SPNDC_MOUSE
ID SPNDC_MOUSE Reviewed; 381 AA.
AC Q05AH6; Q3TI49; Q3TQH2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Spindlin interactor and repressor of chromatin-binding protein {ECO:0000305};
DE AltName: Full=SPIN1-docking protein {ECO:0000303|PubMed:29061846};
DE Short=SPIN-DOC {ECO:0000303|PubMed:29061846};
GN Name=Spindoc {ECO:0000303|PubMed:29061846, ECO:0000312|MGI:MGI:2147611};
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Adipose tissue;
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 [LARGE SCALE MRNA] (ISOFORM 1).
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249 AND SER-313, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas, 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).
RN [4]
RP FUNCTION.
RX PubMed=29061846; DOI=10.1074/jbc.m117.814913;
RA Bae N., Gao M., Li X., Premkumar T., Sbardella G., Chen J., Bedford M.T.;
RT "A transcriptional coregulator, SPIN-DOC, attenuates the coactivator
RT activity of Spindlin1.";
RL J. Biol. Chem. 292:20808-20817(2017).
CC -!- FUNCTION: Negatively regulates the transcriptional activator activity
CC of SPIN1 via inhibition of its histone methyl-binding ability.
CC Represses the expression of a number of SPIN1-regulated genes and the
CC SPIN1-mediated activation of the Wnt signaling pathway
CC (PubMed:29061846). Can also inhibit the histone methyl-binding
CC abilities of SPIN2A, SPIN2B, SPIN3 and SPIN4 (By similarity).
CC {ECO:0000250|UniProtKB:Q9BUA3, ECO:0000269|PubMed:29061846}.
CC -!- SUBUNIT: Interacts with SPIN1, SPIN2A, SPIN2B, SPIN3 and SPIN4.
CC Interacts with TCF7L2 in a SPIN1-dependent manner.
CC {ECO:0000250|UniProtKB:Q9BUA3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q05AH6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q05AH6-2; Sequence=VSP_031789, VSP_031790;
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DR EMBL; AK163590; BAE37410.1; -; mRNA.
DR EMBL; AK168010; BAE39997.1; -; mRNA.
DR EMBL; BC125249; AAI25250.1; -; mRNA.
DR CCDS; CCDS29523.1; -. [Q05AH6-1]
DR RefSeq; NP_001028311.2; NM_001033139.3. [Q05AH6-1]
DR RefSeq; NP_001161303.1; NM_001167831.1. [Q05AH6-2]
DR AlphaFoldDB; Q05AH6; -.
DR SMR; Q05AH6; -.
DR STRING; 10090.ENSMUSP00000025924; -.
DR iPTMnet; Q05AH6; -.
DR PhosphoSitePlus; Q05AH6; -.
DR EPD; Q05AH6; -.
DR jPOST; Q05AH6; -.
DR MaxQB; Q05AH6; -.
DR PaxDb; Q05AH6; -.
DR PeptideAtlas; Q05AH6; -.
DR PRIDE; Q05AH6; -.
DR ProteomicsDB; 257353; -. [Q05AH6-1]
DR ProteomicsDB; 257354; -. [Q05AH6-2]
DR Antibodypedia; 51569; 49 antibodies from 12 providers.
DR Ensembl; ENSMUST00000025924; ENSMUSP00000025924; ENSMUSG00000024970. [Q05AH6-1]
DR GeneID; 68229; -.
DR KEGG; mmu:68229; -.
DR UCSC; uc008gkv.2; mouse. [Q05AH6-1]
DR UCSC; uc008gkw.2; mouse. [Q05AH6-2]
DR CTD; 144097; -.
DR MGI; MGI:2147611; Spindoc.
DR VEuPathDB; HostDB:ENSMUSG00000024970; -.
DR eggNOG; ENOG502S4I6; Eukaryota.
DR GeneTree; ENSGT00410000025985; -.
DR HOGENOM; CLU_061399_0_0_1; -.
DR InParanoid; Q05AH6; -.
DR OMA; DTARSHI; -.
DR OrthoDB; 570589at2759; -.
DR PhylomeDB; Q05AH6; -.
DR TreeFam; TF337165; -.
DR BioGRID-ORCS; 68229; 6 hits in 72 CRISPR screens.
DR ChiTaRS; Spindoc; mouse.
DR PRO; PR:Q05AH6; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q05AH6; protein.
DR Bgee; ENSMUSG00000024970; Expressed in ventricular zone and 177 other tissues.
DR ExpressionAtlas; Q05AH6; baseline and differential.
DR Genevisible; Q05AH6; MM.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR InterPro; IPR040647; SPIN-DOC_Znf-C2H2.
DR Pfam; PF18658; zf-C2H2_12; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Isopeptide bond; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..381
FT /note="Spindlin interactor and repressor of chromatin-
FT binding protein"
FT /id="PRO_0000321529"
FT REGION 148..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUA3"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUA3"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUA3"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUA3"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 49
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BUA3"
FT CROSSLNK 190
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BUA3"
FT CROSSLNK 221
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BUA3"
FT CROSSLNK 291
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BUA3"
FT CROSSLNK 295
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BUA3"
FT VAR_SEQ 312..315
FT /note="ASPP -> GEPC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031789"
FT VAR_SEQ 316..381
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031790"
FT CONFLICT 55
FT /note="P -> H (in Ref. 1; BAE39997)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="F -> L (in Ref. 1; BAE37410)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 381 AA; 41245 MW; 2141DADB77D1F143 CRC64;
MALKAKGAAA LDCFEVTLKC EEGDDDDEAV VVAVIPRPEP MLRVTQQEKT PPPRPNLLEA
GVEGCEELKQ QVSWEQEFLV GNSPGGSGRA LCMVCGAEIR SPSADTARAH ILEQHPHTLD
LSPSEKSNIL EAWSEGVALL QDIQADQPSL PSLESGQDGQ PDPISNPDPV RMPAEIVVLL
DSEDNPSLPK RLRPRGLRPL ELPVTPVIEQ GNKKPRGQRW KESPENEPAR KKRSRHMTKI
LDPDPDPPSP ESPTETFAAP AEVRHFTDGS FPPGFVLQLF SHTQLRTTDC KDSSKDSRAA
EGLPQPQNPS SASPPGLRGT LDLQVIRVRM EEPPAVSLLQ DWSKHPQGTK GVGTGDKPDW
PTVLSESSAT VKGQPKAGSG V
