ID SPIN1_HUMAN Reviewed; 262 AA. AC Q9Y657; A8K0X6; B3KRQ4; Q7KZJ8; Q9GZT2; Q9H0N7; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 18-APR-2006, sequence version 3. DT 13-SEP-2023, entry version 172. DE RecName: Full=Spindlin-1; DE AltName: Full=Ovarian cancer-related protein; DE AltName: Full=Spindlin1; GN Name=SPIN1; Synonyms=OCR, SPIN; 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]. RC TISSUE=Pituitary; RA Peng Y., Song H., Dai M., Huang Q., Mao Y., Zhang Q., Mao M., Fu G., RA Luo M., Chen J., Hu R.; RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Zhang H.L., Yu L., Wang X., Chen Z., Tu Q., Chen J.Q., Ding J.B., Gao J., RA Zhao S.Y.; RT "Cloning, characterization and mapping of human SPIN to human chromosome RT 9q22.1-22.3."; RL Chin. Sci. Bull. 45:909-914(2000). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION. RC TISSUE=Ovarian carcinoma; RX PubMed=16098913; DOI=10.1016/j.bbrc.2005.07.087; RA Gao Y., Yue W., Zhang P., Li L., Xie X., Yuan H., Chen L., Liu D., Yan F., RA Pei X.; RT "Spindlin1, a novel nuclear protein with a role in the transformation of RT NIH3T3 cells."; RL Biochem. Biophys. Res. Commun. 335:343-350(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Fetal kidney; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Amygdala, Hippocampus, and Trachea; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton 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 [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=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 [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-225. 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND SER-199, 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND IDENTIFICATION BY RP 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 [13] RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PHE-141 AND TYR-170. RX PubMed=21960006; DOI=10.1038/embor.2011.184; RA Wang W., Chen Z., Mao Z., Zhang H., Ding X., Chen S., Zhang X., Xu R., RA Zhu B.; RT "Nucleolar protein Spindlin1 recognizes H3K4 methylation and stimulates the RT expression of rRNA genes."; RL EMBO Rep. 12:1160-1166(2011). RN [14] RP FUNCTION, INTERACTION WITH TCF7L2, PHOSPHORYLATION AT SER-109 AND SER-124, RP MUTAGENESIS OF SER-109 AND SER-124, AND TISSUE SPECIFICITY. RX PubMed=22258766; DOI=10.1158/1541-7786.mcr-11-0440; RA Wang J.X., Zeng Q., Chen L., Du J.C., Yan X.L., Yuan H.F., Zhai C., RA Zhou J.N., Jia Y.L., Yue W., Pei X.T.; RT "SPINDLIN1 promotes cancer cell proliferation through activation of RT WNT/TCF-4 signaling."; RL Mol. Cancer Res. 10:326-335(2012). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND SER-199, AND 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). RN [17] RP FUNCTION, INTERACTION WITH TCF7L2 AND C11ORF84/SPINDOC, AND SUBCELLULAR RP LOCATION. 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 [18] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-7; LYS-28 AND LYS-44, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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). RN [19] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 26-262 IN COMPLEX WITH PHOSPHATE RP IONS, DNA-BINDING, SUBUNIT, AND DOMAINS TUDOR-LIKE. RX PubMed=17082182; DOI=10.1074/jbc.m604029200; RA Zhao Q., Qin L., Jiang F., Wu B., Yue W., Xu F., Rong Z., Yuan H., Xie X., RA Gao Y., Bai C., Bartlam M., Pei X., Rao Z.; RT "Structure of human spindlin1. Tandem tudor-like domains for cell cycle RT regulation."; RL J. Biol. Chem. 282:647-656(2007). RN [20] RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 27-262 IN COMPLEX WITH METHYLATED RP HISTONE H3, AND MUTAGENESIS OF ASP-184 AND ASP-189. RX PubMed=23077255; DOI=10.1073/pnas.1208517109; RA Yang N., Wang W., Wang Y., Wang M., Zhao Q., Rao Z., Zhu B., Xu R.M.; RT "Distinct mode of methylated lysine-4 of histone H3 recognition by tandem RT tudor-like domains of Spindlin1."; RL Proc. Natl. Acad. Sci. U.S.A. 109:17954-17959(2012). RN [21] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 50-262 IN COMPLEX WITH METHYLATED RP HISTONE H3, FUNCTION, INTERACTION WITH TCF7L2, AND MUTAGENESIS OF TRP-72; RP TYR-98; PHE-141; GLU-142; TYR-170; TYR-177; ASP-184 AND PHE-251. RX PubMed=24589551; DOI=10.1101/gad.233239.113; RA Su X., Zhu G., Ding X., Lee S.Y., Dou Y., Zhu B., Wu W., Li H.; RT "Molecular basis underlying histone H3 lysine-arginine methylation pattern RT readout by Spin/Ssty repeats of Spindlin1."; RL Genes Dev. 28:622-636(2014). CC -!- FUNCTION: Chromatin reader that specifically recognizes and binds CC histone H3 both trimethylated at 'Lys-4' and asymmetrically CC dimethylated at 'Arg-8' (H3K4me3 and H3R8me2a) and acts as an activator CC of Wnt signaling pathway downstream of PRMT2. In case of cancer, CC promotes cell cancer proliferation via activation of the Wnt signaling CC pathway (PubMed:24589551). Overexpression induces metaphase arrest and CC chromosomal instability. Localizes to active rDNA loci and promotes the CC expression of rRNA genes (PubMed:21960006). May play a role in cell- CC cycle regulation during the transition from gamete to embryo. Involved CC in oocyte meiotic resumption, a process that takes place before CC ovulation to resume meiosis of oocytes blocked in prophase I: may act CC by regulating maternal transcripts to control meiotic resumption. CC {ECO:0000269|PubMed:21960006, ECO:0000269|PubMed:22258766, CC ECO:0000269|PubMed:24589551, ECO:0000269|PubMed:29061846}. CC -!- SUBUNIT: Homodimer; may form higher-order oligomers (PubMed:17082182). CC Interacts with TCF7L2/TCF4; the interaction is direct (PubMed:22258766, CC PubMed:24589551, PubMed:29061846). Interacts with HABP4 and SERBP1 (By CC similarity). Interacts with C11orf84/SPINDOC (PubMed:29061846). CC {ECO:0000250|UniProtKB:Q61142, ECO:0000269|PubMed:17082182, CC ECO:0000269|PubMed:22258766, ECO:0000269|PubMed:23077255, CC ECO:0000269|PubMed:24589551, ECO:0000269|PubMed:29061846}. CC -!- INTERACTION: CC Q9Y657; P04792: HSPB1; NbExp=2; IntAct=EBI-727129, EBI-352682; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16098913, CC ECO:0000269|PubMed:29061846}. Nucleus, nucleolus CC {ECO:0000269|PubMed:21960006}. CC -!- TISSUE SPECIFICITY: Highly expressed in ovarian cancer tissues. CC {ECO:0000269|PubMed:22258766}. CC -!- DOMAIN: The 3 tudor-like domains (also named Spin/Ssty repeats) CC specifically recognize and bind methylated histones (PubMed:23077255, CC PubMed:24589551). H3K4me3 and H3R8me2a are recognized by tudor-like CC domains 2 and 1, respectively (PubMed:24589551). CC {ECO:0000269|PubMed:17082182, ECO:0000269|PubMed:23077255, CC ECO:0000269|PubMed:24589551}. CC -!- PTM: Phosphorylated during oocyte meiotic maturation. CC {ECO:0000250|UniProtKB:Q61142}. CC -!- SIMILARITY: Belongs to the SPIN/STSY family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD43035.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAG38112.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAG48367.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=CAB66653.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305}; CC Sequence=CAG38515.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF106682; AAD43035.1; ALT_FRAME; mRNA. DR EMBL; AF087864; AAG48367.1; ALT_INIT; mRNA. DR EMBL; AF317228; AAG38112.1; ALT_INIT; mRNA. DR EMBL; AL136719; CAB66653.1; ALT_SEQ; mRNA. DR EMBL; BT007314; AAP35978.1; -; mRNA. DR EMBL; AK092017; BAG52466.1; -; mRNA. DR EMBL; AK289691; BAF82380.1; -; mRNA. DR EMBL; AK290009; BAF82698.1; -; mRNA. DR EMBL; AK315854; BAF98745.1; -; mRNA. DR EMBL; AL353748; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471089; EAW62753.1; -; Genomic_DNA. DR EMBL; BC013571; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC114515; AAI14516.1; -; mRNA. DR EMBL; BC114565; AAI14566.1; -; mRNA. DR EMBL; CR533484; CAG38515.1; ALT_SEQ; mRNA. DR CCDS; CCDS43843.1; -. DR RefSeq; NP_006708.2; NM_006717.2. DR PDB; 2NS2; X-ray; 2.20 A; A/B=26-262. DR PDB; 4H75; X-ray; 2.10 A; A=27-262. DR PDB; 4MZF; X-ray; 2.10 A; B=50-262. DR PDB; 4MZG; X-ray; 1.70 A; B/D=50-262. DR PDB; 4MZH; X-ray; 2.20 A; A=50-262. DR PDB; 5JSG; X-ray; 2.50 A; A/B=50-262. DR PDB; 5JSJ; X-ray; 2.35 A; A/B=50-262. DR PDB; 5Y5W; X-ray; 3.30 A; A/B/C/D=51-262. DR PDB; 6I8B; X-ray; 1.76 A; B/E=48-262. DR PDB; 6I8L; X-ray; 1.58 A; B=48-262. DR PDB; 6I8Y; X-ray; 1.52 A; A=48-262. DR PDB; 6QPL; X-ray; 1.60 A; B=48-262. DR PDB; 7BQZ; X-ray; 3.10 A; A/C/E/G=45-262. DR PDB; 7BU9; X-ray; 3.50 A; A/C/E/G=45-262. DR PDB; 7CNA; X-ray; 1.60 A; A/D=51-262. DR PDB; 7E9M; X-ray; 2.50 A; A/C=1-262. DR PDB; 7EA1; X-ray; 2.70 A; A/C=50-262. DR PDB; 7OCB; X-ray; 1.42 A; B=48-262. DR PDBsum; 2NS2; -. DR PDBsum; 4H75; -. DR PDBsum; 4MZF; -. DR PDBsum; 4MZG; -. DR PDBsum; 4MZH; -. DR PDBsum; 5JSG; -. DR PDBsum; 5JSJ; -. DR PDBsum; 5Y5W; -. DR PDBsum; 6I8B; -. DR PDBsum; 6I8L; -. DR PDBsum; 6I8Y; -. DR PDBsum; 6QPL; -. DR PDBsum; 7BQZ; -. DR PDBsum; 7BU9; -. DR PDBsum; 7CNA; -. DR PDBsum; 7E9M; -. DR PDBsum; 7EA1; -. DR PDBsum; 7OCB; -. DR AlphaFoldDB; Q9Y657; -. DR SMR; Q9Y657; -. DR BioGRID; 116130; 100. DR DIP; DIP-40062N; -. DR IntAct; Q9Y657; 33. DR MINT; Q9Y657; -. DR STRING; 9606.ENSP00000365019; -. DR BindingDB; Q9Y657; -. DR ChEMBL; CHEMBL4523509; -. DR GlyGen; Q9Y657; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9Y657; -. DR PhosphoSitePlus; Q9Y657; -. DR BioMuta; SPIN1; -. DR DMDM; 93141317; -. DR EPD; Q9Y657; -. DR jPOST; Q9Y657; -. DR MassIVE; Q9Y657; -. DR MaxQB; Q9Y657; -. DR PaxDb; Q9Y657; -. DR PeptideAtlas; Q9Y657; -. DR ProteomicsDB; 86603; -. DR Antibodypedia; 6817; 235 antibodies from 30 providers. DR DNASU; 10927; -. DR Ensembl; ENST00000375859.4; ENSP00000365019.3; ENSG00000106723.17. DR GeneID; 10927; -. DR KEGG; hsa:10927; -. DR MANE-Select; ENST00000375859.4; ENSP00000365019.3; NM_006717.3; NP_006708.2. DR UCSC; uc004apy.4; human. DR AGR; HGNC:11243; -. DR CTD; 10927; -. DR DisGeNET; 10927; -. DR GeneCards; SPIN1; -. DR HGNC; HGNC:11243; SPIN1. DR HPA; ENSG00000106723; Low tissue specificity. DR MIM; 609936; gene. DR neXtProt; NX_Q9Y657; -. DR OpenTargets; ENSG00000106723; -. DR PharmGKB; PA162404504; -. DR VEuPathDB; HostDB:ENSG00000106723; -. DR eggNOG; ENOG502QRYD; Eukaryota. DR GeneTree; ENSGT00950000182925; -. DR HOGENOM; CLU_068595_0_0_1; -. DR InParanoid; Q9Y657; -. DR OMA; GAKDEWR; -. DR OrthoDB; 3949689at2759; -. DR PhylomeDB; Q9Y657; -. DR TreeFam; TF332665; -. DR PathwayCommons; Q9Y657; -. DR SignaLink; Q9Y657; -. DR BioGRID-ORCS; 10927; 15 hits in 1167 CRISPR screens. DR ChiTaRS; SPIN1; human. DR EvolutionaryTrace; Q9Y657; -. DR GeneWiki; SPIN1; -. DR GenomeRNAi; 10927; -. DR Pharos; Q9Y657; Tchem. DR PRO; PR:Q9Y657; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q9Y657; Protein. DR Bgee; ENSG00000106723; Expressed in postcentral gyrus and 203 other tissues. DR ExpressionAtlas; Q9Y657; baseline and differential. DR Genevisible; Q9Y657; HS. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0031965; C:nuclear membrane; IDA:HPA. DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005819; C:spindle; IEA:Ensembl. DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB. DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW. DR GO; GO:0007276; P:gamete generation; IEA:InterPro. DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IDA:UniProtKB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central. DR GO; GO:0009303; P:rRNA transcription; IDA:UniProtKB. DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW. DR Gene3D; 2.80.10.70; Spindlin/Ssty; 1. DR IDEAL; IID00591; -. DR InterPro; IPR003671; SPIN/Ssty. DR InterPro; IPR042567; SPIN/Ssty_sf. DR PANTHER; PTHR10405; SPINDLIN; 1. DR PANTHER; PTHR10405:SF15; SPINDLIN-1; 1. DR Pfam; PF02513; Spin-Ssty; 3. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cell cycle; Chromatin regulator; KW Developmental protein; Isopeptide bond; Meiosis; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Ubl conjugation; Wnt signaling pathway. FT CHAIN 1..262 FT /note="Spindlin-1" FT /id="PRO_0000181367" FT REGION 1..51 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 53..116 FT /note="Tudor-like domain 1" FT REGION 93..98 FT /note="Histone H3K4me3 and H3R8me2a binding" FT REGION 132..193 FT /note="Tudor-like domain 2" FT REGION 142 FT /note="Histone H3K4me3 and H3R8me2a binding" FT REGION 213..262 FT /note="Tudor-like domain 3" FT REGION 250..252 FT /note="Histone H3K4me3 and H3R8me2a binding" FT SITE 173 FT /note="Histone H3K4me3 and H3R8me2a binding" FT SITE 180 FT /note="Histone H3K4me3 and H3R8me2a binding" FT SITE 184 FT /note="Histone H3K4me3 and H3R8me2a binding" FT MOD_RES 44 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q61142" FT MOD_RES 109 FT /note="Phosphoserine; by AURKA" FT /evidence="ECO:0000269|PubMed:22258766" FT MOD_RES 124 FT /note="Phosphoserine; by AURKA" FT /evidence="ECO:0000269|PubMed:22258766, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 199 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT CROSSLNK 7 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 28 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 44 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:28112733" FT VARIANT 221 FT /note="A -> P (in dbSNP:rs34794905)" FT /id="VAR_053690" FT MUTAGEN 72 FT /note="W->A,R: Impaired binding to histone H3K4me3 and FT H3R8me2a and impaired ability to activate the Wnt signaling FT pathway." FT /evidence="ECO:0000269|PubMed:24589551" FT MUTAGEN 98 FT /note="Y->R: Impaired binding to histone H3K4me3 and FT H3R8me2a and impaired ability to activate the Wnt signaling FT pathway." FT /evidence="ECO:0000269|PubMed:24589551" FT MUTAGEN 109 FT /note="S->A: Impaired phosphorylation." FT /evidence="ECO:0000269|PubMed:22258766" FT MUTAGEN 124 FT /note="S->A: Impaired phosphorylation." FT /evidence="ECO:0000269|PubMed:22258766" FT MUTAGEN 141 FT /note="F->A: Impaired binding to histone H3K4me3 and FT H3R8me2a and impaired ability to activate the Wnt signaling FT pathway. Impaired ability to activate expression of pre- FT rRNA." FT /evidence="ECO:0000269|PubMed:21960006, FT ECO:0000269|PubMed:24589551" FT MUTAGEN 142 FT /note="E->A: Impaired binding to histone H3K4me3 and FT H3R8me2a." FT /evidence="ECO:0000269|PubMed:24589551" FT MUTAGEN 170 FT /note="Y->A: Impaired binding to histone H3K4me3 and FT H3R8me2a and impaired ability to activate the Wnt signaling FT pathway. Impaired ability to activate expression of pre- FT rRNA." FT /evidence="ECO:0000269|PubMed:21960006, FT ECO:0000269|PubMed:24589551" FT MUTAGEN 177 FT /note="Y->A: Impaired binding to histone H3K4me3 and FT H3R8me2a." FT /evidence="ECO:0000269|PubMed:24589551" FT MUTAGEN 184 FT /note="D->A,R: Impaired binding to histone H3K4me3 and FT H3R8me2a." FT /evidence="ECO:0000269|PubMed:23077255, FT ECO:0000269|PubMed:24589551" FT MUTAGEN 189 FT /note="D->A,R: Impaired binding to histone H3K4me3." FT /evidence="ECO:0000269|PubMed:23077255" FT MUTAGEN 251 FT /note="F->R: Impaired binding to histone H3K4me3 and FT H3R8me2a and impaired ability to activate the Wnt signaling FT pathway." FT /evidence="ECO:0000269|PubMed:24589551" FT CONFLICT 49 FT /note="P -> S (in Ref. 6; BAG52466)" FT /evidence="ECO:0000305" FT STRAND 57..62 FT /evidence="ECO:0007829|PDB:7OCB" FT STRAND 65..67 FT /evidence="ECO:0007829|PDB:4MZH" FT STRAND 70..79 FT /evidence="ECO:0007829|PDB:7OCB" FT STRAND 86..91 FT /evidence="ECO:0007829|PDB:7OCB" FT STRAND 98..101 FT /evidence="ECO:0007829|PDB:7OCB" FT TURN 102..104 FT /evidence="ECO:0007829|PDB:7OCB" FT STRAND 108..113 FT /evidence="ECO:0007829|PDB:7OCB" FT STRAND 117..119 FT /evidence="ECO:0007829|PDB:6I8B" FT HELIX 126..132 FT /evidence="ECO:0007829|PDB:7OCB" FT STRAND 136..142 FT /evidence="ECO:0007829|PDB:7OCB" FT STRAND 144..146 FT /evidence="ECO:0007829|PDB:2NS2" FT STRAND 148..158 FT /evidence="ECO:0007829|PDB:7OCB" FT STRAND 160..162 FT /evidence="ECO:0007829|PDB:7OCB" FT STRAND 166..170 FT /evidence="ECO:0007829|PDB:7OCB" FT STRAND 173..179 FT /evidence="ECO:0007829|PDB:7OCB" FT HELIX 181..186 FT /evidence="ECO:0007829|PDB:7OCB" FT STRAND 190..192 FT /evidence="ECO:0007829|PDB:7OCB" FT HELIX 206..209 FT /evidence="ECO:0007829|PDB:7CNA" FT STRAND 217..220 FT /evidence="ECO:0007829|PDB:7OCB" FT TURN 223..225 FT /evidence="ECO:0007829|PDB:4H75" FT STRAND 228..235 FT /evidence="ECO:0007829|PDB:7OCB" FT STRAND 237..239 FT /evidence="ECO:0007829|PDB:4H75" FT STRAND 242..247 FT /evidence="ECO:0007829|PDB:7OCB" FT STRAND 254..257 FT /evidence="ECO:0007829|PDB:7OCB" SQ SEQUENCE 262 AA; 29601 MW; 49F86CBCC7A0AA01 CRC64; MKTPFGKTPG QRSRADAGHA GVSANMMKKR TSHKKHRSSV GPSKPVSQPR RNIVGCRIQH GWKEGNGPVT QWKGTVLDQV PVNPSLYLIK YDGFDCVYGL ELNKDERVSA LEVLPDRVAT SRISDAHLAD TMIGKAVEHM FETEDGSKDE WRGMVLARAP VMNTWFYITY EKDPVLYMYQ LLDDYKEGDL RIMPDSNDSP PAEREPGEVV DSLVGKQVEY AKEDGSKRTG MVIHQVEAKP SVYFIKFDDD FHIYVYDLVK TS //