ID   SELH_HUMAN              Reviewed;         122 AA.
AC   Q8IZQ5; Q8N672;
DT   04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   12-AUG-2020, entry version 137.
DE   RecName: Full=Selenoprotein H {ECO:0000305};
DE            Short=SelH;
GN   Name=SELENOH {ECO:0000303|PubMed:27645994, ECO:0000312|HGNC:HGNC:18251};
GN   Synonyms=C11orf31 {ECO:0000312|HGNC:HGNC:18251}, SELH;
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].
RX   PubMed=12775843; DOI=10.1126/science.1083516;
RA   Kryukov G.V., Castellano S., Novoselov S.V., Lobanov A.V., Zehtab O.,
RA   Guigo R., Gladyshev V.N.;
RT   "Characterization of mammalian selenoproteomes.";
RL   Science 300:1439-1443(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=B-cell;
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   [3]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-20, 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   [4]
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [6]
RP   NOMENCLATURE.
RX   PubMed=27645994; DOI=10.1074/jbc.m116.756155;
RA   Gladyshev V.N., Arner E.S., Berry M.J., Brigelius-Flohe R., Bruford E.A.,
RA   Burk R.F., Carlson B.A., Castellano S., Chavatte L., Conrad M.,
RA   Copeland P.R., Diamond A.M., Driscoll D.M., Ferreiro A., Flohe L.,
RA   Green F.R., Guigo R., Handy D.E., Hatfield D.L., Hesketh J., Hoffmann P.R.,
RA   Holmgren A., Hondal R.J., Howard M.T., Huang K., Kim H.Y., Kim I.Y.,
RA   Koehrle J., Krol A., Kryukov G.V., Lee B.J., Lee B.C., Lei X.G., Liu Q.,
RA   Lescure A., Lobanov A.V., Loscalzo J., Maiorino M., Mariotti M.,
RA   Sandeep Prabhu K., Rayman M.P., Rozovsky S., Salinas G., Schmidt E.E.,
RA   Schomburg L., Schweizer U., Simonovic M., Sunde R.A., Tsuji P.A.,
RA   Tweedie S., Ursini F., Whanger P.D., Zhang Y.;
RT   "Selenoprotein gene nomenclature.";
RL   J. Biol. Chem. 291:24036-24040(2016).
CC   -!- FUNCTION: May be involved in a redox-related process. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the SelWTH family. {ECO:0000305}.
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DR   EMBL; AF536829; AAN61472.1; -; mRNA.
DR   EMBL; BC021122; AAH21122.2; -; mRNA.
DR   CCDS; CCDS44602.1; -.
DR   RefSeq; NP_001308264.1; NM_001321335.1.
DR   RefSeq; NP_734467.1; NM_170746.3.
DR   BioGRID; 129373; 6.
DR   IntAct; Q8IZQ5; 8.
DR   STRING; 9606.ENSP00000373509; -.
DR   iPTMnet; Q8IZQ5; -.
DR   PhosphoSitePlus; Q8IZQ5; -.
DR   SwissPalm; Q8IZQ5; -.
DR   BioMuta; SELENOH; -.
DR   DMDM; 190352213; -.
DR   EPD; Q8IZQ5; -.
DR   jPOST; Q8IZQ5; -.
DR   MassIVE; Q8IZQ5; -.
DR   MaxQB; Q8IZQ5; -.
DR   PaxDb; Q8IZQ5; -.
DR   PeptideAtlas; Q8IZQ5; -.
DR   PRIDE; Q8IZQ5; -.
DR   ProteomicsDB; 71406; -.
DR   Antibodypedia; 62795; 12 antibodies.
DR   DNASU; 280636; -.
DR   Ensembl; ENST00000388857; ENSP00000373509; ENSG00000211450.
DR   Ensembl; ENST00000534355; ENSP00000434511; ENSG00000211450.
DR   GeneID; 280636; -.
DR   KEGG; hsa:280636; -.
DR   UCSC; uc021qjj.2; human.
DR   CTD; 280636; -.
DR   DisGeNET; 280636; -.
DR   EuPathDB; HostDB:ENSG00000211450.9; -.
DR   GeneCards; SELENOH; -.
DR   HGNC; HGNC:18251; SELENOH.
DR   HPA; ENSG00000211450; Low tissue specificity.
DR   MIM; 607914; gene.
DR   neXtProt; NX_Q8IZQ5; -.
DR   OpenTargets; ENSG00000211450; -.
DR   PharmGKB; PA25495; -.
DR   eggNOG; ENOG502S3QJ; Eukaryota.
DR   GeneTree; ENSGT00940000163915; -.
DR   HOGENOM; CLU_164858_0_0_1; -.
DR   InParanoid; Q8IZQ5; -.
DR   OMA; VIEHRVY; -.
DR   OrthoDB; 1563553at2759; -.
DR   PhylomeDB; Q8IZQ5; -.
DR   TreeFam; TF343373; -.
DR   PathwayCommons; Q8IZQ5; -.
DR   BioGRID-ORCS; 280636; 10 hits in 871 CRISPR screens.
DR   ChiTaRS; SELENOH; human.
DR   GenomeRNAi; 280636; -.
DR   Pharos; Q8IZQ5; Tdark.
DR   PRO; PR:Q8IZQ5; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q8IZQ5; protein.
DR   Bgee; ENSG00000211450; Expressed in metanephros and 211 other tissues.
DR   ExpressionAtlas; Q8IZQ5; baseline and differential.
DR   Genevisible; Q8IZQ5; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR   Gene3D; 3.40.30.10; -; 1.
DR   InterPro; IPR011893; Selenoprotein_Rdx-typ.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF10262; Rdx; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR02174; CXXU_selWTH; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Redox-active center; Reference proteome; Selenocysteine.
FT   CHAIN           1..122
FT                   /note="Selenoprotein H"
FT                   /id="PRO_0000097667"
FT   NON_STD         44
FT                   /note="Selenocysteine"
FT   MOD_RES         20
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000244|PubMed:19608861"
FT   CROSSLNK        41..44
FT                   /note="Cysteinyl-selenocysteine (Cys-Sec); redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   122 AA;  13453 MW;  B7EF30180573D4D5 CRC64;
     MAPRGRKRKA EAAVVAVAEK REKLANGGEG MEEATVVIEH CTSURVYGRN AAALSQALRL
     EAPELPVKVN PTKPRRGSFE VTLLRPDGSS AELWTGIKKG PPRKLKFPEP QEVVEELKKY
     LS
//