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SPA24_MOUSE
ID   SPA24_MOUSE             Reviewed;         205 AA.
AC   Q6P926; Q5MMR1; Q9D4P6;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Spermatogenesis-associated protein 24;
DE   AltName: Full=TATA-binding protein-like factor-interacting protein;
DE            Short=TLF-interacting protein;
DE   AltName: Full=TRF2-interacting protein in testis;
DE   AltName: Full=Testis protein T6441 homolog;
GN   Name=Spata24; Synonyms=Tipt, Tipt2;
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 3), FUNCTION, SUBUNIT, INTERACTION WITH
RP   CBX3; CBX5 AND TBPL1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=129S2/SvPas; TISSUE=Testis;
RX   PubMed=18418073; DOI=10.4161/cc.7.10.5835;
RA   Brancorsini S., Davidson I., Sassone-Corsi P.;
RT   "TIPT, a male germ cell-specific partner of TRF2, is chromatin-associated
RT   and interacts with HP1.";
RL   Cell Cycle 7:1415-1422(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
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   TISSUE=Testis;
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, SUBUNIT, INTERACTION WITH GMNN; GTF2B; PHCF1; RNF2; SCHM1 AND
RP   TBPL1, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP   186-LYS--LYS-188.
RX   PubMed=19515240; DOI=10.1186/1471-2091-10-16;
RA   Pitulescu M.E., Teichmann M., Luo L., Kessel M.;
RT   "TIPT2 and geminin interact with basal transcription factors to synergize
RT   in transcriptional regulation.";
RL   BMC Biochem. 10:16-16(2009).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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: Binds DNA with high affinity but does not bind to TATA boxes.
CC       Synergises with GMNN and TBP in activation of TATA box-containing
CC       promoters and with GMNN and TBPL1 in activation of the NF1 TATA-less
CC       promoter. May play a role in cytoplasm movement and removal during
CC       spermiogenesis. {ECO:0000269|PubMed:18418073,
CC       ECO:0000269|PubMed:19515240}.
CC   -!- SUBUNIT: Homodimer. Interacts with CBX3, CBX5, GMNN, GTF2B, TBPL1 and
CC       the polycomb proteins PHCF2, RNF2 and SCMH1 but not with CBX1 or PCGF2.
CC       {ECO:0000269|PubMed:18418073, ECO:0000269|PubMed:19515240}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. Nucleus,
CC       nucleoplasm. Note=Associated with chromatin.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q6P926-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6P926-2; Sequence=VSP_032868, VSP_032869;
CC       Name=3;
CC         IsoId=Q6P926-3; Sequence=VSP_032869;
CC   -!- TISSUE SPECIFICITY: Testis-specific (at protein level).
CC       {ECO:0000269|PubMed:18418073}.
CC   -!- DEVELOPMENTAL STAGE: In the embryo, abundant at 7.5 dpc and 8.5 dpc
CC       with higher levels at 9.5 dpc, 10.5 dpc and 11.5 dpc. Expression is low
CC       during the first two weeks after birth, increases during the third week
CC       and remains elevated in 4-week-old and adult mice. During
CC       spermatogenesis, expressed in spermatocytes mainly from zygotene to
CC       meiotic metaphase divisions and increases post-meiotically in round
CC       spermatids. Expression decreases in stage IV spermatids.
CC       {ECO:0000269|PubMed:18418073, ECO:0000269|PubMed:19515240}.
CC   -!- SIMILARITY: Belongs to the SPATA24 family. {ECO:0000305}.
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DR   EMBL; AY730532; AAV97890.1; -; mRNA.
DR   EMBL; AK016341; BAB30197.1; -; mRNA.
DR   EMBL; BC060950; AAH60950.1; -; mRNA.
DR   CCDS; CCDS29146.1; -. [Q6P926-1]
DR   CCDS; CCDS29147.1; -. [Q6P926-3]
DR   RefSeq; NP_082009.3; NM_027733.5. [Q6P926-3]
DR   RefSeq; NP_083761.1; NM_029485.2. [Q6P926-1]
DR   AlphaFoldDB; Q6P926; -.
DR   SMR; Q6P926; -.
DR   BioGRID; 214576; 10.
DR   STRING; 10090.ENSMUSP00000025209; -.
DR   iPTMnet; Q6P926; -.
DR   PhosphoSitePlus; Q6P926; -.
DR   PaxDb; Q6P926; -.
DR   PRIDE; Q6P926; -.
DR   ProteomicsDB; 257292; -. [Q6P926-1]
DR   ProteomicsDB; 257293; -. [Q6P926-2]
DR   ProteomicsDB; 257294; -. [Q6P926-3]
DR   DNASU; 71242; -.
DR   Ensembl; ENSMUST00000025209; ENSMUSP00000025209; ENSMUSG00000024352. [Q6P926-1]
DR   Ensembl; ENSMUST00000096573; ENSMUSP00000094324; ENSMUSG00000024352. [Q6P926-3]
DR   GeneID; 71242; -.
DR   KEGG; mmu:71242; -.
DR   UCSC; uc008emn.1; mouse. [Q6P926-1]
DR   UCSC; uc008emo.2; mouse. [Q6P926-3]
DR   UCSC; uc008emp.2; mouse. [Q6P926-2]
DR   CTD; 202051; -.
DR   MGI; MGI:1918492; Spata24.
DR   VEuPathDB; HostDB:ENSMUSG00000024352; -.
DR   eggNOG; ENOG502S3HF; Eukaryota.
DR   GeneTree; ENSGT00390000007817; -.
DR   HOGENOM; CLU_115899_0_0_1; -.
DR   InParanoid; Q6P926; -.
DR   OMA; HITKQED; -.
DR   OrthoDB; 1521659at2759; -.
DR   PhylomeDB; Q6P926; -.
DR   TreeFam; TF338733; -.
DR   BioGRID-ORCS; 71242; 4 hits in 72 CRISPR screens.
DR   ChiTaRS; Spata24; mouse.
DR   PRO; PR:Q6P926; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   RNAct; Q6P926; protein.
DR   Bgee; ENSMUSG00000024352; Expressed in spermatid and 173 other tissues.
DR   ExpressionAtlas; Q6P926; baseline and differential.
DR   Genevisible; Q6P926; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR   InterPro; IPR029176; SPATA24.
DR   PANTHER; PTHR35155; PTHR35155; 1.
DR   Pfam; PF15175; SPATA24; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Developmental protein;
KW   Differentiation; DNA-binding; Nucleus; Reference proteome; Spermatogenesis;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..205
FT                   /note="Spermatogenesis-associated protein 24"
FT                   /id="PRO_0000328981"
FT   REGION          138..185
FT                   /note="Required for interaction with CBX5 and TBPL1"
FT                   /evidence="ECO:0000269|PubMed:18418073"
FT   REGION          185..205
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          17..167
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..39
FT                   /note="MATPLGWSQGGSGSVCLAFDQLRDVIESQEELIHQLRNV -> MCPCPFLSQ
FT                   ALLQ (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_032868"
FT   VAR_SEQ         129..205
FT                   /note="EIESHIIKQEDILNGKENEIKELQQVISQQKQNFRNHISDFRIQKQQETYMA
FT                   QVLDQKRKKATGMRRARSRQCSREK -> GRREARAAPQVNIHGLFTNSPMTVPKAGLY
FT                   PNFCPRLRIQASPVLRKCLQGPGRSRK (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072,
FT                   ECO:0000303|PubMed:18418073"
FT                   /id="VSP_032869"
FT   MUTAGEN         186..188
FT                   /note="KRK->DRD: Abolishes binding to GMNN."
FT                   /evidence="ECO:0000269|PubMed:19515240"
SQ   SEQUENCE   205 AA;  23769 MW;  2FE57212C343AF1D CRC64;
     MATPLGWSQG GSGSVCLAFD QLRDVIESQE ELIHQLRNVM VLQDENFVSK EEFHEIEKKL
     VEEKAAHAKT KALLAKEEEK LQFALGEVEV LSKQLEKEKM AFEKALSSVK SRVLQESSKK
     DQLITKCNEI ESHIIKQEDI LNGKENEIKE LQQVISQQKQ NFRNHISDFR IQKQQETYMA
     QVLDQKRKKA TGMRRARSRQ CSREK
 
 
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