SPNDC_HUMAN
ID SPNDC_HUMAN Reviewed; 381 AA.
AC Q9BUA3; Q68CV7; Q6PHS2; Q96IH0;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 3.
DT 03-AUG-2022, entry version 151.
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|HGNC:HGNC:25115};
GN Synonyms=C11orf84;
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 [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP PROTEIN SEQUENCE OF 108-143; 171-190; 195-212 AND 295-344, PHOSPHORYLATION
RP AT SER-308, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma, Colon carcinoma, and Mammary carcinoma;
RA Bienvenut W.V., Calvo F., Matallanas D., Cooper W.N., Zebisch A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 291-381.
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148 AND SER-308, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148 AND SER-248, AND
RP IDENTIFICATION BY 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308 AND SER-310, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148 AND SER-308, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121; SER-148; SER-248;
RP SER-251 AND SER-308, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-220; LYS-290 AND LYS-374, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-220 AND LYS-374, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-220 AND LYS-374, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [16]
RP FUNCTION, AND INTERACTION WITH SPIN1; SPIN2A; SPIN2B; SPIN3; SPIN4 AND
RP TCF7L2.
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).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-48; LYS-189; LYS-220; LYS-290;
RP LYS-294 AND LYS-374, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(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. Can also
CC inhibit the histone methyl-binding abilities of SPIN2A, SPIN2B, SPIN3
CC and SPIN4 (PubMed:29061846). {ECO:0000269|PubMed:29061846}.
CC -!- SUBUNIT: Interacts with SPIN1, SPIN2A, SPIN2B, SPIN3 and SPIN4
CC (PubMed:29061846). Interacts with TCF7L2 in a SPIN1-dependent manner
CC (PubMed:29061846). {ECO:0000269|PubMed:29061846}.
CC -!- INTERACTION:
CC Q9BUA3; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-1773488, EBI-741158;
CC Q9BUA3; O75928-2: PIAS2; NbExp=3; IntAct=EBI-1773488, EBI-348567;
CC Q9BUA3; P31930: UQCRC1; NbExp=3; IntAct=EBI-1773488, EBI-1052596;
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DR EMBL; CH471076; EAW74172.1; -; Genomic_DNA.
DR EMBL; BC002782; AAH02782.3; -; mRNA.
DR EMBL; BC007540; AAH07540.2; -; mRNA.
DR EMBL; BC056402; AAH56402.1; -; mRNA.
DR EMBL; CR749697; CAH18477.1; -; mRNA.
DR CCDS; CCDS31594.1; -.
DR RefSeq; NP_612480.1; NM_138471.2.
DR PDB; 7CNA; X-ray; 1.60 A; B/E=254-283.
DR PDBsum; 7CNA; -.
DR AlphaFoldDB; Q9BUA3; -.
DR SMR; Q9BUA3; -.
DR BioGRID; 126827; 51.
DR IntAct; Q9BUA3; 17.
DR STRING; 9606.ENSP00000294244; -.
DR GlyGen; Q9BUA3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BUA3; -.
DR PhosphoSitePlus; Q9BUA3; -.
DR BioMuta; C11orf84; -.
DR DMDM; 74733196; -.
DR EPD; Q9BUA3; -.
DR jPOST; Q9BUA3; -.
DR MassIVE; Q9BUA3; -.
DR MaxQB; Q9BUA3; -.
DR PaxDb; Q9BUA3; -.
DR PeptideAtlas; Q9BUA3; -.
DR PRIDE; Q9BUA3; -.
DR ProteomicsDB; 79066; -.
DR Antibodypedia; 51569; 49 antibodies from 12 providers.
DR DNASU; 144097; -.
DR Ensembl; ENST00000294244.9; ENSP00000294244.3; ENSG00000168005.9.
DR GeneID; 144097; -.
DR KEGG; hsa:144097; -.
DR MANE-Select; ENST00000294244.9; ENSP00000294244.3; NM_138471.3; NP_612480.1.
DR UCSC; uc001nxt.4; human.
DR CTD; 144097; -.
DR DisGeNET; 144097; -.
DR GeneCards; SPINDOC; -.
DR HGNC; HGNC:25115; SPINDOC.
DR HPA; ENSG00000168005; Low tissue specificity.
DR neXtProt; NX_Q9BUA3; -.
DR OpenTargets; ENSG00000168005; -.
DR PharmGKB; PA162377769; -.
DR VEuPathDB; HostDB:ENSG00000168005; -.
DR eggNOG; ENOG502S4I6; Eukaryota.
DR GeneTree; ENSGT00410000025985; -.
DR HOGENOM; CLU_061399_0_0_1; -.
DR InParanoid; Q9BUA3; -.
DR OMA; DTARSHI; -.
DR OrthoDB; 570589at2759; -.
DR PhylomeDB; Q9BUA3; -.
DR TreeFam; TF337165; -.
DR PathwayCommons; Q9BUA3; -.
DR SignaLink; Q9BUA3; -.
DR BioGRID-ORCS; 144097; 20 hits in 1055 CRISPR screens.
DR ChiTaRS; C11orf84; human.
DR GenomeRNAi; 144097; -.
DR Pharos; Q9BUA3; Tdark.
DR PRO; PR:Q9BUA3; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9BUA3; protein.
DR Bgee; ENSG00000168005; Expressed in left testis and 132 other tissues.
DR ExpressionAtlas; Q9BUA3; baseline and differential.
DR Genevisible; Q9BUA3; HS.
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 3D-structure; Direct protein sequencing; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..381
FT /note="Spindlin interactor and repressor of chromatin-
FT binding protein"
FT /id="PRO_0000321528"
FT REGION 42..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CROSSLNK 48
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 189
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 220
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 290
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 294
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 374
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT VARIANT 58
FT /note="E -> Q (in dbSNP:rs35875163)"
FT /id="VAR_061607"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:7CNA"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:7CNA"
SQ SEQUENCE 381 AA; 41037 MW; DC8AB56B1B224D73 CRC64;
MALKAEGAAL DCFEVTLKCE EGEDEEEAMV VAVIPRPEPM LRVTQQEKTP PPRPSPLEAG
SDGCEEPKQQ VSWEQEFLVG SSPGGSGRAL CMVCGAEIRA PSADTARSHI LEQHPHTLDL
SPSEKSNILE AWSEGVALLQ DVRAEQPSPP NSDSGQDAHP DPDANPDAAR MPAEIVVLLD
SEDNPSLPKR SRPRGLRPLE LPAVPATEPG NKKPRGQRWK EPPGEEPVRK KRGRPMTKNL
DPDPEPPSPD SPTETFAAPA EVRHFTDGSF PAGFVLQLFS HTQLRGPDSK DSPKDREVAE
GGLPRAESPS PAPPPGLRGT LDLQVIRVRM EEPPAVSLLQ DWSRHPQGTK RVGAGDTSDW
PTVLSESSTT VAGKPEKGNG V
