TOB2_HUMAN
ID TOB2_HUMAN Reviewed; 344 AA.
AC Q14106; Q6FHR7; Q6PIT9; Q9BY97; Q9UBI0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Protein Tob2;
DE AltName: Full=Protein Tob4;
DE AltName: Full=Transducer of erbB-2 2;
GN Name=TOB2; Synonyms=KIAA1663, TOB4, TROB2;
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=10602502; DOI=10.1038/sj.onc.1203193;
RA Ikematsu N., Yoshida Y., Kawamura-Tsuzuku J., Ohsugi M., Onda M., Hirai M.,
RA Fujimoto J., Yamamoto T.;
RT "Tob2, a novel anti-proliferative Tob/BTG1 family member, associates with a
RT component of the CCR4 transcriptional regulatory complex capable of binding
RT cyclin-dependent kinases.";
RL Oncogene 18:7432-7441(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=11258795; DOI=10.1093/dnares/8.1.1;
RA Hirosawa M., Nagase T., Murahashi Y., Kikuno R., Ohara O.;
RT "Identification of novel transcribed sequences on human chromosome 22 by
RT expressed sequence tag mapping.";
RL DNA Res. 8:1-9(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254, AND IDENTIFICATION BY
RP 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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Anti-proliferative protein inhibits cell cycle progression
CC from the G0/G1 to S phases.
CC -!- SUBUNIT: Associates with CAF1.
CC -!- INTERACTION:
CC Q14106; O14503: BHLHE40; NbExp=3; IntAct=EBI-2562000, EBI-711810;
CC Q14106; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-2562000, EBI-742887;
CC Q14106; Q9UIV1: CNOT7; NbExp=7; IntAct=EBI-2562000, EBI-2105113;
CC Q14106; Q9UFF9: CNOT8; NbExp=3; IntAct=EBI-2562000, EBI-742299;
CC Q14106; P11940: PABPC1; NbExp=6; IntAct=EBI-2562000, EBI-81531;
CC Q14106; Q60809: Cnot7; Xeno; NbExp=4; IntAct=EBI-2562000, EBI-2104739;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q14106-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14106-2; Sequence=VSP_055557;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the BTG family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB33333.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D64109; BAA10971.1; -; mRNA.
DR EMBL; AB035207; BAA87042.1; -; mRNA.
DR EMBL; AB051450; BAB33333.1; ALT_INIT; mRNA.
DR EMBL; CR456594; CAG30480.1; -; mRNA.
DR EMBL; CR541684; CAG46485.1; -; mRNA.
DR EMBL; AL008582; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028919; AAH28919.1; -; mRNA.
DR EMBL; BC038957; AAH38957.1; -; mRNA.
DR CCDS; CCDS14015.1; -. [Q14106-1]
DR RefSeq; NP_057356.1; NM_016272.3. [Q14106-1]
DR RefSeq; XP_005261372.1; XM_005261315.2. [Q14106-1]
DR RefSeq; XP_006724168.1; XM_006724105.3. [Q14106-1]
DR RefSeq; XP_016884028.1; XM_017028539.1. [Q14106-1]
DR AlphaFoldDB; Q14106; -.
DR SMR; Q14106; -.
DR BioGRID; 115985; 31.
DR DIP; DIP-41990N; -.
DR ELM; Q14106; -.
DR IntAct; Q14106; 13.
DR MINT; Q14106; -.
DR STRING; 9606.ENSP00000331305; -.
DR iPTMnet; Q14106; -.
DR PhosphoSitePlus; Q14106; -.
DR BioMuta; TOB2; -.
DR DMDM; 12643431; -.
DR EPD; Q14106; -.
DR jPOST; Q14106; -.
DR MassIVE; Q14106; -.
DR MaxQB; Q14106; -.
DR PaxDb; Q14106; -.
DR PeptideAtlas; Q14106; -.
DR PRIDE; Q14106; -.
DR ProteomicsDB; 59815; -. [Q14106-1]
DR Antibodypedia; 26928; 157 antibodies from 26 providers.
DR DNASU; 10766; -.
DR Ensembl; ENST00000327492.4; ENSP00000331305.3; ENSG00000183864.5. [Q14106-1]
DR GeneID; 10766; -.
DR KEGG; hsa:10766; -.
DR MANE-Select; ENST00000327492.4; ENSP00000331305.3; NM_016272.4; NP_057356.1.
DR UCSC; uc003azz.2; human. [Q14106-1]
DR CTD; 10766; -.
DR DisGeNET; 10766; -.
DR GeneCards; TOB2; -.
DR HGNC; HGNC:11980; TOB2.
DR HPA; ENSG00000183864; Low tissue specificity.
DR MIM; 607396; gene.
DR neXtProt; NX_Q14106; -.
DR OpenTargets; ENSG00000183864; -.
DR PharmGKB; PA36664; -.
DR VEuPathDB; HostDB:ENSG00000183864; -.
DR eggNOG; KOG4006; Eukaryota.
DR GeneTree; ENSGT00940000154208; -.
DR HOGENOM; CLU_034687_0_0_1; -.
DR InParanoid; Q14106; -.
DR OMA; TQPMQPH; -.
DR OrthoDB; 1439942at2759; -.
DR PhylomeDB; Q14106; -.
DR TreeFam; TF105274; -.
DR PathwayCommons; Q14106; -.
DR SignaLink; Q14106; -.
DR BioGRID-ORCS; 10766; 15 hits in 1082 CRISPR screens.
DR ChiTaRS; TOB2; human.
DR GeneWiki; TOB2; -.
DR GenomeRNAi; 10766; -.
DR Pharos; Q14106; Tbio.
DR PRO; PR:Q14106; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q14106; protein.
DR Bgee; ENSG00000183864; Expressed in cranial nerve II and 208 other tissues.
DR ExpressionAtlas; Q14106; baseline and differential.
DR Genevisible; Q14106; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042809; F:nuclear vitamin D receptor binding; IEA:Ensembl.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0007292; P:female gamete generation; TAS:ProtInc.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0030316; P:osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0045778; P:positive regulation of ossification; IEA:Ensembl.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR Gene3D; 3.90.640.90; -; 1.
DR InterPro; IPR002087; Anti_prolifrtn.
DR InterPro; IPR009818; Ataxin-2_C.
DR InterPro; IPR036054; BTG-like_sf.
DR InterPro; IPR015676; Tob1/2.
DR InterPro; IPR015678; Tob2.
DR PANTHER; PTHR17537; PTHR17537; 1.
DR PANTHER; PTHR17537:SF3; PTHR17537:SF3; 1.
DR Pfam; PF07742; BTG; 1.
DR Pfam; PF07145; PAM2; 2.
DR PRINTS; PR00310; ANTIPRLFBTG1.
DR SMART; SM00099; btg1; 1.
DR SUPFAM; SSF160696; SSF160696; 1.
DR PROSITE; PS00960; BTG_1; 1.
DR PROSITE; PS01203; BTG_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..344
FT /note="Protein Tob2"
FT /id="PRO_0000143815"
FT REGION 144..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VAR_SEQ 245..344
FT /note="ANPAPQSQLSPNAKEFVYNGGGSPSLFFDAADGQGSGTPGPFGGSGAGTCNS
FT SSFDMAQVFGGGANSLFLEKTPFVEGLSYNLNTMQYPSQQFQPVVLAN -> DYNHDQ
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055557"
FT CONFLICT 34..35
FT /note="RL -> QA (in Ref. 1; BAA10971)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="P -> H (in Ref. 1; BAA10971)"
FT /evidence="ECO:0000305"
FT CONFLICT 278..317
FT /note="QGSGTPGPFGGSGAGTCNSSSFDMAQVFGGGANSLFLEKT -> RAAAPQAR
FT LEAVGLAPATAAALTWPRYLEVVPTASSWRRH (in Ref. 1; BAA10971)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 344 AA; 36632 MW; ACE4CD8939641BD5 CRC64;
MQLEIKVALN FIISYLYNKL PRRRADLFGE ELERLLKKKY EGHWYPEKPL KGSGFRCVHI
GEMVDPVVEL AAKRSGLAVE DVRANVPEEL SVWIDPFEVS YQIGEKGAVK VLYLDDSEGC
GAPELDKEIK SSFNPDAQVF VPIGSQDSSL SNSPSPSFGQ SPSPTFIPRS AQPITFTTAS
FAATKFGSTK MKKGGGAASG GGVASSGAGG QQPPQQPRMA RSPTNSLLKH KSLSLSMHSL
NFITANPAPQ SQLSPNAKEF VYNGGGSPSL FFDAADGQGS GTPGPFGGSG AGTCNSSSFD
MAQVFGGGAN SLFLEKTPFV EGLSYNLNTM QYPSQQFQPV VLAN
