ID   ANKZ1_HUMAN             Reviewed;         726 AA.
AC   Q9H8Y5; Q9NVZ4;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 184.
DE   RecName: Full=tRNA endonuclease ANKZF1 {ECO:0000305};
DE            EC=3.1.-.- {ECO:0000269|PubMed:30244831, ECO:0000269|PubMed:31011209};
DE   AltName: Full=Ankyrin repeat and zinc finger domain-containing protein 1 {ECO:0000305};
DE   AltName: Full=Zinc finger protein 744 {ECO:0000305};
GN   Name=ANKZF1 {ECO:0000303|PubMed:21896481,
GN   ECO:0000312|HGNC:HGNC:25527};
GN   Synonyms=ZNF744 {ECO:0000303|PubMed:21896481};
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].
RA   Zhao Y., Li Y., Yuan W., Wu X., Liu M.;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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].
RC   TISSUE=Colon, and Eye;
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 BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein phosphorylation
RT   analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT   phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258; SER-398; SER-533 AND
RP   THR-607, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [10]
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   [11]
RP   INTERACTION WITH VCP, VIM MOTI, AND MUTAGENESIS OF 661-ARG-ARG-662.
RX   PubMed=21896481; DOI=10.1074/jbc.m111.274472;
RA   Stapf C., Cartwright E., Bycroft M., Hofmann K., Buchberger A.;
RT   "The general definition of the p97/valosin-containing protein (VCP)-
RT   interacting motif (VIM) delineates a new family of p97 cofactors.";
RL   J. Biol. Chem. 286:38670-38678(2011).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361; SER-533; THR-607;
RP   SER-675 AND SER-680, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [14]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH VPC, VARIANTS
RP   32-VAL--GLN-87 DEL; LYS-152; GLN-585 AND PRO-638, AND CHARACTERIZATION OF
RP   VARIANTS LYS-152 AND GLN-585.
RX   PubMed=28302725; DOI=10.1074/jbc.m116.772038;
RA   van Haaften-Visser D.Y., Harakalova M., Mocholi E., van Montfrans J.M.,
RA   Elkadri A., Rieter E., Fiedler K., van Hasselt P.M., Triffaux E.M.M.,
RA   van Haelst M.M., Nijman I.J., Kloosterman W.P., Nieuwenhuis E.E.S.,
RA   Muise A.M., Cuppen E., Houwen R.H.J., Coffer P.J.;
RT   "Ankyrin repeat and zinc-finger domain-containing 1 mutations are
RT   associated with infantile-onset inflammatory bowel disease.";
RL   J. Biol. Chem. 292:7904-7920(2017).
RN   [15]
RP   FUNCTION, ACTIVE SITE, AND MUTAGENESIS OF GLN-246.
RX   PubMed=30244831; DOI=10.1016/j.molcel.2018.08.022;
RA   Kuroha K., Zinoviev A., Hellen C.U.T., Pestova T.V.;
RT   "Release of ubiquitinated and non-ubiquitinated nascent chains from stalled
RT   mammalian ribosomal complexes by ANKZF1 and Ptrh1.";
RL   Mol. Cell 72:286-302(2018).
RN   [16]
RP   FUNCTION, ACTIVE SITE, AND MUTAGENESIS OF GLN-246.
RX   PubMed=29632312; DOI=10.1038/s41586-018-0022-5;
RA   Verma R., Reichermeier K.M., Burroughs A.M., Oania R.S., Reitsma J.M.,
RA   Aravind L., Deshaies R.J.;
RT   "Vms1 and ANKZF1 peptidyl-tRNA hydrolases release nascent chains from
RT   stalled ribosomes.";
RL   Nature 557:446-451(2018).
RN   [17]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=31011209; DOI=10.1038/s41594-019-0211-4;
RA   Yip M.C.J., Keszei A.F.A., Feng Q., Chu V., McKenna M.J., Shao S.;
RT   "Mechanism for recycling tRNAs on stalled ribosomes.";
RL   Nat. Struct. Mol. Biol. 26:343-349(2019).
RN   [18]
RP   FUNCTION.
RX   PubMed=32075755; DOI=10.1016/j.celrep.2020.01.082;
RA   Yip M.C.J., Savickas S., Gygi S.P., Shao S.;
RT   "ELAC1 repairs tRNAs cleaved during ribosome-associated quality control.";
RL   Cell Rep. 30:2106-2114(2020).
CC   -!- FUNCTION: Endonuclease that cleaves polypeptidyl-tRNAs downstream of
CC       the ribosome-associated quality control (RQC) pathway to release
CC       incompletely synthesized polypeptides for degradation (PubMed:30244831,
CC       PubMed:29632312, PubMed:31011209). The RQC pathway disassembles
CC       aberrantly stalled translation complexes to recycle or degrade the
CC       constituent parts (PubMed:30244831, PubMed:29632312, PubMed:31011209).
CC       ANKZF1 acts downstream disassembly of stalled ribosomes and
CC       specifically cleaves off the terminal 3'-CCA nucleotides universal to
CC       all tRNAs from polypeptidyl-tRNAs, releasing (1) ubiquitinated
CC       polypeptides from 60S ribosomal subunit for degradation and (2) cleaved
CC       tRNAs (PubMed:31011209). ANKZF1-cleaved tRNAs are then repaired and
CC       recycled by ELAC1 and TRNT1 (PubMed:31011209, PubMed:32075755). Also
CC       plays a role in the cellular response to hydrogen peroxide and in the
CC       maintenance of mitochondrial integrity under conditions of cellular
CC       stress (PubMed:28302725). {ECO:0000269|PubMed:28302725,
CC       ECO:0000269|PubMed:29632312, ECO:0000269|PubMed:30244831,
CC       ECO:0000269|PubMed:31011209, ECO:0000269|PubMed:32075755}.
CC   -!- SUBUNIT: Interacts (via VIM motif) with VCP.
CC       {ECO:0000269|PubMed:21896481, ECO:0000269|PubMed:28302725}.
CC   -!- INTERACTION:
CC       Q9H8Y5; Q9Q2G4: ORF; Xeno; NbExp=2; IntAct=EBI-724848, EBI-6248094;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28302725}.
CC       Note=Translocates to the mitochondria upon exposure to hydrogen
CC       peroxide. {ECO:0000269|PubMed:28302725}.
CC   -!- DOMAIN: The VLRF1 domain mediates binding to the 60S ribosomal subunit.
CC       {ECO:0000250|UniProtKB:Q04311}.
CC   -!- SIMILARITY: Belongs to the ANKZF1/VMS1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABD65410.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAA91596.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; DQ412564; ABD65410.1; ALT_FRAME; mRNA.
DR   EMBL; AK001277; BAA91596.1; ALT_FRAME; mRNA.
DR   EMBL; AK023206; BAB14462.1; -; mRNA.
DR   EMBL; BC000238; AAH00238.1; -; mRNA.
DR   EMBL; BC008948; AAH08948.1; -; mRNA.
DR   CCDS; CCDS42821.1; -.
DR   RefSeq; NP_001035869.1; NM_001042410.1.
DR   RefSeq; NP_060559.2; NM_018089.2.
DR   AlphaFoldDB; Q9H8Y5; -.
DR   SMR; Q9H8Y5; -.
DR   BioGRID; 120443; 44.
DR   IntAct; Q9H8Y5; 12.
DR   MINT; Q9H8Y5; -.
DR   STRING; 9606.ENSP00000321617; -.
DR   GlyGen; Q9H8Y5; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9H8Y5; -.
DR   MetOSite; Q9H8Y5; -.
DR   PhosphoSitePlus; Q9H8Y5; -.
DR   SwissPalm; Q9H8Y5; -.
DR   BioMuta; ANKZF1; -.
DR   DMDM; 74761542; -.
DR   EPD; Q9H8Y5; -.
DR   jPOST; Q9H8Y5; -.
DR   MassIVE; Q9H8Y5; -.
DR   MaxQB; Q9H8Y5; -.
DR   PaxDb; 9606-ENSP00000321617; -.
DR   PeptideAtlas; Q9H8Y5; -.
DR   ProteomicsDB; 81256; -.
DR   Pumba; Q9H8Y5; -.
DR   ABCD; Q9H8Y5; 5 sequenced antibodies.
DR   Antibodypedia; 34312; 162 antibodies from 26 providers.
DR   DNASU; 55139; -.
DR   Ensembl; ENST00000323348.10; ENSP00000321617.5; ENSG00000163516.14.
DR   Ensembl; ENST00000410034.7; ENSP00000386337.3; ENSG00000163516.14.
DR   GeneID; 55139; -.
DR   KEGG; hsa:55139; -.
DR   MANE-Select; ENST00000323348.10; ENSP00000321617.5; NM_018089.3; NP_060559.2.
DR   UCSC; uc002vkg.3; human.
DR   AGR; HGNC:25527; -.
DR   CTD; 55139; -.
DR   DisGeNET; 55139; -.
DR   GeneCards; ANKZF1; -.
DR   HGNC; HGNC:25527; ANKZF1.
DR   HPA; ENSG00000163516; Low tissue specificity.
DR   MIM; 617541; gene.
DR   neXtProt; NX_Q9H8Y5; -.
DR   OpenTargets; ENSG00000163516; -.
DR   PharmGKB; PA143485305; -.
DR   VEuPathDB; HostDB:ENSG00000163516; -.
DR   eggNOG; KOG2505; Eukaryota.
DR   GeneTree; ENSGT00390000005911; -.
DR   InParanoid; Q9H8Y5; -.
DR   OMA; GPHIFMC; -.
DR   OrthoDB; 8371at2759; -.
DR   PhylomeDB; Q9H8Y5; -.
DR   TreeFam; TF313431; -.
DR   BRENDA; 3.1.1.29; 2681.
DR   PathwayCommons; Q9H8Y5; -.
DR   SignaLink; Q9H8Y5; -.
DR   BioGRID-ORCS; 55139; 13 hits in 1160 CRISPR screens.
DR   ChiTaRS; ANKZF1; human.
DR   GeneWiki; ANKZF1; -.
DR   GenomeRNAi; 55139; -.
DR   Pharos; Q9H8Y5; Tbio.
DR   PRO; PR:Q9H8Y5; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q9H8Y5; Protein.
DR   Bgee; ENSG00000163516; Expressed in right uterine tube and 136 other cell types or tissues.
DR   ExpressionAtlas; Q9H8Y5; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0140101; F:catalytic activity, acting on a tRNA; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004521; F:RNA endonuclease activity; IDA:UniProtKB.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; IMP:UniProtKB.
DR   GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IDA:UniProtKB.
DR   GO; GO:0072344; P:rescue of stalled ribosome; IDA:UniProtKB.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR047139; ANKZ1/VMS1.
DR   InterPro; IPR041540; VATC.
DR   InterPro; IPR041175; VLRF1/Vms1.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR16036; ANKYRIN REPEAT AND ZINC FINGER DOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR16036:SF2; ANKYRIN REPEAT AND ZINC FINGER DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF18826; bVLRF1; 1.
DR   Pfam; PF18716; VATC; 1.
DR   SMART; SM00248; ANK; 2.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   Genevisible; Q9H8Y5; HS.
PE   1: Evidence at protein level;
KW   ANK repeat; Coiled coil; Cytoplasm; Endonuclease; Hydrolase; Metal-binding;
KW   Nuclease; Phosphoprotein; Reference proteome; Repeat; Zinc; Zinc-finger.
FT   CHAIN           1..726
FT                   /note="tRNA endonuclease ANKZF1"
FT                   /id="PRO_0000247278"
FT   DOMAIN          208..350
FT                   /note="VLRF1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          493..526
FT                   /note="ANK 1"
FT   REPEAT          534..563
FT                   /note="ANK 2"
FT   ZN_FING         72..96
FT                   /note="C2H2-type"
FT   REGION          40..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          120..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          387..409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          436..474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          588..656
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          654..666
FT                   /note="VCP/p97-interacting motif (VIM)"
FT                   /evidence="ECO:0000269|PubMed:21896481"
FT   COILED          609..659
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        454..474
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        612..656
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        246
FT                   /evidence="ECO:0000305|PubMed:29632312,
FT                   ECO:0000305|PubMed:30244831"
FT   MOD_RES         258
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         361
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         398
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692"
FT   MOD_RES         533
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         607
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         675
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         680
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VARIANT         32..87
FT                   /note="Missing (found in a patient with infantile-onset
FT                   inflammatory bowel disease; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:28302725"
FT                   /id="VAR_079136"
FT   VARIANT         152
FT                   /note="E -> K (found in a patient with infantile-onset
FT                   inflammatory bowel disease; uncertain significance;
FT                   decreased function in cellular response to hydrogen
FT                   peroxide; does not affect protein abundance; does not
FT                   affect interaction with VCP; dbSNP:rs149382949)"
FT                   /evidence="ECO:0000269|PubMed:28302725"
FT                   /id="VAR_079137"
FT   VARIANT         569
FT                   /note="R -> W (in dbSNP:rs2293076)"
FT                   /id="VAR_048269"
FT   VARIANT         585
FT                   /note="R -> Q (found in a patient with infantile-onset
FT                   inflammatory bowel disease; uncertain significance;
FT                   decreased function in cellular response to hydrogen
FT                   peroxide; decreased protein abundance; does not affect
FT                   interaction with VCP; dbSNP:rs189875478)"
FT                   /evidence="ECO:0000269|PubMed:28302725"
FT                   /id="VAR_079138"
FT   VARIANT         638
FT                   /note="Q -> P"
FT                   /evidence="ECO:0000269|PubMed:28302725"
FT                   /id="VAR_079139"
FT   VARIANT         676
FT                   /note="P -> L (in dbSNP:rs2293079)"
FT                   /id="VAR_048270"
FT   MUTAGEN         246
FT                   /note="Q->L: Abolished ability to cleave
FT                   polypeptidyl-tRNAs."
FT                   /evidence="ECO:0000269|PubMed:29632312,
FT                   ECO:0000269|PubMed:30244831"
FT   MUTAGEN         661..662
FT                   /note="AA->LL: Abolishes interaction with VCP."
FT                   /evidence="ECO:0000269|PubMed:21896481"
SQ   SEQUENCE   726 AA;  80927 MW;  44F7930A530F1355 CRC64;
     MSPAPDAAPA PASISLFDLS ADAPVFQGLS LVSHAPGEAL ARAPRTSCSG SGERESPERK
     LLQGPMDISE KLFCSTCDQT FQNHQEQREH YKLDWHRFNL KQRLKDKPLL SALDFEKQSS
     TGDLSSISGS EDSDSASEED LQTLDRERAT FEKLSRPPGF YPHRVLFQNA QGQFLYAYRC
     VLGPHQDPPE EAELLLQNLQ SRGPRDCVVL MAAAGHFAGA IFQGREVVTH KTFHRYTVRA
     KRGTAQGLRD ARGGPSHSAG ANLRRYNEAT LYKDVRDLLA GPSWAKALEE AGTILLRAPR
     SGRSLFFGGK GAPLQRGDPR LWDIPLATRR PTFQELQRVL HKLTTLHVYE EDPREAVRLH
     SPQTHWKTVR EERKKPTEEE IRKICRDEKE ALGQNEESPK QGSGSEGEDG FQVELELVEL
     TVGTLDLCES EVLPKRRRRK RNKKEKSRDQ EAGAHRTLLQ QTQEEEPSTQ SSQAVAAPLG
     PLLDEAKAPG QPELWNALLA ACRAGDVGVL KLQLAPSPAD PRVLSLLSAP LGSGGFTLLH
     AAAAAGRGSV VRLLLEAGAD PTVQDSRARP PYTVAADKST RNEFRRFMEK NPDAYDYNKA
     QVPGPLTPEM EARQATRKRE QKAARRQREE QQQRQQEQEE REREEQRRFA ALSDREKRAL
     AAERRLAAQL GAPTSPIPDS AIVNTRRCWS CGASLQGLTP FHYLDFSFCS TRCLQDHRRQ
     AGRPSS
//