HEMGN_HUMAN
ID HEMGN_HUMAN Reviewed; 484 AA.
AC Q9BXL5; Q6XAR3; Q86XY5; Q9NPC0;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Hemogen;
DE AltName: Full=Erythroid differentiation-associated gene protein;
DE Short=EDAG-1;
DE AltName: Full=Hemopoietic gene protein;
DE AltName: Full=Negative differentiation regulator protein;
GN Name=HEMGN; Synonyms=EDAG, NDR; ORFNames=PRO1037, PRO1620;
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], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Bone marrow;
RX PubMed=11404085; DOI=10.1016/s0925-4773(01)00376-8;
RA Yang L.V., Nicholson R.H., Kaplan J., Galy A., Li L.;
RT "Hemogen is a novel nuclear factor specifically expressed in mouse
RT hematopoietic development and its human homologue EDAG maps to chromosome
RT 9q22, a region containing breakpoints of hematological neoplasms.";
RL Mech. Dev. 104:105-111(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=14648837; DOI=10.1002/dvdy.10399;
RA Yang L.V., Heng H.H., Wan J., Southwood C.M., Gow A., Li L.;
RT "Alternative promoters and polyadenylation regulate tissue-specific
RT expression of Hemogen isoforms during hematopoiesis and spermatogenesis.";
RL Dev. Dyn. 228:606-616(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=15332117; DOI=10.1038/sj.cdd.4401490;
RA Li C.Y., Zhan Y.Q., Xu C.W., Xu W.X., Wang S.Y., Lv J., Zhou Y., Yue P.B.,
RA Chen B., Yang X.M.;
RT "EDAG regulates the proliferation and differentiation of hematopoietic
RT cells and resists cell apoptosis through the activation of nuclear factor-
RT kappa B.";
RL Cell Death Differ. 11:1299-1308(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=14730214; DOI=10.1159/000075293;
RA Liu C.C., Chou Y.L., Ch'ang L.Y.;
RT "Down-regulation of human NDR gene in megakaryocytic differentiation of
RT erythroleukemia K562 cells.";
RL J. Biomed. Sci. 11:104-116(2004).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-484.
RC TISSUE=Fetal liver;
RA Zhang C., Yu Y., Zhang S., Wei H., Bi J., Zhou G., Dong C., Zai Y., Xu W.,
RA Gao F., Liu M., He F.;
RT "Functional prediction of the coding sequences of 75 new genes deduced by
RT analysis of cDNA clones from human fetal liver.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 115-484.
RC TISSUE=Fetal liver;
RA Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Ouyang S., Luo L., Bi J.,
RA Liu M., He F.;
RT "Functional prediction of the coding sequences of 121 new genes deduced by
RT analysis of cDNA clones from human fetal liver.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15920494; DOI=10.1038/sj.leu.2403808;
RA An L.-L., Li G., Wu K.-F., Ma X.-T., Zheng G.-G., Qiu L.-G., Song Y.-H.;
RT "High expression of EDAG and its significance in AML.";
RL Leukemia 19:1499-1502(2005).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123; SER-181; SER-188;
RP SER-201; SER-349; SER-353; THR-360 AND SER-363, 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 [12]
RP TISSUE SPECIFICITY.
RX PubMed=23436708; DOI=10.1002/pmic.201200489;
RA Liu M., Hu Z., Qi L., Wang J., Zhou T., Guo Y., Zeng Y., Zheng B., Wu Y.,
RA Zhang P., Chen X., Tu W., Zhang T., Zhou Q., Jiang M., Guo X., Zhou Z.,
RA Sha J.;
RT "Scanning of novel cancer/testis proteins by human testis proteomic
RT analysis.";
RL Proteomics 13:1200-1210(2013).
CC -!- FUNCTION: Regulates the proliferation and differentiation of
CC hematopoietic cells. Overexpression block the TPA-induced
CC megakaryocytic differentiation in the K562 cell model. May also prevent
CC cell apoptosis through the activation of the nuclear factor-kappa B
CC (NF-kB). {ECO:0000269|PubMed:14730214, ECO:0000269|PubMed:15332117,
CC ECO:0000269|PubMed:15920494}.
CC -!- INTERACTION:
CC Q9BXL5; Q13363: CTBP1; NbExp=2; IntAct=EBI-3916399, EBI-908846;
CC Q9BXL5; P06748: NPM1; NbExp=7; IntAct=EBI-3916399, EBI-78579;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14730214}.
CC -!- TISSUE SPECIFICITY: Expressed in hematopoietic precursor cells, thyroid
CC and spermatids (at protein level). Expressed in bone marrow, testis,
CC thymus. Expressed in prostate cancer and ovarian cancer. Also expressed
CC in thymus and thyroid tumors, non-Hodgkin lymphoma, various leukemia
CC cell lines, peripheral blood mononuclear cells (PBMCs) and bone marrow
CC mononuclear cells (BMMCs) of patients with leukemia.
CC {ECO:0000269|PubMed:11404085, ECO:0000269|PubMed:14648837,
CC ECO:0000269|PubMed:14730214, ECO:0000269|PubMed:15332117,
CC ECO:0000269|PubMed:15920494, ECO:0000269|PubMed:23436708}.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal liver, kidney and brain.
CC {ECO:0000269|PubMed:11404085, ECO:0000269|PubMed:14730214}.
CC -!- INDUCTION: Down-regulated during megakaryocytic differentiation of K562
CC cells by 12-O-tetradecanoylphorbol-13-acetate (TPA) (at protein level).
CC Up-regulated in normal PBMCs by mitogens. {ECO:0000269|PubMed:14730214,
CC ECO:0000269|PubMed:15332117}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF67133.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAF71041.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAG35488.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF322875; AAK26295.1; -; mRNA.
DR EMBL; AY244805; AAP75762.1; -; mRNA.
DR EMBL; AY255672; AAP81221.1; -; mRNA.
DR EMBL; AF228713; AAF67133.1; ALT_INIT; mRNA.
DR EMBL; AL499604; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC048324; AAH48324.1; -; mRNA.
DR EMBL; AF130060; AAG35488.1; ALT_INIT; mRNA.
DR EMBL; AF116617; AAF71041.1; ALT_INIT; mRNA.
DR CCDS; CCDS6731.1; -.
DR RefSeq; NP_060907.2; NM_018437.4.
DR RefSeq; NP_932095.1; NM_197978.2.
DR RefSeq; XP_005252143.1; XM_005252086.1.
DR RefSeq; XP_011517147.1; XM_011518845.2.
DR RefSeq; XP_011517148.1; XM_011518846.2.
DR AlphaFoldDB; Q9BXL5; -.
DR BioGRID; 120641; 41.
DR IntAct; Q9BXL5; 32.
DR MINT; Q9BXL5; -.
DR STRING; 9606.ENSP00000480020; -.
DR iPTMnet; Q9BXL5; -.
DR PhosphoSitePlus; Q9BXL5; -.
DR BioMuta; HEMGN; -.
DR DMDM; 74752432; -.
DR MassIVE; Q9BXL5; -.
DR MaxQB; Q9BXL5; -.
DR PaxDb; Q9BXL5; -.
DR PeptideAtlas; Q9BXL5; -.
DR PRIDE; Q9BXL5; -.
DR ProteomicsDB; 79448; -.
DR Antibodypedia; 14425; 206 antibodies from 24 providers.
DR DNASU; 55363; -.
DR Ensembl; ENST00000259456.7; ENSP00000259456.2; ENSG00000136929.13.
DR Ensembl; ENST00000616898.2; ENSP00000480020.1; ENSG00000136929.13.
DR GeneID; 55363; -.
DR KEGG; hsa:55363; -.
DR MANE-Select; ENST00000616898.2; ENSP00000480020.1; NM_197978.3; NP_932095.1.
DR UCSC; uc004axy.4; human.
DR CTD; 55363; -.
DR DisGeNET; 55363; -.
DR GeneCards; HEMGN; -.
DR HGNC; HGNC:17509; HEMGN.
DR HPA; ENSG00000136929; Tissue enriched (bone).
DR MIM; 610715; gene.
DR neXtProt; NX_Q9BXL5; -.
DR OpenTargets; ENSG00000136929; -.
DR PharmGKB; PA38458; -.
DR VEuPathDB; HostDB:ENSG00000136929; -.
DR eggNOG; ENOG502SBFR; Eukaryota.
DR GeneTree; ENSGT00390000004522; -.
DR HOGENOM; CLU_569802_0_0_1; -.
DR InParanoid; Q9BXL5; -.
DR OMA; EIHQETP; -.
DR OrthoDB; 801077at2759; -.
DR PhylomeDB; Q9BXL5; -.
DR TreeFam; TF338654; -.
DR PathwayCommons; Q9BXL5; -.
DR SignaLink; Q9BXL5; -.
DR BioGRID-ORCS; 55363; 19 hits in 1072 CRISPR screens.
DR ChiTaRS; HEMGN; human.
DR GeneWiki; HEMGN; -.
DR GenomeRNAi; 55363; -.
DR Pharos; Q9BXL5; Tbio.
DR PRO; PR:Q9BXL5; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9BXL5; protein.
DR Bgee; ENSG00000136929; Expressed in trabecular bone tissue and 94 other tissues.
DR ExpressionAtlas; Q9BXL5; baseline and differential.
DR Genevisible; Q9BXL5; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0045667; P:regulation of osteoblast differentiation; IBA:GO_Central.
DR InterPro; IPR033272; Hemogen.
DR PANTHER; PTHR15993; PTHR15993; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Differentiation; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..484
FT /note="Hemogen"
FT /id="PRO_0000245361"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 7..87
FT /note="Necessary for nuclear localization"
FT REGION 44..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERZ0"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 246
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERZ0"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 360
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AZ54"
FT CONFLICT 78
FT /note="R -> K (in Ref. 2; AAP75762 and 3; AAF67133)"
FT /evidence="ECO:0000305"
FT CONFLICT 96..97
FT /note="IV -> M (in Ref. 6; AAH48324)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 484 AA; 55341 MW; E1464D1C7BEA1F07 CRC64;
MDLGKDQSHL KHHQTPDPHQ EENHSPEVIG TWSLRNRELL RKRKAEVHEK ETSQWLFGEQ
KKRKQQRTGK GNRRGRKRQQ NTELKVEPQP QIEKEIVEKA LAPIEKKTEP PGSITKVFPS
VASPQKVVPE EHFSEICQES NIYQENFSEY QEIAVQNHSS ETCQHVSEPE DLSPKMYQEI
SVLQDNSSKI CQDMKEPEDN SPNTCQVISV IQDHPFKMYQ DMAKREDLAP KMCQEAAVPK
ILPCPTSEDT ADLAGCSLQA YPKPDVPKGY ILDTDQNPAE PEEYNETDQG IAETEGLFPK
IQEIAEPKDL STKTHQESAE PKYLPHKTCN EIIVPKAPSH KTIQETPHSE DYSIEINQET
PGSEKYSPET YQEIPGLEEY SPEIYQETSQ LEEYSPEIYQ ETPGPEDLST ETYKNKDVPK
ECFPEPHQET GGPQGQDPKA HQEDAKDAYT FPQEMKEKPK EEPGIPAILN ESHPENDVYS
YVLF
