ZER1_HUMAN
ID ZER1_HUMAN Reviewed; 766 AA.
AC Q7Z7L7; O00156; Q5T272; Q5T273;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Protein zer-1 homolog {ECO:0000305};
DE AltName: Full=Hzyg;
DE AltName: Full=Zyg-11 homolog B-like protein;
DE AltName: Full=Zyg11b-like protein;
GN Name=ZER1 {ECO:0000312|HGNC:HGNC:30960};
GN Synonyms=C9orf60, ZYG, ZYG11BL {ECO:0000303|PubMed:17304241};
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], AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=11719588; DOI=10.1093/molehr/7.12.1115;
RA Feral C., Wu Y.-Q., Pawlak A., Guellaen G.;
RT "Meiotic human sperm cells express a leucine-rich homologue of
RT Caenorhabditis elegans early embryogenesis gene, Zyg-11.";
RL Mol. Hum. Reprod. 7:1115-1122(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
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 FUNCTION, INTERACTION WITH ELOC, IDENTIFICATION IN COMPLEX WITH ELOB; ELOC
RP AND CUL2, AND MUTAGENESIS OF LEU-9.
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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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 (PubMed:17304241,
CC PubMed:31273098). Acts redudantly with ZYG11B to target substrates
CC bearing N-terminal glycine degrons for proteasomal degradation
CC (PubMed:33093214). 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 (PubMed:31273098). {ECO:0000269|PubMed:17304241,
CC ECO:0000269|PubMed:31273098, ECO:0000269|PubMed:33093214}.
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:0000269|PubMed:17304241}.
CC -!- TISSUE SPECIFICITY: Expressed in testis, spermatocytes and spermatids
CC (at protein level). Expressed in spermatocytes, spermatids, prostate,
CC skeletal muscle, ovary, small intestine, heart, brain and pancreas.
CC {ECO:0000269|PubMed:11719588}.
CC -!- SIMILARITY: Belongs to the zyg-11 family. {ECO:0000305}.
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DR EMBL; X99802; CAA68137.1; -; mRNA.
DR EMBL; AL441992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC052563; AAH52563.1; -; mRNA.
DR CCDS; CCDS6910.1; -.
DR RefSeq; NP_006327.2; NM_006336.3.
DR RefSeq; XP_005251702.1; XM_005251645.2.
DR RefSeq; XP_011516424.1; XM_011518122.2.
DR RefSeq; XP_016869674.1; XM_017014185.1.
DR PDB; 7EP3; X-ray; 1.51 A; A=520-766.
DR PDB; 7EP4; X-ray; 2.07 A; A/B=518-766.
DR PDB; 7EP5; X-ray; 2.02 A; A/B=518-766.
DR PDBsum; 7EP3; -.
DR PDBsum; 7EP4; -.
DR PDBsum; 7EP5; -.
DR AlphaFoldDB; Q7Z7L7; -.
DR SMR; Q7Z7L7; -.
DR BioGRID; 115709; 87.
DR IntAct; Q7Z7L7; 28.
DR MINT; Q7Z7L7; -.
DR STRING; 9606.ENSP00000291900; -.
DR iPTMnet; Q7Z7L7; -.
DR PhosphoSitePlus; Q7Z7L7; -.
DR BioMuta; ZER1; -.
DR DMDM; 68566100; -.
DR EPD; Q7Z7L7; -.
DR jPOST; Q7Z7L7; -.
DR MassIVE; Q7Z7L7; -.
DR MaxQB; Q7Z7L7; -.
DR PaxDb; Q7Z7L7; -.
DR PeptideAtlas; Q7Z7L7; -.
DR PRIDE; Q7Z7L7; -.
DR ProteomicsDB; 69562; -.
DR Antibodypedia; 31261; 72 antibodies from 21 providers.
DR DNASU; 10444; -.
DR Ensembl; ENST00000291900.7; ENSP00000291900.2; ENSG00000160445.11.
DR GeneID; 10444; -.
DR KEGG; hsa:10444; -.
DR MANE-Select; ENST00000291900.7; ENSP00000291900.2; NM_006336.4; NP_006327.2.
DR UCSC; uc004bwa.3; human.
DR CTD; 10444; -.
DR DisGeNET; 10444; -.
DR GeneCards; ZER1; -.
DR HGNC; HGNC:30960; ZER1.
DR HPA; ENSG00000160445; Low tissue specificity.
DR MIM; 617764; gene.
DR neXtProt; NX_Q7Z7L7; -.
DR OpenTargets; ENSG00000160445; -.
DR PharmGKB; PA162409637; -.
DR VEuPathDB; HostDB:ENSG00000160445; -.
DR eggNOG; KOG3665; Eukaryota.
DR GeneTree; ENSGT00530000063187; -.
DR HOGENOM; CLU_011533_0_0_1; -.
DR InParanoid; Q7Z7L7; -.
DR OMA; MFDAPAS; -.
DR OrthoDB; 374821at2759; -.
DR PhylomeDB; Q7Z7L7; -.
DR TreeFam; TF313007; -.
DR PathwayCommons; Q7Z7L7; -.
DR SignaLink; Q7Z7L7; -.
DR BioGRID-ORCS; 10444; 15 hits in 1074 CRISPR screens.
DR ChiTaRS; ZER1; human.
DR GenomeRNAi; 10444; -.
DR Pharos; Q7Z7L7; Tbio.
DR PRO; PR:Q7Z7L7; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q7Z7L7; protein.
DR Bgee; ENSG00000160445; Expressed in right frontal lobe and 175 other tissues.
DR ExpressionAtlas; Q7Z7L7; baseline and differential.
DR Genevisible; Q7Z7L7; 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; IPR000225; Armadillo.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR040368; Zer-1.
DR PANTHER; PTHR12904:SF23; PTHR12904:SF23; 1.
DR SMART; SM00185; ARM; 4.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Leucine-rich repeat; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..766
FT /note="Protein zer-1 homolog"
FT /id="PRO_0000066598"
FT REPEAT 226..245
FT /note="LRR 1"
FT REPEAT 246..268
FT /note="LRR 2"
FT REPEAT 278..302
FT /note="LRR 3"
FT REPEAT 427..467
FT /note="ARM 1"
FT REPEAT 511..556
FT /note="ARM 2"
FT REPEAT 558..600
FT /note="ARM 3"
FT REPEAT 602..643
FT /note="ARM 4"
FT REPEAT 714..756
FT /note="ARM 5"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VARIANT 539
FT /note="T -> I (in dbSNP:rs13299702)"
FT /id="VAR_060159"
FT MUTAGEN 9
FT /note="L->S: Abolishes interaction with ELOC."
FT /evidence="ECO:0000269|PubMed:17304241"
FT CONFLICT 249
FT /note="R -> G (in Ref. 1; CAA68137)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="A -> L (in Ref. 1; CAA68137)"
FT /evidence="ECO:0000305"
FT CONFLICT 588
FT /note="H -> I (in Ref. 1; CAA68137)"
FT /evidence="ECO:0000305"
FT CONFLICT 653
FT /note="E -> K (in Ref. 1; CAA68137)"
FT /evidence="ECO:0000305"
FT HELIX 520..536
FT /evidence="ECO:0007829|PDB:7EP3"
FT HELIX 542..554
FT /evidence="ECO:0007829|PDB:7EP3"
FT TURN 555..557
FT /evidence="ECO:0007829|PDB:7EP3"
FT HELIX 559..567
FT /evidence="ECO:0007829|PDB:7EP3"
FT HELIX 570..580
FT /evidence="ECO:0007829|PDB:7EP3"
FT HELIX 585..599
FT /evidence="ECO:0007829|PDB:7EP3"
FT HELIX 602..608
FT /evidence="ECO:0007829|PDB:7EP3"
FT HELIX 611..620
FT /evidence="ECO:0007829|PDB:7EP3"
FT TURN 625..628
FT /evidence="ECO:0007829|PDB:7EP3"
FT HELIX 629..643
FT /evidence="ECO:0007829|PDB:7EP3"
FT HELIX 646..648
FT /evidence="ECO:0007829|PDB:7EP3"
FT HELIX 656..669
FT /evidence="ECO:0007829|PDB:7EP3"
FT HELIX 684..687
FT /evidence="ECO:0007829|PDB:7EP3"
FT HELIX 696..712
FT /evidence="ECO:0007829|PDB:7EP3"
FT HELIX 714..723
FT /evidence="ECO:0007829|PDB:7EP3"
FT HELIX 726..734
FT /evidence="ECO:0007829|PDB:7EP3"
FT STRAND 737..739
FT /evidence="ECO:0007829|PDB:7EP3"
FT HELIX 741..758
FT /evidence="ECO:0007829|PDB:7EP3"
SQ SEQUENCE 766 AA; 88169 MW; 0B023E692CDE5520 CRC64;
MASDTPESLM ALCTDFCLRN LDGTLGYLLD KETLRLHPDI FLPSEICDRL VNEYVELVNA
ACNFEPHESF FSLFSDPRST RLTRIHLRED LVQDQDLEAI RKQDLVELYL TNCEKLSAKS
LQTLRSFSHT LVSLSLFGCT NIFYEEENPG GCEDEYLVNP TCQVLVKDFT FEGFSRLRFL
NLGRMIDWVP VESLLRPLNS LAALDLSGIQ TSDAAFLTQW KDSLVSLVLY NMDLSDDHIR
VIVQLHKLRH LDISRDRLSS YYKFKLTREV LSLFVQKLGN LMSLDISGHM ILENCSISKM
EEEAGQTSIE PSKSSIIPFR ALKRPLQFLG LFENSLCRLT HIPAYKVSGD KNEEQVLNAI
EAYTEHRPEI TSRAINLLFD IARIERCNQL LRALKLVITA LKCHKYDRNI QVTGSAALFY
LTNSEYRSEQ SVKLRRQVIQ VVLNGMESYQ EVTVQRNCCL TLCNFSIPEE LEFQYRRVNE
LLLSILNPTR QDESIQRIAV HLCNALVCQV DNDHKEAVGK MGFVVTMLKL IQKKLLDKTC
DQVMEFSWSA LWNITDETPD NCEMFLNFNG MKLFLDCLKE FPEKQELHRN MLGLLGNVAE
VKELRPQLMT SQFISVFSNL LESKADGIEV SYNACGVLSH IMFDGPEAWG VCEPQREEVE
ERMWAAIQSW DINSRRNINY RSFEPILRLL PQGISPVSQH WATWALYNLV SVYPDKYCPL
LIKEGGMPLL RDIIKMATAR QETKEMARKV IEHCSNFKEE NMDTSR
