SPT2_MOUSE
ID SPT2_MOUSE Reviewed; 682 AA.
AC Q68FG3; Q8BIR1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Protein SPT2 homolog;
DE AltName: Full=SPT2 domain-containing protein 1;
GN Name=Spty2d1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
CC -!- FUNCTION: Histone chaperone that stabilizes pre-existing histone
CC tetramers and regulates replication-independent histone exchange on
CC chromatin. Required for normal chromatin refolding in the coding region
CC of transcribed genes, and for the suppression of spurious
CC transcription. Binds DNA and histones and promotes nucleosome assembly
CC (in vitro). Facilitates formation of tetrameric histone complexes
CC containing histone H3 and H4 (By similarity). Modulates RNA polymerase
CC 1-mediated transcription (By similarity). Binds DNA, with a preference
CC for branched DNA species, such as Y-form DNA and Holliday junction DNA
CC (By similarity). {ECO:0000250|UniProtKB:E1BUG7,
CC ECO:0000250|UniProtKB:Q68D10}.
CC -!- SUBUNIT: Interacts with histones. Interacts with a heterotetrameric
CC complex formed by histone H3 and H4, especially when the histone
CC tetramer is not bound to DNA. Interacts with histone H3.3 (By
CC similarity). {ECO:0000250|UniProtKB:Q68D10}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:E1BUG7}.
CC -!- DOMAIN: The acidic C-terminal domain mediates interaction with histone
CC H3/H4 complexes. {ECO:0000250|UniProtKB:Q68D10}.
CC -!- SIMILARITY: Belongs to the SPT2 family. {ECO:0000305}.
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DR EMBL; AK030869; BAC27165.1; -; mRNA.
DR EMBL; BC079859; AAH79859.1; -; mRNA.
DR CCDS; CCDS21293.1; -.
DR RefSeq; NP_780527.2; NM_175318.4.
DR AlphaFoldDB; Q68FG3; -.
DR SMR; Q68FG3; -.
DR STRING; 10090.ENSMUSP00000059457; -.
DR iPTMnet; Q68FG3; -.
DR PhosphoSitePlus; Q68FG3; -.
DR EPD; Q68FG3; -.
DR jPOST; Q68FG3; -.
DR MaxQB; Q68FG3; -.
DR PaxDb; Q68FG3; -.
DR PeptideAtlas; Q68FG3; -.
DR PRIDE; Q68FG3; -.
DR ProteomicsDB; 263334; -.
DR Antibodypedia; 64057; 16 antibodies from 8 providers.
DR Ensembl; ENSMUST00000061639; ENSMUSP00000059457; ENSMUSG00000049516.
DR GeneID; 101685; -.
DR KEGG; mmu:101685; -.
DR UCSC; uc009gzx.2; mouse.
DR CTD; 144108; -.
DR MGI; MGI:2142062; Spty2d1.
DR VEuPathDB; HostDB:ENSMUSG00000049516; -.
DR eggNOG; ENOG502QWHS; Eukaryota.
DR GeneTree; ENSGT00940000154133; -.
DR HOGENOM; CLU_025934_0_0_1; -.
DR InParanoid; Q68FG3; -.
DR OMA; MMDFDNI; -.
DR OrthoDB; 1092455at2759; -.
DR PhylomeDB; Q68FG3; -.
DR TreeFam; TF350176; -.
DR BioGRID-ORCS; 101685; 9 hits in 72 CRISPR screens.
DR ChiTaRS; Spty2d1; mouse.
DR PRO; PR:Q68FG3; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q68FG3; protein.
DR Bgee; ENSMUSG00000049516; Expressed in humerus cartilage element and 222 other tissues.
DR Genevisible; Q68FG3; MM.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0140713; F:histone chaperone activity; ISS:UniProtKB.
DR GO; GO:0001042; F:RNA polymerase I core binding; ISS:UniProtKB.
DR GO; GO:0031507; P:heterochromatin assembly; ISS:UniProtKB.
DR GO; GO:0043486; P:histone exchange; IBA:GO_Central.
DR GO; GO:0006334; P:nucleosome assembly; ISS:UniProtKB.
DR GO; GO:0010847; P:regulation of chromatin assembly; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR InterPro; IPR013256; Chromatin_SPT2.
DR Pfam; PF08243; SPT2; 1.
DR SMART; SM00784; SPT2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Coiled coil; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..682
FT /note="Protein SPT2 homolog"
FT /id="PRO_0000315737"
FT REGION 1..569
FT /note="Important for interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:Q68D10"
FT REGION 80..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..682
FT /note="Important for interaction with histones"
FT /evidence="ECO:0000250|UniProtKB:Q68D10"
FT REGION 641..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 46..82
FT /evidence="ECO:0000255"
FT COILED 642..682
FT /evidence="ECO:0000255"
FT COMPBIAS 80..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..146
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..674
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68D10"
FT MOD_RES 581
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q68D10"
FT MOD_RES 596
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68D10"
FT CROSSLNK 37
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q68D10"
FT CROSSLNK 186
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q68D10"
FT CONFLICT 147
FT /note="E -> K (in Ref. 1; BAC27165)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 682 AA; 74818 MW; C48029515D8CB0AE CRC64;
MDFREILLIA SKGQGVNHVP KRYSLAVGPP KKDPKVKGVQ SAAVQAFLRR KEEELRQKAL
EEKKRKEELV KKRIELKHDK KARAMAKRTK DNFHGYDGIP VEEKTKKKQL VESHLNQGTD
QEYDVEEEDF IDYNQAELDQ DYEEEQEPPK AESKPKAPLK SAPSPMNFTD LLRLAEKKQF
EPVEIKVVKK AEDRPLTAEE LREREFLERK HRKKKPEPDA KLPPPVLKKA PSHKDIMGTK
PSRGAGDRQL ASKGLPFPQA EKKFRPSTAS EKQAALSSPK SLPGERTKVG SGSSTQPSLR
EGHNRPVFNG AGKPRPSTCS PSVPKTPASG TQKSASEHKA KKPLPSHPSH SKPGPTVLSH
NKSKSPGVRQ PGSNSGSAPG QPNPGTARPT LSSGPVPRRQ NGSSSSGPEQ SAGGIRKLAS
NSHLSGRTLN GTNGPGRPAS SSSGPGRPIS GSAGSGRPVG SSGGPGQPVN NPHDLRRPMN
SLSSPGRAVS GPGRSISGSI PAGRTVNSGP GRPVSSLGPG RAVSNPGLPT KPRCTVVSET
ISSKNIISRS SNGQINGMKP LLSGYRSAQG PQRLPFPTGY KRPREYEEDD DDEYDSEMDD
FIEDEGEPQE EISKHIREIF GYDRKKYKDE SDYALRYMES SWKEQQKEEA KSLRLGMQED
LEEMRREEEE LKRRKAKKLK RH
