RN151_MOUSE
ID RN151_MOUSE Reviewed; 239 AA.
AC Q9CQ29;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=RING finger protein 151;
GN Name=Rnf151;
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 STRAIN=C57BL/6J; TISSUE=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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP DTNBP1.
RX PubMed=17577571; DOI=10.1016/j.abb.2007.05.013;
RA Nian H., Fan C., Liao S., Shi Y., Zhang K., Liu Y., Han C.;
RT "RNF151, a testis-specific RING finger protein, interacts with dysbindin.";
RL Arch. Biochem. Biophys. 465:157-163(2007).
CC -!- FUNCTION: May be involved in acrosome formation of spermatids.
CC {ECO:0000269|PubMed:17577571}.
CC -!- SUBUNIT: Interacts with DTNBP1. {ECO:0000269|PubMed:17577571}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17577571}. Nucleus
CC {ECO:0000269|PubMed:17577571}.
CC -!- TISSUE SPECIFICITY: Expressed in testis. Expressed in round spermatids
CC of the stages VII-VIII semniniferous tubules. Expressed in elongating
CC spermatids of stages VIII-IX seminiferous tubules (at protein level).
CC {ECO:0000269|PubMed:17577571}.
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DR EMBL; AK005854; BAB24277.1; -; mRNA.
DR EMBL; BC049562; AAH49562.1; -; mRNA.
DR CCDS; CCDS37492.1; -.
DR RefSeq; NP_080481.1; NM_026205.3.
DR AlphaFoldDB; Q9CQ29; -.
DR SMR; Q9CQ29; -.
DR STRING; 10090.ENSMUSP00000008626; -.
DR PhosphoSitePlus; Q9CQ29; -.
DR PaxDb; Q9CQ29; -.
DR PRIDE; Q9CQ29; -.
DR ProteomicsDB; 300491; -.
DR Antibodypedia; 23363; 27 antibodies from 14 providers.
DR Ensembl; ENSMUST00000008626; ENSMUSP00000008626; ENSMUSG00000008482.
DR GeneID; 67504; -.
DR KEGG; mmu:67504; -.
DR UCSC; uc008axw.1; mouse.
DR CTD; 146310; -.
DR MGI; MGI:1914754; Rnf151.
DR VEuPathDB; HostDB:ENSMUSG00000008482; -.
DR eggNOG; KOG0297; Eukaryota.
DR GeneTree; ENSGT00530000063647; -.
DR HOGENOM; CLU_076732_3_0_1; -.
DR InParanoid; Q9CQ29; -.
DR OMA; HNCYKQL; -.
DR OrthoDB; 918518at2759; -.
DR PhylomeDB; Q9CQ29; -.
DR TreeFam; TF351947; -.
DR BioGRID-ORCS; 67504; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q9CQ29; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9CQ29; protein.
DR Bgee; ENSMUSG00000008482; Expressed in seminiferous tubule of testis and 19 other tissues.
DR ExpressionAtlas; Q9CQ29; baseline and differential.
DR Genevisible; Q9CQ29; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR InterPro; IPR013010; Znf_SIAH.
DR InterPro; IPR001293; Znf_TRAF.
DR Pfam; PF02176; zf-TRAF; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS51081; ZF_SIAH; 1.
DR PROSITE; PS50145; ZF_TRAF; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Differentiation; Metal-binding; Nucleus; Reference proteome;
KW Spermatogenesis; Zinc; Zinc-finger.
FT CHAIN 1..239
FT /note="RING finger protein 151"
FT /id="PRO_0000255255"
FT ZN_FING 20..58
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 101..156
FT /note="TRAF-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00207"
SQ SEQUENCE 239 AA; 27175 MW; D332071F44766031 CRC64;
MSGGYDLNLF ASPPDCKFLC SVCHGVLKRP TRLPCSHIFC KKCIFRWLAR QNTCPCCRKE
VTRRKMVEVN KLRKTIGRLQ VKCKNAAAGC LDTHPLAHRK EHQDSCPFEL MACPNEGCTV
QVLRGVLDEH RQHCQQNGQQ RCPLGCGSTL AALEGEHHNC YRELRDAWVQ RHERNRTLLL
GLLGRVRRVH LTTSIIHQQL AQLSNFLEDD DNLLLNAQVQ ETEVTPEAEM RGTQGQSVL
