ARCH_HUMAN
ID ARCH_HUMAN Reviewed; 167 AA.
AC Q8IWT0; Q5TGK5; Q6PDA1; Q8IWS9; Q8NEV6; Q8NEV7;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Protein archease;
DE AltName: Full=Protein ZBTB8OS;
DE AltName: Full=Zinc finger and BTB domain-containing opposite strand protein 8;
GN Name=ZBTB8OS; Synonyms=ARCH;
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] (ISOFORMS 1 AND 2).
RA Alliel P.M., Goudou D., Bitoun M., Langlois C., Rieger F., Seddiqi N.,
RA Perin J.P.;
RT "Structure, expression and sequence comparison of human and murine
RT archease.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 IDENTIFICATION.
RX PubMed=15162483; DOI=10.1002/prot.20141;
RA Canaves J.M.;
RT "Predicted role for the archease protein family based on structural and
RT sequence analysis of TM1083 and MTH1598, two proteins structurally
RT characterized through structural genomics efforts.";
RL Proteins 56:19-27(2004).
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=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
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 [7]
RP FUNCTION, IDENTIFICATION IN THE TRNA SPLICING LIGASE COMPLEX, AND
RP MUTAGENESIS OF ASP-39 AND LYS-144.
RX PubMed=24870230; DOI=10.1038/nature13284;
RA Popow J., Jurkin J., Schleiffer A., Martinez J.;
RT "Analysis of orthologous groups reveals archease and DDX1 as tRNA splicing
RT factors.";
RL Nature 511:104-107(2014).
CC -!- FUNCTION: Component of the tRNA-splicing ligase complex required to
CC facilitate the enzymatic turnover of catalytic subunit RTCB. Together
CC with DDX1, acts by facilitating the guanylylation of RTCB, a key
CC intermediate step in tRNA ligation. {ECO:0000269|PubMed:24870230}.
CC -!- SUBUNIT: Component of the tRNA-splicing ligase complex.
CC {ECO:0000269|PubMed:24870230}.
CC -!- INTERACTION:
CC Q8IWT0; Q9Y3I0: RTCB; NbExp=2; IntAct=EBI-2808825, EBI-2107208;
CC Q8IWT0-2; P46379-2: BAG6; NbExp=3; IntAct=EBI-12956041, EBI-10988864;
CC Q8IWT0-2; P55212: CASP6; NbExp=3; IntAct=EBI-12956041, EBI-718729;
CC Q8IWT0-2; P06307: CCK; NbExp=3; IntAct=EBI-12956041, EBI-6624398;
CC Q8IWT0-2; O95872: GPANK1; NbExp=3; IntAct=EBI-12956041, EBI-751540;
CC Q8IWT0-2; O00291: HIP1; NbExp=3; IntAct=EBI-12956041, EBI-473886;
CC Q8IWT0-2; O14901: KLF11; NbExp=3; IntAct=EBI-12956041, EBI-948266;
CC Q8IWT0-2; P13473-2: LAMP2; NbExp=3; IntAct=EBI-12956041, EBI-21591415;
CC Q8IWT0-2; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-12956041, EBI-2811583;
CC Q8IWT0-2; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-12956041, EBI-5280197;
CC Q8IWT0-2; P62826: RAN; NbExp=3; IntAct=EBI-12956041, EBI-286642;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8IWT0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IWT0-2; Sequence=VSP_024926;
CC -!- SIMILARITY: Belongs to the archease family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM34477.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAN75223.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAN75224.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY099493; AAM34477.1; ALT_INIT; mRNA.
DR EMBL; AY099494; AAM34478.1; -; mRNA.
DR EMBL; AY151084; AAN75223.1; ALT_INIT; mRNA.
DR EMBL; AY151085; AAN75224.1; ALT_INIT; mRNA.
DR EMBL; AC114489; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL033529; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC058843; AAH58843.1; -; mRNA.
DR CCDS; CCDS365.1; -. [Q8IWT0-1]
DR RefSeq; NP_001295065.1; NM_001308136.1.
DR RefSeq; NP_001295068.1; NM_001308139.1.
DR RefSeq; NP_848642.1; NM_178547.3. [Q8IWT0-1]
DR AlphaFoldDB; Q8IWT0; -.
DR SMR; Q8IWT0; -.
DR BioGRID; 130893; 12.
DR ComplexPortal; CPX-6411; tRNA-splicing ligase complex.
DR DIP; DIP-61031N; -.
DR IntAct; Q8IWT0; 15.
DR STRING; 9606.ENSP00000417677; -.
DR iPTMnet; Q8IWT0; -.
DR PhosphoSitePlus; Q8IWT0; -.
DR BioMuta; ZBTB8OS; -.
DR DMDM; 146286037; -.
DR EPD; Q8IWT0; -.
DR jPOST; Q8IWT0; -.
DR MassIVE; Q8IWT0; -.
DR MaxQB; Q8IWT0; -.
DR PaxDb; Q8IWT0; -.
DR PeptideAtlas; Q8IWT0; -.
DR PRIDE; Q8IWT0; -.
DR ProteomicsDB; 70887; -. [Q8IWT0-1]
DR ProteomicsDB; 70888; -. [Q8IWT0-2]
DR TopDownProteomics; Q8IWT0-1; -. [Q8IWT0-1]
DR TopDownProteomics; Q8IWT0-2; -. [Q8IWT0-2]
DR Antibodypedia; 54681; 58 antibodies from 15 providers.
DR DNASU; 339487; -.
DR Ensembl; ENST00000436661.6; ENSP00000413485.2; ENSG00000176261.16. [Q8IWT0-2]
DR Ensembl; ENST00000468695.6; ENSP00000417677.2; ENSG00000176261.16. [Q8IWT0-1]
DR GeneID; 339487; -.
DR KEGG; hsa:339487; -.
DR MANE-Select; ENST00000468695.6; ENSP00000417677.2; NM_178547.5; NP_848642.2.
DR UCSC; uc057elg.1; human. [Q8IWT0-1]
DR CTD; 339487; -.
DR DisGeNET; 339487; -.
DR GeneCards; ZBTB8OS; -.
DR HGNC; HGNC:24094; ZBTB8OS.
DR HPA; ENSG00000176261; Low tissue specificity.
DR neXtProt; NX_Q8IWT0; -.
DR PharmGKB; PA142670540; -.
DR VEuPathDB; HostDB:ENSG00000176261; -.
DR eggNOG; KOG4528; Eukaryota.
DR GeneTree; ENSGT00390000003245; -.
DR InParanoid; Q8IWT0; -.
DR OrthoDB; 1360804at2759; -.
DR PhylomeDB; Q8IWT0; -.
DR BioCyc; MetaCyc:ENSG00000176261-MON; -.
DR PathwayCommons; Q8IWT0; -.
DR Reactome; R-HSA-6784531; tRNA processing in the nucleus.
DR SignaLink; Q8IWT0; -.
DR BioGRID-ORCS; 339487; 415 hits in 1088 CRISPR screens.
DR ChiTaRS; ZBTB8OS; human.
DR GenomeRNAi; 339487; -.
DR Pharos; Q8IWT0; Tbio.
DR PRO; PR:Q8IWT0; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8IWT0; protein.
DR Bgee; ENSG00000176261; Expressed in monocyte and 178 other tissues.
DR ExpressionAtlas; Q8IWT0; baseline and differential.
DR Genevisible; Q8IWT0; HS.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0072669; C:tRNA-splicing ligase complex; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IDA:UniProtKB.
DR Gene3D; 3.55.10.10; -; 1.
DR InterPro; IPR002804; Archease.
DR InterPro; IPR023572; Archease_dom.
DR InterPro; IPR036820; Archease_dom_sf.
DR PANTHER; PTHR12682; PTHR12682; 1.
DR Pfam; PF01951; Archease; 1.
DR SUPFAM; SSF69819; SSF69819; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Calcium; Metal-binding;
KW Reference proteome; tRNA processing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..167
FT /note="Protein archease"
FT /id="PRO_0000285950"
FT BINDING 39
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT VAR_SEQ 110..167
FT /note="EVKVLSIDQRNFKLRSIGWGEEFSLSKHPQGTEVKAITYSAMQVYNEENPEV
FT FVIIDI -> VGRRIFIVQAPSGNRSQSNNIFSNAGL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_024926"
FT MUTAGEN 39
FT /note="D->A: Abolishes ability to activate tRNA ligase
FT activity of RTCB."
FT /evidence="ECO:0000269|PubMed:24870230"
FT MUTAGEN 144
FT /note="K->A: Abolishes ability to activate tRNA ligase
FT activity of RTCB."
FT /evidence="ECO:0000269|PubMed:24870230"
FT CONFLICT 51
FT /note="E -> V (in Ref. 1; AAM34478)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="V -> A (in Ref. 1; AAM34478)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="L -> S (in Ref. 1; AAM34478)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="R -> G (in Ref. 1; AAM34478)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="H -> R (in Ref. 1; AAM34478)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 167 AA; 19491 MW; 26EC7F03CA7B42F1 CRC64;
MAQEEEDVRD YNLTEEQKAI KAKYPPVNRK YEYLDHTADV QLHAWGDTLE EAFEQCAMAM
FGYMTDTGTV EPLQTVEVET QGDDLQSLLF HFLDEWLYKF SADEFFIPRE VKVLSIDQRN
FKLRSIGWGE EFSLSKHPQG TEVKAITYSA MQVYNEENPE VFVIIDI
