SPIN1_HUMAN
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 03-AUG-2022, entry version 166.
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 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 AlphaFoldDB; Q9Y657; -.
DR SMR; Q9Y657; -.
DR BioGRID; 116130; 89.
DR DIP; DIP-40062N; -.
DR IntAct; Q9Y657; 33.
DR MINT; Q9Y657; -.
DR STRING; 9606.ENSP00000365019; -.
DR BindingDB; Q9Y657; -.
DR ChEMBL; CHEMBL4523509; -.
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 PRIDE; Q9Y657; -.
DR ProteomicsDB; 86603; -.
DR Antibodypedia; 6817; 209 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 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; CMCEYRK; -.
DR OrthoDB; 1027563at2759; -.
DR PhylomeDB; Q9Y657; -.
DR TreeFam; TF332665; -.
DR PathwayCommons; Q9Y657; -.
DR SignaLink; Q9Y657; -.
DR BioGRID-ORCS; 10927; 13 hits in 1089 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 transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; 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; -; 1.
DR IDEAL; IID00591; -.
DR InterPro; IPR003671; SPIN/Ssty.
DR InterPro; IPR042567; SPIN/Ssty_sf.
DR InterPro; IPR029565; Spindlin-1.
DR PANTHER; PTHR10405; PTHR10405; 1.
DR PANTHER; PTHR10405:SF15; PTHR10405:SF15; 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:6I8Y"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:4MZH"
FT STRAND 70..79
FT /evidence="ECO:0007829|PDB:6I8Y"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:6I8Y"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:6I8Y"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:6I8Y"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:6I8Y"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:6I8B"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:5Y5W"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:6I8Y"
FT STRAND 136..142
FT /evidence="ECO:0007829|PDB:6I8Y"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:2NS2"
FT STRAND 148..158
FT /evidence="ECO:0007829|PDB:6I8Y"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:6I8Y"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:6I8Y"
FT STRAND 173..179
FT /evidence="ECO:0007829|PDB:6I8Y"
FT HELIX 181..186
FT /evidence="ECO:0007829|PDB:6I8Y"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:6I8Y"
FT HELIX 206..209
FT /evidence="ECO:0007829|PDB:7CNA"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:6I8Y"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:4H75"
FT STRAND 228..235
FT /evidence="ECO:0007829|PDB:6I8Y"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:4H75"
FT STRAND 242..247
FT /evidence="ECO:0007829|PDB:6I8Y"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:6I8Y"
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
