SPI2B_HUMAN
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 03-AUG-2022, entry version 150.
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 -!- INTERACTION:
CC Q9BPZ2; P13473-2: LAMP2; NbExp=3; IntAct=EBI-21726245, EBI-21591415;
CC Q9BPZ2; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-21726245, EBI-2623095;
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 AlphaFoldDB; Q9BPZ2; -.
DR SMR; Q9BPZ2; -.
DR BioGRID; 138877; 49.
DR IntAct; Q9BPZ2; 20.
DR STRING; 9606.ENSP00000335008; -.
DR BindingDB; Q9BPZ2; -.
DR ChEMBL; CHEMBL4523440; -.
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 PRIDE; Q9BPZ2; -.
DR ProteomicsDB; 78597; -.
DR Antibodypedia; 26988; 89 antibodies from 18 providers.
DR DNASU; 474343; -.
DR Ensembl; ENST00000275988.5; ENSP00000275988.5; ENSG00000186787.10.
DR Ensembl; ENST00000333933.3; ENSP00000335008.3; ENSG00000186787.10.
DR Ensembl; ENST00000434397.3; ENSP00000404314.2; ENSG00000186787.10.
DR GeneID; 474343; -.
DR KEGG; hsa:474343; -.
DR MANE-Select; ENST00000434397.3; ENSP00000404314.2; NM_001006681.2; NP_001006682.1.
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 VEuPathDB; HostDB:ENSG00000186787; -.
DR eggNOG; ENOG502QRYD; Eukaryota.
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 PathwayCommons; Q9BPZ2; -.
DR SignaLink; Q9BPZ2; -.
DR BioGRID-ORCS; 474343; 3 hits in 627 CRISPR screens.
DR GenomeRNAi; 474343; -.
DR Pharos; Q9BPZ2; Tchem.
DR PRO; PR:Q9BPZ2; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9BPZ2; protein.
DR Bgee; ENSG00000186787; Expressed in hypothalamus and 97 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 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"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:5LUG"
FT STRAND 66..75
FT /evidence="ECO:0007829|PDB:5LUG"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:5LUG"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:5LUG"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:5LUG"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:5LUG"
FT HELIX 122..128
FT /evidence="ECO:0007829|PDB:5LUG"
FT STRAND 132..138
FT /evidence="ECO:0007829|PDB:5LUG"
FT STRAND 142..154
FT /evidence="ECO:0007829|PDB:5LUG"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:5LUG"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:5LUG"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:5LUG"
FT HELIX 177..182
FT /evidence="ECO:0007829|PDB:5LUG"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:5LUG"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:5LUG"
FT STRAND 221..231
FT /evidence="ECO:0007829|PDB:5LUG"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:5LUG"
FT STRAND 250..253
FT /evidence="ECO:0007829|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
