ID   SPI2B_HUMAN             Reviewed;         258 AA.
AC   Q9BPZ2; Q7Z2M0;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   22-APR-2020, entry version 140.
DE   RecName: Full=Spindlin-2B;
DE   AltName: Full=Spindlin-like protein 2B;
DE            Short=SPIN-2;
DE            Short=SPIN-2B;
GN   Name=SPIN2B; Synonyms=SPIN2;
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], FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=12145692; DOI=10.1038/sj.leu.2402557;
RA   Fletcher B.S., Dragstedt C., Notterpek L., Nolan G.P.;
RT   "Functional cloning of SPIN-2, a nuclear anti-apoptotic protein with roles
RT   in cell cycle progression.";
RL   Leukemia 16:1507-1518(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland, and Placenta;
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   [4]
RP   FUNCTION, AND INTERACTION WITH C11ORF84/SPINDOC.
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).
CC   -!- FUNCTION: Involved in the regulation of cell cycle progression, this
CC       activity is related to the inhibition of apoptosis following the
CC       removal of essential growth factors (PubMed:12145692). Exhibits
CC       H3K4me3-binding activity (PubMed:29061846).
CC       {ECO:0000269|PubMed:12145692, ECO:0000269|PubMed:29061846}.
CC   -!- SUBUNIT: Interacts with C11orf84/SPINDOC (PubMed:29061846).
CC       {ECO:0000269|PubMed:29061846}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12145692}.
CC   -!- TISSUE SPECIFICITY: Detected in all the examined tissues with highest
CC       expression in liver, followed by heart, stomach, kidney, skeletal
CC       muscle, placenta, and pancreas.
CC   -!- MISCELLANEOUS: Overexpression in murine myeloid cell line 32Dcl3 causes
CC       G2/M arrest.
CC   -!- SIMILARITY: Belongs to the SPIN/STSY family. {ECO:0000305}.
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DR   EMBL; AF356353; AAK37566.1; -; mRNA.
DR   EMBL; AL022157; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC000044; AAH00044.1; -; mRNA.
DR   EMBL; BC071974; AAH71974.1; -; mRNA.
DR   CCDS; CCDS35311.1; -.
DR   RefSeq; NP_001006682.1; NM_001006681.1.
DR   RefSeq; NP_001006683.1; NM_001006682.1.
DR   RefSeq; NP_001006684.1; NM_001006683.1.
DR   RefSeq; XP_005262066.2; XM_005262009.4.
DR   RefSeq; XP_005262067.1; XM_005262010.1.
DR   RefSeq; XP_011529090.1; XM_011530788.2.
DR   RefSeq; XP_016885041.1; XM_017029552.1.
DR   PDB; 5LUG; X-ray; 1.70 A; A/B/C/D=44-258.
DR   PDBsum; 5LUG; -.
DR   SMR; Q9BPZ2; -.
DR   BioGrid; 138877; 24.
DR   IntAct; Q9BPZ2; 18.
DR   STRING; 9606.ENSP00000335008; -.
DR   iPTMnet; Q9BPZ2; -.
DR   PhosphoSitePlus; Q9BPZ2; -.
DR   BioMuta; SPIN2B; -.
DR   DMDM; 23822181; -.
DR   EPD; Q9BPZ2; -.
DR   jPOST; Q9BPZ2; -.
DR   MassIVE; Q9BPZ2; -.
DR   MaxQB; Q9BPZ2; -.
DR   PaxDb; Q9BPZ2; -.
DR   PeptideAtlas; Q9BPZ2; -.
DR   PRIDE; Q9BPZ2; -.
DR   ProteomicsDB; 78597; -.
DR   Antibodypedia; 26988; 69 antibodies.
DR   DNASU; 474343; -.
DR   Ensembl; ENST00000275988; ENSP00000275988; ENSG00000186787.
DR   Ensembl; ENST00000333933; ENSP00000335008; ENSG00000186787.
DR   GeneID; 474343; -.
DR   KEGG; hsa:474343; -.
DR   UCSC; uc004duy.5; human.
DR   CTD; 474343; -.
DR   GeneCards; SPIN2B; -.
DR   HGNC; HGNC:33147; SPIN2B.
DR   HPA; ENSG00000186787; Low tissue specificity.
DR   MIM; 300517; gene.
DR   neXtProt; NX_Q9BPZ2; -.
DR   PharmGKB; PA162404530; -.
DR   eggNOG; ENOG410IGUH; Eukaryota.
DR   eggNOG; ENOG410XQI2; LUCA.
DR   GeneTree; ENSGT00950000182925; -.
DR   HOGENOM; CLU_068595_0_0_1; -.
DR   InParanoid; Q9BPZ2; -.
DR   OMA; NTQEAEG; -.
DR   OrthoDB; 1027563at2759; -.
DR   PhylomeDB; Q9BPZ2; -.
DR   TreeFam; TF332665; -.
DR   GenomeRNAi; 474343; -.
DR   Pharos; Q9BPZ2; Tdark.
DR   PRO; PR:Q9BPZ2; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; Q9BPZ2; protein.
DR   Bgee; ENSG00000186787; Expressed in fundus of stomach and 91 other tissues.
DR   ExpressionAtlas; Q9BPZ2; baseline and differential.
DR   Genevisible; Q9BPZ2; HS.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0035064; F:methylated histone binding; IDA: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   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
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   1: Evidence at protein level;
KW   3D-structure; Apoptosis; Cell cycle; Nucleus; Reference proteome.
FT   CHAIN           1..258
FT                   /note="Spindlin-2B"
FT                   /id="PRO_0000181369"
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   BINDING         169
FT                   /note="Histone H3K4me3 and H3R8me2a"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y657"
FT   BINDING         176
FT                   /note="Histone H3K4me3 and H3R8me2a"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y657"
FT   BINDING         180
FT                   /note="Histone H3K4me3 and H3R8me2a"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y657"
FT   STRAND          53..58
FT                   /evidence="ECO:0000244|PDB:5LUG"
FT   STRAND          66..75
FT                   /evidence="ECO:0000244|PDB:5LUG"
FT   STRAND          83..87
FT                   /evidence="ECO:0000244|PDB:5LUG"
FT   STRAND          94..96
FT                   /evidence="ECO:0000244|PDB:5LUG"
FT   TURN            98..100
FT                   /evidence="ECO:0000244|PDB:5LUG"
FT   STRAND          104..110
FT                   /evidence="ECO:0000244|PDB:5LUG"
FT   HELIX           122..128
FT                   /evidence="ECO:0000244|PDB:5LUG"
FT   STRAND          132..138
FT                   /evidence="ECO:0000244|PDB:5LUG"
FT   STRAND          142..154
FT                   /evidence="ECO:0000244|PDB:5LUG"
FT   STRAND          156..158
FT                   /evidence="ECO:0000244|PDB:5LUG"
FT   STRAND          161..166
FT                   /evidence="ECO:0000244|PDB:5LUG"
FT   STRAND          169..175
FT                   /evidence="ECO:0000244|PDB:5LUG"
FT   HELIX           177..182
FT                   /evidence="ECO:0000244|PDB:5LUG"
FT   STRAND          186..188
FT                   /evidence="ECO:0000244|PDB:5LUG"
FT   STRAND          213..217
FT                   /evidence="ECO:0000244|PDB:5LUG"
FT   STRAND          221..231
FT                   /evidence="ECO:0000244|PDB:5LUG"
FT   STRAND          238..243
FT                   /evidence="ECO:0000244|PDB:5LUG"
FT   STRAND          250..253
FT                   /evidence="ECO:0000244|PDB:5LUG"
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
//