ID   SPI2A_HUMAN             Reviewed;         258 AA.
AC   Q99865; O75650; Q6IPW2; Q9UJJ0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 3.
DT   24-JAN-2024, entry version 168.
DE   RecName: Full=Spindlin-2A;
DE   AltName: Full=Protein DXF34;
DE   AltName: Full=Spindlin-like protein 2A;
DE            Short=SPIN-2;
DE            Short=SPIN-2A;
GN   Name=SPIN2A; Synonyms=DXF34, 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].
RC   TISSUE=Fetal brain;
RX   PubMed=9271673; DOI=10.1007/s003359900538;
RA   Laval S.H., Reed V., Blair H.J., Boyd Y.;
RT   "The structure of DXF34, a human X-linked sequence family with homology to
RT   a transcribed mouse Y-linked repeat.";
RL   Mamm. Genome 8:689-691(1997).
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=Lung;
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   PROTEIN SEQUENCE OF 70-86 AND 114-131, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RA   Bienvenut W.V., Calvo F., Kolch W.;
RL   Submitted (MAR-2008) to UniProtKB.
RN   [5]
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: May be involved in the regulation of cell cycle progression
CC       (By similarity). Exhibits H3K4me3-binding activity (PubMed:29061846).
CC       {ECO:0000250|UniProtKB:Q9BPZ2, ECO:0000269|PubMed:29061846}.
CC   -!- SUBUNIT: Interacts with C11orf84/SPINDOC (PubMed:29061846).
CC       {ECO:0000269|PubMed:29061846}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BPZ2}.
CC   -!- SIMILARITY: Belongs to the SPIN/STSY family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA70988.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; Y09858; CAA70988.1; ALT_FRAME; mRNA.
DR   EMBL; AL022157; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC071694; AAH71694.1; -; mRNA.
DR   CCDS; CCDS35312.1; -.
DR   RefSeq; NP_061876.3; NM_019003.3.
DR   RefSeq; XP_005262073.3; XM_005262016.4.
DR   RefSeq; XP_005262074.3; XM_005262017.4.
DR   RefSeq; XP_005262076.1; XM_005262019.3.
DR   RefSeq; XP_016885087.1; XM_017029598.1.
DR   AlphaFoldDB; Q99865; -.
DR   SMR; Q99865; -.
DR   BioGRID; 119972; 20.
DR   IntAct; Q99865; 2.
DR   MINT; Q99865; -.
DR   STRING; 9606.ENSP00000364043; -.
DR   GlyGen; Q99865; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q99865; -.
DR   PhosphoSitePlus; Q99865; -.
DR   BioMuta; SPIN2A; -.
DR   DMDM; 116242797; -.
DR   EPD; Q99865; -.
DR   jPOST; Q99865; -.
DR   MassIVE; Q99865; -.
DR   MaxQB; Q99865; -.
DR   PaxDb; 9606-ENSP00000364043; -.
DR   PeptideAtlas; Q99865; -.
DR   Pumba; Q99865; -.
DR   Antibodypedia; 55479; 60 antibodies from 17 providers.
DR   DNASU; 54466; -.
DR   Ensembl; ENST00000374906.4; ENSP00000364041.3; ENSG00000147059.9.
DR   Ensembl; ENST00000374908.1; ENSP00000364043.1; ENSG00000147059.9.
DR   GeneID; 54466; -.
DR   KEGG; hsa:54466; -.
DR   MANE-Select; ENST00000374906.4; ENSP00000364041.3; NM_019003.5; NP_061876.3.
DR   UCSC; uc004dvb.3; human.
DR   AGR; HGNC:20694; -.
DR   CTD; 54466; -.
DR   DisGeNET; 54466; -.
DR   GeneCards; SPIN2A; -.
DR   HGNC; HGNC:20694; SPIN2A.
DR   HPA; ENSG00000147059; Low tissue specificity.
DR   MIM; 300621; gene.
DR   neXtProt; NX_Q99865; -.
DR   OpenTargets; ENSG00000147059; -.
DR   PharmGKB; PA144596490; -.
DR   VEuPathDB; HostDB:ENSG00000147059; -.
DR   eggNOG; ENOG502QRYD; Eukaryota.
DR   GeneTree; ENSGT00950000182925; -.
DR   HOGENOM; CLU_068595_0_0_1; -.
DR   InParanoid; Q99865; -.
DR   OMA; IWAPEAR; -.
DR   OrthoDB; 5246248at2759; -.
DR   PhylomeDB; Q99865; -.
DR   TreeFam; TF332665; -.
DR   PathwayCommons; Q99865; -.
DR   SignaLink; Q99865; -.
DR   BioGRID-ORCS; 54466; 31 hits in 651 CRISPR screens.
DR   GenomeRNAi; 54466; -.
DR   Pharos; Q99865; Tdark.
DR   PRO; PR:Q99865; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; Q99865; Protein.
DR   Bgee; ENSG00000147059; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 96 other cell types or tissues.
DR   ExpressionAtlas; Q99865; baseline and differential.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0007276; P:gamete generation; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR   Gene3D; 2.80.10.70; Spindlin/Ssty; 1.
DR   InterPro; IPR003671; SPIN/Ssty.
DR   InterPro; IPR042567; SPIN/Ssty_sf.
DR   PANTHER; PTHR10405; SPINDLIN; 1.
DR   PANTHER; PTHR10405:SF13; SPINDLIN-2A-RELATED; 1.
DR   Pfam; PF02513; Spin-Ssty; 3.
DR   Genevisible; Q99865; HS.
PE   1: Evidence at protein level;
KW   Cell cycle; Direct protein sequencing; Nucleus; Reference proteome.
FT   CHAIN           1..258
FT                   /note="Spindlin-2A"
FT                   /id="PRO_0000181371"
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   CONFLICT        46
FT                   /note="R -> C (in Ref. 1; CAA70988 and 3; AAH71694)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   258 AA;  29188 MW;  DE860789970B4BCD CRC64;
     MKTPNAQEAE GQQTRAAAGR ATGSANMTKK KVSQKKQRGR PSSQPRRNIV GCRISHGWKE
     GDEPITQWKG TVLDQVPINP SLYLVKYDGI DCVYGLELHR DERVLSLKIL SDRVASSHIS
     DANLANTIIG KAVEHMFEGE HGSKDEWRGM VLAQAPIMKA WFYITYEKDP VLYMYQLLDD
     YKEGDLRIMP ESSESPPTER EPGGVVDGLI GKHVEYTKED GSKRIGMVIH QVETKPSVYF
     IKFDDDFHIY VYDLVKKS
//