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RN150_MOUSE
ID   RN150_MOUSE             Reviewed;         437 AA.
AC   Q5DTZ6;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 2.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=RING finger protein 150;
DE   Flags: Precursor;
GN   Name=Rnf150; Synonyms=Kiaa1214;
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] (ISOFORM 3).
RC   TISSUE=Brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT   complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT   screening of terminal sequences of cDNA clones randomly sampled from size-
RT   fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=NOD;
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 GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q5DTZ6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5DTZ6-2; Sequence=VSP_023848;
CC       Name=3;
CC         IsoId=Q5DTZ6-3; Sequence=VSP_023849, VSP_023850;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD90433.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK220374; BAD90433.1; ALT_INIT; mRNA.
DR   EMBL; AK041412; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AC124757; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC132372; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC166939; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS40402.1; -. [Q5DTZ6-1]
DR   RefSeq; NP_796352.2; NM_177378.4. [Q5DTZ6-1]
DR   AlphaFoldDB; Q5DTZ6; -.
DR   SMR; Q5DTZ6; -.
DR   STRING; 10090.ENSMUSP00000077610; -.
DR   GlyGen; Q5DTZ6; 4 sites.
DR   PhosphoSitePlus; Q5DTZ6; -.
DR   MaxQB; Q5DTZ6; -.
DR   PaxDb; Q5DTZ6; -.
DR   PRIDE; Q5DTZ6; -.
DR   ProteomicsDB; 299918; -. [Q5DTZ6-1]
DR   ProteomicsDB; 299919; -. [Q5DTZ6-2]
DR   ProteomicsDB; 299920; -. [Q5DTZ6-3]
DR   Antibodypedia; 27282; 153 antibodies from 22 providers.
DR   DNASU; 330812; -.
DR   Ensembl; ENSMUST00000078525; ENSMUSP00000077610; ENSMUSG00000047747. [Q5DTZ6-1]
DR   GeneID; 330812; -.
DR   KEGG; mmu:330812; -.
DR   UCSC; uc009mjt.2; mouse. [Q5DTZ6-1]
DR   UCSC; uc029wub.2; mouse. [Q5DTZ6-3]
DR   CTD; 57484; -.
DR   MGI; MGI:2443860; Rnf150.
DR   VEuPathDB; HostDB:ENSMUSG00000047747; -.
DR   eggNOG; KOG0800; Eukaryota.
DR   GeneTree; ENSGT00940000156171; -.
DR   HOGENOM; CLU_049885_2_1_1; -.
DR   InParanoid; Q5DTZ6; -.
DR   OMA; VNITYMD; -.
DR   OrthoDB; 1487241at2759; -.
DR   PhylomeDB; Q5DTZ6; -.
DR   TreeFam; TF317486; -.
DR   BioGRID-ORCS; 330812; 2 hits in 74 CRISPR screens.
DR   ChiTaRS; Rnf150; mouse.
DR   PRO; PR:Q5DTZ6; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q5DTZ6; protein.
DR   Bgee; ENSMUSG00000047747; Expressed in pigmented layer of retina and 196 other tissues.
DR   Genevisible; Q5DTZ6; MM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR003137; PA_domain.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Glycoprotein; Membrane; Metal-binding;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix; Zinc;
KW   Zinc-finger.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000255"
FT   CHAIN           35..437
FT                   /note="RING finger protein 150"
FT                   /id="PRO_0000280698"
FT   TOPO_DOM        35..207
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        208..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        229..437
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          80..182
FT                   /note="PA"
FT   ZN_FING         277..318
FT                   /note="RING-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   CARBOHYD        45
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        124
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        152
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        185
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..90
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_023848"
FT   VAR_SEQ         245..286
FT                   /note="RRLGDAAKKAISKLQVRTIRKGDKETESDFDNCAVCIEGYKP -> VSSSLR
FT                   KAWLCKLSANHTCQGINVVAHKSRDSKCLLTPPHTC (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_023849"
FT   VAR_SEQ         287..437
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_023850"
FT   CONFLICT        108
FT                   /note="A -> V (in Ref. 1; BAD90433)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        342
FT                   /note="E -> K (in Ref. 2; AK041412)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   437 AA;  48013 MW;  148A94349EDD2CD9 CRC64;
     MTMSLIQACR SLALSTWLLS FCFVHLLCLD FTVAEKEEWY TAFVNITYLE PEPGAAVAGS
     GGGAELHTEK SECGRYGEHS PKQDARGEVV MASSAQDRLA CDPNTKFAAP AHGKHWIALI
     PKGNCTYRDK IRNAFLQNAS AVVIFNVGSN TNETITMPHA GVEDIVAIMI PEPKGKEIVS
     LLERNITVTM YITIGTRNLQ KYVSRTSVVF VSISFIVLMI ISLAWLVFYY IQRFRYANAR
     DRNQRRLGDA AKKAISKLQV RTIRKGDKET ESDFDNCAVC IEGYKPNDVV RILPCRHLFH
     KSCVDPWLLD HRTCPMCKMN ILKALGIPPN ADCMDDLPID FEGSLGGPPT NQITGASDTT
     VNESSVTLDP AVRTVGALQV VQDPDPAPQE GEAIFTTNSG QEPALSSDSD ISLIMALEVG
     LSDVELSTDQ DCEEVKS
 
 
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