TI17B_HUMAN
ID TI17B_HUMAN Reviewed; 172 AA.
AC O60830; A8K2E2; J3KPV3; Q9UJV0;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit Tim17-B;
GN Name=TIMM17B; Synonyms=TIM17B; ORFNames=JM3;
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] (ISOFORM 1).
RX PubMed=10339406; DOI=10.1006/jmbi.1999.2751;
RA Bauer M.F., Gempel K., Reichert A.S., Rappold G.A., Lichtner P.,
RA Gerbitz K.-D., Neupert W., Brunner M., Hofmann S.;
RT "Genetic and structural characterization of the human mitochondrial inner
RT membrane translocase.";
RL J. Mol. Biol. 289:69-82(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Peripheral blood leukocyte;
RA Strom T.M., Nyakatura G., Hellebrand H., Drescher B., Rosenthal A.,
RA Meindl A.;
RT "Transcription map in Xp11.23.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta, and Uterus;
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 [8]
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 [9]
RP INTERACTION WITH DNAJC15.
RX PubMed=23263864; DOI=10.1093/hmg/dds541;
RA Schusdziarra C., Blamowska M., Azem A., Hell K.;
RT "Methylation-controlled J-protein MCJ acts in the import of proteins into
RT human mitochondria.";
RL Hum. Mol. Genet. 22:1348-1357(2013).
RN [10]
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 [11]
RP DISULFIDE BOND.
RX PubMed=27265872; DOI=10.1038/srep27484;
RA Wrobel L., Sokol A.M., Chojnacka M., Chacinska A.;
RT "The presence of disulfide bonds reveals an evolutionarily conserved
RT mechanism involved in mitochondrial protein translocase assembly.";
RL Sci. Rep. 6:27484-27484(2016).
CC -!- FUNCTION: Essential component of the TIM23 complex, a complex that
CC mediates the translocation of transit peptide-containing proteins
CC across the mitochondrial inner membrane.
CC -!- SUBUNIT: Component of the TIM23 complex at least composed of TIMM23,
CC TIMM17 (TIMM17A or TIMM17B) and TIMM50. The complex interacts with the
CC TIMM44 component of the PAM complex and with DNAJC15.
CC {ECO:0000269|PubMed:23263864}.
CC -!- INTERACTION:
CC O60830; Q86V38: ATN1; NbExp=3; IntAct=EBI-2372529, EBI-11954292;
CC O60830; Q9UHD4: CIDEB; NbExp=5; IntAct=EBI-2372529, EBI-7062247;
CC O60830; P02489: CRYAA; NbExp=3; IntAct=EBI-2372529, EBI-6875961;
CC O60830; Q14204: DYNC1H1; NbExp=3; IntAct=EBI-2372529, EBI-356015;
CC O60830; P00488: F13A1; NbExp=3; IntAct=EBI-2372529, EBI-2565863;
CC O60830; P22607: FGFR3; NbExp=3; IntAct=EBI-2372529, EBI-348399;
CC O60830; O14908-2: GIPC1; NbExp=3; IntAct=EBI-2372529, EBI-25913156;
CC O60830; Q14957: GRIN2C; NbExp=3; IntAct=EBI-2372529, EBI-8285963;
CC O60830; P28799: GRN; NbExp=3; IntAct=EBI-2372529, EBI-747754;
CC O60830; P06396: GSN; NbExp=3; IntAct=EBI-2372529, EBI-351506;
CC O60830; P04792: HSPB1; NbExp=3; IntAct=EBI-2372529, EBI-352682;
CC O60830; O60333-2: KIF1B; NbExp=3; IntAct=EBI-2372529, EBI-10975473;
CC O60830; O95563: MPC2; NbExp=3; IntAct=EBI-2372529, EBI-719403;
CC O60830; Q9HB07: MYG1; NbExp=3; IntAct=EBI-2372529, EBI-709754;
CC O60830; Q13153: PAK1; NbExp=3; IntAct=EBI-2372529, EBI-1307;
CC O60830; Q6NTF9-3: RHBDD2; NbExp=3; IntAct=EBI-2372529, EBI-17589229;
CC O60830; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-2372529, EBI-396669;
CC O60830; Q53QW1: TEX44; NbExp=3; IntAct=EBI-2372529, EBI-10278496;
CC O60830; O14925: TIMM23; NbExp=4; IntAct=EBI-2372529, EBI-1047996;
CC O60830; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-2372529, EBI-741480;
CC O60830; O76024: WFS1; NbExp=3; IntAct=EBI-2372529, EBI-720609;
CC O60830; Q9Y649; NbExp=3; IntAct=EBI-2372529, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O60830-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60830-2; Sequence=VSP_047215;
CC -!- TISSUE SPECIFICITY: Expression is abundant in heart and skeletal
CC muscle, intermediate in brain, and weak in pancreas, placenta, kidney
CC and liver.
CC -!- PTM: Forms one disulfide bond. {ECO:0000269|PubMed:27265872}.
CC -!- SIMILARITY: Belongs to the Tim17/Tim22/Tim23 family. {ECO:0000305}.
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DR EMBL; AF034790; AAC24694.1; -; mRNA.
DR EMBL; AJ005895; CAA06752.1; -; mRNA.
DR EMBL; AF077039; AAD27772.1; -; mRNA.
DR EMBL; AK290207; BAF82896.1; -; mRNA.
DR EMBL; AF196971; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF207550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471224; EAW50741.1; -; Genomic_DNA.
DR EMBL; BC010142; AAH10142.1; -; mRNA.
DR EMBL; BC091473; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS14308.1; -. [O60830-1]
DR CCDS; CCDS55411.1; -. [O60830-2]
DR RefSeq; NP_001161419.1; NM_001167947.2. [O60830-2]
DR RefSeq; NP_005825.1; NM_005834.4. [O60830-1]
DR AlphaFoldDB; O60830; -.
DR SMR; O60830; -.
DR BioGRID; 115539; 40.
DR ComplexPortal; CPX-6130; TIM23 mitochondrial inner membrane pre-sequence translocase complex, TIM17B variant.
DR CORUM; O60830; -.
DR IntAct; O60830; 39.
DR MINT; O60830; -.
DR GlyGen; O60830; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O60830; -.
DR PhosphoSitePlus; O60830; -.
DR SwissPalm; O60830; -.
DR BioMuta; TIMM17B; -.
DR EPD; O60830; -.
DR jPOST; O60830; -.
DR MassIVE; O60830; -.
DR MaxQB; O60830; -.
DR PeptideAtlas; O60830; -.
DR PRIDE; O60830; -.
DR ProteomicsDB; 49622; -. [O60830-1]
DR TopDownProteomics; O60830-1; -. [O60830-1]
DR Antibodypedia; 25886; 77 antibodies from 19 providers.
DR DNASU; 10245; -.
DR Ensembl; ENST00000376582.7; ENSP00000365766.3; ENSG00000126768.12. [O60830-1]
DR Ensembl; ENST00000396779.7; ENSP00000379999.3; ENSG00000126768.12. [O60830-2]
DR Ensembl; ENST00000465150.6; ENSP00000477073.1; ENSG00000126768.12. [O60830-2]
DR GeneID; 10245; -.
DR KEGG; hsa:10245; -.
DR UCSC; uc004dla.3; human. [O60830-1]
DR CTD; 10245; -.
DR GeneCards; TIMM17B; -.
DR HGNC; HGNC:17310; TIMM17B.
DR HPA; ENSG00000126768; Low tissue specificity.
DR MIM; 300249; gene.
DR neXtProt; NX_O60830; -.
DR OpenTargets; ENSG00000126768; -.
DR PharmGKB; PA38226; -.
DR VEuPathDB; HostDB:ENSG00000126768; -.
DR GeneTree; ENSGT00390000017780; -.
DR HOGENOM; CLU_087811_1_1_1; -.
DR InParanoid; O60830; -.
DR OMA; CPWVILS; -.
DR OrthoDB; 1590221at2759; -.
DR PhylomeDB; O60830; -.
DR TreeFam; TF106195; -.
DR PathwayCommons; O60830; -.
DR Reactome; R-HSA-1268020; Mitochondrial protein import.
DR SignaLink; O60830; -.
DR BioGRID-ORCS; 10245; 6 hits in 697 CRISPR screens.
DR ChiTaRS; TIMM17B; human.
DR GenomeRNAi; 10245; -.
DR Pharos; O60830; Tdark.
DR PRO; PR:O60830; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; O60830; protein.
DR Bgee; ENSG00000126768; Expressed in apex of heart and 174 other tissues.
DR ExpressionAtlas; O60830; baseline and differential.
DR Genevisible; O60830; HS.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IDA:BHF-UCL.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:GO_Central.
DR GO; GO:0005744; C:TIM23 mitochondrial import inner membrane translocase complex; IDA:BHF-UCL.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IC:ComplexPortal.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0006626; P:protein targeting to mitochondrion; TAS:ProtInc.
DR InterPro; IPR005678; Tim17.
DR TIGRFAMs; TIGR00980; 3a0801so1tim17; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Protein transport; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..172
FT /note="Mitochondrial import inner membrane translocase
FT subunit Tim17-B"
FT /id="PRO_0000210287"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 146..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 9..78
FT /evidence="ECO:0000250|UniProtKB:P39515"
FT VAR_SEQ 42
FT /note="V -> VCRLLSEAPLFIYSCSRSVSPTVNVSSERAESRPTLFMAVSLHMAWC
FT LAHI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_047215"
SQ SEQUENCE 172 AA; 18273 MW; 5DF3926F815E835A CRC64;
MEEYAREPCP WRIVDDCGGA FTMGVIGGGV FQAIKGFRNA PVGIRHRLRG SANAVRIRAP
QIGGSFAVWG GLFSTIDCGL VRLRGKEDPW NSITSGALTG AVLAARSGPL AMVGSAMMGG
ILLALIEGVG ILLTRYTAQQ FRNAPPFLED PSQLPPKDGT PAPGYPSYQQ YH
