SPIN2_PONAB
ID SPIN2_PONAB Reviewed; 258 AA.
AC Q5RA80;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Spindlin-2;
DE AltName: Full=Spindlin-like protein 2;
DE Short=SPIN-2;
GN Name=SPIN2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be involved in the regulation of cell cycle progression.
CC Exhibits H3K4me3-binding activity. {ECO:0000250|UniProtKB:Q99865}.
CC -!- SUBUNIT: Interacts with C11orf84/SPINDOC.
CC {ECO:0000250|UniProtKB:Q99865}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BPZ2}.
CC -!- SIMILARITY: Belongs to the SPIN/STSY family. {ECO:0000305}.
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DR EMBL; CR859138; CAH91330.1; -; mRNA.
DR RefSeq; NP_001125785.1; NM_001132313.2.
DR AlphaFoldDB; Q5RA80; -.
DR SMR; Q5RA80; -.
DR STRING; 9601.ENSPPYP00000022839; -.
DR GeneID; 100172713; -.
DR KEGG; pon:100172713; -.
DR CTD; 474343; -.
DR eggNOG; ENOG502QRYD; Eukaryota.
DR InParanoid; Q5RA80; -.
DR OrthoDB; 1027563at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007276; P:gamete generation; IEA:InterPro.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
DR Gene3D; 2.80.10.70; -; 1.
DR InterPro; IPR029564; SPIN-2.
DR InterPro; IPR003671; SPIN/Ssty.
DR InterPro; IPR042567; SPIN/Ssty_sf.
DR PANTHER; PTHR10405; PTHR10405; 1.
DR PANTHER; PTHR10405:SF13; PTHR10405:SF13; 1.
DR Pfam; PF02513; Spin-Ssty; 3.
PE 2: Evidence at transcript level;
KW Apoptosis; Cell cycle; Nucleus; Reference proteome.
FT CHAIN 1..258
FT /note="Spindlin-2"
FT /id="PRO_0000181370"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..99
FT /note="Tudor-like domain 1"
FT /evidence="ECO:0000255"
FT REGION 129..178
FT /note="Tudor-like domain 2"
FT /evidence="ECO:0000255"
FT REGION 138
FT /note="Histone H3K4me3 and H3R8me2a binding"
FT /evidence="ECO:0000250|UniProtKB:Q9Y657"
FT REGION 210..255
FT /note="Tudor-like domain 3"
FT /evidence="ECO:0000255"
FT REGION 246..248
FT /note="Histone H3K4me3 and H3R8me2a binding"
FT /evidence="ECO:0000250|UniProtKB:Q9Y657"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 169
FT /note="Histone H3K4me3 and H3R8me2a binding"
FT /evidence="ECO:0000250|UniProtKB:Q9Y657"
FT SITE 176
FT /note="Histone H3K4me3 and H3R8me2a binding"
FT /evidence="ECO:0000250|UniProtKB:Q9Y657"
FT SITE 180
FT /note="Histone H3K4me3 and H3R8me2a binding"
FT /evidence="ECO:0000250|UniProtKB:Q9Y657"
SQ SEQUENCE 258 AA; 29158 MW; CAD74289970B4BCD CRC64;
MKTPNAQEAE GQQTRAAAGR ATGSANMTKK KVSQKKQRGR PSSQPRRNIV GCRISHGWKE
GDEPITQWKG TVLDQVPINP SLYLVKYDGI DCVYGLELHR DERVLSLKIL SDRVASSHIS
DANLANTIIG KAVEHMFEGE HGSKDEWRGM VLAQAPIMKA WFYITYEKDP VLYMYQLLDD
YKEGDLRIMP ESSESPPTER EPGGVVDGLI GKHVEYTKED GSKRIGMVIH QVEAKPSVYF
IKFDDDFHIY VYDLVKKS