LIN9_MOUSE
ID LIN9_MOUSE Reviewed; 542 AA.
AC Q8C735; Q5TKA0; Q8C9D8;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Protein lin-9 homolog;
DE Short=mLin-9;
DE AltName: Full=TUDOR gene similar 1 protein;
DE AltName: Full=Type I interferon receptor beta chain-associated protein;
GN Name=Lin9; Synonyms=Bara, Tgs1;
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 [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 2-205 (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Kidney, and 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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-537 (ISOFORM 1).
RX PubMed=16730350; DOI=10.1016/j.yexcr.2006.04.002;
RA Sandoval R., Xue J., Tian X., Barrett K., Pilkinton M., Ucker D.S.,
RA Raychaudhuri P., Kineman R.D., Luque R.M., Baida G., Zou X., Valli V.E.,
RA Cook J.L., Kiyokawa H., Colamonici O.R.;
RT "A mutant allele of BARA/LIN-9 rescues the cdk4-/- phenotype by releasing
RT the repression on E2F-regulated genes.";
RL Exp. Cell Res. 312:2465-2475(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95; THR-304; SER-309 AND
RP SER-321, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, 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: Acts as a tumor suppressor. Inhibits DNA synthesis. Its
CC ability to inhibit oncogenic transformation is mediated through its
CC association with RB1. Plays a role in the expression of genes required
CC for the G1/S transition (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the DREAM complex (also named LINC complex) at
CC least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2,
CC RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in quiescent
CC cells where it represses cell cycle-dependent genes. It dissociates in
CC S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds
CC to MYBL2. Interacts with RB1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. Note=Found in
CC perinucleolar structures. Associated with chromatin. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8C735-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C735-2; Sequence=VSP_020513;
CC Name=3;
CC IsoId=Q8C735-3; Sequence=VSP_020511, VSP_020512;
CC -!- SIMILARITY: Belongs to the lin-9 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ13712.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC31235.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK042357; BAC31235.1; ALT_FRAME; mRNA.
DR EMBL; AK052618; BAC35065.1; -; mRNA.
DR EMBL; AF190325; AAQ13712.1; ALT_INIT; mRNA.
DR CCDS; CCDS48468.2; -. [Q8C735-1]
DR AlphaFoldDB; Q8C735; -.
DR SMR; Q8C735; -.
DR STRING; 10090.ENSMUSP00000082959; -.
DR iPTMnet; Q8C735; -.
DR PhosphoSitePlus; Q8C735; -.
DR EPD; Q8C735; -.
DR jPOST; Q8C735; -.
DR MaxQB; Q8C735; -.
DR PaxDb; Q8C735; -.
DR PeptideAtlas; Q8C735; -.
DR PRIDE; Q8C735; -.
DR ProteomicsDB; 286206; -. [Q8C735-1]
DR ProteomicsDB; 286207; -. [Q8C735-2]
DR ProteomicsDB; 286208; -. [Q8C735-3]
DR UCSC; uc007dwk.3; mouse. [Q8C735-1]
DR UCSC; uc007dwl.3; mouse. [Q8C735-2]
DR MGI; MGI:1919818; Lin9.
DR eggNOG; KOG1019; Eukaryota.
DR InParanoid; Q8C735; -.
DR PhylomeDB; Q8C735; -.
DR TreeFam; TF314315; -.
DR Reactome; R-MMU-1538133; G0 and Early G1.
DR ChiTaRS; Lin9; mouse.
DR PRO; PR:Q8C735; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8C735; protein.
DR Genevisible; Q8C735; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0017053; C:transcription repressor complex; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0000003; P:reproduction; IBA:GO_Central.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR033471; DIRP.
DR InterPro; IPR010561; LIN-9/ALY1.
DR InterPro; IPR045831; LIN9_C.
DR PANTHER; PTHR21689; PTHR21689; 1.
DR Pfam; PF06584; DIRP; 1.
DR Pfam; PF19438; LIN9_C; 1.
DR SMART; SM01135; DIRP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell cycle; Coiled coil; DNA synthesis;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Tumor suppressor; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q5TKA1"
FT CHAIN 2..542
FT /note="Protein lin-9 homolog"
FT /id="PRO_0000249548"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q5TKA1"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5TKA1"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 96
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5TKA1"
FT MOD_RES 304
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 21
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5TKA1"
FT VAR_SEQ 176..205
FT /note="CSSAFFEEERSALKQKRQKIRLLQQRKVAD -> EISLKTEAAENQAVTTKE
FT SCRCFTVQRSPR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020511"
FT VAR_SEQ 206..542
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020512"
FT VAR_SEQ 416..542
FT /note="LAPDQGLQPADQPTDMRRRCEEEAQEIVRQANSASGQPCVENENLTDLISRL
FT TAILLQIKCLAEGGDLNSFEFKSLTDSLNDIKNTIDASNISCFQNNVEIHVAHIQSGLS
FT QMGNLHAFAANNTNRD -> VSGVYCFHWCFVLFCFVILVFFEMGSHSVAMAALETSLA
FT SSSEIRLFLPPSAGIKGVRHHAQPNVCCFPSMFCYLKLNDFTFTFCKL (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020513"
FT CONFLICT 152
FT /note="N -> K (in Ref. 1; BAC35065)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 542 AA; 61759 MW; 9F99F9DB3D2568E4 CRC64;
MAELDQLPDE SSSAKALVSL KEGSLSNTWN EKYSSLQKTP VWKGRNAGPA VEMPFRNSKR
SRLFSDEDDR QINTKSPKRN QRVAMIPQKF TATMSTPDKK ASQKIGFRLR NLLKLPKAHK
WCIYEWFYSN IDKPLFEGDN DFCVCLKESF PNLKTRKLTR VEWGKIRRLM GKPRRCSSAF
FEEERSALKQ KRQKIRLLQQ RKVADVSQFK DLPDEIPLPL VIGTKVTARL RGIHDGLFTG
QIDAVDTLNA TYRVTFDRTG LGTHTIPDYE VLSNEPHETM PISAFGQKQR PSRFFMTPPR
LHYTPPLQSP ITDGDPLLGQ SPWRSKVSGS DTETLGGFPV EFLIQVTKLS KILMIKKEHI
KKLREMNTEA EKLKSYSMPI GIEFQRRYAT IVLELEQLNK DLNKVLHKVQ QYCYELAPDQ
GLQPADQPTD MRRRCEEEAQ EIVRQANSAS GQPCVENENL TDLISRLTAI LLQIKCLAEG
GDLNSFEFKS LTDSLNDIKN TIDASNISCF QNNVEIHVAH IQSGLSQMGN LHAFAANNTN
RD
