SPI2A_HUMAN
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 03-AUG-2022, entry version 160.
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 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; Q99865; -.
DR PeptideAtlas; Q99865; -.
DR PRIDE; Q99865; -.
DR Antibodypedia; 55479; 57 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 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; FYITCEK; -.
DR OrthoDB; 1027563at2759; -.
DR PhylomeDB; Q99865; -.
DR TreeFam; TF332665; -.
DR PathwayCommons; Q99865; -.
DR SignaLink; Q99865; -.
DR BioGRID-ORCS; 54466; 31 hits in 603 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 stromal cell of endometrium and 96 other tissues.
DR ExpressionAtlas; Q99865; baseline and differential.
DR Genevisible; Q99865; 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: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 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