Full text data of TOM1
TOM1
[Confidence: low (only semi-automatic identification from reviews)]
Target of Myb protein 1
Target of Myb protein 1
UniProt
O60784
ID TOM1_HUMAN Reviewed; 492 AA.
AC O60784; B4DEL9; B4DNA1; Q5TIJ6; Q86X74;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-AUG-1999, sequence version 2.
DT 22-JAN-2014, entry version 128.
DE RecName: Full=Target of Myb protein 1;
GN Name=TOM1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT and 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA 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.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA 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.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160; THR-164; SER-355
RP AND SER-462, AND MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
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
RP SCALE ANALYSIS] AT SER-11; SER-160; THR-164 AND SER-355, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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 MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
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
RT into interactions with proteins and membranes.";
RL Biochemistry 39:11282-11290(2000).
RN [15]
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
CC it to endosomes.
CC -!- INTERACTION:
CC O75674:TOM1L1; NbExp=2; IntAct=EBI-74634, EBI-712991;
CC Q7Z3T8:ZFYVE16; NbExp=5; IntAct=EBI-74634, EBI-298055;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable). Membrane; Peripheral
CC membrane protein (Probable).
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 Note=No experimental confirmation available;
CC Name=3;
CC IsoId=O60784-3; Sequence=VSP_038365;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=O60784-4; Sequence=VSP_038364, VSP_038366;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in skeletal
CC muscle, heart, placenta and liver.
CC -!- SIMILARITY: Belongs to the TOM1 family.
CC -!- SIMILARITY: Contains 1 GAT domain.
CC -!- SIMILARITY: Contains 1 VHS domain.
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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; CAI21633.1; -; Genomic_DNA.
DR EMBL; Z82244; CAI21633.1; JOINED; Genomic_DNA.
DR EMBL; Z82244; CAI17951.1; -; Genomic_DNA.
DR EMBL; AL008635; CAI17951.1; JOINED; Genomic_DNA.
DR EMBL; CH471095; EAW60055.1; -; Genomic_DNA.
DR EMBL; BC046151; AAH46151.1; -; mRNA.
DR RefSeq; NP_001129201.1; NM_001135729.1.
DR RefSeq; NP_001129202.1; NM_001135730.1.
DR RefSeq; NP_001129204.1; NM_001135732.1.
DR RefSeq; NP_005479.1; NM_005488.2.
DR UniGene; Hs.474705; -.
DR PDB; 1ELK; X-ray; 1.50 A; A/B=2-153.
DR PDB; 1WRD; X-ray; 1.75 A; A=215-312.
DR PDBsum; 1ELK; -.
DR PDBsum; 1WRD; -.
DR ProteinModelPortal; O60784; -.
DR SMR; O60784; 2-153, 215-307.
DR IntAct; O60784; 11.
DR MINT; MINT-275660; -.
DR STRING; 9606.ENSP00000413697; -.
DR PhosphoSite; O60784; -.
DR PaxDb; O60784; -.
DR PRIDE; O60784; -.
DR DNASU; 10043; -.
DR Ensembl; ENST00000411850; ENSP00000413697; ENSG00000100284.
DR Ensembl; ENST00000425375; ENSP00000394924; ENSG00000100284.
DR Ensembl; ENST00000447733; ENSP00000398876; ENSG00000100284.
DR Ensembl; ENST00000449058; ENSP00000394466; ENSG00000100284.
DR GeneID; 10043; -.
DR KEGG; hsa:10043; -.
DR UCSC; uc003ann.3; human.
DR CTD; 10043; -.
DR GeneCards; GC22P035695; -.
DR H-InvDB; HIX0175450; -.
DR HGNC; HGNC:11982; TOM1.
DR HPA; HPA001749; -.
DR MIM; 604700; gene.
DR neXtProt; NX_O60784; -.
DR PharmGKB; PA36666; -.
DR eggNOG; NOG118960; -.
DR HOGENOM; HOG000285970; -.
DR HOVERGEN; HBG025068; -.
DR InParanoid; O60784; -.
DR OMA; EEPKGVT; -.
DR PhylomeDB; O60784; -.
DR EvolutionaryTrace; O60784; -.
DR GeneWiki; TOM1; -.
DR GenomeRNAi; 10043; -.
DR NextBio; 37933; -.
DR PMAP-CutDB; O60784; -.
DR PRO; PR:O60784; -.
DR ArrayExpress; O60784; -.
DR Bgee; O60784; -.
DR CleanEx; HS_TOM1; -.
DR Genevestigator; O60784; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0030276; F:clathrin binding; IDA:UniProtKB.
DR GO; GO:0006897; P:endocytosis; NAS:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; NAS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; NAS:UniProtKB.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR004152; GAT.
DR InterPro; IPR014645; TOM1.
DR InterPro; IPR002014; VHS.
DR InterPro; IPR018205; VHS_subgr.
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; Complete proteome;
KW Cytoplasm; Membrane; Phosphoprotein; Polymorphism; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1 492 Target of Myb protein 1.
FT /FTId=PRO_0000072628.
FT DOMAIN 20 152 VHS.
FT DOMAIN 215 303 GAT.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 11 11 Phosphoserine.
FT MOD_RES 160 160 Phosphoserine.
FT MOD_RES 164 164 Phosphothreonine.
FT MOD_RES 176 176 Phosphoserine (By similarity).
FT MOD_RES 355 355 Phosphoserine.
FT MOD_RES 462 462 Phosphoserine.
FT VAR_SEQ 1 33 Missing (in isoform 4).
FT /FTId=VSP_038364.
FT VAR_SEQ 123 167 Missing (in isoform 3).
FT /FTId=VSP_038365.
FT VAR_SEQ 441 442 EE -> EGK (in isoform 2 and isoform 4).
FT /FTId=VSP_038366.
FT VARIANT 84 84 R -> H (in dbSNP:rs11558473).
FT /FTId=VAR_053845.
FT VARIANT 264 264 M -> V (in dbSNP:rs34371697).
FT /FTId=VAR_034567.
FT CONFLICT 215 215 E -> G (in Ref. 3; BAG60163).
FT CONFLICT 249 249 A -> V (in Ref. 3; BAG57130).
FT CONFLICT 346 346 S -> P (in Ref. 3; BAG60163).
FT HELIX 8 10
FT HELIX 12 20
FT HELIX 30 42
FT STRAND 43 45
FT HELIX 46 58
FT HELIX 64 80
FT HELIX 83 89
FT HELIX 92 98
FT HELIX 100 103
FT TURN 105 107
FT HELIX 111 128
FT HELIX 135 147
FT HELIX 217 240
FT TURN 243 245
FT HELIX 248 274
FT HELIX 278 305
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
//
ID TOM1_HUMAN Reviewed; 492 AA.
AC O60784; B4DEL9; B4DNA1; Q5TIJ6; Q86X74;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-AUG-1999, sequence version 2.
DT 22-JAN-2014, entry version 128.
DE RecName: Full=Target of Myb protein 1;
GN Name=TOM1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT and 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA 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.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA 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.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160; THR-164; SER-355
RP AND SER-462, AND MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
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
RP SCALE ANALYSIS] AT SER-11; SER-160; THR-164 AND SER-355, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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 MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
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
RT into interactions with proteins and membranes.";
RL Biochemistry 39:11282-11290(2000).
RN [15]
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
CC it to endosomes.
CC -!- INTERACTION:
CC O75674:TOM1L1; NbExp=2; IntAct=EBI-74634, EBI-712991;
CC Q7Z3T8:ZFYVE16; NbExp=5; IntAct=EBI-74634, EBI-298055;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable). Membrane; Peripheral
CC membrane protein (Probable).
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 Note=No experimental confirmation available;
CC Name=3;
CC IsoId=O60784-3; Sequence=VSP_038365;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=O60784-4; Sequence=VSP_038364, VSP_038366;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in skeletal
CC muscle, heart, placenta and liver.
CC -!- SIMILARITY: Belongs to the TOM1 family.
CC -!- SIMILARITY: Contains 1 GAT domain.
CC -!- SIMILARITY: Contains 1 VHS domain.
CC -----------------------------------------------------------------------
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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; CAI21633.1; -; Genomic_DNA.
DR EMBL; Z82244; CAI21633.1; JOINED; Genomic_DNA.
DR EMBL; Z82244; CAI17951.1; -; Genomic_DNA.
DR EMBL; AL008635; CAI17951.1; JOINED; Genomic_DNA.
DR EMBL; CH471095; EAW60055.1; -; Genomic_DNA.
DR EMBL; BC046151; AAH46151.1; -; mRNA.
DR RefSeq; NP_001129201.1; NM_001135729.1.
DR RefSeq; NP_001129202.1; NM_001135730.1.
DR RefSeq; NP_001129204.1; NM_001135732.1.
DR RefSeq; NP_005479.1; NM_005488.2.
DR UniGene; Hs.474705; -.
DR PDB; 1ELK; X-ray; 1.50 A; A/B=2-153.
DR PDB; 1WRD; X-ray; 1.75 A; A=215-312.
DR PDBsum; 1ELK; -.
DR PDBsum; 1WRD; -.
DR ProteinModelPortal; O60784; -.
DR SMR; O60784; 2-153, 215-307.
DR IntAct; O60784; 11.
DR MINT; MINT-275660; -.
DR STRING; 9606.ENSP00000413697; -.
DR PhosphoSite; O60784; -.
DR PaxDb; O60784; -.
DR PRIDE; O60784; -.
DR DNASU; 10043; -.
DR Ensembl; ENST00000411850; ENSP00000413697; ENSG00000100284.
DR Ensembl; ENST00000425375; ENSP00000394924; ENSG00000100284.
DR Ensembl; ENST00000447733; ENSP00000398876; ENSG00000100284.
DR Ensembl; ENST00000449058; ENSP00000394466; ENSG00000100284.
DR GeneID; 10043; -.
DR KEGG; hsa:10043; -.
DR UCSC; uc003ann.3; human.
DR CTD; 10043; -.
DR GeneCards; GC22P035695; -.
DR H-InvDB; HIX0175450; -.
DR HGNC; HGNC:11982; TOM1.
DR HPA; HPA001749; -.
DR MIM; 604700; gene.
DR neXtProt; NX_O60784; -.
DR PharmGKB; PA36666; -.
DR eggNOG; NOG118960; -.
DR HOGENOM; HOG000285970; -.
DR HOVERGEN; HBG025068; -.
DR InParanoid; O60784; -.
DR OMA; EEPKGVT; -.
DR PhylomeDB; O60784; -.
DR EvolutionaryTrace; O60784; -.
DR GeneWiki; TOM1; -.
DR GenomeRNAi; 10043; -.
DR NextBio; 37933; -.
DR PMAP-CutDB; O60784; -.
DR PRO; PR:O60784; -.
DR ArrayExpress; O60784; -.
DR Bgee; O60784; -.
DR CleanEx; HS_TOM1; -.
DR Genevestigator; O60784; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0030276; F:clathrin binding; IDA:UniProtKB.
DR GO; GO:0006897; P:endocytosis; NAS:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; NAS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; NAS:UniProtKB.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR004152; GAT.
DR InterPro; IPR014645; TOM1.
DR InterPro; IPR002014; VHS.
DR InterPro; IPR018205; VHS_subgr.
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; Complete proteome;
KW Cytoplasm; Membrane; Phosphoprotein; Polymorphism; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1 492 Target of Myb protein 1.
FT /FTId=PRO_0000072628.
FT DOMAIN 20 152 VHS.
FT DOMAIN 215 303 GAT.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 11 11 Phosphoserine.
FT MOD_RES 160 160 Phosphoserine.
FT MOD_RES 164 164 Phosphothreonine.
FT MOD_RES 176 176 Phosphoserine (By similarity).
FT MOD_RES 355 355 Phosphoserine.
FT MOD_RES 462 462 Phosphoserine.
FT VAR_SEQ 1 33 Missing (in isoform 4).
FT /FTId=VSP_038364.
FT VAR_SEQ 123 167 Missing (in isoform 3).
FT /FTId=VSP_038365.
FT VAR_SEQ 441 442 EE -> EGK (in isoform 2 and isoform 4).
FT /FTId=VSP_038366.
FT VARIANT 84 84 R -> H (in dbSNP:rs11558473).
FT /FTId=VAR_053845.
FT VARIANT 264 264 M -> V (in dbSNP:rs34371697).
FT /FTId=VAR_034567.
FT CONFLICT 215 215 E -> G (in Ref. 3; BAG60163).
FT CONFLICT 249 249 A -> V (in Ref. 3; BAG57130).
FT CONFLICT 346 346 S -> P (in Ref. 3; BAG60163).
FT HELIX 8 10
FT HELIX 12 20
FT HELIX 30 42
FT STRAND 43 45
FT HELIX 46 58
FT HELIX 64 80
FT HELIX 83 89
FT HELIX 92 98
FT HELIX 100 103
FT TURN 105 107
FT HELIX 111 128
FT HELIX 135 147
FT HELIX 217 240
FT TURN 243 245
FT HELIX 248 274
FT HELIX 278 305
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
//
MIM
604700
*RECORD*
*FIELD* NO
604700
*FIELD* TI
*604700 TARGET OF MYB1, CHICKEN, HOMOLOG OF; TOM1
*FIELD* TX
DESCRIPTION
TOM1 is the founding member of a family of proteins involved in
read moreendocytosis. These proteins have an N-terminal Vps27/HGS (604375)/STAM
(601899) (VHS) domain, followed by a GGA (see 606004)/TOM1 (GAT) domain
(Katoh et al., 2006).
CLONING
The retroviral oncogene v-myb of avian myeloblastosis virus (AMV) and
avian leukemia virus E26 is a mutated and truncated version of the c-myb
protooncogene (see 189990), which encodes a transcription factor. In a
differential display study of v-myb oncogene-transformed chicken
myelomonocytic cells, Burk et al. (1997) identified the tom1 gene as a
specific target of the v-myb oncogene.
By assembling the sequences of a group of human TOM1 ESTs, Seroussi et
al. (1999) determined a full-length TOM1 coding sequence. The deduced
492-amino acid TOM1 protein has an N-terminal domain that shares
sequence similarity to the N-terminal domains of human HGS (604375),
human STAM (601899), and yeast VPS27, all of which are proteins
associated with vesicular trafficking at the endosome. TOM1 also has a
predicted central coiled-coil domain. Human TOM1 shares 76% amino acid
sequence identity with chicken tom1 and 89% identity with mouse Tom1,
the cDNA of which Seroussi et al. (1999) also cloned. Northern blot
analysis of human tissues detected a ubiquitously expressed 2.3-kb TOM1
transcript, with the highest expression in skeletal muscle, placenta,
heart, and liver, and lower expression in brain, lung, kidney, and
pancreas. In situ hybridization of a 17.5-day mouse embryo showed
ubiquitous Tom1 expression, with the highest level in the intestines. In
situ hybridization of a section from the mesencephalic level of adult
mouse brain detected Tom1 expression throughout brain, with high levels
in the thalamic area, cerebellum, hippocampal formation, and medial
lemniscus. In the cerebellum, Tom1 was expressed strongly in Purkinje
cells and the granular layers.
By PCR of a human liver cDNA library, Katoh et al. (2006) cloned human
TOM1. The deduced 492-amino acid protein has an N-terminal VHS domain, a
central GAT domain, and a C-terminal domain with a clathrin (see 118955)
box sequence.
GENE FUNCTION
Using yeast 2-hybrid analysis with the C-terminal portion of endofin
(608880) as bait against a human brain cDNA library, Seet et al. (2004)
identified TOM1 as an endofin binding partner. GST pull-down and
coimmunoprecipitation assays confirmed that the C-terminal region of
endofin binds to the C-terminal region of TOM1. While immunofluorescence
showed a cytosolic distribution of TOM1, density gradient analysis
showed partially overlapping expression of TOM1 and endofin in early
endosomes. Overexpression of endofin recruits TOM1 to endosomal
aggregates.
Katoh et al. (2006) stated that the GAT domain of human TOM1 interacts
with the endosomal protein TOLLIP (606277) and that the C-terminal
domain TOM1 interacts with clathrin heavy chain (CLTC; 118955). They
found that the related proteins TOM1L1 (604701) and TOM1L2 (615519) also
interacted with TOLLIP and clathrin. When coexpressed, TOM1 and TOM1L1
were recruited onto TOLLIP-positive endosomes. Katoh et al. (2006)
concluded that, in conjunction with TOLLIP, TOM1 family proteins recruit
clathrin onto endosomes and modulate endosomal function.
GENE STRUCTURE
Seroussi et al. (1999) determined that the TOM1 gene contains 15 exons,
with a 17.9-kb first intron.
MAPPING
Seroussi et al. (1999) characterized a 190.3-kb contig in human 22q13.1
and identified the TOM1 and HMG2L1 (604702) genes, as well as the
previously identified HMOX1 (141250) and MCM5 (602696) genes. The order
of these genes is cen--THC211630--HMG2L1--TOM1--HMOX1--MCM5--tel. All
are oriented in a 5-prime to 3-prime direction from centromere to
telomere. By FISH, Seroussi et al. (1999) mapped the mouse Tom1 gene to
chromosome 8C1.
*FIELD* RF
1. Burk, O.; Worpenberg, S.; Haenig, B.; Klempnauer, K. H.: tom-1,
a novel v-Myb target gene expressed in AMV- and E26-transformed myelomonocytic
cells. EMBO J. 16: 1371-1380, 1997.
2. Katoh, Y.; Imakagura, H.; Futatsumori, M.; Nakayama, K.: Recruitment
of clathrin onto endosomes by the Tom1-Tollip complex. Biochem. Biophys.
Res. Commun. 341: 143-149, 2006.
3. Seet, L.-F.; Liu, N.; Hanson, B. J.; Hong, W.: Endofin recruits
TOM1 to endosomes. J. Biol. Chem. 279: 4670-4679, 2004.
4. Seroussi, E.; Kedra, D.; Kost-Alimova, M.; Sandberg-Nordqvist,
A.-C.; Fransson, I.; Jacobs, J. F. M.; Fu, Y.; Pan, H.-Q.; Roe, B.
A.; Imreh, S.; Dumanski, J. P.: TOM1 genes map to human chromosome
22q13.1 and mouse chromosome 8C1 and encode proteins similar to the
endosomal proteins HGS and STAM. Genomics 57: 380-388, 1999.
*FIELD* CN
Laura L. Baxter - updated: 8/30/2004
*FIELD* CD
Patti M. Sherman: 3/20/2000
*FIELD* ED
carol: 01/30/2014
mgross: 11/15/2013
mcolton: 11/11/2013
carol: 9/8/2010
terry: 2/3/2006
alopez: 8/30/2004
mcapotos: 3/30/2000
psherman: 3/21/2000
*RECORD*
*FIELD* NO
604700
*FIELD* TI
*604700 TARGET OF MYB1, CHICKEN, HOMOLOG OF; TOM1
*FIELD* TX
DESCRIPTION
TOM1 is the founding member of a family of proteins involved in
read moreendocytosis. These proteins have an N-terminal Vps27/HGS (604375)/STAM
(601899) (VHS) domain, followed by a GGA (see 606004)/TOM1 (GAT) domain
(Katoh et al., 2006).
CLONING
The retroviral oncogene v-myb of avian myeloblastosis virus (AMV) and
avian leukemia virus E26 is a mutated and truncated version of the c-myb
protooncogene (see 189990), which encodes a transcription factor. In a
differential display study of v-myb oncogene-transformed chicken
myelomonocytic cells, Burk et al. (1997) identified the tom1 gene as a
specific target of the v-myb oncogene.
By assembling the sequences of a group of human TOM1 ESTs, Seroussi et
al. (1999) determined a full-length TOM1 coding sequence. The deduced
492-amino acid TOM1 protein has an N-terminal domain that shares
sequence similarity to the N-terminal domains of human HGS (604375),
human STAM (601899), and yeast VPS27, all of which are proteins
associated with vesicular trafficking at the endosome. TOM1 also has a
predicted central coiled-coil domain. Human TOM1 shares 76% amino acid
sequence identity with chicken tom1 and 89% identity with mouse Tom1,
the cDNA of which Seroussi et al. (1999) also cloned. Northern blot
analysis of human tissues detected a ubiquitously expressed 2.3-kb TOM1
transcript, with the highest expression in skeletal muscle, placenta,
heart, and liver, and lower expression in brain, lung, kidney, and
pancreas. In situ hybridization of a 17.5-day mouse embryo showed
ubiquitous Tom1 expression, with the highest level in the intestines. In
situ hybridization of a section from the mesencephalic level of adult
mouse brain detected Tom1 expression throughout brain, with high levels
in the thalamic area, cerebellum, hippocampal formation, and medial
lemniscus. In the cerebellum, Tom1 was expressed strongly in Purkinje
cells and the granular layers.
By PCR of a human liver cDNA library, Katoh et al. (2006) cloned human
TOM1. The deduced 492-amino acid protein has an N-terminal VHS domain, a
central GAT domain, and a C-terminal domain with a clathrin (see 118955)
box sequence.
GENE FUNCTION
Using yeast 2-hybrid analysis with the C-terminal portion of endofin
(608880) as bait against a human brain cDNA library, Seet et al. (2004)
identified TOM1 as an endofin binding partner. GST pull-down and
coimmunoprecipitation assays confirmed that the C-terminal region of
endofin binds to the C-terminal region of TOM1. While immunofluorescence
showed a cytosolic distribution of TOM1, density gradient analysis
showed partially overlapping expression of TOM1 and endofin in early
endosomes. Overexpression of endofin recruits TOM1 to endosomal
aggregates.
Katoh et al. (2006) stated that the GAT domain of human TOM1 interacts
with the endosomal protein TOLLIP (606277) and that the C-terminal
domain TOM1 interacts with clathrin heavy chain (CLTC; 118955). They
found that the related proteins TOM1L1 (604701) and TOM1L2 (615519) also
interacted with TOLLIP and clathrin. When coexpressed, TOM1 and TOM1L1
were recruited onto TOLLIP-positive endosomes. Katoh et al. (2006)
concluded that, in conjunction with TOLLIP, TOM1 family proteins recruit
clathrin onto endosomes and modulate endosomal function.
GENE STRUCTURE
Seroussi et al. (1999) determined that the TOM1 gene contains 15 exons,
with a 17.9-kb first intron.
MAPPING
Seroussi et al. (1999) characterized a 190.3-kb contig in human 22q13.1
and identified the TOM1 and HMG2L1 (604702) genes, as well as the
previously identified HMOX1 (141250) and MCM5 (602696) genes. The order
of these genes is cen--THC211630--HMG2L1--TOM1--HMOX1--MCM5--tel. All
are oriented in a 5-prime to 3-prime direction from centromere to
telomere. By FISH, Seroussi et al. (1999) mapped the mouse Tom1 gene to
chromosome 8C1.
*FIELD* RF
1. Burk, O.; Worpenberg, S.; Haenig, B.; Klempnauer, K. H.: tom-1,
a novel v-Myb target gene expressed in AMV- and E26-transformed myelomonocytic
cells. EMBO J. 16: 1371-1380, 1997.
2. Katoh, Y.; Imakagura, H.; Futatsumori, M.; Nakayama, K.: Recruitment
of clathrin onto endosomes by the Tom1-Tollip complex. Biochem. Biophys.
Res. Commun. 341: 143-149, 2006.
3. Seet, L.-F.; Liu, N.; Hanson, B. J.; Hong, W.: Endofin recruits
TOM1 to endosomes. J. Biol. Chem. 279: 4670-4679, 2004.
4. Seroussi, E.; Kedra, D.; Kost-Alimova, M.; Sandberg-Nordqvist,
A.-C.; Fransson, I.; Jacobs, J. F. M.; Fu, Y.; Pan, H.-Q.; Roe, B.
A.; Imreh, S.; Dumanski, J. P.: TOM1 genes map to human chromosome
22q13.1 and mouse chromosome 8C1 and encode proteins similar to the
endosomal proteins HGS and STAM. Genomics 57: 380-388, 1999.
*FIELD* CN
Laura L. Baxter - updated: 8/30/2004
*FIELD* CD
Patti M. Sherman: 3/20/2000
*FIELD* ED
carol: 01/30/2014
mgross: 11/15/2013
mcolton: 11/11/2013
carol: 9/8/2010
terry: 2/3/2006
alopez: 8/30/2004
mcapotos: 3/30/2000
psherman: 3/21/2000