";
RL Arch. Biochem. Biophys. 400:105-110(2002).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160 AND SER-186, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-197, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Plays a role in the import of cytosolically synthesized
CC preproteins into mitochondria. Binds the mature portion of precursor
CC proteins. Interacts with cellular components, and possesses weak ATPase
CC activity. May be a chaperone-like protein that helps to keep newly
CC synthesized precursors in an unfolded import compatible state.
CC {ECO:0000269|PubMed:10101285, ECO:0000269|PubMed:11913975,
CC ECO:0000269|PubMed:9324309}.
CC -!- SUBUNIT: Interacts with HSP90A, VCP, ATP6V1D, KIAA0665, AMPK, and DMAP1
CC through its TPR repeat. {ECO:0000269|PubMed:11913976,
CC ECO:0000269|PubMed:9660753}.
CC -!- INTERACTION:
CC Q15785; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-1054499, EBI-717399;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10101285}.
CC Mitochondrion outer membrane {ECO:0000269|PubMed:10101285}; Peripheral
CC membrane protein {ECO:0000269|PubMed:10101285}; Cytoplasmic side
CC {ECO:0000269|PubMed:10101285}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the Tom34 family. {ECO:0000305}.
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DR EMBL; U58970; AAC64484.1; -; mRNA.
DR EMBL; AB085681; BAF32949.1; -; mRNA.
DR EMBL; BT020008; AAV38811.1; -; mRNA.
DR EMBL; BT020009; AAV38812.1; -; mRNA.
DR EMBL; CR456765; CAG33046.1; -; mRNA.
DR EMBL; AK222952; BAD96672.1; -; mRNA.
DR EMBL; AL109839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75886.1; -; Genomic_DNA.
DR EMBL; BC007423; AAH07423.1; -; mRNA.
DR EMBL; BC001763; AAH01763.1; -; mRNA.
DR EMBL; BC014907; AAH14907.1; -; mRNA.
DR CCDS; CCDS13340.1; -.
DR RefSeq; NP_006800.2; NM_006809.4.
DR AlphaFoldDB; Q15785; -.
DR SMR; Q15785; -.
DR BioGRID; 116153; 120.
DR IntAct; Q15785; 24.
DR STRING; 9606.ENSP00000361900; -.
DR iPTMnet; Q15785; -.
DR MetOSite; Q15785; -.
DR PhosphoSitePlus; Q15785; -.
DR SwissPalm; Q15785; -.
DR BioMuta; TOMM34; -.
DR DMDM; 24212065; -.
DR EPD; Q15785; -.
DR jPOST; Q15785; -.
DR MassIVE; Q15785; -.
DR MaxQB; Q15785; -.
DR PaxDb; Q15785; -.
DR PeptideAtlas; Q15785; -.
DR PRIDE; Q15785; -.
DR ProteomicsDB; 60760; -.
DR Antibodypedia; 12625; 327 antibodies from 26 providers.
DR DNASU; 10953; -.
DR Ensembl; ENST00000372813.4; ENSP00000361900.3; ENSG00000025772.8.
DR GeneID; 10953; -.
DR KEGG; hsa:10953; -.
DR MANE-Select; ENST00000372813.4; ENSP00000361900.3; NM_006809.5; NP_006800.2.
DR UCSC; uc002xmy.4; human.
DR CTD; 10953; -.
DR DisGeNET; 10953; -.
DR GeneCards; TOMM34; -.
DR HGNC; HGNC:15746; TOMM34.
DR HPA; ENSG00000025772; Tissue enhanced (testis).
DR MIM; 616049; gene.
DR neXtProt; NX_Q15785; -.
DR OpenTargets; ENSG00000025772; -.
DR PharmGKB; PA38032; -.
DR VEuPathDB; HostDB:ENSG00000025772; -.
DR eggNOG; KOG1124; Eukaryota.
DR GeneTree; ENSGT00940000161058; -.
DR HOGENOM; CLU_061396_0_0_1; -.
DR InParanoid; Q15785; -.
DR OMA; KRWECLP; -.
DR OrthoDB; 1428825at2759; -.
DR PhylomeDB; Q15785; -.
DR TreeFam; TF106202; -.
DR PathwayCommons; Q15785; -.
DR SignaLink; Q15785; -.
DR BioGRID-ORCS; 10953; 9 hits in 1079 CRISPR screens.
DR ChiTaRS; TOMM34; human.
DR GeneWiki; TOMM34; -.
DR GenomeRNAi; 10953; -.
DR Pharos; Q15785; Tbio.
DR PRO; PR:Q15785; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q15785; protein.
DR Bgee; ENSG00000025772; Expressed in right testis and 190 other tissues.
DR Genevisible; Q15785; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0031072; F:heat shock protein binding; IPI:UniProtKB.
DR GO; GO:0006626; P:protein targeting to mitochondrion; IMP:UniProtKB.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00515; TPR_1; 1.
DR SMART; SM00028; TPR; 6.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 5.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW Chaperone; Cytoplasm; Isopeptide bond; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Phosphoprotein; Reference proteome; Repeat;
KW TPR repeat; Ubl conjugation.
FT CHAIN 1..309
FT /note="Mitochondrial import receptor subunit TOM34"
FT /id="PRO_0000106334"
FT REPEAT 9..42
FT /note="TPR 1"
FT REPEAT 51..84
FT /note="TPR 2"
FT REPEAT 86..118
FT /note="TPR 3"
FT REPEAT 193..226
FT /note="TPR 4"
FT REPEAT 227..260
FT /note="TPR 5"
FT REPEAT 262..294
FT /note="TPR 6"
FT REGION 161..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CYG7"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 197
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 293
FT /note="R -> K (in dbSNP:rs6094061)"
FT /id="VAR_059860"
FT CONFLICT 62..64
FT /note="LKD -> WKN (in Ref. 1; AAC64484)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="N -> S (in Ref. 5; BAD96672)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="I -> F (in Ref. 1; AAC64484)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="S -> F (in Ref. 1; AAC64484)"
FT /evidence="ECO:0000305"
SQ 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
