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ZER1_MOUSE
ID   ZER1_MOUSE              Reviewed;         779 AA.
AC   Q80ZJ6; A2BEA2; Q6PGH5; Q8BG38;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Protein zer-1 homolog {ECO:0000305};
DE   AltName: Full=Zyg-11 homolog B-like protein;
GN   Name=Zer1 {ECO:0000312|MGI:MGI:2442511}; Synonyms=Zyg, Zyg11bl;
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   STRAIN=C57BL/6J; TISSUE=Cerebellum, Head, Lung, and Olfactory bulb;
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 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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryonic brain, and Olfactory epithelium;
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   PROTEIN SEQUENCE OF 504-510, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Spleen, 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: Serves as substrate adapter subunit in the E3 ubiquitin
CC       ligase complex ZYG11B-CUL2-Elongin BC. Acts redudantly with ZYG11B to
CC       target substrates bearing N-terminal glycine degrons for proteasomal
CC       degradation. Involved in the clearance of proteolytic fragments
CC       generated by caspase cleavage during apoptosis since N-terminal glycine
CC       degrons are strongly enriched at caspase cleavage sites. Also important
CC       in the quality control of protein N-myristoylation in which N-terminal
CC       glycine degrons are conditionally exposed after a failure of N-
CC       myristoylation. {ECO:0000250|UniProtKB:Q7Z7L7}.
CC   -!- SUBUNIT: Interacts with the ELOC-ELOB/Elongin BC complex. Part of an E3
CC       ubiquitin ligase complex including ZER1, CUL2 and Elongin BC.
CC       {ECO:0000250|UniProtKB:Q7Z7L7}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q80ZJ6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80ZJ6-2; Sequence=VSP_014425;
CC       Name=3;
CC         IsoId=Q80ZJ6-3; Sequence=VSP_014425, VSP_014426, VSP_014427;
CC   -!- SIMILARITY: Belongs to the zyg-11 family. {ECO:0000305}.
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DR   EMBL; AK029290; BAC26374.1; -; mRNA.
DR   EMBL; AK032318; BAC27811.1; -; mRNA.
DR   EMBL; AK048853; BAC33474.1; -; mRNA.
DR   EMBL; AK087046; BAC39788.1; -; mRNA.
DR   EMBL; BX005298; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC048924; AAH48924.1; -; mRNA.
DR   EMBL; BC057021; AAH57021.1; -; mRNA.
DR   CCDS; CCDS15870.1; -. [Q80ZJ6-1]
DR   CCDS; CCDS71017.1; -. [Q80ZJ6-2]
DR   RefSeq; NP_001277432.1; NM_001290503.1. [Q80ZJ6-2]
DR   RefSeq; NP_848809.2; NM_178694.4. [Q80ZJ6-1]
DR   AlphaFoldDB; Q80ZJ6; -.
DR   SMR; Q80ZJ6; -.
DR   BioGRID; 230663; 19.
DR   STRING; 10090.ENSMUSP00000046441; -.
DR   iPTMnet; Q80ZJ6; -.
DR   PhosphoSitePlus; Q80ZJ6; -.
DR   EPD; Q80ZJ6; -.
DR   MaxQB; Q80ZJ6; -.
DR   PaxDb; Q80ZJ6; -.
DR   PRIDE; Q80ZJ6; -.
DR   ProteomicsDB; 274978; -. [Q80ZJ6-1]
DR   ProteomicsDB; 274979; -. [Q80ZJ6-2]
DR   ProteomicsDB; 274980; -. [Q80ZJ6-3]
DR   Antibodypedia; 31261; 72 antibodies from 21 providers.
DR   DNASU; 227693; -.
DR   Ensembl; ENSMUST00000044751; ENSMUSP00000046441; ENSMUSG00000039686. [Q80ZJ6-1]
DR   Ensembl; ENSMUST00000113677; ENSMUSP00000109307; ENSMUSG00000039686. [Q80ZJ6-2]
DR   GeneID; 227693; -.
DR   KEGG; mmu:227693; -.
DR   UCSC; uc008jbf.2; mouse. [Q80ZJ6-1]
DR   UCSC; uc008jbh.2; mouse. [Q80ZJ6-3]
DR   CTD; 10444; -.
DR   MGI; MGI:2442511; Zer1.
DR   VEuPathDB; HostDB:ENSMUSG00000039686; -.
DR   eggNOG; KOG3665; Eukaryota.
DR   GeneTree; ENSGT00530000063187; -.
DR   HOGENOM; CLU_011533_0_0_1; -.
DR   InParanoid; Q80ZJ6; -.
DR   OMA; MFDAPAS; -.
DR   OrthoDB; 374821at2759; -.
DR   PhylomeDB; Q80ZJ6; -.
DR   TreeFam; TF313007; -.
DR   BioGRID-ORCS; 227693; 5 hits in 74 CRISPR screens.
DR   ChiTaRS; Zer1; mouse.
DR   PRO; PR:Q80ZJ6; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q80ZJ6; protein.
DR   Bgee; ENSMUSG00000039686; Expressed in primary visual cortex and 145 other tissues.
DR   ExpressionAtlas; Q80ZJ6; baseline and differential.
DR   GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; ISS:UniProtKB.
DR   Gene3D; 1.25.10.10; -; 1.
DR   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR040368; Zer-1.
DR   PANTHER; PTHR12904:SF23; PTHR12904:SF23; 1.
DR   SMART; SM00185; ARM; 5.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Direct protein sequencing;
KW   Leucine-rich repeat; Reference proteome; Repeat; Ubl conjugation pathway.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z7L7"
FT   CHAIN           2..779
FT                   /note="Protein zer-1 homolog"
FT                   /id="PRO_0000066599"
FT   REPEAT          226..245
FT                   /note="LRR 1"
FT   REPEAT          246..281
FT                   /note="LRR 2"
FT   REPEAT          291..315
FT                   /note="LRR 3"
FT   REPEAT          440..480
FT                   /note="ARM 1"
FT   REPEAT          524..569
FT                   /note="ARM 2"
FT   REPEAT          571..613
FT                   /note="ARM 3"
FT   REPEAT          615..656
FT                   /note="ARM 4"
FT   REPEAT          727..769
FT                   /note="ARM 5"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z7L7"
FT   VAR_SEQ         250..262
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_014425"
FT   VAR_SEQ         468..490
FT                   /note="QRNCCLTLCNFSIPEELEFQYRR -> SPCLLRPACLGPVSLPAPQAPQA
FT                   (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_014426"
FT   VAR_SEQ         491..779
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_014427"
SQ   SEQUENCE   779 AA;  89076 MW;  825D4B2E2E47A16D CRC64;
     MASDTPESLM ALCTDFCLRN LDGTLGYLLD KETLRLHPDI FLPSEICDQL VNEYVELVSA
     ACTFEPHETF FSLFSDPRST RLTRIHLRED LVQDQDLEAI RKQDLVELYL TNCEKLSAKS
     LQTLRSFRHS LVSLSLSGCA NIFYEEDNPG GCEDECLVNP TCQVLVKDFT FEGFSRLRFL
     NLGRMIDGIP VESLLRPLNS LAALDLSGIQ TSDATFLTQW KDSLMSLVLY NMDLSDDHIR
     VIVQLHKLRS KILTCGPHLI SSHLDISRDR LSSYYKFKLT RKVLSLLVQK LGNLMSLDIS
     GHMILENCSI SKTDEEAGQT STEPSKSSIM PFRALKRPLQ FLGLFETSLC RLTHIPAYKV
     SGDKNEEQVL NAIEAYTEHR PEITSRAINL LFDIARIERC NQLLRALKLV ITALKCHKYD
     KNIQVTGSAA LFYLTNSEYR SEQSVKLRRQ VIQVVLNGME SYQEVTVQRN CCLTLCNFSI
     PEELEFQYRR VNELLLGILS PTRQDESIQR IAVHLCNALV CQVDNDHKEA VGKMGFVVTM
     LKLIQKKLLD KTCDQVMEFS WSALWNITDE TPDNCEMFLN FNGMKLFLDC LKEFPEKQEL
     HRNMLGLLGN VAEVKELRPQ LMTSQFISVF SNLLESKADG IEVSYNACGV LSHIMFDGPE
     AWGVCEPQRA EVEDRMWAAI QSWDINSRRN INYRSFEPIL RLLPQGISPV SQHWATWALY
     NLVSVYPDKY CPLLIKEGGM PLLRDLIKMA TARQETKEMA RKVIEHCSNF REENMDTSR
 
 
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