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SNPC4_MOUSE
ID   SNPC4_MOUSE             Reviewed;        1333 AA.
AC   Q8BP86; Q6PGG7; Q80UG9; Q810L1;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 2.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=snRNA-activating protein complex subunit 4;
DE            Short=SNAPc subunit 4;
DE   AltName: Full=snRNA-activating protein complex 190 kDa subunit;
DE            Short=SNAPc 190 kDa subunit;
GN   Name=Snapc4 {ECO:0000312|MGI:MGI:2443935};
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] {ECO:0000305, ECO:0000312|EMBL:BAC36843.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC36843.1};
RC   TISSUE=Embryo {ECO:0000312|EMBL:BAC36843.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAH57031.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 498-1325 (ISOFORM 1).
RC   STRAIN=129 {ECO:0000312|EMBL:AAH44754.1},
RC   C57BL/6J {ECO:0000312|EMBL:AAH57031.1}, and FVB/N;
RC   TISSUE=Brain {ECO:0000312|EMBL:AAH57031.1}, and
RC   Mammary gland {ECO:0000312|EMBL:AAH44754.1};
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1301 AND SER-1309, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, and 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: Part of the SNAPc complex required for the transcription of
CC       both RNA polymerase II and III small-nuclear RNA genes. Binds to the
CC       proximal sequence element (PSE), a non-TATA-box basal promoter element
CC       common to these 2 types of genes. Recruits TBP and BRF2 to the U6 snRNA
CC       TATA box (By similarity). {ECO:0000250|UniProtKB:Q5SXM2}.
CC   -!- SUBUNIT: Part of the SNAPc composed of 5 subunits: SNAPC1, SNAPC2,
CC       SNAPC3, SNAPC4 and SNAPC5. SNAPC4 interacts with SNAPC1, SNAPC2,
CC       SNAPC5, BRF2 and TBP (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1 {ECO:0000305};
CC         IsoId=Q8BP86-1; Sequence=Displayed;
CC       Name=2 {ECO:0000305};
CC         IsoId=Q8BP86-2; Sequence=VSP_051857;
CC       Name=3 {ECO:0000305};
CC         IsoId=Q8BP86-3; Sequence=VSP_051855, VSP_051857;
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DR   EMBL; AK077522; BAC36843.1; -; mRNA.
DR   EMBL; BC044754; AAH44754.1; -; mRNA.
DR   EMBL; BC057031; AAH57031.1; -; mRNA.
DR   CCDS; CCDS15802.1; -. [Q8BP86-2]
DR   RefSeq; NP_001277348.1; NM_001290419.1. [Q8BP86-3]
DR   RefSeq; NP_758842.1; NM_172339.4. [Q8BP86-2]
DR   AlphaFoldDB; Q8BP86; -.
DR   SMR; Q8BP86; -.
DR   BioGRID; 230655; 3.
DR   IntAct; Q8BP86; 2.
DR   STRING; 10090.ENSMUSP00000109750; -.
DR   iPTMnet; Q8BP86; -.
DR   PhosphoSitePlus; Q8BP86; -.
DR   MaxQB; Q8BP86; -.
DR   PaxDb; Q8BP86; -.
DR   PRIDE; Q8BP86; -.
DR   ProteomicsDB; 261391; -. [Q8BP86-1]
DR   ProteomicsDB; 261392; -. [Q8BP86-2]
DR   ProteomicsDB; 261393; -. [Q8BP86-3]
DR   Antibodypedia; 18701; 195 antibodies from 20 providers.
DR   DNASU; 227644; -.
DR   Ensembl; ENSMUST00000035427; ENSMUSP00000041767; ENSMUSG00000036281. [Q8BP86-2]
DR   GeneID; 227644; -.
DR   KEGG; mmu:227644; -.
DR   UCSC; uc008iuu.2; mouse. [Q8BP86-1]
DR   UCSC; uc008iuv.2; mouse. [Q8BP86-2]
DR   UCSC; uc008iuw.2; mouse. [Q8BP86-3]
DR   CTD; 6621; -.
DR   MGI; MGI:2443935; Snapc4.
DR   VEuPathDB; HostDB:ENSMUSG00000036281; -.
DR   eggNOG; KOG0049; Eukaryota.
DR   GeneTree; ENSGT00940000160404; -.
DR   HOGENOM; CLU_004641_0_0_1; -.
DR   InParanoid; Q8BP86; -.
DR   OMA; LWHGTFQ; -.
DR   OrthoDB; 219341at2759; -.
DR   PhylomeDB; Q8BP86; -.
DR   Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
DR   Reactome; R-MMU-76071; RNA Polymerase III Transcription Initiation From Type 3 Promoter.
DR   BioGRID-ORCS; 227644; 28 hits in 77 CRISPR screens.
DR   ChiTaRS; Snapc4; mouse.
DR   PRO; PR:Q8BP86; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q8BP86; protein.
DR   Bgee; ENSMUSG00000036281; Expressed in superior frontal gyrus and 200 other tissues.
DR   ExpressionAtlas; Q8BP86; baseline and differential.
DR   Genevisible; Q8BP86; MM.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0019185; C:snRNA-activating protein complex; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; ISO:MGI.
DR   GO; GO:0000995; F:RNA polymerase III general transcription initiation factor activity; ISO:MGI.
DR   GO; GO:0001006; F:RNA polymerase III type 3 promoter sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0042795; P:snRNA transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0042796; P:snRNA transcription by RNA polymerase III; ISS:UniProtKB.
DR   CDD; cd00167; SANT; 3.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017930; Myb_dom.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR017884; SANT_dom.
DR   SMART; SM00717; SANT; 5.
DR   SUPFAM; SSF46689; SSF46689; 3.
DR   PROSITE; PS51294; HTH_MYB; 3.
DR   PROSITE; PS50090; MYB_LIKE; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; DNA-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Transcription; Transcription regulation.
FT   CHAIN           1..1333
FT                   /note="snRNA-activating protein complex subunit 4"
FT                   /id="PRO_0000197121"
FT   DOMAIN          250..288
FT                   /note="Myb-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT   DOMAIN          289..343
FT                   /note="HTH myb-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DOMAIN          344..395
FT                   /note="Myb-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT   DOMAIN          396..451
FT                   /note="HTH myb-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DOMAIN          452..503
FT                   /note="HTH myb-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DNA_BIND        317..341
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DNA_BIND        424..447
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DNA_BIND        476..499
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   REGION          29..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          84..133
FT                   /note="SNAPC5-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SXM2"
FT   REGION          503..558
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          662..702
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          811..842
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1079..1117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1131..1247
FT                   /note="SNAPC2-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SXM2"
FT   REGION          1282..1333
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        515..549
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        672..686
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        811..828
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         68
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SXM2"
FT   MOD_RES         1252
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SXM2"
FT   MOD_RES         1254
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SXM2"
FT   MOD_RES         1301
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1309
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         1..90
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_051855"
FT   VAR_SEQ         1290..1297
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_051857"
FT   CONFLICT        498..505
FT                   /note="LARKKQHL -> DAWADAWV (in Ref. 2; AAH44754)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1333 AA;  147413 MW;  586798D3A7D59B4E CRC64;
     MDIDAEREKI TQEIQELERI LYPGSTSVHF EVSESSLSSD SEADSLPDED LETAGAPILE
     EEGSSESSND EEDPKDKALP EDPETCLQLN MVYQEVIREK LAEVSQLLAQ NQEQQEEILF
     DLSGTKCPKV KDGRSLPSYM YIGHFLKPYF KDKVTGVGPP ANEETREKAT QGIKAFEQLL
     VTKWKHWEKA LLRKSVVSDR LQRLLQPKLL KLEYLHEKQS RVSSELERQA LEKQIKEAEK
     EIQDINQLPE EALLGNRLDS HDWEKISNIN FEGARSAEEI RKFWQSSEHP SISKQEWSTE
     EVERLKAIAA THGHLEWHLV AEELGTSRSA FQCLQKFQQY NKTLKRKEWT EEEDHMLTQL
     VQEMRVGNHI PYRKIVYFME GRDSMQLIYR WTKSLDPSLK RGFWAPEEDA KLLQAVAKYG
     AQDWFKIREE VPGRSDAQCR DRYIRRLHFS LKKGRWNAKE EQQLIQLIEK YGVGHWARIA
     SELPHRSGSQ CLSKWKILAR KKQHLQRKRG QRPRHSSQWS SSGSSSSSSE DYGSSSGSDG
     SSGSENSDVE LEASLEKSRA LTPQQYRVPD IDLWVPTRLI TSQSQREGTG CYPQHPAVSC
     CTQDASQNHH KEGSTTVSAA EKNQLQVPYE THSTVPRGDR FLHFSDTHSA SLKDPACKSH
     TLMKERPKQP LLPSSRSGSD PGNNTAGPHL RQLWHGTYQN KQRRKRQALH RRLLKHRLLL
     AVIPWVGDIN LACTQAPRRP ATVQTKADSI RMQLECARLA STPVFTLLIQ LLQIDTAGCM
     EVVRERKSQP PALLQPGTRN TQPHLLQASS NAKNNTGCLP SMTGEQTAKR ASHKGRPRLG
     SCRTEATPFQ VPVAAPRGLR PKPKTVSELL REKRLRESHA KKATQALGLN SQLLVSSPVI
     LQPPLLPVPH GSPVVGPATS SVELSVPVAP VMVSSSPSGS WPVGGISATD KQPPNLQTIS
     LNPPHKGTQV AAPAAFRSLA LAPGQVPTGG HLSTLGQTST TSQKQSLPKV LPILRAAPSL
     TQLSVQPPVS GQPLATKSSL PVNWVLTTQK LLSVQVPAVV GLPQSVMTPE TIGLQAKQLP
     SPAKTPAFLE QPPASTDTEP KGPQGQEIPP TPGPEKAALD LSLLSQESEA AIVTWLKGCQ
     GAFVPPLGSR MPYHPPSLCS LRALSSLLLQ KQDLEQKASS LAASQAAGAQ PDPKAGALQA
     SLELVQRQFR DNPAYLLLKT RFLAIFSLPA FLATLPPNSI PTTLSPDVAV VSESDSEDLG
     DLELKDRARQ LDCMACRVQA SPAAPDPVQS HLVSPGQRAP SPGEVSAPSP LDASDGLDDL
     NVLRTRRARH SRR
 
 
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