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RRP5_MOUSE
ID   RRP5_MOUSE              Reviewed;        1862 AA.
AC   Q6NS46; Q3TSU4; Q3UGG2; Q3URK0; Q6PIA8; Q6ZQH2; Q7TPE2; Q9CTD8; Q9R1Z2;
AC   Q9WTU7;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 2.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Protein RRP5 homolog;
DE   AltName: Full=Apoptosis-linked gene 4 protein;
DE   AltName: Full=Programmed cell death protein 11;
GN   Name=Pdcd11; Synonyms=Alg4, Kiaa0185;
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   TISSUE=Embryonic tail;
RX   PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Embryonic brain, Eye, and Mammary tumor;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1438, AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 1568-1862.
RC   STRAIN=C57BL/6J;
RC   TISSUE=Embryo, Embryonic spinal cord, Embryonic testis, and Melanocyte;
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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 394-1163, AND TISSUE SPECIFICITY.
RX   PubMed=10229231; DOI=10.1038/8420;
RA   Lacana' E., D'Adamio L.;
RT   "Regulation of Fas ligand expression and cell death by apoptosis-linked
RT   gene 4.";
RL   Nat. Med. 5:542-547(1999).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1468 AND SER-1490, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Lung, Pancreas, 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: Essential for the generation of mature 18S rRNA, specifically
CC       necessary for cleavages at sites A0, 1 and 2 of the 47S precursor.
CC       Directly interacts with U3 snoRNA (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with NF-kappa-B p50/NFKB1 and NF-kappa-B p65/RELA.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10229231}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD20941.1; Type=Miscellaneous discrepancy; Note=The mRNA 5'- and 3'-ends do not match to the genomic DNA.; Evidence={ECO:0000305};
CC       Sequence=BAB23064.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAC97890.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK129080; BAC97890.1; ALT_INIT; mRNA.
DR   EMBL; BC038503; AAH38503.1; -; mRNA.
DR   EMBL; BC055276; AAH55276.3; -; mRNA.
DR   EMBL; BC070468; AAH70468.1; -; mRNA.
DR   EMBL; AK003899; BAB23064.2; ALT_INIT; mRNA.
DR   EMBL; AK141450; BAE24688.1; -; mRNA.
DR   EMBL; AK147950; BAE28246.1; -; mRNA.
DR   EMBL; AK161803; BAE36581.1; -; mRNA.
DR   EMBL; AF055668; AAD20941.1; ALT_SEQ; mRNA.
DR   EMBL; AF055669; AAD20942.1; -; mRNA.
DR   CCDS; CCDS29888.1; -.
DR   RefSeq; NP_035183.2; NM_011053.2.
DR   AlphaFoldDB; Q6NS46; -.
DR   SMR; Q6NS46; -.
DR   BioGRID; 202073; 33.
DR   STRING; 10090.ENSMUSP00000072008; -.
DR   iPTMnet; Q6NS46; -.
DR   PhosphoSitePlus; Q6NS46; -.
DR   SwissPalm; Q6NS46; -.
DR   EPD; Q6NS46; -.
DR   jPOST; Q6NS46; -.
DR   MaxQB; Q6NS46; -.
DR   PaxDb; Q6NS46; -.
DR   PeptideAtlas; Q6NS46; -.
DR   PRIDE; Q6NS46; -.
DR   ProteomicsDB; 299898; -.
DR   Antibodypedia; 31534; 46 antibodies from 16 providers.
DR   DNASU; 18572; -.
DR   Ensembl; ENSMUST00000072141; ENSMUSP00000072008; ENSMUSG00000025047.
DR   GeneID; 18572; -.
DR   KEGG; mmu:18572; -.
DR   UCSC; uc008hup.1; mouse.
DR   CTD; 22984; -.
DR   MGI; MGI:1341788; Pdcd11.
DR   VEuPathDB; HostDB:ENSMUSG00000025047; -.
DR   eggNOG; KOG1070; Eukaryota.
DR   GeneTree; ENSGT00390000012228; -.
DR   HOGENOM; CLU_000845_1_1_1; -.
DR   InParanoid; Q6NS46; -.
DR   OMA; GQYLRAY; -.
DR   OrthoDB; 23482at2759; -.
DR   PhylomeDB; Q6NS46; -.
DR   TreeFam; TF105697; -.
DR   Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   BioGRID-ORCS; 18572; 24 hits in 79 CRISPR screens.
DR   ChiTaRS; Pdcd11; mouse.
DR   PRO; PR:Q6NS46; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; Q6NS46; protein.
DR   Bgee; ENSMUSG00000025047; Expressed in cleaving embryo and 232 other tissues.
DR   Genevisible; Q6NS46; MM.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR   GO; GO:0051059; F:NF-kappaB binding; ISO:MGI.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.10; -; 1.
DR   Gene3D; 2.40.50.140; -; 9.
DR   InterPro; IPR003107; HAT.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR045209; Rrp5.
DR   InterPro; IPR022967; S1_dom.
DR   InterPro; IPR003029; S1_domain.
DR   InterPro; IPR008847; Suf.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR23270; PTHR23270; 4.
DR   Pfam; PF00575; S1; 4.
DR   Pfam; PF05843; Suf; 1.
DR   SMART; SM00386; HAT; 7.
DR   SMART; SM00316; S1; 13.
DR   SUPFAM; SSF48452; SSF48452; 2.
DR   SUPFAM; SSF50249; SSF50249; 11.
DR   PROSITE; PS50126; S1; 12.
PE   1: Evidence at protein level;
KW   Acetylation; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; rRNA processing; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q14690"
FT   CHAIN           2..1862
FT                   /note="Protein RRP5 homolog"
FT                   /id="PRO_0000364200"
FT   DOMAIN          83..171
FT                   /note="S1 motif 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   DOMAIN          187..258
FT                   /note="S1 motif 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   DOMAIN          281..346
FT                   /note="S1 motif 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   DOMAIN          365..436
FT                   /note="S1 motif 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   DOMAIN          453..522
FT                   /note="S1 motif 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   DOMAIN          542..611
FT                   /note="S1 motif 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   DOMAIN          636..707
FT                   /note="S1 motif 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   DOMAIN          729..798
FT                   /note="S1 motif 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   DOMAIN          846..911
FT                   /note="S1 motif 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   DOMAIN          1047..1120
FT                   /note="S1 motif 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   DOMAIN          1160..1233
FT                   /note="S1 motif 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   DOMAIN          1241..1309
FT                   /note="S1 motif 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   DOMAIN          1335..1407
FT                   /note="S1 motif 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   REPEAT          1590..1622
FT                   /note="HAT 1"
FT   REPEAT          1696..1728
FT                   /note="HAT 2"
FT   REPEAT          1766..1798
FT                   /note="HAT 3"
FT   REPEAT          1800..1835
FT                   /note="HAT 4"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          999..1036
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1406..1520
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1545..1577
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1016..1031
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1420..1509
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1546..1577
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14690"
FT   MOD_RES         7
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14690"
FT   MOD_RES         438
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14690"
FT   MOD_RES         1468
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1490
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CROSSLNK        1424
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q14690"
FT   CONFLICT        38
FT                   /note="E -> A (in Ref. 3; BAE28246)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        187
FT                   /note="G -> D (in Ref. 3; BAE28246)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        531
FT                   /note="S -> P (in Ref. 1; BAC97890)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        919
FT                   /note="T -> P (in Ref. 1; BAC97890)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1027..1028
FT                   /note="Missing (in Ref. 1; BAC97890)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1337
FT                   /note="L -> H (in Ref. 3; BAE28246)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1469..1471
FT                   /note="ESE -> TRP (in Ref. 2; AAH38503)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1519
FT                   /note="E -> Q (in Ref. 2; AAH38503)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1556
FT                   /note="P -> L (in Ref. 1; BAC97890 and 2; AAH38503)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1851
FT                   /note="E -> D (in Ref. 2; AAH70468)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1862 AA;  207779 MW;  F2045A86EE8C9626 CRC64;
     MANLEESFPR GGTRKLHKSE KSSQQVVEQD NLFDVSTEEG PIKRKKSQKG PAKTKKLKIE
     KRKSIKSIKE KFEILSLESL CEGMRILGCV KEVSELELVV SLPNGLQGFV QVTEVCDAYT
     QKLNEQVAQE EPLEDLLRLP ELFSPGMLVR CVVSSLDVTE SGKKSVKLSV NPKRVNKVLS
     ADALRPGMLL TGTVSSLEDH GYLVDIGVGG TRAFLSLKKA QEYIRQKNKG AKFKVGQYLT
     CVVEEVKSNG GVVSLSVEHS EVSSAFATEE QSWNLNNLLP GLLVKAQVQK VTQFGLQLNF
     LTFFKGLVDF MHLEPKKMGS YSSNQTVKAC ILCVHPRTRV VRLSLRPIFL HPGRPLTRIS
     YQQLGAVLDD VPVQGFFKNA GAIFRLKDGV LAYARVSHLS DSKKAFNAEA FKPGSTHKCR
     IIDYSQMDEL ALLSLRKSII AAPFLRYHDI KIGTVVKGTV LAIKPFGILV KVGEQIKGLV
     PSMHLADIMM KNPEKKYSPG DEVKCRVLLC DPEAKKLIMT LKKTLVTSKL SLITCYEGAK
     PGLQTHGVII RVKDYGCIVK FYNDVQGLVP KHELSTQHIP DPETVFYTGQ VVKVAVLSCE
     PSKERMLLSF RLLSDSRPKD PGVESSQKKT GAVRIGQLVD VKVLEKTKTG LEVAILPHNT
     PAFLPTPHLS DHAANGPLLH HWLQTGDTLH RVLCLSQSER HILLCRKPAL VSTVEGGQDP
     KSLSEIQPGM LLIGFVKCIK EYGVFVQFPS GLSGLSPKTI MSDKFVTTPS EHFVEGQTVV
     AKVTNVDESK QRMLLSLRLS DCSLGDSAST SFLLLCQCLE ELQGIRSLMS NQDSVLIQTL
     ADMTPGMVLD AVVHEVLEDG SVVFSSDPVP DLVLRASRYH RAGQEVEPGQ KKKVVVLHVD
     MLKLEVHVSL HQDLVNRKTR KLRKSSRHQG IVQHLEESFA VASLVETGHL VAFSLISHLN
     DTFHFDSEKL RVGQGVCLTL KTTEPGVTGL ILAVEGPASK RTRMPVQRDS ETVDDKGEEK
     EEEEEEEEKE EENLTVKSKK RHSLAIGDKV TGTIKAVKAT HVVVTLADGF VGCIHASRIL
     DDVPVGTSPT TTLKAGKKVT ARVIGGRDVK TSKFLPISHP RFVLTILELS VRPSELKGSY
     SALNTHSESP VEKIRQYQAG QTVTCFFKKY NVMKKWLEVD IGPDIRGRIP LLLTSLSFKV
     LKHPDKKFQV GQAIEATVVD PDVPRAFLCL SLIGPYRLEE GEVAMGRVMK VVPNRGLTVS
     FPFGKIGKVS MFHLSDSYSE APLEDFCPQK IVRCYILSTA HRVLALSLRS SRTNRETKNR
     IEDPEINSIE DVKEGQLLRG YVKCVLPSSV IIGLGPSVLG LAKYSHVSEC VPPEKELYNG
     CLPEGKLVTA KVLRVNPMKN LIELSLLPSD TGRPDVFSPA PEPKQEERSG GAEEGQKRKE
     KNQKRREEKE EPQKSQRGGR GKRERQESES EQELVNKRPK KSGAAEEDDS GVEVYYREGE
     DEVGEPKLPP RGKQTKSTEV PRLHLSSGFL WDVGLDSLTP ALPLREESSD SEDEQPHQAK
     KKKGKKEREL EKQKAEKELS RIEEALMDPG RQPESADDFD RLVLSSPNSS ILWLQYMAFH
     LQATEIEKAR AVAERALKTI SFREEQEKLN VWVALLNLEN MYGSQESLTK VFERAVQYNE
     PLKVFLHLAD IYTKSEKYKE AGELYNRMLK RFRQEKAVWI KYGAFVLGRS QAGASHRVLQ
     RALECLPAKE HVDVIVKFAQ LEFQLGDVER AKAIFENTLS TYPKRTDVWS VYIDMTIKHG
     SQTAVRDIFE RVIHLSLAPK RMKFFFKRYL DYEKQHGTEK DVQAVKAKAL EYVEAKSSAL
     ED
 
 
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