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RN141_MOUSE
ID   RN141_MOUSE             Reviewed;         230 AA.
AC   Q99MB7; Q9D040; Q9D5C4; Q9D9L0;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 2.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=RING finger protein 141;
DE   AltName: Full=Zinc finger protein 230;
GN   Name=Rnf141; Synonyms=Znf230;
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], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP   STAGE, AND ALTERNATIVE SPLICING.
RC   STRAIN=Kunming; TISSUE=Testis;
RX   PubMed=12804569; DOI=10.1016/s0006-291x(03)00970-7;
RA   Qiu W., Zhang S., Xiao C., Xu W., Ma Y., Liu Y., Wu Q.;
RT   "Molecular cloning and characterization of a mouse spermatogenesis-related
RT   ring finger gene znf230.";
RL   Biochem. Biophys. Res. Commun. 306:347-353(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Testis;
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 MRNA].
RC   STRAIN=FVB/N; TISSUE=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   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Testis;
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: May be involved in spermatogenesis.
CC       {ECO:0000269|PubMed:12804569}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8WVD5}; Lipid-
CC       anchor {ECO:0000250|UniProtKB:Q8WVD5}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q99MB7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99MB7-2; Sequence=Not described;
CC       Name=3;
CC         IsoId=Q99MB7-3; Sequence=Not described;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is testis-specific. Isoform 2 is
CC       expressed in heart, brain, skeletal muscle, kidney, pancreas, lung,
CC       liver and testis. Isoform 3 is expressed in heart, liver, and kidney.
CC       {ECO:0000269|PubMed:12804569}.
CC   -!- DEVELOPMENTAL STAGE: Expression was first detected at postnatal day 6,
CC       and reached the adult level between postnatal day 14 and 21.
CC       {ECO:0000269|PubMed:12804569}.
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DR   EMBL; AF353167; AAK31205.1; -; mRNA.
DR   EMBL; AK006791; BAB24742.1; -; mRNA.
DR   EMBL; AK011839; BAB27871.1; -; mRNA.
DR   EMBL; AK015505; BAB29874.1; -; mRNA.
DR   EMBL; BC018553; AAH18553.1; -; mRNA.
DR   CCDS; CCDS40086.1; -. [Q99MB7-1]
DR   RefSeq; NP_080275.2; NM_025999.3. [Q99MB7-1]
DR   RefSeq; XP_006508186.1; XM_006508123.2. [Q99MB7-1]
DR   RefSeq; XP_006508187.1; XM_006508124.2. [Q99MB7-1]
DR   AlphaFoldDB; Q99MB7; -.
DR   BioGRID; 211978; 1.
DR   STRING; 10090.ENSMUSP00000134781; -.
DR   iPTMnet; Q99MB7; -.
DR   PhosphoSitePlus; Q99MB7; -.
DR   MaxQB; Q99MB7; -.
DR   PaxDb; Q99MB7; -.
DR   PRIDE; Q99MB7; -.
DR   ProteomicsDB; 300413; -. [Q99MB7-1]
DR   Antibodypedia; 11671; 193 antibodies from 31 providers.
DR   DNASU; 67150; -.
DR   Ensembl; ENSMUST00000106682; ENSMUSP00000102293; ENSMUSG00000030788. [Q99MB7-1]
DR   Ensembl; ENSMUST00000177236; ENSMUSP00000134781; ENSMUSG00000030788. [Q99MB7-1]
DR   GeneID; 67150; -.
DR   KEGG; mmu:67150; -.
DR   UCSC; uc009jfp.1; mouse. [Q99MB7-1]
DR   CTD; 50862; -.
DR   MGI; MGI:1914400; Rnf141.
DR   VEuPathDB; HostDB:ENSMUSG00000030788; -.
DR   eggNOG; KOG1039; Eukaryota.
DR   GeneTree; ENSGT00390000003145; -.
DR   HOGENOM; CLU_080007_0_0_1; -.
DR   InParanoid; Q99MB7; -.
DR   OMA; TAANDSW; -.
DR   OrthoDB; 49756at2759; -.
DR   PhylomeDB; Q99MB7; -.
DR   TreeFam; TF323284; -.
DR   BioGRID-ORCS; 67150; 0 hits in 71 CRISPR screens.
DR   ChiTaRS; Rnf141; mouse.
DR   PRO; PR:Q99MB7; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q99MB7; protein.
DR   Bgee; ENSMUSG00000030788; Expressed in animal zygote and 256 other tissues.
DR   ExpressionAtlas; Q99MB7; baseline and differential.
DR   Genevisible; Q99MB7; MM.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
DR   GO; GO:0051865; P:protein autoubiquitination; ISO:MGI.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR   CDD; cd16545; RING-HC_RNF141; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR043400; RING-HC_RNF141.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Lipoprotein; Membrane; Metal-binding; Myristate;
KW   Reference proteome; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WVD5"
FT   CHAIN           2..230
FT                   /note="RING finger protein 141"
FT                   /id="PRO_0000056102"
FT   ZN_FING         155..192
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WVD5"
FT   CONFLICT        10..11
FT                   /note="QL -> HV (in Ref. 2; BAB27871)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        139
FT                   /note="A -> S (in Ref. 1; AAK31205)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        148
FT                   /note="Q -> R (in Ref. 2; BAB24742)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   230 AA;  25529 MW;  D2196217AB2973E6 CRC64;
     MGQQISDQTQ LVINKLPEKV AKHVTLVRES GSLTYEEFLG RVAELNDVTA KVAAGQEKHL
     LFEVQPGSDS SAFWKVVVRV VCTKINKSSG IVEASRIMNL YQFIQLYKDI TSQAAGVLAQ
     SSTSEEPDEN PSSVTSCQAS LWMGRVKQLT DEEECCICMD GRADLILPCA HSFCQKCIDK
     WSDRHRNCPI CRLQMTGANE SWVVSDAPTE DDMANYILNM ADEAGQPHRP
 
 
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