TOM1_HUMAN
ID TOM1_HUMAN Reviewed; 492 AA.
AC O60784; B4DEL9; B4DNA1; Q5TIJ6; Q86X74;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1999, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Target of Myb protein 1;
GN Name=TOM1;
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), AND TISSUE SPECIFICITY.
RX PubMed=10329004; DOI=10.1006/geno.1998.5739;
RA Seroussi E., Kedra D., Kost-Alimova M., Sandberg-Nordqvist A.-C.,
RA Fransson I., Jacobs J.F.M., Fu Y., Pan H.-Q., Roe B.A., Imreh S.,
RA Dumanski J.P.;
RT "TOM1 genes map to human chromosome 22q13.1 and mouse chromosome 8C1 and
RT encode proteins similar to the endosomal proteins HGS and STAM.";
RL Genomics 57:380-388(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum;
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Heart;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=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 [7]
RP IDENTIFICATION BY 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160; THR-164; SER-355 AND
RP SER-462, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160 AND THR-164, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-11; SER-160; THR-164 AND SER-355, 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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355, 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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355, AND IDENTIFICATION BY
RP 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355; SER-376 AND SER-461, AND
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 [17]
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 [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-385, 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).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF VHS DOMAIN.
RX PubMed=10985773; DOI=10.1021/bi0013546;
RA Misra S., Beach B.M., Hurley J.H.;
RT "Structure of the VHS domain of human Tom1 (target of myb 1): insights into
RT interactions with proteins and membranes.";
RL Biochemistry 39:11282-11290(2000).
RN [20]
RP INTERACTION WITH ZFYVE16.
RX PubMed=14613930; DOI=10.1074/jbc.m311228200;
RA Seet L.-F., Liu N., Hanson B.J., Hong W.;
RT "Endofin recruits TOM1 to endosomes.";
RL J. Biol. Chem. 279:4670-4679(2004).
CC -!- FUNCTION: May be involved in intracellular trafficking. Probable
CC association with membranes.
CC -!- SUBUNIT: Interacts with ZFYVE16; interaction is required to target it
CC to endosomes. {ECO:0000269|PubMed:14613930}.
CC -!- INTERACTION:
CC O60784; Q6FIE9: TOLLIP; NbExp=3; IntAct=EBI-74634, EBI-10249783;
CC O60784; Q9H0E2: TOLLIP; NbExp=5; IntAct=EBI-74634, EBI-74615;
CC O60784; Q9H0E2-1: TOLLIP; NbExp=4; IntAct=EBI-74634, EBI-16173683;
CC O60784; O75674: TOM1L1; NbExp=2; IntAct=EBI-74634, EBI-712991;
CC O60784; Q7Z3T8: ZFYVE16; NbExp=5; IntAct=EBI-74634, EBI-298055;
CC O60784-2; Q9UL15: BAG5; NbExp=3; IntAct=EBI-12117154, EBI-356517;
CC O60784-2; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-12117154, EBI-1383687;
CC O60784-2; P29466-3: CASP1; NbExp=3; IntAct=EBI-12117154, EBI-12248206;
CC O60784-2; Q15038: DAZAP2; NbExp=3; IntAct=EBI-12117154, EBI-724310;
CC O60784-2; P14136: GFAP; NbExp=3; IntAct=EBI-12117154, EBI-744302;
CC O60784-2; P05556: ITGB1; NbExp=3; IntAct=EBI-12117154, EBI-703066;
CC O60784-2; Q99732: LITAF; NbExp=3; IntAct=EBI-12117154, EBI-725647;
CC O60784-2; Q8TCA0: LRRC20; NbExp=3; IntAct=EBI-12117154, EBI-10274039;
CC O60784-2; Q9BSU3: NAA11; NbExp=3; IntAct=EBI-12117154, EBI-2585120;
CC O60784-2; P27986-2: PIK3R1; NbExp=3; IntAct=EBI-12117154, EBI-9090282;
CC O60784-2; C9JJ79: PILRA; NbExp=3; IntAct=EBI-12117154, EBI-12117156;
CC O60784-2; P17612: PRKACA; NbExp=3; IntAct=EBI-12117154, EBI-476586;
CC O60784-2; P63000: RAC1; NbExp=3; IntAct=EBI-12117154, EBI-413628;
CC O60784-2; P34741: SDC2; NbExp=3; IntAct=EBI-12117154, EBI-1172957;
CC O60784-2; Q9H0E2: TOLLIP; NbExp=5; IntAct=EBI-12117154, EBI-74615;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Membrane {ECO:0000305};
CC Peripheral membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O60784-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60784-2; Sequence=VSP_038366;
CC Name=3;
CC IsoId=O60784-3; Sequence=VSP_038365;
CC Name=4;
CC IsoId=O60784-4; Sequence=VSP_038364, VSP_038366;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in skeletal
CC muscle, heart, placenta and liver. {ECO:0000269|PubMed:10329004}.
CC -!- SIMILARITY: Belongs to the TOM1 family. {ECO:0000305}.
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DR EMBL; AJ006973; CAA07362.1; -; mRNA.
DR EMBL; CR456595; CAG30481.1; -; mRNA.
DR EMBL; AK293694; BAG57130.1; -; mRNA.
DR EMBL; AK297827; BAG60163.1; -; mRNA.
DR EMBL; AL008635; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z82244; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW60055.1; -; Genomic_DNA.
DR EMBL; BC046151; AAH46151.1; -; mRNA.
DR CCDS; CCDS13913.1; -. [O60784-1]
DR CCDS; CCDS46696.1; -. [O60784-2]
DR CCDS; CCDS46697.1; -. [O60784-3]
DR CCDS; CCDS46698.1; -. [O60784-4]
DR RefSeq; NP_001129201.1; NM_001135729.1. [O60784-4]
DR RefSeq; NP_001129202.1; NM_001135730.1. [O60784-3]
DR RefSeq; NP_001129204.1; NM_001135732.1. [O60784-2]
DR RefSeq; NP_005479.1; NM_005488.2. [O60784-1]
DR PDB; 1ELK; X-ray; 1.50 A; A/B=1-153.
DR PDB; 1WRD; X-ray; 1.75 A; A=215-312.
DR PDB; 2N2N; NMR; -; A=215-309.
DR PDB; 2N9D; NMR; -; A=215-309.
DR PDB; 6J56; X-ray; 1.80 A; C/D=437-462.
DR PDBsum; 1ELK; -.
DR PDBsum; 1WRD; -.
DR PDBsum; 2N2N; -.
DR PDBsum; 2N9D; -.
DR PDBsum; 6J56; -.
DR AlphaFoldDB; O60784; -.
DR SMR; O60784; -.
DR BioGRID; 115354; 82.
DR DIP; DIP-30844N; -.
DR IntAct; O60784; 39.
DR MINT; O60784; -.
DR STRING; 9606.ENSP00000413697; -.
DR TCDB; 9.B.278.1.6; the organellar-targeting adaptor protein complex (o-apc) family.
DR iPTMnet; O60784; -.
DR PhosphoSitePlus; O60784; -.
DR BioMuta; TOM1; -.
DR EPD; O60784; -.
DR jPOST; O60784; -.
DR MassIVE; O60784; -.
DR MaxQB; O60784; -.
DR PaxDb; O60784; -.
DR PeptideAtlas; O60784; -.
DR PRIDE; O60784; -.
DR ProteomicsDB; 49597; -. [O60784-1]
DR ProteomicsDB; 49598; -. [O60784-2]
DR ProteomicsDB; 49599; -. [O60784-3]
DR ProteomicsDB; 49600; -. [O60784-4]
DR TopDownProteomics; O60784-2; -. [O60784-2]
DR Antibodypedia; 208; 206 antibodies from 27 providers.
DR DNASU; 10043; -.
DR Ensembl; ENST00000411850.5; ENSP00000413697.1; ENSG00000100284.22. [O60784-2]
DR Ensembl; ENST00000425375.5; ENSP00000394924.1; ENSG00000100284.22. [O60784-3]
DR Ensembl; ENST00000447733.5; ENSP00000398876.1; ENSG00000100284.22. [O60784-4]
DR Ensembl; ENST00000449058.7; ENSP00000394466.2; ENSG00000100284.22. [O60784-1]
DR GeneID; 10043; -.
DR KEGG; hsa:10043; -.
DR MANE-Select; ENST00000449058.7; ENSP00000394466.2; NM_005488.3; NP_005479.1.
DR UCSC; uc003ann.3; human. [O60784-1]
DR CTD; 10043; -.
DR DisGeNET; 10043; -.
DR GeneCards; TOM1; -.
DR HGNC; HGNC:11982; TOM1.
DR HPA; ENSG00000100284; Tissue enhanced (skeletal).
DR MIM; 604700; gene.
DR neXtProt; NX_O60784; -.
DR OpenTargets; ENSG00000100284; -.
DR Orphanet; 391487; Autoimmune enteropathy and endocrinopathy-susceptibility to chronic infections syndrome.
DR PharmGKB; PA36666; -.
DR VEuPathDB; HostDB:ENSG00000100284; -.
DR eggNOG; KOG1087; Eukaryota.
DR GeneTree; ENSGT00940000156865; -.
DR HOGENOM; CLU_043812_3_0_1; -.
DR InParanoid; O60784; -.
DR OMA; RETHRVS; -.
DR PhylomeDB; O60784; -.
DR TreeFam; TF314105; -.
DR PathwayCommons; O60784; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; O60784; -.
DR BioGRID-ORCS; 10043; 11 hits in 1075 CRISPR screens.
DR ChiTaRS; TOM1; human.
DR EvolutionaryTrace; O60784; -.
DR GeneWiki; TOM1; -.
DR GenomeRNAi; 10043; -.
DR Pharos; O60784; Tbio.
DR PRO; PR:O60784; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; O60784; protein.
DR Bgee; ENSG00000100284; Expressed in lower esophagus mucosa and 128 other tissues.
DR ExpressionAtlas; O60784; baseline and differential.
DR Genevisible; O60784; HS.
DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0030276; F:clathrin binding; IDA:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; NAS:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; TAS:UniProtKB.
DR GO; GO:0015031; P:protein transport; NAS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 1.20.58.160; -; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR004152; GAT_dom.
DR InterPro; IPR038425; GAT_sf.
DR InterPro; IPR014645; TOM1.
DR InterPro; IPR002014; VHS_dom.
DR Pfam; PF03127; GAT; 1.
DR Pfam; PF00790; VHS; 1.
DR PIRSF; PIRSF036948; TOM1; 1.
DR SMART; SM00288; VHS; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR PROSITE; PS50909; GAT; 1.
DR PROSITE; PS50179; VHS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Isopeptide bond; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport; Ubl conjugation.
FT CHAIN 1..492
FT /note="Target of Myb protein 1"
FT /id="PRO_0000072628"
FT DOMAIN 20..152
FT /note="VHS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT DOMAIN 215..303
FT /note="GAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00373"
FT REGION 171..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..455
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 164
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88746"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88746"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CROSSLNK 385
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..33
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038364"
FT VAR_SEQ 123..167
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038365"
FT VAR_SEQ 441..442
FT /note="EE -> EGK (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_038366"
FT VARIANT 84
FT /note="R -> H (in dbSNP:rs11558473)"
FT /id="VAR_053845"
FT VARIANT 264
FT /note="M -> V (in dbSNP:rs34371697)"
FT /id="VAR_034567"
FT CONFLICT 215
FT /note="E -> G (in Ref. 3; BAG60163)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="A -> V (in Ref. 3; BAG57130)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="S -> P (in Ref. 3; BAG60163)"
FT /evidence="ECO:0000305"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:1ELK"
FT HELIX 12..20
FT /evidence="ECO:0007829|PDB:1ELK"
FT HELIX 30..42
FT /evidence="ECO:0007829|PDB:1ELK"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:1ELK"
FT HELIX 46..58
FT /evidence="ECO:0007829|PDB:1ELK"
FT HELIX 64..80
FT /evidence="ECO:0007829|PDB:1ELK"
FT HELIX 83..89
FT /evidence="ECO:0007829|PDB:1ELK"
FT HELIX 92..98
FT /evidence="ECO:0007829|PDB:1ELK"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:1ELK"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:1ELK"
FT HELIX 111..128
FT /evidence="ECO:0007829|PDB:1ELK"
FT HELIX 135..147
FT /evidence="ECO:0007829|PDB:1ELK"
FT HELIX 217..240
FT /evidence="ECO:0007829|PDB:1WRD"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:1WRD"
FT HELIX 248..274
FT /evidence="ECO:0007829|PDB:1WRD"
FT HELIX 278..305
FT /evidence="ECO:0007829|PDB:1WRD"
FT HELIX 439..452
FT /evidence="ECO:0007829|PDB:6J56"
FT TURN 453..456
FT /evidence="ECO:0007829|PDB:6J56"
SQ SEQUENCE 492 AA; 53818 MW; C7D77B5669476242 CRC64;
MDFLLGNPFS SPVGQRIEKA TDGSLQSEDW ALNMEICDII NETEEGPKDA LRAVKKRIVG
NKNFHEVMLA LTVLETCVKN CGHRFHVLVA SQDFVESVLV RTILPKNNPP TIVHDKVLNL
IQSWADAFRS SPDLTGVVTI YEDLRRKGLE FPMTDLDMLS PIHTPQRTVF NSETQSGQDS
VGTDSSQQED SGQHAAPLPA PPILSGDTPI APTPEQIGKL RSELEMVSGN VRVMSEMLTE
LVPTQAEPAD LELLQELNRT CRAMQQRVLE LIPQIANEQL TEELLIVNDN LNNVFLRHER
FERFRTGQTT KAPSEAEPAA DLIDMGPDPA ATGNLSSQLA GMNLGSSSVR AGLQSLEASG
RLEDEFDMFA LTRGSSLADQ RKEVKYEAPQ ATDGLAGALD ARQQSTGAIP VTQACLMEDI
EQWLSTDVGN DAEEPKGVTS EEFDKFLEER AKAADRLPNL SSPSAEGPPG PPSGPAPRKK
TQEKDDDMLF AL
