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RNF10_MOUSE
ID   RNF10_MOUSE             Reviewed;         804 AA.
AC   Q3UIW5; Q6PDS8; Q6ZQE8; Q91YZ9; Q9R0P0;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=RING finger protein 10;
DE   AltName: Full=Sid 2705;
GN   Name=Rnf10; Synonyms=Kiaa0262, Rie2, Sid2705;
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 1).
RX   PubMed=10697961; DOI=10.1007/s100380050007;
RA   Seki N., Hattori A., Sugano S., Muramatsu M., Saito T.;
RT   "cDNA cloning, expression profile, and genomic structure of human and mouse
RT   RNF10/Rnf 10 genes, encoding a novel RING finger protein.";
RL   J. Hum. Genet. 45:38-42(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Heart, and Spleen;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, 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).
CC   -!- FUNCTION: Transcriptional factor involved in the regulation of MAG
CC       (Myelin-associated glycoprotein) expression and myelin formation in
CC       Schwann cells. {ECO:0000250|UniProtKB:Q5XI59}.
CC   -!- SUBUNIT: Interacts with MEOX2. {ECO:0000250|UniProtKB:Q8N5U6}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8N5U6}. Nucleus
CC       {ECO:0000250|UniProtKB:Q5XI59}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3UIW5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UIW5-2; Sequence=VSP_021479, VSP_021480, VSP_021481;
CC   -!- SIMILARITY: Belongs to the RNF10 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC97916.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB026621; BAA84700.1; -; mRNA.
DR   EMBL; AK129106; BAC97916.1; ALT_INIT; mRNA.
DR   EMBL; AK146728; BAE27391.1; -; mRNA.
DR   EMBL; AK165617; BAE38297.1; -; mRNA.
DR   EMBL; AK168523; BAE40402.1; -; mRNA.
DR   EMBL; AK172065; BAE42807.1; -; mRNA.
DR   EMBL; BC010342; AAH10342.1; -; mRNA.
DR   EMBL; BC058527; AAH58527.1; -; mRNA.
DR   CCDS; CCDS19584.1; -. [Q3UIW5-1]
DR   RefSeq; NP_001289377.1; NM_001302448.1.
DR   RefSeq; NP_001289378.1; NM_001302449.1.
DR   RefSeq; NP_057907.2; NM_016698.2. [Q3UIW5-1]
DR   AlphaFoldDB; Q3UIW5; -.
DR   BioGRID; 206133; 2.
DR   IntAct; Q3UIW5; 1.
DR   STRING; 10090.ENSMUSP00000107725; -.
DR   iPTMnet; Q3UIW5; -.
DR   PhosphoSitePlus; Q3UIW5; -.
DR   EPD; Q3UIW5; -.
DR   MaxQB; Q3UIW5; -.
DR   PaxDb; Q3UIW5; -.
DR   PeptideAtlas; Q3UIW5; -.
DR   PRIDE; Q3UIW5; -.
DR   ProteomicsDB; 299853; -. [Q3UIW5-1]
DR   ProteomicsDB; 299854; -. [Q3UIW5-2]
DR   Antibodypedia; 18977; 196 antibodies from 25 providers.
DR   DNASU; 50849; -.
DR   Ensembl; ENSMUST00000112096; ENSMUSP00000107725; ENSMUSG00000041740. [Q3UIW5-1]
DR   GeneID; 50849; -.
DR   KEGG; mmu:50849; -.
DR   UCSC; uc008zdl.2; mouse. [Q3UIW5-1]
DR   CTD; 9921; -.
DR   MGI; MGI:1859162; Rnf10.
DR   VEuPathDB; HostDB:ENSMUSG00000041740; -.
DR   eggNOG; KOG2164; Eukaryota.
DR   GeneTree; ENSGT00390000001731; -.
DR   InParanoid; Q3UIW5; -.
DR   OMA; PCLLHYL; -.
DR   OrthoDB; 1373540at2759; -.
DR   TreeFam; TF323455; -.
DR   BioGRID-ORCS; 50849; 7 hits in 73 CRISPR screens.
DR   ChiTaRS; Rnf10; mouse.
DR   PRO; PR:Q3UIW5; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q3UIW5; protein.
DR   Bgee; ENSMUSG00000041740; Expressed in blood and 262 other tissues.
DR   ExpressionAtlas; Q3UIW5; baseline and differential.
DR   Genevisible; Q3UIW5; MM.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0099147; C:extrinsic component of postsynaptic density membrane; ISO:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR   GO; GO:0010626; P:negative regulation of Schwann cell proliferation; ISS:UniProtKB.
DR   GO; GO:0031643; P:positive regulation of myelination; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR   GO; GO:0099527; P:postsynapse to nucleus signaling pathway; ISO:MGI.
DR   GO; GO:0051865; P:protein autoubiquitination; ISO:MGI.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR039739; Mag2/Rnf10.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR12983; PTHR12983; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..804
FT                   /note="RING finger protein 10"
FT                   /id="PRO_0000259586"
FT   ZN_FING         225..267
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          1..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          589..611
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          646..665
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          715..804
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..72
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        746..762
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         5
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N5U6"
FT   MOD_RES         110
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N5U6"
FT   MOD_RES         128
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N5U6"
FT   VAR_SEQ         1..99
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_021479"
FT   VAR_SEQ         100..107
FT                   /note="GGGSSKPF -> MDKNSGSN (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_021480"
FT   VAR_SEQ         780
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_021481"
FT   CONFLICT        596..598
FT                   /note="QRQ -> PTK (in Ref. 1; BAA84700)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        660..661
FT                   /note="LS -> YP (in Ref. 1; BAA84700)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   804 AA;  88345 MW;  A4E2231892D4F085 CRC64;
     MPQSSPSAAA TASDMDKNSG SNSSSASSGS SKGQQPPRSA SAGPAGESKP KSDGKNSNGS
     KRYNRKREPS YPKNENFSNQ SRRSNSQKSK TFNKMPPQRG GGSSKPFSSS SNGGRRDEVA
     EAQRAEFSPA QFSGPKKINL NHLLNFTFEP RGQAGHFEGS GHGGWGKRNK WGHKPFNKEL
     FLQANCQFVV SEDQDYAAHF ADPDTLVNWD FVEQVRICSH EVPSCPICLY PPTAAKITRC
     GHIFCWACIL HYLSLSEKTW SKCPICYSSV HKKDLKSVVA TESRQYAVGD TITMQLMKRE
     KGVLVALPKS KWVNVDHPIN LGDEQLSQYS KLLLASKEQV LHRVVLEEKG ALEQQLAEEK
     HTPESCFIEA AIQEVKIREE ALSGVAGGGG EVTGVVAALE HLVLMAPLAT ESAFQPRKGV
     LEYLSAFDDE AAQVCSLDPP GPLALPLVEE EEAVSEPEAC EDAEVADDSL GEGTVGPEMS
     QEEPITKPGF TQLSSSPCYY FYQAEDGQHM FLHPVNVRCL VREYGSLEQS PEKISATVVE
     IAGYSMSEDV RQRHRYLSHL PLTCEFSICE LALQPPVVSK ETLEMFSDDI EKRKRQRQKK
     AREERRRERR IEMEENKRQG RYPEVHIPLE NLQQFPAFNS YTCPSDSALG PTSTEGHGAL
     SLSPLSRSPG SHADFLLTPL SPTASQGSPS FCVGSLEDDS PFLSFAQMLR VGKAKADGWP
     KTAPKKDDNS LVPPAPVDSD GESDNSDRVP VPSFQNSFSQ AIEAAFMKLD TPATSDPLSE
     DRGGKKRKRQ KQKLLFSTSV VHTK
 
 
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