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Protein Tob2 (Protein Tob4) (Transducer of erbB-2 2)

 TOB2_HUMAN              Reviewed;         344 AA.
Q14106; Q6FHR7; Q6PIT9; Q9BY97; Q9UBI0;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
24-JAN-2001, sequence version 2.
12-SEP-2018, entry version 147.
RecName: Full=Protein Tob2;
AltName: Full=Protein Tob4;
AltName: Full=Transducer of erbB-2 2;
Name=TOB2; Synonyms=KIAA1663, TOB4, TROB2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=10602502; DOI=10.1038/sj.onc.1203193;
Ikematsu N., Yoshida Y., Kawamura-Tsuzuku J., Ohsugi M., Onda M.,
Hirai M., Fujimoto J., Yamamoto T.;
"Tob2, a novel anti-proliferative Tob/BTG1 family member, associates
with a component of the CCR4 transcriptional regulatory complex
capable of binding cyclin-dependent kinases.";
Oncogene 18:7432-7441(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=11258795; DOI=10.1093/dnares/8.1.1;
Hirosawa M., Nagase T., Murahashi Y., Kikuno R., Ohara O.;
"Identification of novel transcribed sequences on human chromosome 22
by expressed sequence tag mapping.";
DNA Res. 8:1-9(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- FUNCTION: Anti-proliferative protein inhibits cell cycle
progression from the G0/G1 to S phases.
-!- SUBUNIT: Associates with CAF1.
-!- INTERACTION:
Q9UFF9:-; NbExp=3; IntAct=EBI-2562000, EBI-742299;
O14503:BHLHE40; NbExp=3; IntAct=EBI-2562000, EBI-711810;
Q8TAP6:CEP76; NbExp=3; IntAct=EBI-2562000, EBI-742887;
Q9UIV1:CNOT7; NbExp=5; IntAct=EBI-2562000, EBI-2105113;
Q60809:Cnot7 (xeno); NbExp=4; IntAct=EBI-2562000, EBI-2104739;
P11940:PABPC1; NbExp=4; IntAct=EBI-2562000, EBI-81531;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q14106-1; Sequence=Displayed;
Name=2;
IsoId=Q14106-2; Sequence=VSP_055557;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- SIMILARITY: Belongs to the BTG family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB33333.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; D64109; BAA10971.1; -; mRNA.
EMBL; AB035207; BAA87042.1; -; mRNA.
EMBL; AB051450; BAB33333.1; ALT_INIT; mRNA.
EMBL; CR456594; CAG30480.1; -; mRNA.
EMBL; CR541684; CAG46485.1; -; mRNA.
EMBL; AL008582; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC028919; AAH28919.1; -; mRNA.
EMBL; BC038957; AAH38957.1; -; mRNA.
CCDS; CCDS14015.1; -. [Q14106-1]
RefSeq; NP_057356.1; NM_016272.3. [Q14106-1]
RefSeq; XP_005261372.1; XM_005261315.2. [Q14106-1]
RefSeq; XP_006724168.1; XM_006724105.3. [Q14106-1]
RefSeq; XP_016884028.1; XM_017028539.1. [Q14106-1]
UniGene; Hs.474978; -.
ProteinModelPortal; Q14106; -.
SMR; Q14106; -.
BioGrid; 115985; 14.
DIP; DIP-41990N; -.
ELM; Q14106; -.
IntAct; Q14106; 11.
MINT; Q14106; -.
STRING; 9606.ENSP00000331305; -.
iPTMnet; Q14106; -.
PhosphoSitePlus; Q14106; -.
BioMuta; TOB2; -.
DMDM; 12643431; -.
EPD; Q14106; -.
MaxQB; Q14106; -.
PaxDb; Q14106; -.
PeptideAtlas; Q14106; -.
PRIDE; Q14106; -.
ProteomicsDB; 59815; -.
DNASU; 10766; -.
Ensembl; ENST00000327492; ENSP00000331305; ENSG00000183864. [Q14106-1]
GeneID; 10766; -.
KEGG; hsa:10766; -.
UCSC; uc003azz.2; human. [Q14106-1]
CTD; 10766; -.
DisGeNET; 10766; -.
EuPathDB; HostDB:ENSG00000183864.4; -.
GeneCards; TOB2; -.
HGNC; HGNC:11980; TOB2.
HPA; HPA016603; -.
HPA; HPA054112; -.
MIM; 607396; gene.
neXtProt; NX_Q14106; -.
OpenTargets; ENSG00000183864; -.
PharmGKB; PA36664; -.
eggNOG; KOG4006; Eukaryota.
eggNOG; ENOG410ZZC0; LUCA.
GeneTree; ENSGT00550000074461; -.
HOGENOM; HOG000253939; -.
HOVERGEN; HBG006617; -.
InParanoid; Q14106; -.
KO; K14443; -.
OMA; MQYPSQS; -.
OrthoDB; EOG091G0LEQ; -.
PhylomeDB; Q14106; -.
TreeFam; TF105274; -.
ChiTaRS; TOB2; human.
GeneWiki; TOB2; -.
GenomeRNAi; 10766; -.
PRO; PR:Q14106; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000183864; Expressed in 214 organ(s), highest expression level in paraflocculus.
CleanEx; HS_TOB2; -.
ExpressionAtlas; Q14106; baseline and differential.
Genevisible; Q14106; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
GO; GO:0042809; F:vitamin D receptor binding; IEA:Ensembl.
GO; GO:0007292; P:female gamete generation; TAS:ProtInc.
GO; GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
GO; GO:0045671; P:negative regulation of osteoclast differentiation; IEA:Ensembl.
GO; GO:0045778; P:positive regulation of ossification; IEA:Ensembl.
GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
GO; GO:0023052; P:signaling; IBA:GO_Central.
Gene3D; 1.20.120.1120; -; 1.
InterPro; IPR002087; Anti_prolifrtn.
InterPro; IPR009818; Ataxin-2_C.
InterPro; IPR036054; BTG-like_sf.
InterPro; IPR015676; Tob1/2.
InterPro; IPR015678; Tob2.
PANTHER; PTHR17537; PTHR17537; 1.
PANTHER; PTHR17537:SF3; PTHR17537:SF3; 1.
Pfam; PF07742; BTG; 1.
Pfam; PF07145; PAM2; 2.
PRINTS; PR00310; ANTIPRLFBTG1.
SMART; SM00099; btg1; 1.
SUPFAM; SSF160696; SSF160696; 1.
PROSITE; PS00960; BTG_1; 1.
PROSITE; PS01203; BTG_2; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; Phosphoprotein;
Reference proteome.
CHAIN 1 344 Protein Tob2.
/FTId=PRO_0000143815.
MOD_RES 254 254 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
VAR_SEQ 245 344 ANPAPQSQLSPNAKEFVYNGGGSPSLFFDAADGQGSGTPGP
FGGSGAGTCNSSSFDMAQVFGGGANSLFLEKTPFVEGLSYN
LNTMQYPSQQFQPVVLAN -> DYNHDQ (in isoform
2). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_055557.
CONFLICT 34 35 RL -> QA (in Ref. 1; BAA10971).
{ECO:0000305}.
CONFLICT 214 214 P -> H (in Ref. 1; BAA10971).
{ECO:0000305}.
CONFLICT 278 317 QGSGTPGPFGGSGAGTCNSSSFDMAQVFGGGANSLFLEKT
-> RAAAPQARLEAVGLAPATAAALTWPRYLEVVPTASSWR
RH (in Ref. 1; BAA10971). {ECO:0000305}.
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


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