SP20H_MOUSE
ID SP20H_MOUSE Reviewed; 530 AA.
AC Q7TT00; Q8BG53; Q9JLS9;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Transcription factor SPT20 homolog;
DE AltName: Full=p38-interacting protein;
DE Short=p38IP;
GN Name=Supt20h; Synonyms=D3Ertd300e, Fam48a, Supt20;
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 [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY,
RP DISRUPTION PHENOTYPE, AND INTERACTION WITH MAPK14.
RX PubMed=16751104; DOI=10.1016/j.cell.2006.03.048;
RA Zohn I.E., Li Y., Skolnik E.Y., Anderson K.V., Han J., Niswander L.;
RT "p38 and a p38-interacting protein are critical for downregulation of E-
RT cadherin during mouse gastrulation.";
RL Cell 125:957-969(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296 AND SER-520, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Required for MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or
CC MAPK14) activation during gastrulation. Required for down-regulation of
CC E-cadherin during gastrulation by regulating E-cadherin protein level
CC downstream from NCK-interacting kinase (NIK) and independently of the
CC regulation of transcription by FGF signaling and Snail. Required for
CC starvation-induced ATG9A trafficking during autophagy.
CC {ECO:0000269|PubMed:16751104}.
CC -!- SUBUNIT: Interacts with ATG9A (By similarity). Interacts with MAPK14.
CC {ECO:0000250, ECO:0000269|PubMed:16751104}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q7TT00-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TT00-2; Sequence=VSP_014880;
CC Name=3;
CC IsoId=Q7TT00-3; Sequence=VSP_014881, VSP_014882;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed throughout development.
CC {ECO:0000269|PubMed:16751104}.
CC -!- DISRUPTION PHENOTYPE: Mice show gastrulation defects in which mesoderm
CC migration is defective due to deficiency in E-cadherin protein down-
CC regulation in the primitive streak. A weaker mutation named droopy eye
CC (drey), which affects splicing causes incompletely penetrant defects in
CC neural tube closure, eye development and gastrulation.
CC {ECO:0000269|PubMed:16751104}.
CC -!- SIMILARITY: Belongs to the SPT20 family. {ECO:0000305}.
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DR EMBL; AF139179; AAF61447.1; -; mRNA.
DR EMBL; AK050619; BAC34346.1; -; mRNA.
DR EMBL; AK083379; BAC38893.1; -; mRNA.
DR EMBL; BC052702; AAH52702.1; -; mRNA.
DR CCDS; CCDS38431.1; -. [Q7TT00-2]
DR RefSeq; NP_064379.1; NM_019995.3. [Q7TT00-2]
DR AlphaFoldDB; Q7TT00; -.
DR SMR; Q7TT00; -.
DR BioGRID; 208175; 4.
DR ComplexPortal; CPX-6803; SAGA complex, KAT2B variant.
DR ComplexPortal; CPX-920; SAGA complex, KAT2A variant.
DR IntAct; Q7TT00; 1.
DR STRING; 10090.ENSMUSP00000131454; -.
DR iPTMnet; Q7TT00; -.
DR PhosphoSitePlus; Q7TT00; -.
DR EPD; Q7TT00; -.
DR jPOST; Q7TT00; -.
DR MaxQB; Q7TT00; -.
DR PaxDb; Q7TT00; -.
DR PeptideAtlas; Q7TT00; -.
DR PRIDE; Q7TT00; -.
DR Antibodypedia; 49228; 89 antibodies from 20 providers.
DR DNASU; 56790; -.
DR Ensembl; ENSMUST00000170552; ENSMUSP00000131454; ENSMUSG00000027751. [Q7TT00-2]
DR Ensembl; ENSMUST00000200439; ENSMUSP00000143059; ENSMUSG00000027751. [Q7TT00-1]
DR GeneID; 56790; -.
DR KEGG; mmu:56790; -.
DR UCSC; uc008pfk.1; mouse. [Q7TT00-3]
DR UCSC; uc008pfl.1; mouse. [Q7TT00-2]
DR CTD; 56790; -.
DR MGI; MGI:1929651; Supt20.
DR VEuPathDB; HostDB:ENSMUSG00000027751; -.
DR eggNOG; ENOG502QS30; Eukaryota.
DR GeneTree; ENSGT00390000013549; -.
DR HOGENOM; CLU_020200_2_0_1; -.
DR InParanoid; Q7TT00; -.
DR OrthoDB; 369747at2759; -.
DR PhylomeDB; Q7TT00; -.
DR TreeFam; TF329155; -.
DR BioGRID-ORCS; 56790; 14 hits in 74 CRISPR screens.
DR ChiTaRS; Supt20; mouse.
DR PRO; PR:Q7TT00; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q7TT00; protein.
DR Bgee; ENSMUSG00000027751; Expressed in spermatocyte and 250 other tissues.
DR ExpressionAtlas; Q7TT00; baseline and differential.
DR Genevisible; Q7TT00; MM.
DR GO; GO:0000124; C:SAGA complex; IBA:GO_Central.
DR GO; GO:0070461; C:SAGA-type complex; ISO:MGI.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0007369; P:gastrulation; IEA:UniProtKB-KW.
DR GO; GO:0043966; P:histone H3 acetylation; IC:ComplexPortal.
DR GO; GO:0045722; P:positive regulation of gluconeogenesis; IGI:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0006282; P:regulation of DNA repair; IC:ComplexPortal.
DR GO; GO:0043484; P:regulation of RNA splicing; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR021950; Spt20.
DR PANTHER; PTHR13526; PTHR13526; 1.
DR Pfam; PF12090; Spt20; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Gastrulation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..530
FT /note="Transcription factor SPT20 homolog"
FT /id="PRO_0000187040"
FT REGION 419..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 491
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEM7"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEM7"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 55
FT /note="K -> KQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16751104"
FT /id="VSP_014880"
FT VAR_SEQ 384
FT /note="H -> Q (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014881"
FT VAR_SEQ 385..530
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014882"
SQ SEQUENCE 530 AA; 59519 MW; 44CCC752310C0F5D CRC64;
MQQAVEQALD CAEYIVESAQ QRPPKRKYLS SGRKSIFQKL YDLYVEECEK EPEVKKLRRN
VNLLEKLVMQ ETLSCLVVNL YPGNEGYSLM LRGKNGSDSE TIRLPYEEGE LLEYLDAEEL
PPILVDLLEK SQVNIFHCGC VIAEIRDYRQ SSNMKSPGYQ SRHILLRPTM QTLVCDVHSI
TSDNHKWTQE DKLLLESQLI LATAEPLCLD PSVAVACTAN RLLYNRQKMN TRPMKRCWKR
YSRSSLNRQQ DLSHGPPPPQ LRLLDFLQKR KERKAGQHYD LKISKAGNCV DMWKRSPCNL
AVPSEVDVEK YAKVEESIKS DDSQPTMWPA HDVKDDYVFE CEGGNQYQKT KLTILQSLGD
PLYYGKIQPW KADEENDSQM SPSHSSADDH SNWFVIGSKT DAERVVNQYQ ELVQNEAKCP
VKMSHSSSGS AALSPGEEAE QAETSSIQSS VLGKGVKHRP PPIKLPSGSG NSSSGNYFTA
QQASSFLKSP TPPPSCKPSL SRKSSVDLSQ VSMLSPAALS PASSSQRHES
