ZY11B_MOUSE
ID ZY11B_MOUSE Reviewed; 744 AA.
AC Q3UFS0; B9EID5; Q148T6; Q3TM33; Q3TMB0; Q3TRM3; Q3UFA3; Q80TA0;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Protein zyg-11 homolog B {ECO:0000305};
GN Name=Zyg11b {ECO:0000312|MGI:MGI:2685277}; Synonyms=Kiaa1730;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RC TISSUE=Bone, Lung, Mammary gland, and Sympathetic ganglion;
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 3).
RC TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 482-744 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Pancreas, and Spleen;
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 ZER1 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:Q9C0D3}.
CC -!- SUBUNIT: Interacts with ELOC/Elongin C. Part of an E3 ubiquitin ligase
CC complex including ZYG11B, CUL2 and Elongin BC.
CC {ECO:0000250|UniProtKB:Q9C0D3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3UFS0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UFS0-2; Sequence=VSP_028225, VSP_028226;
CC Name=3;
CC IsoId=Q3UFS0-3; Sequence=VSP_028227, VSP_028228;
CC -!- SIMILARITY: Belongs to the zyg-11 family. {ECO:0000305}.
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DR EMBL; AK148335; BAE28490.1; -; mRNA.
DR EMBL; AK148760; BAE28658.1; -; mRNA.
DR EMBL; AK162646; BAE37005.1; -; mRNA.
DR EMBL; AK166031; BAE38532.1; -; mRNA.
DR EMBL; AK166174; BAE38609.1; -; mRNA.
DR EMBL; AL627238; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX293563; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC117977; AAI17978.1; -; mRNA.
DR EMBL; BC117978; AAI17979.1; -; mRNA.
DR EMBL; BC139383; AAI39384.1; -; mRNA.
DR EMBL; BC139384; AAI39385.1; -; mRNA.
DR EMBL; AK122545; BAC65827.1; -; mRNA.
DR CCDS; CCDS18448.1; -. [Q3UFS0-1]
DR RefSeq; NP_001028806.2; NM_001033634.3. [Q3UFS0-1]
DR AlphaFoldDB; Q3UFS0; -.
DR SMR; Q3UFS0; -.
DR STRING; 10090.ENSMUSP00000043844; -.
DR iPTMnet; Q3UFS0; -.
DR PhosphoSitePlus; Q3UFS0; -.
DR EPD; Q3UFS0; -.
DR MaxQB; Q3UFS0; -.
DR PaxDb; Q3UFS0; -.
DR PeptideAtlas; Q3UFS0; -.
DR PRIDE; Q3UFS0; -.
DR ProteomicsDB; 275321; -. [Q3UFS0-1]
DR ProteomicsDB; 275322; -. [Q3UFS0-2]
DR ProteomicsDB; 275323; -. [Q3UFS0-3]
DR Antibodypedia; 33029; 54 antibodies from 11 providers.
DR Ensembl; ENSMUST00000043616; ENSMUSP00000043844; ENSMUSG00000034636. [Q3UFS0-1]
DR GeneID; 414872; -.
DR KEGG; mmu:414872; -.
DR UCSC; uc008uax.2; mouse. [Q3UFS0-1]
DR UCSC; uc008uay.2; mouse. [Q3UFS0-2]
DR CTD; 79699; -.
DR MGI; MGI:2685277; Zyg11b.
DR VEuPathDB; HostDB:ENSMUSG00000034636; -.
DR eggNOG; KOG3665; Eukaryota.
DR GeneTree; ENSGT00530000063187; -.
DR HOGENOM; CLU_011533_1_0_1; -.
DR InParanoid; Q3UFS0; -.
DR OMA; QAWTLSH; -.
DR OrthoDB; 374821at2759; -.
DR PhylomeDB; Q3UFS0; -.
DR TreeFam; TF313007; -.
DR BioGRID-ORCS; 414872; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Zyg11b; mouse.
DR PRO; PR:Q3UFS0; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q3UFS0; protein.
DR Bgee; ENSMUSG00000034636; Expressed in medial vestibular nucleus and 238 other tissues.
DR Genevisible; Q3UFS0; MM.
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; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR040367; ZYG11B.
DR PANTHER; PTHR12904:SF21; PTHR12904:SF21; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51450; LRR; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Leucine-rich repeat; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..744
FT /note="Protein zyg-11 homolog B"
FT /id="PRO_0000305088"
FT REPEAT 185..208
FT /note="LRR 1"
FT REPEAT 216..236
FT /note="LRR 2"
FT REPEAT 237..261
FT /note="LRR 3"
FT VAR_SEQ 446..447
FT /note="FE -> QV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028225"
FT VAR_SEQ 448..744
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028226"
FT VAR_SEQ 471..477
FT /note="IISILAA -> LALNSKH (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028227"
FT VAR_SEQ 478..744
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028228"
FT CONFLICT 263
FT /note="D -> G (in Ref. 1; BAE28490)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="Q -> K (in Ref. 1; BAE37005)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="M -> T (in Ref. 1; BAE38609)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="C -> S (in Ref. 1; BAE28658)"
FT /evidence="ECO:0000305"
FT CONFLICT 576
FT /note="S -> P (in Ref. 1; BAE28490)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 744 AA; 83991 MW; C08B0CF8381622F6 CRC64;
MPEDQAHAAM EEASPYSLLD ICLSFLTTNL EKFCSARQDG TLCLQEPGVF PQEVADRLLQ
TIAFHGLLND GTVGIFRGNQ MRLKRACIRK AKISAVAFRK AFCHHKLVEL DATGVNADIT
ITDIISGLGS NKWIQQNLQC LVLNSLTLSL EDPYERCFSR LSGLRALSIT NVLFYNEDLA
EVASLPRLES LDISNTSITD ITALLACKDR LKSLTMHHLK CLKMTTTQIL DVVRELKHLN
HLDISDDKQF TSDIALRLLE QKDILPNLVS LDVSGRKHVT DKAVEAFIQQ RPSMQFVGLL
ATDAGYSEFL MGKGHLKVSG EANETQIAEA LRRYSERAFF VREALFHLFS LTHVMEKTKP
DILKLVVTGM RNHPMNLPVQ LAASACVFNL TKQDLALGMP VRLLADVTHL LLKAMEHFPN
HQQLQKNCLL SLCSDRILQD VPFNRFEAAK LVMQWLCNHE DQNMQRMAVA IISILAAKLS
TEQTAQLGAE LFIVRQLLQI VKQKTNQNSV DTTLKFTLSA LWNLTDESPT TCRHFIENQG
LELFMRVLES FPTESSIQQK VLGLLNNIAE VQELHSELMW KDFIDHISSL LHSVEVEVSY
FAAGIIAHLI SRGEQAWTLS RSQRNSLLDD LHSAILKWPT PECEMVAYRS FNPFFPLLGC
FTTPGVQLWA VWAMQHVCSK NPSRYCSMLI EEGGLQHLYN IKEHEQTDPY VQQIAVAILD
SLEKHIVRHG RPPPCKKQPQ ARLN
