位置:首页 > 蛋白库 > RN141_HUMAN
RN141_HUMAN
ID   RN141_HUMAN             Reviewed;         230 AA.
AC   Q8WVD5; A8K149; Q9NZB4;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=RING finger protein 141;
DE   AltName: Full=Zinc finger protein 230;
GN   Name=RNF141; Synonyms=ZNF230;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND ALTERNATIVE
RP   SPLICING.
RX   PubMed=11672448; DOI=10.1042/0264-6021:3590721;
RA   Zhang S., Qiu W., Wu H., Zhang G., Huang M., Xiao C., Yang J., Kamp C.,
RA   Huang X., Huellen K., Yue Y., Pan A., Lebo R., Milunsky A., Vogt P.H.;
RT   "The shorter zinc finger protein ZNF230 gene message is transcribed in
RT   fertile male testes and may be related to human spermatogenesis.";
RL   Biochem. J. 359:721-727(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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   [6]
RP   MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=25255805; DOI=10.1038/ncomms5919;
RA   Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H.,
RA   Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
RT   "Global profiling of co- and post-translationally N-myristoylated proteomes
RT   in human cells.";
RL   Nat. Commun. 5:4919-4919(2014).
RN   [7]
RP   MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=25807930; DOI=10.1002/anie.201500342;
RA   Broncel M., Serwa R.A., Ciepla P., Krause E., Dallman M.J., Magee A.I.,
RA   Tate E.W.;
RT   "Multifunctional reagents for quantitative proteome-wide analysis of
RT   protein modification in human cells and dynamic profiling of protein
RT   lipidation during vertebrate development.";
RL   Angew. Chem. Int. Ed. 54:5948-5951(2015).
RN   [8]
RP   STRUCTURE BY NMR OF 144-201.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the RING domain of the human RING finger protein
RT   141.";
RL   Submitted (AUG-2007) to the PDB data bank.
CC   -!- FUNCTION: May be involved in spermatogenesis.
CC       {ECO:0000269|PubMed:11672448}.
CC   -!- INTERACTION:
CC       Q8WVD5; Q03426: MVK; NbExp=3; IntAct=EBI-4308142, EBI-740630;
CC       Q8WVD5; Q9H4B4: PLK3; NbExp=3; IntAct=EBI-4308142, EBI-751877;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Short;
CC         IsoId=Q8WVD5-1; Sequence=Displayed;
CC       Name=2; Synonyms=Long;
CC         IsoId=Q8WVD5-2; Sequence=Not described;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is testis-specific. Isoform 2 is
CC       expressed in heart, brain, skeletal muscle, kidney and pancreas.
CC       Isoform 1 is not expressed in fetus or in azoospermic patients.
CC       {ECO:0000269|PubMed:11672448}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF214680; AAF30180.1; -; mRNA.
DR   EMBL; AK289764; BAF82453.1; -; mRNA.
DR   EMBL; CH471064; EAW68566.1; -; Genomic_DNA.
DR   EMBL; BC018104; AAH18104.1; -; mRNA.
DR   EMBL; BT006662; AAP35308.1; -; mRNA.
DR   CCDS; CCDS7803.1; -. [Q8WVD5-1]
DR   RefSeq; NP_057506.2; NM_016422.3. [Q8WVD5-1]
DR   PDB; 2ECN; NMR; -; A=145-201.
DR   PDB; 5XEK; NMR; -; A=152-193.
DR   PDBsum; 2ECN; -.
DR   PDBsum; 5XEK; -.
DR   AlphaFoldDB; Q8WVD5; -.
DR   BMRB; Q8WVD5; -.
DR   SMR; Q8WVD5; -.
DR   BioGRID; 119162; 11.
DR   IntAct; Q8WVD5; 6.
DR   STRING; 9606.ENSP00000265981; -.
DR   iPTMnet; Q8WVD5; -.
DR   PhosphoSitePlus; Q8WVD5; -.
DR   BioMuta; RNF141; -.
DR   DMDM; 74751546; -.
DR   EPD; Q8WVD5; -.
DR   jPOST; Q8WVD5; -.
DR   MassIVE; Q8WVD5; -.
DR   MaxQB; Q8WVD5; -.
DR   PaxDb; Q8WVD5; -.
DR   PeptideAtlas; Q8WVD5; -.
DR   PRIDE; Q8WVD5; -.
DR   ProteomicsDB; 74780; -. [Q8WVD5-1]
DR   Antibodypedia; 11671; 193 antibodies from 31 providers.
DR   DNASU; 50862; -.
DR   Ensembl; ENST00000265981.7; ENSP00000265981.2; ENSG00000110315.7. [Q8WVD5-1]
DR   GeneID; 50862; -.
DR   KEGG; hsa:50862; -.
DR   MANE-Select; ENST00000265981.7; ENSP00000265981.2; NM_016422.4; NP_057506.2.
DR   UCSC; uc001mis.2; human. [Q8WVD5-1]
DR   CTD; 50862; -.
DR   DisGeNET; 50862; -.
DR   GeneCards; RNF141; -.
DR   HGNC; HGNC:21159; RNF141.
DR   HPA; ENSG00000110315; Low tissue specificity.
DR   MIM; 616641; gene.
DR   neXtProt; NX_Q8WVD5; -.
DR   OpenTargets; ENSG00000110315; -.
DR   PharmGKB; PA134981805; -.
DR   VEuPathDB; HostDB:ENSG00000110315; -.
DR   eggNOG; KOG1039; Eukaryota.
DR   GeneTree; ENSGT00390000003145; -.
DR   HOGENOM; CLU_080007_0_0_1; -.
DR   InParanoid; Q8WVD5; -.
DR   OMA; TAANDSW; -.
DR   OrthoDB; 1106056at2759; -.
DR   PhylomeDB; Q8WVD5; -.
DR   TreeFam; TF323284; -.
DR   PathwayCommons; Q8WVD5; -.
DR   SignaLink; Q8WVD5; -.
DR   BioGRID-ORCS; 50862; 10 hits in 1118 CRISPR screens.
DR   ChiTaRS; RNF141; human.
DR   EvolutionaryTrace; Q8WVD5; -.
DR   GenomeRNAi; 50862; -.
DR   Pharos; Q8WVD5; Tbio.
DR   PRO; PR:Q8WVD5; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q8WVD5; protein.
DR   Bgee; ENSG00000110315; Expressed in endothelial cell and 188 other tissues.
DR   ExpressionAtlas; Q8WVD5; baseline and differential.
DR   Genevisible; Q8WVD5; HS.
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; IDA:FlyBase.
DR   GO; GO:0051865; P:protein autoubiquitination; IDA:FlyBase.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:Ensembl.
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   3D-structure; Alternative splicing; Lipoprotein; Membrane; Metal-binding;
KW   Myristate; Reference proteome; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:25255805,
FT                   ECO:0000269|PubMed:25807930"
FT   CHAIN           2..230
FT                   /note="RING finger protein 141"
FT                   /id="PRO_0000056101"
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:0000269|PubMed:25255805,
FT                   ECO:0000269|PubMed:25807930"
FT   CONFLICT        118
FT                   /note="L -> S (in Ref. 1; AAF30180)"
FT                   /evidence="ECO:0000305"
FT   STRAND          156..158
FT                   /evidence="ECO:0007829|PDB:2ECN"
FT   STRAND          164..167
FT                   /evidence="ECO:0007829|PDB:2ECN"
FT   TURN            168..170
FT                   /evidence="ECO:0007829|PDB:2ECN"
FT   STRAND          171..173
FT                   /evidence="ECO:0007829|PDB:2ECN"
FT   HELIX           175..180
FT                   /evidence="ECO:0007829|PDB:2ECN"
FT   HELIX           189..193
FT                   /evidence="ECO:0007829|PDB:2ECN"
SQ   SEQUENCE   230 AA;  25535 MW;  730950F8A6E47129 CRC64;
     MGQQISDQTQ LVINKLPEKV AKHVTLVRES GSLTYEEFLG RVAELNDVTA KVASGQEKHL
     LFEVQPGSDS SAFWKVVVRV VCTKINKSSG IVEASRIMNL YQFIQLYKDI TSQAAGVLAQ
     SSTSEEPDEN SSSVTSCQAS LWMGRVKQLT DEEECCICMD GRADLILPCA HSFCQKCIDK
     WSDRHRNCPI CRLQMTGANE SWVVSDAPTE DDMANYILNM ADEAGQPHRP
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024