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SYF1_MOUSE
ID   SYF1_MOUSE              Reviewed;         855 AA.
AC   Q9DCD2; Q8VDT5; Q9CVD8;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 164.
DE   RecName: Full=Pre-mRNA-splicing factor SYF1;
DE   AltName: Full=XPA-binding protein 2;
GN   Name=Xab2; Synonyms=Syf1;
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 {ECO:0000312|EMBL:BAB22435.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney, and Stomach;
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].
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   [3]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=15725628; DOI=10.1016/j.dnarep.2004.12.004;
RA   Yonemasu R., Minami M., Nakatsu Y., Takeuchi M., Kuraoka I., Matsuda Y.,
RA   Higashi Y., Kondoh H., Tanaka K.;
RT   "Disruption of mouse XAB2 gene involved in pre-mRNA splicing, transcription
RT   and transcription-coupled DNA repair results in preimplantation
RT   lethality.";
RL   DNA Repair 4:479-491(2005).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Spleen;
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: Involved in pre-mRNA splicing as component of the
CC       spliceosome. Involved in transcription-coupled repair (TCR),
CC       transcription and pre-mRNA splicing. {ECO:0000250|UniProtKB:Q9HCS7}.
CC   -!- SUBUNIT: Associates with RNA polymerase II, the TCR-specific proteins
CC       CKN1/CSA and ERCC6/CSB, and XPA. Identified in the spliceosome C
CC       complex. Component of the XAB2 complex, a multimeric protein complex
CC       composed of XAB2, PRPF19, AQR, ZNF830, ISY1, and PPIE. Identified in a
CC       pentameric intron-binding (IB) complex composed of AQR, XAB2, ISY1,
CC       ZNF830 and PPIE that is incorporated into the spliceosome as a
CC       preassembled complex. The IB complex does not contain PRPF19.
CC       {ECO:0000250|UniProtKB:Q9HCS7}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q99PK0}.
CC       Note=Detected in the splicing complex carrying pre-mRNA.
CC       {ECO:0000250|UniProtKB:Q99PK0}.
CC   -!- DISRUPTION PHENOTYPE: Complete embryonic lethality before 13.5 dpc.
CC       Already at 3.5 dpc, the number of homozygous mutant embryos is lower
CC       than expected. {ECO:0000269|PubMed:15725628}.
CC   -!- SIMILARITY: Belongs to the crooked-neck family. {ECO:0000305}.
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DR   EMBL; AK002890; BAB22435.1; -; mRNA.
DR   EMBL; AK008628; BAB25790.1; -; mRNA.
DR   EMBL; BC021341; AAH21341.1; -; mRNA.
DR   CCDS; CCDS22065.1; -.
DR   RefSeq; NP_080432.1; NM_026156.2.
DR   AlphaFoldDB; Q9DCD2; -.
DR   SMR; Q9DCD2; -.
DR   BioGRID; 212186; 3.
DR   IntAct; Q9DCD2; 1.
DR   STRING; 10090.ENSMUSP00000019614; -.
DR   iPTMnet; Q9DCD2; -.
DR   PhosphoSitePlus; Q9DCD2; -.
DR   EPD; Q9DCD2; -.
DR   MaxQB; Q9DCD2; -.
DR   PaxDb; Q9DCD2; -.
DR   PRIDE; Q9DCD2; -.
DR   ProteomicsDB; 258788; -.
DR   Antibodypedia; 12104; 304 antibodies from 35 providers.
DR   DNASU; 67439; -.
DR   Ensembl; ENSMUST00000019614; ENSMUSP00000019614; ENSMUSG00000019470.
DR   GeneID; 67439; -.
DR   KEGG; mmu:67439; -.
DR   UCSC; uc009kry.1; mouse.
DR   CTD; 56949; -.
DR   MGI; MGI:1914689; Xab2.
DR   VEuPathDB; HostDB:ENSMUSG00000019470; -.
DR   eggNOG; KOG2047; Eukaryota.
DR   GeneTree; ENSGT00550000075140; -.
DR   HOGENOM; CLU_007736_2_1_1; -.
DR   InParanoid; Q9DCD2; -.
DR   OMA; FLMQQPL; -.
DR   OrthoDB; 370051at2759; -.
DR   PhylomeDB; Q9DCD2; -.
DR   TreeFam; TF300866; -.
DR   Reactome; R-MMU-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-MMU-6782135; Dual incision in TC-NER.
DR   Reactome; R-MMU-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR   BioGRID-ORCS; 67439; 25 hits in 104 CRISPR screens.
DR   ChiTaRS; Xab2; mouse.
DR   PRO; PR:Q9DCD2; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q9DCD2; protein.
DR   Bgee; ENSMUSG00000019470; Expressed in floor plate of midbrain and 263 other tissues.
DR   ExpressionAtlas; Q9DCD2; baseline and differential.
DR   Genevisible; Q9DCD2; MM.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0071014; C:post-mRNA release spliceosomal complex; IBA:GO_Central.
DR   GO; GO:0000974; C:Prp19 complex; IBA:GO_Central.
DR   GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; ISS:UniProtKB.
DR   GO; GO:0001824; P:blastocyst development; IMP:MGI.
DR   GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR   GO; GO:0000349; P:generation of catalytic spliceosome for first transesterification step; IBA:GO_Central.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0006351; P:transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; ISS:UniProtKB.
DR   Gene3D; 1.25.40.10; -; 5.
DR   InterPro; IPR003107; HAT.
DR   InterPro; IPR045075; Syf1-like.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR11246; PTHR11246; 1.
DR   Pfam; PF13181; TPR_8; 2.
DR   SMART; SM00386; HAT; 10.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF48452; SSF48452; 4.
PE   1: Evidence at protein level;
KW   Acetylation; DNA damage; DNA repair; mRNA processing; mRNA splicing;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat; Spliceosome;
KW   Transcription.
FT   CHAIN           1..855
FT                   /note="Pre-mRNA-splicing factor SYF1"
FT                   /id="PRO_0000106415"
FT   REPEAT          15..47
FT                   /note="HAT 1"
FT                   /evidence="ECO:0000305"
FT   REPEAT          48..80
FT                   /note="HAT 2"
FT                   /evidence="ECO:0000305"
FT   REPEAT          90..122
FT                   /note="HAT 3"
FT                   /evidence="ECO:0000305"
FT   REPEAT          124..158
FT                   /note="HAT 4"
FT                   /evidence="ECO:0000305"
FT   REPEAT          160..192
FT                   /note="HAT 5"
FT                   /evidence="ECO:0000305"
FT   REPEAT          198..230
FT                   /note="HAT 6"
FT   REPEAT          235..268
FT                   /note="HAT 7"
FT   REPEAT          270..305
FT                   /note="HAT 8"
FT   REPEAT          369..407
FT                   /note="HAT 9"
FT   REPEAT          498..530
FT                   /note="HAT 10"
FT   REPEAT          532..566
FT                   /note="HAT 11"
FT   REPEAT          571..605
FT                   /note="HAT 12"
FT   REPEAT          643..677
FT                   /note="HAT 13"
FT   REPEAT          679..713
FT                   /note="HAT 14"
FT   REGION          808..855
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        819..834
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         420
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HCS7"
FT   MOD_RES         851
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HCS7"
FT   CONFLICT        684
FT                   /note="A -> T (in Ref. 2; AAH21341)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        842
FT                   /note="Q -> L (in Ref. 1; BAB25790)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   855 AA;  99988 MW;  6A5DA6A74E7FCB1D CRC64;
     MVVMARVPRS ERPDLVFEEE DLPYEEEIMR NQFSVKCWLR YIEFKQGAPK PRLNQLYERA
     LKLLPCSYKL WYRYLKARRA QVKHRCVTDP AYEDVNNCHE RAFVFMHKMP RLWLDYCQFL
     MDQGRVTHTR RTFDRALRAL PITQHSRIWP LYLRFLRSHP LPETAVRGYR RFLKLSPESA
     EEYIEYLKSS DRLDEAAQRL ATVVNDERFV SKAGKSNYQL WHELCDLISQ NPDKVQSLNV
     DAIIRGGLTR FTDQLGKLWC SLADYYIRSG HFEKARDVYE EAIRTVMTVR DFTQVFDSYA
     QFEESMIAAK METASELGRE EEDDVDLELR LARFEQLISR RPLLLNSVLL RQNPHHVHEW
     HKRVALHQGR PREIINTYTE AVQTVDPFKA TGKPHTLWVA FAKFYEDNGQ LDDARVILEK
     ATKVNFKQVD DLASVWCQCG ELELRHENYD EALKLLRKAT ALPARRAEYF DGSEPVQNRV
     YKSLKVWSML ADLEESLGTF QSTKAVYDRI LDLRIATPQI VINYAMFLEE HKYFEESFKA
     YERGISLFKW PNVSDIWSTY LTKFISRYGG RKLERARDLF EQALDGCPPK YAKTLYLLYA
     QLEEEWGLAR HAMAVYDRAT RAVEPAQQYD MFNIYIKRAA EIYGVTHTRG IYQKAIEVLS
     DEHAREMCLR FADMECKLGE IDRARAIYSF CSQICDPRTT GAFWQTWKDF EVRHGNEDTI
     REMLRIRRSV QATYNTQVNF MASQMLKVSG SATGTVSDLA PGQSGMDDMK LLEQRAEQLA
     AEAERDQPPR AQSKIFFVRS DASREELAEL AQQANPEEIQ LGEDEDEDEM DLEPNEVRLE
     QQSVPAAVFG SLKED
 
 
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