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Spindlin-1 (Ovarian cancer-related protein) (Spindlin1)

 SPIN1_HUMAN             Reviewed;         262 AA.
Q9Y657; A8K0X6; B3KRQ4; Q7KZJ8; Q9GZT2; Q9H0N7;
20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
18-APR-2006, sequence version 3.
16-OCT-2019, entry version 152.
RecName: Full=Spindlin-1;
AltName: Full=Ovarian cancer-related protein;
AltName: Full=Spindlin1;
Name=SPIN1; Synonyms=OCR, SPIN;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Pituitary;
Peng Y., Song H., Dai M., Huang Q., Mao Y., Zhang Q., Mao M., Fu G.,
Luo M., Chen J., Hu R.;
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Zhang H.L., Yu L., Wang X., Chen Z., Tu Q., Chen J.Q., Ding J.B.,
Gao J., Zhao S.Y.;
"Cloning, characterization and mapping of human SPIN to human
chromosome 9q22.1-22.3.";
Chin. Sci. Bull. 45:909-914(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
TISSUE=Ovarian carcinoma;
PubMed=16098913; DOI=10.1016/j.bbrc.2005.07.087;
Gao Y., Yue W., Zhang P., Li L., Xie X., Yuan H., Chen L., Liu D.,
Yan F., Pei X.;
"Spindlin1, a novel nuclear protein with a role in the transformation
of NIH3T3 cells.";
Biochem. Biophys. Res. Commun. 335:343-350(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Fetal kidney;
PubMed=11230166; DOI=10.1101/gr.gr1547r;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Amygdala, Hippocampus, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-225.
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND SER-199, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[13]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PHE-141 AND
TYR-170.
PubMed=21960006; DOI=10.1038/embor.2011.184;
Wang W., Chen Z., Mao Z., Zhang H., Ding X., Chen S., Zhang X., Xu R.,
Zhu B.;
"Nucleolar protein Spindlin1 recognizes H3K4 methylation and
stimulates the expression of rRNA genes.";
EMBO Rep. 12:1160-1166(2011).
[14]
FUNCTION, INTERACTION WITH TCF7L2, PHOSPHORYLATION AT SER-109 AND
SER-124, MUTAGENESIS OF SER-109 AND SER-124, AND TISSUE SPECIFICITY.
PubMed=22258766; DOI=10.1158/1541-7786.mcr-11-0440;
Wang J.X., Zeng Q., Chen L., Du J.C., Yan X.L., Yuan H.F., Zhai C.,
Zhou J.N., Jia Y.L., Yue W., Pei X.T.;
"SPINDLIN1 promotes cancer cell proliferation through activation of
WNT/TCF-4 signaling.";
Mol. Cancer Res. 10:326-335(2012).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND SER-199, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
FUNCTION, INTERACTION WITH TCF7L2 AND C11ORF84/SPINDOC, AND
SUBCELLULAR LOCATION.
PubMed=29061846; DOI=10.1074/jbc.m117.814913;
Bae N., Gao M., Li X., Premkumar T., Sbardella G., Chen J.,
Bedford M.T.;
"A transcriptional coregulator, SPIN-DOC, attenuates the coactivator
activity of Spindlin1.";
J. Biol. Chem. 292:20808-20817(2017).
[18]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-7; LYS-28 AND LYS-44, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[19]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 26-262 IN COMPLEX WITH
PHOSPHATE IONS, DNA-BINDING, SUBUNIT, AND DOMAINS TUDOR-LIKE.
PubMed=17082182; DOI=10.1074/jbc.m604029200;
Zhao Q., Qin L., Jiang F., Wu B., Yue W., Xu F., Rong Z., Yuan H.,
Xie X., Gao Y., Bai C., Bartlam M., Pei X., Rao Z.;
"Structure of human spindlin1. Tandem tudor-like domains for cell
cycle regulation.";
J. Biol. Chem. 282:647-656(2007).
[20]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 27-262 IN COMPLEX WITH
METHYLATED HISTONE H3, AND MUTAGENESIS OF ASP-184 AND ASP-189.
PubMed=23077255; DOI=10.1073/pnas.1208517109;
Yang N., Wang W., Wang Y., Wang M., Zhao Q., Rao Z., Zhu B., Xu R.M.;
"Distinct mode of methylated lysine-4 of histone H3 recognition by
tandem tudor-like domains of Spindlin1.";
Proc. Natl. Acad. Sci. U.S.A. 109:17954-17959(2012).
[21]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 50-262 IN COMPLEX WITH
METHYLATED HISTONE H3, FUNCTION, INTERACTION WITH TCF7L2, AND
MUTAGENESIS OF TRP-72; TYR-98; PHE-141; GLU-142; TYR-170; TYR-177;
ASP-184 AND PHE-251.
PubMed=24589551; DOI=10.1101/gad.233239.113;
Su X., Zhu G., Ding X., Lee S.Y., Dou Y., Zhu B., Wu W., Li H.;
"Molecular basis underlying histone H3 lysine-arginine methylation
pattern readout by Spin/Ssty repeats of Spindlin1.";
Genes Dev. 28:622-636(2014).
-!- FUNCTION: Chromatin reader that specifically recognizes and binds
histone H3 both trimethylated at 'Lys-4' and asymmetrically
dimethylated at 'Arg-8' (H3K4me3 and H3R8me2a) and acts as an
activator of Wnt signaling pathway downstream of PRMT2. In case of
cancer, promotes cell cancer proliferation via activation of the
Wnt signaling pathway (PubMed:24589551). Overexpression induces
metaphase arrest and chromosomal instability. Localizes to active
rDNA loci and promotes the expression of rRNA genes
(PubMed:21960006). May play a role in cell-cycle regulation during
the transition from gamete to embryo. Involved in oocyte meiotic
resumption, a process that takes place before ovulation to resume
meiosis of oocytes blocked in prophase I: may act by regulating
maternal transcripts to control meiotic resumption.
{ECO:0000269|PubMed:21960006, ECO:0000269|PubMed:22258766,
ECO:0000269|PubMed:24589551, ECO:0000269|PubMed:29061846}.
-!- SUBUNIT: Homodimer; may form higher-order oligomers
(PubMed:17082182). Interacts with TCF7L2/TCF4; the interaction is
direct (PubMed:22258766, PubMed:24589551, PubMed:29061846).
Interacts with HABP4 and SERBP1 (By similarity). Interacts with
C11orf84/SPINDOC (PubMed:29061846). {ECO:0000250|UniProtKB:Q61142,
ECO:0000269|PubMed:17082182, ECO:0000269|PubMed:22258766,
ECO:0000269|PubMed:23077255, ECO:0000269|PubMed:24589551,
ECO:0000269|PubMed:29061846}.
-!- INTERACTION:
P04792:HSPB1; NbExp=2; IntAct=EBI-727129, EBI-352682;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16098913,
ECO:0000269|PubMed:29061846}. Nucleus, nucleolus
{ECO:0000269|PubMed:21960006}.
-!- TISSUE SPECIFICITY: Highly expressed in ovarian cancer tissues.
{ECO:0000269|PubMed:22258766}.
-!- DOMAIN: The 3 tudor-like domains (also named Spin/Ssty repeats)
specifically recognize and bind methylated histones
(PubMed:23077255, PubMed:24589551). H3K4me3 and H3R8me2a are
recognized by tudor-like domains 2 and 1, respectively
(PubMed:24589551). {ECO:0000269|PubMed:17082182,
ECO:0000269|PubMed:23077255, ECO:0000269|PubMed:24589551}.
-!- PTM: Phosphorylated during oocyte meiotic maturation.
{ECO:0000250|UniProtKB:Q61142}.
-!- SIMILARITY: Belongs to the SPIN/STSY family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD43035.1; Type=Frameshift; Evidence={ECO:0000305};
Sequence=AAG38112.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
Sequence=AAG48367.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
Sequence=CAB66653.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
Sequence=CAG38515.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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EMBL; AF106682; AAD43035.1; ALT_FRAME; mRNA.
EMBL; AF087864; AAG48367.1; ALT_INIT; mRNA.
EMBL; AF317228; AAG38112.1; ALT_INIT; mRNA.
EMBL; AL136719; CAB66653.1; ALT_SEQ; mRNA.
EMBL; BT007314; AAP35978.1; -; mRNA.
EMBL; AK092017; BAG52466.1; -; mRNA.
EMBL; AK289691; BAF82380.1; -; mRNA.
EMBL; AK290009; BAF82698.1; -; mRNA.
EMBL; AK315854; BAF98745.1; -; mRNA.
EMBL; AL353748; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471089; EAW62753.1; -; Genomic_DNA.
EMBL; BC013571; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC114515; AAI14516.1; -; mRNA.
EMBL; BC114565; AAI14566.1; -; mRNA.
EMBL; CR533484; CAG38515.1; ALT_SEQ; mRNA.
CCDS; CCDS43843.1; -.
RefSeq; NP_006708.2; NM_006717.2.
PDB; 2NS2; X-ray; 2.20 A; A/B=26-262.
PDB; 4H75; X-ray; 2.10 A; A=27-262.
PDB; 4MZF; X-ray; 2.10 A; B=50-262.
PDB; 4MZG; X-ray; 1.70 A; B/D=50-262.
PDB; 4MZH; X-ray; 2.20 A; A=50-262.
PDB; 5JSG; X-ray; 2.50 A; A/B=50-262.
PDB; 5JSJ; X-ray; 2.35 A; A/B=50-262.
PDB; 5Y5W; X-ray; 3.30 A; A/B/C/D=51-262.
PDB; 6I8B; X-ray; 1.76 A; B/E=48-262.
PDB; 6I8L; X-ray; 1.58 A; B=48-262.
PDB; 6I8Y; X-ray; 1.52 A; A=48-262.
PDB; 6QPL; X-ray; 1.60 A; B=48-262.
PDBsum; 2NS2; -.
PDBsum; 4H75; -.
PDBsum; 4MZF; -.
PDBsum; 4MZG; -.
PDBsum; 4MZH; -.
PDBsum; 5JSG; -.
PDBsum; 5JSJ; -.
PDBsum; 5Y5W; -.
PDBsum; 6I8B; -.
PDBsum; 6I8L; -.
PDBsum; 6I8Y; -.
PDBsum; 6QPL; -.
SMR; Q9Y657; -.
BioGrid; 116130; 49.
DIP; DIP-40062N; -.
IntAct; Q9Y657; 22.
MINT; Q9Y657; -.
STRING; 9606.ENSP00000365019; -.
iPTMnet; Q9Y657; -.
PhosphoSitePlus; Q9Y657; -.
BioMuta; SPIN1; -.
DMDM; 93141317; -.
EPD; Q9Y657; -.
jPOST; Q9Y657; -.
MassIVE; Q9Y657; -.
MaxQB; Q9Y657; -.
PaxDb; Q9Y657; -.
PeptideAtlas; Q9Y657; -.
PRIDE; Q9Y657; -.
ProteomicsDB; 86603; -.
Ensembl; ENST00000375859; ENSP00000365019; ENSG00000106723.
GeneID; 10927; -.
KEGG; hsa:10927; -.
UCSC; uc004apy.4; human.
CTD; 10927; -.
DisGeNET; 10927; -.
GeneCards; SPIN1; -.
HGNC; HGNC:11243; SPIN1.
HPA; HPA000162; -.
HPA; HPA068784; -.
MIM; 609936; gene.
neXtProt; NX_Q9Y657; -.
OpenTargets; ENSG00000106723; -.
PharmGKB; PA162404504; -.
eggNOG; ENOG410IGUH; Eukaryota.
eggNOG; ENOG410XQI2; LUCA.
GeneTree; ENSGT00950000182925; -.
HOGENOM; HOG000293367; -.
InParanoid; Q9Y657; -.
OMA; MKSTPGH; -.
OrthoDB; 1027563at2759; -.
PhylomeDB; Q9Y657; -.
TreeFam; TF332665; -.
ChiTaRS; SPIN1; human.
EvolutionaryTrace; Q9Y657; -.
GeneWiki; SPIN1; -.
GenomeRNAi; 10927; -.
Pharos; Q9Y657; -.
PRO; PR:Q9Y657; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000106723; Expressed in 229 organ(s), highest expression level in female gonad.
ExpressionAtlas; Q9Y657; baseline and differential.
Genevisible; Q9Y657; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0031965; C:nuclear membrane; IDA:HPA.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005819; C:spindle; IEA:Ensembl.
GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
GO; GO:0007276; P:gamete generation; IEA:InterPro.
GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IDA:UniProtKB.
GO; GO:0009303; P:rRNA transcription; IDA:UniProtKB.
GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
Gene3D; 2.80.10.70; -; 1.
InterPro; IPR003671; SPIN/Ssty.
InterPro; IPR042567; SPIN/Ssty_sf.
InterPro; IPR029565; Spindlin-1.
PANTHER; PTHR10405; PTHR10405; 1.
PANTHER; PTHR10405:SF15; PTHR10405:SF15; 1.
Pfam; PF02513; Spin-Ssty; 3.
1: Evidence at protein level;
3D-structure; Acetylation; Cell cycle; Chromatin regulator;
Complete proteome; Developmental protein; Isopeptide bond; Meiosis;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Ubl conjugation; Wnt signaling pathway.
CHAIN 1 262 Spindlin-1.
/FTId=PRO_0000181367.
REGION 53 116 Tudor-like domain 1.
REGION 93 98 Histone H3K4me3 and H3R8me2a binding.
REGION 132 193 Tudor-like domain 2.
REGION 142 142 Histone H3K4me3 and H3R8me2a binding.
REGION 213 262 Tudor-like domain 3.
REGION 250 252 Histone H3K4me3 and H3R8me2a binding.
BINDING 173 173 Histone H3K4me3 and H3R8me2a.
BINDING 180 180 Histone H3K4me3 and H3R8me2a.
BINDING 184 184 Histone H3K4me3 and H3R8me2a.
MOD_RES 44 44 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q61142}.
MOD_RES 109 109 Phosphoserine; by AURKA.
{ECO:0000269|PubMed:22258766}.
MOD_RES 124 124 Phosphoserine; by AURKA.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:22258766}.
MOD_RES 199 199 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
CROSSLNK 7 7 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 28 28 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 44 44 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
VARIANT 221 221 A -> P (in dbSNP:rs34794905).
/FTId=VAR_053690.
MUTAGEN 72 72 W->A,R: Impaired binding to histone
H3K4me3 and H3R8me2a and impaired ability
to activate the Wnt signaling pathway.
{ECO:0000269|PubMed:24589551}.
MUTAGEN 98 98 Y->R: Impaired binding to histone H3K4me3
and H3R8me2a and impaired ability to
activate the Wnt signaling pathway.
{ECO:0000269|PubMed:24589551}.
MUTAGEN 109 109 S->A: Impaired phosphorylation.
{ECO:0000269|PubMed:22258766}.
MUTAGEN 124 124 S->A: Impaired phosphorylation.
{ECO:0000269|PubMed:22258766}.
MUTAGEN 141 141 F->A: Impaired binding to histone H3K4me3
and H3R8me2a and impaired ability to
activate the Wnt signaling pathway.
Impaired ability to activate expression
of pre-rRNA.
{ECO:0000269|PubMed:21960006,
ECO:0000269|PubMed:24589551}.
MUTAGEN 142 142 E->A: Impaired binding to histone H3K4me3
and H3R8me2a.
{ECO:0000269|PubMed:24589551}.
MUTAGEN 170 170 Y->A: Impaired binding to histone H3K4me3
and H3R8me2a and impaired ability to
activate the Wnt signaling pathway.
Impaired ability to activate expression
of pre-rRNA.
{ECO:0000269|PubMed:21960006,
ECO:0000269|PubMed:24589551}.
MUTAGEN 177 177 Y->A: Impaired binding to histone H3K4me3
and H3R8me2a.
{ECO:0000269|PubMed:24589551}.
MUTAGEN 184 184 D->A,R: Impaired binding to histone
H3K4me3 and H3R8me2a.
{ECO:0000269|PubMed:23077255,
ECO:0000269|PubMed:24589551}.
MUTAGEN 189 189 D->A,R: Impaired binding to histone
H3K4me3. {ECO:0000269|PubMed:23077255}.
MUTAGEN 251 251 F->R: Impaired binding to histone H3K4me3
and H3R8me2a and impaired ability to
activate the Wnt signaling pathway.
{ECO:0000269|PubMed:24589551}.
CONFLICT 49 49 P -> S (in Ref. 6; BAG52466).
{ECO:0000305}.
STRAND 57 62 {ECO:0000244|PDB:6I8Y}.
STRAND 65 67 {ECO:0000244|PDB:4MZH}.
STRAND 70 79 {ECO:0000244|PDB:6I8Y}.
STRAND 86 91 {ECO:0000244|PDB:6I8Y}.
STRAND 98 101 {ECO:0000244|PDB:6I8Y}.
TURN 102 104 {ECO:0000244|PDB:6I8Y}.
STRAND 108 113 {ECO:0000244|PDB:6I8Y}.
STRAND 117 119 {ECO:0000244|PDB:6I8B}.
HELIX 126 129 {ECO:0000244|PDB:5Y5W}.
HELIX 130 132 {ECO:0000244|PDB:6I8Y}.
STRAND 136 142 {ECO:0000244|PDB:6I8Y}.
STRAND 144 146 {ECO:0000244|PDB:2NS2}.
STRAND 148 158 {ECO:0000244|PDB:6I8Y}.
STRAND 160 162 {ECO:0000244|PDB:6I8Y}.
STRAND 166 170 {ECO:0000244|PDB:6I8Y}.
STRAND 173 179 {ECO:0000244|PDB:6I8Y}.
HELIX 181 186 {ECO:0000244|PDB:6I8Y}.
STRAND 190 192 {ECO:0000244|PDB:6I8Y}.
STRAND 217 220 {ECO:0000244|PDB:6I8Y}.
TURN 223 225 {ECO:0000244|PDB:4H75}.
STRAND 228 235 {ECO:0000244|PDB:6I8Y}.
STRAND 237 239 {ECO:0000244|PDB:4H75}.
STRAND 242 247 {ECO:0000244|PDB:6I8Y}.
STRAND 254 257 {ECO:0000244|PDB:6I8Y}.
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


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[MUC16 CA125] Mucin-16 (MUC-16) (Ovarian cancer-related tumor marker CA125) (CA-125) (Ovarian carcinoma antigen CA125)
[GPR68 OGR1] Ovarian cancer G-protein coupled receptor 1 (OGR-1) (G-protein coupled receptor 68) (GPR12A) (Sphingosylphosphorylcholine receptor)
[DPH1 DPH2L DPH2L1 OVCA1] 2-(3-amino-3-carboxypropyl)histidine synthase subunit 1 (EC 2.5.1.108) (Diphthamide biosynthesis protein 1) (Diphtheria toxin resistance protein 1) (Ovarian cancer-associated gene 1 protein) (S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase 1)
[TCF7L2 TCF4] Transcription factor 7-like 2 (HMG box transcription factor 4) (T-cell-specific transcription factor 4) (T-cell factor 4) (TCF-4) (hTCF-4)
[SLC35C2 C20orf5 OVCOV1 CGI-15] Solute carrier family 35 member C2 (Ovarian cancer-overexpressed gene 1 protein)
[Gpr68 Ogr1] Ovarian cancer G-protein coupled receptor 1 (G-protein coupled receptor 68) (Sphingosylphosphorylcholine receptor)
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[ENOX2 COVA1] Ecto-NOX disulfide-thiol exchanger 2 (APK1 antigen) (Cytosolic ovarian carcinoma antigen 1) (Tumor-associated hydroquinone oxidase) (tNOX) [Includes: Hydroquinone [NADH] oxidase (EC 1.-.-.-); Protein disulfide-thiol oxidoreductase (EC 1.-.-.-)]
[FOLR1 FOLR] Folate receptor alpha (FR-alpha) (Adult folate-binding protein) (FBP) (Folate receptor 1) (Folate receptor, adult) (KB cells FBP) (Ovarian tumor-associated antigen MOv18)
[SEPTIN9 KIAA0991 MSF SEPT9] Septin-9 (MLL septin-like fusion protein MSF-A) (MLL septin-like fusion protein) (Ovarian/Breast septin) (Ov/Br septin) (Septin D1)
[Bcl2l11 Bim Bod] Bcl-2-like protein 11 (Bcl2-L-11) (Bcl-2-related ovarian death protein) (Bcl2-interacting mediator of cell death)
[NCOA3 AIB1 BHLHE42 RAC3 TRAM1] Nuclear receptor coactivator 3 (NCoA-3) (EC 2.3.1.48) (ACTR) (Amplified in breast cancer 1 protein) (AIB-1) (CBP-interacting protein) (pCIP) (Class E basic helix-loop-helix protein 42) (bHLHe42) (Receptor-associated coactivator 3) (RAC-3) (Steroid receptor coactivator protein 3) (SRC-3) (Thyroid hormone receptor activator molecule 1) (TRAM-1)
[Bok Mtd] Bcl-2-related ovarian killer protein (Apoptosis activator Mtd) (Protein matador)
[BOK BCL2L9] Bcl-2-related ovarian killer protein (hBOK) (Bcl-2-like protein 9) (Bcl2-L-9)
[Bok] Bcl-2-related ovarian killer protein
[ARID4B BRCAA1 RBBP1L1 RBP1L1 SAP180] AT-rich interactive domain-containing protein 4B (ARID domain-containing protein 4B) (180 kDa Sin3-associated polypeptide) (Sin3-associated polypeptide p180) (Breast cancer-associated antigen BRCAA1) (Histone deacetylase complex subunit SAP180) (Retinoblastoma-binding protein 1-like 1)
[MUC1 PUM] Mucin-1 (MUC-1) (Breast carcinoma-associated antigen DF3) (Cancer antigen 15-3) (CA 15-3) (Carcinoma-associated mucin) (Episialin) (H23AG) (Krebs von den Lungen-6) (KL-6) (PEMT) (Peanut-reactive urinary mucin) (PUM) (Polymorphic epithelial mucin) (PEM) (Tumor-associated epithelial membrane antigen) (EMA) (Tumor-associated mucin) (CD antigen CD227) [Cleaved into: Mucin-1 subunit alpha (MUC1-NT) (MUC1-alpha); Mucin-1 subunit beta (MUC1-beta) (MUC1-CT)]
[Habp4] Intracellular hyaluronan-binding protein 4 (IHABP-4) (IHABP4) (Hyaluronic acid-binding protein 4)
[STRADA LYK5 STRAD] STE20-related kinase adapter protein alpha (STRAD alpha) (STE20-related adapter protein) (Serologically defined breast cancer antigen NY-BR-96)
[BRCA1 RNF53] Breast cancer type 1 susceptibility protein (EC 2.3.2.27) (RING finger protein 53) (RING-type E3 ubiquitin transferase BRCA1)
[ICK KIAA0936] Serine/threonine-protein kinase ICK (EC 2.7.11.1) (Intestinal cell kinase) (hICK) (Laryngeal cancer kinase 2) (LCK2) (MAK-related kinase) (MRK)
[BRCA2 FACD FANCD1] Breast cancer type 2 susceptibility protein (Fanconi anemia group D1 protein)
[AURKA AIK AIRK1 ARK1 AURA AYK1 BTAK IAK1 STK15 STK6] Aurora kinase A (EC 2.7.11.1) (Aurora 2) (Aurora/IPL1-related kinase 1) (ARK-1) (Aurora-related kinase 1) (hARK1) (Breast tumor-amplified kinase) (Serine/threonine-protein kinase 15) (Serine/threonine-protein kinase 6) (Serine/threonine-protein kinase aurora-A)
[SNRK KIAA0096 SNFRK] SNF-related serine/threonine-protein kinase (EC 2.7.11.1) (SNF1-related kinase)
[RHOBTB2 DBC2 KIAA0717] Rho-related BTB domain-containing protein 2 (Deleted in breast cancer 2 gene protein) (p83)
[Brca1] Breast cancer type 1 susceptibility protein homolog (EC 2.3.2.27) (RING-type E3 ubiquitin transferase BRCA1)
[PTK2 FAK FAK1] Focal adhesion kinase 1 (FADK 1) (EC 2.7.10.2) (Focal adhesion kinase-related nonkinase) (FRNK) (Protein phosphatase 1 regulatory subunit 71) (PPP1R71) (Protein-tyrosine kinase 2) (p125FAK) (pp125FAK)
[Foxc1 Fkh1 Fkhl7 Freac3 Mf1] Forkhead box protein C1 (Forkhead-related protein FKHL7) (Forkhead-related transcription factor 3) (FREAC-3) (Mesoderm/mesenchyme forkhead 1) (MF-1) (Transcription factor FKH-1)
[S100A9 CAGB CFAG MRP14] Protein S100-A9 (Calgranulin-B) (Calprotectin L1H subunit) (Leukocyte L1 complex heavy chain) (Migration inhibitory factor-related protein 14) (MRP-14) (p14) (S100 calcium-binding protein A9)
[GPER1 CEPR CMKRL2 DRY12 GPER GPR30] G-protein coupled estrogen receptor 1 (Chemoattractant receptor-like 2) (Flow-induced endothelial G-protein coupled receptor 1) (FEG-1) (G protein-coupled estrogen receptor 1) (G-protein coupled receptor 30) (GPCR-Br) (IL8-related receptor DRY12) (Lymphocyte-derived G-protein coupled receptor) (LYGPR) (Membrane estrogen receptor) (mER)

Bibliography :