ID   THOC7_HUMAN             Reviewed;         204 AA.
AC   Q6I9Y2; Q6P1L3; Q8WUF2; Q9H5H0;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 3.
DT   27-MAR-2024, entry version 140.
DE   RecName: Full=THO complex subunit 7 homolog;
DE   AltName: Full=Functional spliceosome-associated protein 24;
DE            Short=fSAP24;
DE   AltName: Full=Ngg1-interacting factor 3-like protein 1-binding protein 1;
DE            Short=NIF3L1-binding protein 1;
DE   AltName: Full=hTREX30;
GN   Name=THOC7; Synonyms=NIF3L1BP1;
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].
RC   TISSUE=Small intestine;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA   Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA   Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA   Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA   Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA   Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA   Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA   Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA   Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA   Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA   Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA   Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA   Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA   Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA   Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Skin, and Testis;
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   [6]
RP   INTERACTION WITH NIF3L1, REGION, AND SUBCELLULAR LOCATION.
RX   PubMed=12951069; DOI=10.1016/j.bbrc.2003.07.008;
RA   Tascou S., Kang T.W., Trappe R., Engel W., Burfeind P.;
RT   "Identification and characterization of NIF3L1 BP1, a novel cytoplasmic
RT   interaction partner of the NIF3L1 protein.";
RL   Biochem. Biophys. Res. Commun. 309:440-448(2003).
RN   [7]
RP   IDENTIFICATION IN THE TREX COMPLEX, FUNCTION OF THE TREX COMPLEX, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=15833825; DOI=10.1158/0008-5472.can-04-3624;
RA   Guo S., Hakimi M.A., Baillat D., Chen X., Farber M.J., Klein-Szanto A.J.,
RA   Cooch N.S., Godwin A.K., Shiekhattar R.;
RT   "Linking transcriptional elongation and messenger RNA export to metastatic
RT   breast cancers.";
RL   Cancer Res. 65:3011-3016(2005).
RN   [8]
RP   IDENTIFICATION IN THE THO AND TREX COMPLEX, FUNCTION OF THE TREX COMPLEX,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=15998806; DOI=10.1101/gad.1302205;
RA   Masuda S., Das R., Cheng H., Hurt E., Dorman N., Reed R.;
RT   "Recruitment of the human TREX complex to mRNA during splicing.";
RL   Genes Dev. 19:1512-1517(2005).
RN   [9]
RP   FUNCTION OF THE TREX COMPLEX.
RX   PubMed=17190602; DOI=10.1016/j.cell.2006.10.044;
RA   Cheng H., Dufu K., Lee C.-S., Hsu J.L., Dias A., Reed R.;
RT   "Human mRNA export machinery recruited to the 5' end of mRNA.";
RL   Cell 127:1389-1400(2006).
RN   [10]
RP   FUNCTION OF THE TREX COMPLEX.
RX   PubMed=18974867; DOI=10.1371/journal.ppat.1000194;
RA   Boyne J.R., Colgan K.J., Whitehouse A.;
RT   "Recruitment of the complete hTREX complex is required for Kaposi's
RT   sarcoma-associated herpesvirus intronless mRNA nuclear export and virus
RT   replication.";
RL   PLoS Pathog. 4:E1000194-E1000194(2008).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-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   [12]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH THOC5.
RX   PubMed=19059247; DOI=10.1016/j.febslet.2008.11.024;
RA   El Bounkari O., Guria A., Klebba-Faerber S., Claussen M., Pieler T.,
RA   Griffiths J.R., Whetton A.D., Koch A., Tamura T.;
RT   "Nuclear localization of the pre-mRNA associating protein THOC7 depends
RT   upon its direct interaction with Fms tyrosine kinase interacting protein
RT   (FMIP).";
RL   FEBS Lett. 583:13-18(2009).
RN   [13]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-36, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [14]
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   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-5, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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   [16]
RP   FUNCTION.
RX   PubMed=23222130; DOI=10.1093/nar/gks1188;
RA   Chi B., Wang Q., Wu G., Tan M., Wang L., Shi M., Chang X., Cheng H.;
RT   "Aly and THO are required for assembly of the human TREX complex and
RT   association of TREX components with the spliced mRNA.";
RL   Nucleic Acids Res. 41:1294-1306(2013).
RN   [17]
RP   ACETYLATION AT GLY-2, AND CLEAVAGE OF INITIATOR METHIONINE.
RX   PubMed=25489052; DOI=10.1093/hmg/ddu611;
RA   Myklebust L.M., Van Damme P., Stoeve S.I., Doerfel M.J., Abboud A.,
RA   Kalvik T.V., Grauffel C., Jonckheere V., Wu Y., Swensen J., Kaasa H.,
RA   Liszczak G., Marmorstein R., Reuter N., Lyon G.J., Gevaert K., Arnesen T.;
RT   "Biochemical and cellular analysis of Ogden syndrome reveals downstream Nt-
RT   acetylation defects.";
RL   Hum. Mol. Genet. 24:1956-1976(2015).
CC   -!- FUNCTION: Required for efficient export of polyadenylated RNA. Acts as
CC       component of the THO subcomplex of the TREX complex which is thought to
CC       couple mRNA transcription, processing and nuclear export, and which
CC       specifically associates with spliced mRNA and not with unspliced pre-
CC       mRNA. TREX is recruited to spliced mRNAs by a transcription-independent
CC       mechanism, binds to mRNA upstream of the exon-junction complex (EJC)
CC       and is recruited in a splicing- and cap-dependent manner to a region
CC       near the 5' end of the mRNA where it functions in mRNA export to the
CC       cytoplasm via the TAP/NFX1 pathway. {ECO:0000269|PubMed:15833825,
CC       ECO:0000269|PubMed:15998806, ECO:0000269|PubMed:17190602,
CC       ECO:0000269|PubMed:23222130}.
CC   -!- FUNCTION: The TREX complex is essential for the export of Kaposi's
CC       sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious
CC       virus production. {ECO:0000269|PubMed:18974867}.
CC   -!- SUBUNIT: Component of the THO complex, which is composed of THOC1,
CC       THOC2, THOC3, THOC5, THOC6 and THOC7; together with at least
CC       ALYREF/THOC4, DDX39B, SARNP/CIP29 and CHTOP, THO forms the
CC       transcription/export (TREX) complex which seems to have a dynamic
CC       structure involving ATP-dependent remodeling. Interacts with NIF3L1 and
CC       THOC5. {ECO:0000269|PubMed:12951069, ECO:0000269|PubMed:15833825,
CC       ECO:0000269|PubMed:15998806, ECO:0000269|PubMed:19059247}.
CC   -!- INTERACTION:
CC       Q6I9Y2; Q8IYE0: CCDC146; NbExp=3; IntAct=EBI-716286, EBI-10749669;
CC       Q6I9Y2; Q8NEH6: MNS1; NbExp=3; IntAct=EBI-716286, EBI-743811;
CC       Q6I9Y2; O14777: NDC80; NbExp=3; IntAct=EBI-716286, EBI-715849;
CC       Q6I9Y2; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-716286, EBI-358489;
CC       Q6I9Y2; Q13769: THOC5; NbExp=9; IntAct=EBI-716286, EBI-5280316;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12951069}. Nucleus
CC       {ECO:0000269|PubMed:12951069, ECO:0000269|PubMed:19059247}. Nucleus
CC       speckle {ECO:0000305}. Note=Interaction with THOC5 is required for
CC       nuclear localization. {ECO:0000269|PubMed:19059247}.
CC   -!- SIMILARITY: Belongs to the THOC7 family. {ECO:0000305}.
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DR   EMBL; AK027098; BAB15656.1; -; mRNA.
DR   EMBL; CR457373; CAG33654.1; -; mRNA.
DR   EMBL; AC104162; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471055; EAW65418.1; -; Genomic_DNA.
DR   EMBL; BC020599; AAH20599.2; -; mRNA.
DR   EMBL; BC065012; AAH65012.1; -; mRNA.
DR   CCDS; CCDS2900.1; -.
DR   RefSeq; NP_001272333.1; NM_001285404.1.
DR   RefSeq; NP_079351.2; NM_025075.3.
DR   PDB; 7APK; EM; 3.30 A; G/O/g/o=1-204.
DR   PDB; 7ZNK; EM; 3.90 A; G/O/g/o=1-204.
DR   PDB; 7ZNL; EM; 3.45 A; G/O/g/o=1-204.
DR   PDBsum; 7APK; -.
DR   PDBsum; 7ZNK; -.
DR   PDBsum; 7ZNL; -.
DR   AlphaFoldDB; Q6I9Y2; -.
DR   EMDB; EMD-11857; -.
DR   EMDB; EMD-14804; -.
DR   EMDB; EMD-14808; -.
DR   SMR; Q6I9Y2; -.
DR   BioGRID; 123138; 119.
DR   ComplexPortal; CPX-2488; TREX transcription-export complex, DX39B variant.
DR   ComplexPortal; CPX-7261; TREX transcription-export complex, DX39A variant.
DR   CORUM; Q6I9Y2; -.
DR   IntAct; Q6I9Y2; 54.
DR   MINT; Q6I9Y2; -.
DR   STRING; 9606.ENSP00000295899; -.
DR   TCDB; 3.A.22.1.2; the transcription-coupled trex/tap nuclear mrna export complex (trex) family.
DR   iPTMnet; Q6I9Y2; -.
DR   PhosphoSitePlus; Q6I9Y2; -.
DR   BioMuta; THOC7; -.
DR   DMDM; 229462996; -.
DR   EPD; Q6I9Y2; -.
DR   jPOST; Q6I9Y2; -.
DR   MassIVE; Q6I9Y2; -.
DR   MaxQB; Q6I9Y2; -.
DR   PaxDb; 9606-ENSP00000295899; -.
DR   PeptideAtlas; Q6I9Y2; -.
DR   ProteomicsDB; 66355; -.
DR   Pumba; Q6I9Y2; -.
DR   Antibodypedia; 46357; 144 antibodies from 23 providers.
DR   DNASU; 80145; -.
DR   Ensembl; ENST00000295899.10; ENSP00000295899.5; ENSG00000163634.12.
DR   GeneID; 80145; -.
DR   KEGG; hsa:80145; -.
DR   MANE-Select; ENST00000295899.10; ENSP00000295899.5; NM_025075.4; NP_079351.2.
DR   UCSC; uc003dlt.6; human.
DR   AGR; HGNC:29874; -.
DR   CTD; 80145; -.
DR   DisGeNET; 80145; -.
DR   GeneCards; THOC7; -.
DR   HGNC; HGNC:29874; THOC7.
DR   HPA; ENSG00000163634; Low tissue specificity.
DR   MIM; 611965; gene.
DR   neXtProt; NX_Q6I9Y2; -.
DR   OpenTargets; ENSG00000163634; -.
DR   PharmGKB; PA144596266; -.
DR   VEuPathDB; HostDB:ENSG00000163634; -.
DR   eggNOG; KOG3215; Eukaryota.
DR   GeneTree; ENSGT00390000002873; -.
DR   HOGENOM; CLU_087727_0_0_1; -.
DR   InParanoid; Q6I9Y2; -.
DR   OMA; WANSKND; -.
DR   OrthoDB; 3640791at2759; -.
DR   PhylomeDB; Q6I9Y2; -.
DR   TreeFam; TF319308; -.
DR   PathwayCommons; Q6I9Y2; -.
DR   Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR   Reactome; R-HSA-72187; mRNA 3'-end processing.
DR   Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination.
DR   SignaLink; Q6I9Y2; -.
DR   SIGNOR; Q6I9Y2; -.
DR   BioGRID-ORCS; 80145; 752 hits in 1165 CRISPR screens.
DR   ChiTaRS; THOC7; human.
DR   GenomeRNAi; 80145; -.
DR   Pharos; Q6I9Y2; Tbio.
DR   PRO; PR:Q6I9Y2; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q6I9Y2; Protein.
DR   Bgee; ENSG00000163634; Expressed in calcaneal tendon and 203 other cell types or tissues.
DR   ExpressionAtlas; Q6I9Y2; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0000347; C:THO complex; IDA:UniProtKB.
DR   GO; GO:0000445; C:THO complex part of transcription export complex; IDA:UniProtKB.
DR   GO; GO:0000346; C:transcription export complex; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006406; P:mRNA export from nucleus; IDA:UniProtKB.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR008501; THOC7/Mft1.
DR   PANTHER; PTHR23405; MAINTENANCE OF KILLER 16 MAK16 PROTEIN-RELATED; 1.
DR   PANTHER; PTHR23405:SF5; THO COMPLEX SUBUNIT 7 HOMOLOG; 1.
DR   Pfam; PF05615; THOC7; 1.
DR   Genevisible; Q6I9Y2; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Coiled coil; Cytoplasm; mRNA processing;
KW   mRNA splicing; mRNA transport; Nucleus; Phosphoprotein; Reference proteome;
KW   RNA-binding; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:25489052,
FT                   ECO:0007744|PubMed:19413330"
FT   CHAIN           2..204
FT                   /note="THO complex subunit 7 homolog"
FT                   /id="PRO_0000310754"
FT   REGION          50..137
FT                   /note="Interaction with THOC5"
FT                   /evidence="ECO:0000269|PubMed:19059247"
FT   REGION          105..204
FT                   /note="Interaction with NIF3L1"
FT                   /evidence="ECO:0000269|PubMed:12951069"
FT   REGION          182..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          75..194
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000269|PubMed:25489052,
FT                   ECO:0007744|PubMed:19413330"
FT   MOD_RES         5
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         36
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   CONFLICT        23
FT                   /note="D -> G (in Ref. 1; BAB15656)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        187
FT                   /note="L -> P (in Ref. 2; CAG33654)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        200
FT                   /note="T -> S (in Ref. 1; BAB15656 and 2; CAG33654)"
FT                   /evidence="ECO:0000305"
FT   HELIX           7..12
FT                   /evidence="ECO:0007829|PDB:7ZNL"
FT   HELIX           22..38
FT                   /evidence="ECO:0007829|PDB:7APK"
FT   HELIX           47..126
FT                   /evidence="ECO:0007829|PDB:7APK"
FT   HELIX           133..180
FT                   /evidence="ECO:0007829|PDB:7APK"
SQ   SEQUENCE   204 AA;  23743 MW;  CB0D2608A23E5BFC CRC64;
     MGAVTDDEVI RKRLLIDGDG AGDDRRINLL VKSFIKWCNS GSQEEGYSQY QRMLSTLSQC
     EFSMGKTLLV YDMNLREMEN YEKIYKEIEC SIAGAHEKIA ECKKQILQAK RIRKNRQEYD
     ALAKVIQHHP DRHETLKELE ALGKELEHLS HIKESVEDKL ELRRKQFHVL LSTIHELQQT
     LENDEKLSEV EEAQEASMET DPKP
//