TOM1_MOUSE
ID TOM1_MOUSE Reviewed; 492 AA.
AC O88746; Q3V4C6; Q9D120;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Target of Myb protein 1;
GN Name=Tom1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160; THR-164; SER-176;
RP SER-180 AND SER-208, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:0000250}.
CC -!- INTERACTION:
CC O88746; Q9QZ06: Tollip; NbExp=2; IntAct=EBI-74264, EBI-74272;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Membrane {ECO:0000305};
CC Peripheral membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O88746-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O88746-2; Sequence=VSP_003991, VSP_003992;
CC -!- TISSUE SPECIFICITY: Ubiquitous. In adult brain, it is highly expressed
CC at the mesencephalic level, in the hippocampal formation and medial
CC lemniscus. In cerebellum, it is highly expressed in Purkinje cells and
CC granular layers.
CC -!- DEVELOPMENTAL STAGE: Ubiquitously expressed in the embryo, with a
CC higher expression in the intestines.
CC -!- SIMILARITY: Belongs to the TOM1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ006972; CAA07361.1; -; mRNA.
DR EMBL; AK004063; BAE43160.1; -; mRNA.
DR EMBL; AK028398; BAC25932.1; -; mRNA.
DR EMBL; BC021633; AAH21633.1; -; mRNA.
DR CCDS; CCDS52601.1; -. [O88746-1]
DR RefSeq; NP_035752.1; NM_011622.3. [O88746-1]
DR AlphaFoldDB; O88746; -.
DR SMR; O88746; -.
DR BioGRID; 204274; 8.
DR IntAct; O88746; 3.
DR STRING; 10090.ENSMUSP00000077891; -.
DR iPTMnet; O88746; -.
DR PhosphoSitePlus; O88746; -.
DR EPD; O88746; -.
DR jPOST; O88746; -.
DR MaxQB; O88746; -.
DR PaxDb; O88746; -.
DR PeptideAtlas; O88746; -.
DR PRIDE; O88746; -.
DR ProteomicsDB; 258813; -. [O88746-1]
DR ProteomicsDB; 258814; -. [O88746-2]
DR Antibodypedia; 208; 206 antibodies from 27 providers.
DR DNASU; 21968; -.
DR Ensembl; ENSMUST00000165630; ENSMUSP00000130854; ENSMUSG00000042870. [O88746-1]
DR GeneID; 21968; -.
DR KEGG; mmu:21968; -.
DR UCSC; uc009mha.2; mouse. [O88746-1]
DR UCSC; uc009mhb.2; mouse. [O88746-2]
DR CTD; 10043; -.
DR MGI; MGI:1338026; Tom1.
DR VEuPathDB; HostDB:ENSMUSG00000042870; -.
DR eggNOG; KOG1087; Eukaryota.
DR GeneTree; ENSGT00940000156865; -.
DR HOGENOM; CLU_043812_3_0_1; -.
DR InParanoid; O88746; -.
DR OMA; RETHRVS; -.
DR PhylomeDB; O88746; -.
DR TreeFam; TF314105; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 21968; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Tom1; mouse.
DR PRO; PR:O88746; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; O88746; protein.
DR Bgee; ENSMUSG00000042870; Expressed in lens of camera-type eye and 67 other tissues.
DR ExpressionAtlas; O88746; baseline and differential.
DR Genevisible; O88746; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0030276; F:clathrin binding; ISO:MGI.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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 Acetylation; Alternative splicing; Cytoplasm; Isopeptide bond; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport;
KW Ubl conjugation.
FT CHAIN 1..492
FT /note="Target of Myb protein 1"
FT /id="PRO_0000072629"
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 167..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..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:0000250|UniProtKB:O60784"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60784"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 164
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60784"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60784"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60784"
FT CROSSLNK 385
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60784"
FT VAR_SEQ 1..324
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_003991"
FT VAR_SEQ 325..343
FT /note="MGPDPAATNNLSSQLAGMN -> MGRANGTAGLLPGPSVSAD (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_003992"
SQ SEQUENCE 492 AA; 54325 MW; A15F24FD9B4D31C3 CRC64;
MDFLLGNPFS SPVGQRIEKA TDGSLQSEDW ALNMEICDII NETEEGPKDA FRAVKKRIMG
NKNFHEVMLA LTVLETCVKN CGHRFHVLVA NQDFVENVLV RTILPKNNPP TIVHDKVLNL
IQSWADAFRS SPDLTGVVAV YEDLRRKGLE FPMTDLDMLS PIHTPQRTVF NSETPSRQNS
VSSNTSQRGD LSQHATPLPT PAVLPGDSPI TPTPEQIGKL RSELEMVSGN VRVMSEMLTE
LVPTQVEPAD LELLQELNRT CRAMQQRILE LIPRISNEQL TEELLMINDN LNNVFLRHER
FERFRTGQTA KASSEAELAT DLIDMGPDPA ATNNLSSQLA GMNLGSRSVR AGLQSLETSG
HLEDDFDMFA LTRGSSLADQ RKGVKYEAPQ TTDGLAGALD ARQQSTGAIP ATQARIMEDI
EQWLSTDVGN SAEEPSGVTS EEFDKFLEER AKAADRLPNL ASPSAEGPPR PSPGTAPRRK
TQEKDDDMLF AL
