ZY11B_HUMAN
ID ZY11B_HUMAN Reviewed; 744 AA.
AC Q9C0D3; Q8N2X3; Q9H8L8;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Protein zyg-11 homolog B {ECO:0000305};
GN Name=ZYG11B {ECO:0000312|HGNC:HGNC:25820}; Synonyms=KIAA1730;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 265-744 (ISOFORM 1).
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 INTERACTION WITH ELOC, IDENTIFICATION IN COMPLEX WITH ELOC AND CUL2, AND
RP MUTAGENESIS OF LEU-18.
RX PubMed=17304241; DOI=10.1038/sj.embor.7400895;
RA Vasudevan S., Starostina N.G., Kipreos E.T.;
RT "The Caenorhabditis elegans cell-cycle regulator ZYG-11 defines a conserved
RT family of CUL-2 complex components.";
RL EMBO Rep. 8:279-286(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [6]
RP FUNCTION.
RX PubMed=31273098; DOI=10.1126/science.aaw4912;
RA Timms R.T., Zhang Z., Rhee D.Y., Harper J.W., Koren I., Elledge S.J.;
RT "A glycine-specific N-degron pathway mediates the quality control of
RT protein N-myristoylation.";
RL Science 365:0-0(2019).
RN [7]
RP FUNCTION.
RX PubMed=33093214; DOI=10.1126/science.aay2002;
RA Robinson K.S., Teo D.E.T., Tan K.S., Toh G.A., Ong H.H., Lim C.K., Lay K.,
RA Au B.V., Lew T.S., Chu J.J.H., Chow V.T.K., Wang Y., Zhong F.L.,
RA Reversade B.;
RT "Enteroviral 3C protease activates the human NLRP1 inflammasome in airway
RT epithelia.";
RL Science 0:0-0(2020).
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 (PubMed:33093214). Involved in the clearance of proteolytic
CC fragments generated by caspase cleavage during apoptosis since N-
CC terminal glycine degrons are strongly enriched at caspase cleavage
CC sites. Also important in the quality control of protein N-
CC myristoylation in which N-terminal glycine degrons are conditionally
CC exposed after a failure of N-myristoylation (PubMed:31273098).
CC {ECO:0000269|PubMed:31273098, ECO:0000269|PubMed:33093214}.
CC -!- SUBUNIT: Interacts with ELOC/Elongin C. Part of an E3 ubiquitin ligase
CC complex including ZYG11B, CUL2 and Elongin BC.
CC {ECO:0000269|PubMed:17304241}.
CC -!- INTERACTION:
CC Q9C0D3; Q13617: CUL2; NbExp=4; IntAct=EBI-1811414, EBI-456179;
CC Q9C0D3; Q92538-3: GBF1; NbExp=3; IntAct=EBI-1811414, EBI-17724521;
CC Q9C0D3; Q96CV9: OPTN; NbExp=3; IntAct=EBI-1811414, EBI-748974;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C0D3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C0D3-2; Sequence=VSP_028224;
CC -!- SIMILARITY: Belongs to the zyg-11 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB21821.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB051517; BAB21821.1; ALT_INIT; mRNA.
DR EMBL; AK023518; BAB14596.1; -; mRNA.
DR EMBL; BC029832; AAH29832.2; -; mRNA.
DR CCDS; CCDS30717.1; -. [Q9C0D3-1]
DR RefSeq; NP_078922.1; NM_024646.2. [Q9C0D3-1]
DR PDB; 7EP0; X-ray; 2.16 A; A/B=480-728.
DR PDB; 7EP1; X-ray; 1.85 A; A/B=485-728.
DR PDB; 7EP2; X-ray; 2.38 A; A/B/C/D=443-728.
DR PDBsum; 7EP0; -.
DR PDBsum; 7EP1; -.
DR PDBsum; 7EP2; -.
DR AlphaFoldDB; Q9C0D3; -.
DR SMR; Q9C0D3; -.
DR BioGRID; 122820; 114.
DR IntAct; Q9C0D3; 43.
DR MINT; Q9C0D3; -.
DR STRING; 9606.ENSP00000294353; -.
DR iPTMnet; Q9C0D3; -.
DR PhosphoSitePlus; Q9C0D3; -.
DR BioMuta; ZYG11B; -.
DR DMDM; 158706479; -.
DR EPD; Q9C0D3; -.
DR jPOST; Q9C0D3; -.
DR MassIVE; Q9C0D3; -.
DR MaxQB; Q9C0D3; -.
DR PaxDb; Q9C0D3; -.
DR PeptideAtlas; Q9C0D3; -.
DR PRIDE; Q9C0D3; -.
DR ProteomicsDB; 80011; -. [Q9C0D3-1]
DR ProteomicsDB; 80012; -. [Q9C0D3-2]
DR Antibodypedia; 33029; 54 antibodies from 11 providers.
DR DNASU; 79699; -.
DR Ensembl; ENST00000294353.7; ENSP00000294353.6; ENSG00000162378.13. [Q9C0D3-1]
DR GeneID; 79699; -.
DR KEGG; hsa:79699; -.
DR MANE-Select; ENST00000294353.7; ENSP00000294353.6; NM_024646.3; NP_078922.1.
DR UCSC; uc001cuj.4; human. [Q9C0D3-1]
DR CTD; 79699; -.
DR DisGeNET; 79699; -.
DR GeneCards; ZYG11B; -.
DR HGNC; HGNC:25820; ZYG11B.
DR HPA; ENSG00000162378; Tissue enhanced (skeletal muscle, tongue).
DR MIM; 618673; gene.
DR neXtProt; NX_Q9C0D3; -.
DR OpenTargets; ENSG00000162378; -.
DR PharmGKB; PA142670468; -.
DR VEuPathDB; HostDB:ENSG00000162378; -.
DR eggNOG; KOG3665; Eukaryota.
DR GeneTree; ENSGT00530000063187; -.
DR HOGENOM; CLU_011533_1_0_1; -.
DR InParanoid; Q9C0D3; -.
DR OMA; QAWTLSH; -.
DR PhylomeDB; Q9C0D3; -.
DR TreeFam; TF313007; -.
DR PathwayCommons; Q9C0D3; -.
DR SignaLink; Q9C0D3; -.
DR BioGRID-ORCS; 79699; 17 hits in 1118 CRISPR screens.
DR ChiTaRS; ZYG11B; human.
DR GenomeRNAi; 79699; -.
DR Pharos; Q9C0D3; Tbio.
DR PRO; PR:Q9C0D3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9C0D3; protein.
DR Bgee; ENSG00000162378; Expressed in deltoid and 197 other tissues.
DR ExpressionAtlas; Q9C0D3; baseline and differential.
DR Genevisible; Q9C0D3; HS.
DR GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IMP: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 3D-structure; Alternative splicing; Leucine-rich repeat;
KW Reference proteome; Repeat; Ubl conjugation pathway.
FT CHAIN 1..744
FT /note="Protein zyg-11 homolog B"
FT /id="PRO_0000305087"
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 1..578
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_028224"
FT MUTAGEN 18
FT /note="L->S: Abolishes interaction with ELOC."
FT /evidence="ECO:0000269|PubMed:17304241"
FT CONFLICT 672
FT /note="W -> C (in Ref. 2; BAB14596)"
FT /evidence="ECO:0000305"
FT HELIX 447..457
FT /evidence="ECO:0007829|PDB:7EP2"
FT HELIX 462..478
FT /evidence="ECO:0007829|PDB:7EP2"
FT HELIX 485..506
FT /evidence="ECO:0007829|PDB:7EP1"
FT HELIX 512..524
FT /evidence="ECO:0007829|PDB:7EP1"
FT TURN 525..527
FT /evidence="ECO:0007829|PDB:7EP1"
FT HELIX 529..537
FT /evidence="ECO:0007829|PDB:7EP1"
FT HELIX 540..550
FT /evidence="ECO:0007829|PDB:7EP1"
FT HELIX 555..569
FT /evidence="ECO:0007829|PDB:7EP1"
FT HELIX 572..578
FT /evidence="ECO:0007829|PDB:7EP1"
FT HELIX 581..591
FT /evidence="ECO:0007829|PDB:7EP1"
FT HELIX 596..611
FT /evidence="ECO:0007829|PDB:7EP1"
FT TURN 614..616
FT /evidence="ECO:0007829|PDB:7EP1"
FT HELIX 621..637
FT /evidence="ECO:0007829|PDB:7EP1"
FT HELIX 652..654
FT /evidence="ECO:0007829|PDB:7EP1"
FT HELIX 655..658
FT /evidence="ECO:0007829|PDB:7EP1"
FT HELIX 664..680
FT /evidence="ECO:0007829|PDB:7EP1"
FT HELIX 682..691
FT /evidence="ECO:0007829|PDB:7EP1"
FT HELIX 694..703
FT /evidence="ECO:0007829|PDB:7EP1"
FT HELIX 709..722
FT /evidence="ECO:0007829|PDB:7EP1"
SQ SEQUENCE 744 AA; 83921 MW; 0D8C19251CA67573 CRC64;
MPEDQAGAAM EEASPYSLLD ICLNFLTTHL EKFCSARQDG TLCLQEPGVF PQEVADRLLR
TMAFHGLLND GTVGIFRGNQ MRLKRACIRK AKISAVAFRK AFCHHKLVEL DATGVNADIT
ITDIISGLGS NKWIQQNLQC LVLNSLTLSL EDPYERCFSR LSGLRALSIT NVLFYNEDLA
EVASLPRLES LDISNTSITD ITALLACKDR LKSLTMHHLK CLKMTTTQIL DVVRELKHLN
HLDISDDKQF TSDIALRLLE QKDILPNLVS LDVSGRKHVT DKAVEAFIQQ RPSMQFVGLL
ATDAGYSEFL TGEGHLKVSG EANETQIAEA LKRYSERAFF VREALFHLFS LTHVMEKTKP
EILKLVVTGM RNHPMNLPVQ LAASACVFNL TKQDLAAGMP VRLLADVTHL LLKAMEHFPN
HQQLQKNCLL SLCSDRILQD VPFNRFEAAK LVMQWLCNHE DQNMQRMAVA IISILAAKLS
TEQTAQLGTE LFIVRQLLQI VKQKTNQNSV DTTLKFTLSA LWNLTDESPT TCRHFIENQG
LELFMRVLES FPTESSIQQK VLGLLNNIAE VQELHSELMW KDFIDHISSL LHSVEVEVSY
FAAGIIAHLI SRGEQAWTLS RSQRNSLLDD LHSAILKWPT PECEMVAYRS FNPFFPLLGC
FTTPGVQLWA VWAMQHVCSK NPSRYCSMLI EEGGLQHLYN IKDHEHTDPH VQQIAVAILD
SLEKHIVRHG RPPPCKKQPQ ARLN
