Full text data of HDGF
HDGF
(HMG1L2)
[Confidence: low (only semi-automatic identification from reviews)]
Hepatoma-derived growth factor; HDGF (High mobility group protein 1-like 2; HMG-1L2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Hepatoma-derived growth factor; HDGF (High mobility group protein 1-like 2; HMG-1L2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P51858
ID HDGF_HUMAN Reviewed; 240 AA.
AC P51858; B3KU21; D3DVC9; Q5SZ07; Q5SZ08; Q5SZ09;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1996, sequence version 1.
DT 22-JAN-2014, entry version 128.
DE RecName: Full=Hepatoma-derived growth factor;
DE Short=HDGF;
DE AltName: Full=High mobility group protein 1-like 2;
DE Short=HMG-1L2;
GN Name=HDGF; Synonyms=HMG1L2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 4-24.
RC TISSUE=Hepatoma;
RX PubMed=7929202;
RA Nakamura H., Izumoto Y., Kambe H., Kuroda T., Mori T., Kawamura K.,
RA Yamamoto H., Kishimoto T.;
RT "Molecular cloning of complementary DNA for a novel human hepatoma-
RT derived growth factor. Its homology with high mobility group-1
RT protein.";
RL J. Biol. Chem. 269:25143-25149(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
RP LEU-201.
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP SUBCELLULAR LOCATION, AND NUCLEAR LOCALIZATION SIGNAL.
RX PubMed=11751870; DOI=10.1074/jbc.M111122200;
RA Kishima Y., Yamamoto H., Izumoto Y., Yoshida K., Enomoto H.,
RA Yamamoto M., Kuroda T., Ito H., Yoshizaki K., Nakamura H.;
RT "Hepatoma-derived growth factor stimulates cell growth after
RT translocation to the nucleus by nuclear localization signals.";
RL J. Biol. Chem. 277:10315-10322(2002).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=15302935; DOI=10.1073/pnas.0404720101;
RA Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,
RA Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
RT "Large-scale characterization of HeLa cell nuclear phosphoproteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-133 AND
RP SER-165, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165 AND THR-200, AND
RP MASS SPECTROMETRY.
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
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-133, AND
RP MASS SPECTROMETRY.
RC TISSUE=Pituitary;
RX PubMed=16807684; DOI=10.1007/s11102-006-8916-x;
RA Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
RT "Phosphoproteomic analysis of the human pituitary.";
RL Pituitary 9:109-120(2006).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND DNA-BINDING.
RX PubMed=17974029; DOI=10.1186/1471-2199-8-101;
RA Yang J., Everett A.D.;
RT "Hepatoma-derived growth factor binds DNA through the N-terminal PWWP
RT domain.";
RL BMC Mol. Biol. 8:101-101(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-133, AND
RP MASS SPECTROMETRY.
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate
RT cancer cells: identification of phosphoproteins in the LNCaP cell
RT line.";
RL Electrophoresis 28:2027-2034(2007).
RN [13]
RP SUMOYLATION AT LYS-80.
RX PubMed=18331345; DOI=10.1111/j.1742-4658.2008.06303.x;
RA Thakar K., Niedenthal R., Okaz E., Franken S., Jakobs A., Gupta S.,
RA Kelm S., Dietz F.;
RT "SUMOylation of the hepatoma-derived growth factor negatively
RT influences its binding to chromatin.";
RL FEBS J. 275:1411-1426(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-133 AND
RP SER-165, AND MASS SPECTROMETRY.
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using
RT sequential IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-133, AND
RP MASS SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-200; SER-206 AND
RP SER-239, AND MASS SPECTROMETRY.
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-133 AND
RP SER-165, AND MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [19]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND MASS
RP SPECTROMETRY.
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-133 AND
RP SER-165, AND MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-44, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133; SER-165; THR-200
RP AND SER-239, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [24]
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.,
RA Buerckstuemmer T., 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 [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [26]
RP STRUCTURE BY NMR OF 1-100, AND SUBUNIT.
RX PubMed=17270212; DOI=10.1016/j.jmb.2007.01.010;
RA Sue S.C., Lee W.T., Tien S.C., Lee S.C., Yu J.G., Wu W.J., Wu W.G.,
RA Huang T.-H.;
RT "PWWP module of human hepatoma-derived growth factor forms a domain-
RT swapped dimer with much higher affinity for heparin.";
RL J. Mol. Biol. 367:456-472(2007).
RN [27]
RP STRUCTURE BY NMR OF 1-100, AND HEPARIN-BINDING SITES.
RX PubMed=15491618; DOI=10.1016/j.jmb.2004.09.014;
RA Sue S.C., Chen J.Y., Lee S.C., Wu W.G., Huang T.-H.;
RT "Solution structure and heparin interaction of human hepatoma-derived
RT growth factor.";
RL J. Mol. Biol. 343:1365-1377(2004).
CC -!- FUNCTION: Heparin-binding protein, with mitogenic activity for
CC fibroblasts. Acts as a transcriptional repressor.
CC -!- SUBUNIT: Monomer, and domain-swapped homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P51858-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P51858-2; Sequence=VSP_045620;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=P51858-3; Sequence=VSP_047328;
CC Note=Gene prediction based on EST data;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The PWWP domain harbors the heparin-binding sites and is
CC responsible for DNA-binding, while the C-terminal region is
CC essentially unstructured.
CC -!- PTM: Sumoylated with SUMO1. Sumoylation prevents binding to
CC chromatin.
CC -!- SIMILARITY: Belongs to the HDGF family.
CC -!- SIMILARITY: Contains 1 PWWP domain.
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DR EMBL; D16431; BAA03903.1; -; mRNA.
DR EMBL; AK096411; BAG53283.1; -; mRNA.
DR EMBL; AL590666; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW52910.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52911.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52912.1; -; Genomic_DNA.
DR EMBL; BC018991; AAH18991.1; -; mRNA.
DR PIR; A55055; A55055.
DR RefSeq; NP_001119522.1; NM_001126050.1.
DR RefSeq; NP_001119523.1; NM_001126051.1.
DR RefSeq; NP_004485.1; NM_004494.2.
DR UniGene; Hs.743948; -.
DR PDB; 1RI0; NMR; -; A=1-100.
DR PDB; 2NLU; NMR; -; A/B=1-100.
DR PDBsum; 1RI0; -.
DR PDBsum; 2NLU; -.
DR ProteinModelPortal; P51858; -.
DR SMR; P51858; 1-100.
DR IntAct; P51858; 111.
DR MINT; MINT-5003673; -.
DR STRING; 9606.ENSP00000357189; -.
DR PhosphoSite; P51858; -.
DR DMDM; 1708157; -.
DR PaxDb; P51858; -.
DR PeptideAtlas; P51858; -.
DR PRIDE; P51858; -.
DR DNASU; 3068; -.
DR Ensembl; ENST00000357325; ENSP00000349878; ENSG00000143321.
DR Ensembl; ENST00000368206; ENSP00000357189; ENSG00000143321.
DR Ensembl; ENST00000368209; ENSP00000357192; ENSG00000143321.
DR Ensembl; ENST00000537739; ENSP00000443120; ENSG00000143321.
DR GeneID; 3068; -.
DR KEGG; hsa:3068; -.
DR UCSC; uc001fpy.4; human.
DR CTD; 3068; -.
DR GeneCards; GC01M156711; -.
DR HGNC; HGNC:4856; HDGF.
DR HPA; CAB026035; -.
DR MIM; 600339; gene.
DR neXtProt; NX_P51858; -.
DR PharmGKB; PA29234; -.
DR eggNOG; NOG240243; -.
DR HOGENOM; HOG000112874; -.
DR HOVERGEN; HBG010574; -.
DR KO; K16641; -.
DR OMA; EDSPKRL; -.
DR OrthoDB; EOG7NKKMQ; -.
DR PhylomeDB; P51858; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR ChiTaRS; HDGF; human.
DR EvolutionaryTrace; P51858; -.
DR GeneWiki; Hepatoma-derived_growth_factor; -.
DR GenomeRNAi; 3068; -.
DR NextBio; 12137; -.
DR PRO; PR:P51858; -.
DR ArrayExpress; P51858; -.
DR Bgee; P51858; -.
DR CleanEx; HS_HDGF; -.
DR Genevestigator; P51858; -.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0017053; C:transcriptional repressor complex; IDA:BHF-UCL.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008201; F:heparin binding; TAS:ProtInc.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0001106; F:RNA polymerase II transcription corepressor activity; IDA:BHF-UCL.
DR GO; GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; TAS:Reactome.
DR GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
DR GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
DR GO; GO:0034504; P:protein localization to nucleus; IEA:Ensembl.
DR InterPro; IPR000313; PWWP_dom.
DR Pfam; PF00855; PWWP; 1.
DR SMART; SM00293; PWWP; 1.
DR PROSITE; PS50812; PWWP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Direct protein sequencing; DNA-binding; Growth factor;
KW Heparin-binding; Isopeptide bond; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1 240 Hepatoma-derived growth factor.
FT /FTId=PRO_0000191700.
FT DOMAIN 12 69 PWWP.
FT MOTIF 75 80 Nuclear localization signal.
FT MOTIF 155 170 Bipartite nuclear localization signal.
FT COMPBIAS 110 230 Glu-rich.
FT BINDING 19 19 Heparin (Probable).
FT BINDING 21 21 Heparin (Probable).
FT BINDING 72 72 Heparin (Probable).
FT BINDING 75 75 Heparin (Probable).
FT BINDING 79 79 Heparin (Probable).
FT BINDING 80 80 Heparin (Probable).
FT MOD_RES 44 44 N6-acetyllysine.
FT MOD_RES 132 132 Phosphoserine.
FT MOD_RES 133 133 Phosphoserine.
FT MOD_RES 165 165 Phosphoserine.
FT MOD_RES 200 200 Phosphothreonine.
FT MOD_RES 206 206 Phosphoserine.
FT MOD_RES 239 239 Phosphoserine.
FT CROSSLNK 80 80 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in SUMO).
FT VAR_SEQ 1 29 MSRSNRQKEYKCGDLVFAKMKGYPHWPAR -> MEQRAGGN
FT RVQTSTLNCAGAAV (in isoform 2).
FT /FTId=VSP_045620.
FT VAR_SEQ 1 29 MSRSNRQKEYKCGDLVFAKMKGYPHWPAR -> MHPEGGQF
FT VPQLLGHLLATKLKRFLLSKGGRRAQIPDVSRATPHT (in
FT isoform 3).
FT /FTId=VSP_047328.
FT VARIANT 201 201 P -> L (in dbSNP:rs4399146).
FT /FTId=VAR_061209.
FT CONFLICT 206 206 S -> P (in Ref. 2; BAG53283).
FT STRAND 7 9
FT STRAND 15 20
FT STRAND 23 31
FT STRAND 35 38
FT STRAND 45 49
FT TURN 50 53
FT STRAND 54 58
FT HELIX 60 62
FT HELIX 66 72
FT HELIX 80 90
SQ SEQUENCE 240 AA; 26788 MW; DD60D9203BDD4B34 CRC64;
MSRSNRQKEY KCGDLVFAKM KGYPHWPARI DEMPEAAVKS TANKYQVFFF GTHETAFLGP
KDLFPYEESK EKFGKPNKRK GFSEGLWEIE NNPTVKASGY QSSQKKSCVE EPEPEPEAAE
GDGDKKGNAE GSSDEEGKLV IDEPAKEKNE KGALKRRAGD LLEDSPKRPK EAENPEGEEK
EAATLEVERP LPMEVEKNST PSEPGSGRGP PQEEEEEEDE EEEATKEDAE APGIRDHESL
//
ID HDGF_HUMAN Reviewed; 240 AA.
AC P51858; B3KU21; D3DVC9; Q5SZ07; Q5SZ08; Q5SZ09;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1996, sequence version 1.
DT 22-JAN-2014, entry version 128.
DE RecName: Full=Hepatoma-derived growth factor;
DE Short=HDGF;
DE AltName: Full=High mobility group protein 1-like 2;
DE Short=HMG-1L2;
GN Name=HDGF; Synonyms=HMG1L2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 4-24.
RC TISSUE=Hepatoma;
RX PubMed=7929202;
RA Nakamura H., Izumoto Y., Kambe H., Kuroda T., Mori T., Kawamura K.,
RA Yamamoto H., Kishimoto T.;
RT "Molecular cloning of complementary DNA for a novel human hepatoma-
RT derived growth factor. Its homology with high mobility group-1
RT protein.";
RL J. Biol. Chem. 269:25143-25149(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
RP LEU-201.
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP SUBCELLULAR LOCATION, AND NUCLEAR LOCALIZATION SIGNAL.
RX PubMed=11751870; DOI=10.1074/jbc.M111122200;
RA Kishima Y., Yamamoto H., Izumoto Y., Yoshida K., Enomoto H.,
RA Yamamoto M., Kuroda T., Ito H., Yoshizaki K., Nakamura H.;
RT "Hepatoma-derived growth factor stimulates cell growth after
RT translocation to the nucleus by nuclear localization signals.";
RL J. Biol. Chem. 277:10315-10322(2002).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=15302935; DOI=10.1073/pnas.0404720101;
RA Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,
RA Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
RT "Large-scale characterization of HeLa cell nuclear phosphoproteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-133 AND
RP SER-165, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165 AND THR-200, AND
RP MASS SPECTROMETRY.
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
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-133, AND
RP MASS SPECTROMETRY.
RC TISSUE=Pituitary;
RX PubMed=16807684; DOI=10.1007/s11102-006-8916-x;
RA Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
RT "Phosphoproteomic analysis of the human pituitary.";
RL Pituitary 9:109-120(2006).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND DNA-BINDING.
RX PubMed=17974029; DOI=10.1186/1471-2199-8-101;
RA Yang J., Everett A.D.;
RT "Hepatoma-derived growth factor binds DNA through the N-terminal PWWP
RT domain.";
RL BMC Mol. Biol. 8:101-101(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-133, AND
RP MASS SPECTROMETRY.
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate
RT cancer cells: identification of phosphoproteins in the LNCaP cell
RT line.";
RL Electrophoresis 28:2027-2034(2007).
RN [13]
RP SUMOYLATION AT LYS-80.
RX PubMed=18331345; DOI=10.1111/j.1742-4658.2008.06303.x;
RA Thakar K., Niedenthal R., Okaz E., Franken S., Jakobs A., Gupta S.,
RA Kelm S., Dietz F.;
RT "SUMOylation of the hepatoma-derived growth factor negatively
RT influences its binding to chromatin.";
RL FEBS J. 275:1411-1426(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-133 AND
RP SER-165, AND MASS SPECTROMETRY.
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using
RT sequential IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-133, AND
RP MASS SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-200; SER-206 AND
RP SER-239, AND MASS SPECTROMETRY.
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-133 AND
RP SER-165, AND MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [19]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND MASS
RP SPECTROMETRY.
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-133 AND
RP SER-165, AND MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-44, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133; SER-165; THR-200
RP AND SER-239, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [24]
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.,
RA Buerckstuemmer T., 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 [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [26]
RP STRUCTURE BY NMR OF 1-100, AND SUBUNIT.
RX PubMed=17270212; DOI=10.1016/j.jmb.2007.01.010;
RA Sue S.C., Lee W.T., Tien S.C., Lee S.C., Yu J.G., Wu W.J., Wu W.G.,
RA Huang T.-H.;
RT "PWWP module of human hepatoma-derived growth factor forms a domain-
RT swapped dimer with much higher affinity for heparin.";
RL J. Mol. Biol. 367:456-472(2007).
RN [27]
RP STRUCTURE BY NMR OF 1-100, AND HEPARIN-BINDING SITES.
RX PubMed=15491618; DOI=10.1016/j.jmb.2004.09.014;
RA Sue S.C., Chen J.Y., Lee S.C., Wu W.G., Huang T.-H.;
RT "Solution structure and heparin interaction of human hepatoma-derived
RT growth factor.";
RL J. Mol. Biol. 343:1365-1377(2004).
CC -!- FUNCTION: Heparin-binding protein, with mitogenic activity for
CC fibroblasts. Acts as a transcriptional repressor.
CC -!- SUBUNIT: Monomer, and domain-swapped homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P51858-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P51858-2; Sequence=VSP_045620;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=P51858-3; Sequence=VSP_047328;
CC Note=Gene prediction based on EST data;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The PWWP domain harbors the heparin-binding sites and is
CC responsible for DNA-binding, while the C-terminal region is
CC essentially unstructured.
CC -!- PTM: Sumoylated with SUMO1. Sumoylation prevents binding to
CC chromatin.
CC -!- SIMILARITY: Belongs to the HDGF family.
CC -!- SIMILARITY: Contains 1 PWWP domain.
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DR EMBL; D16431; BAA03903.1; -; mRNA.
DR EMBL; AK096411; BAG53283.1; -; mRNA.
DR EMBL; AL590666; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW52910.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52911.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52912.1; -; Genomic_DNA.
DR EMBL; BC018991; AAH18991.1; -; mRNA.
DR PIR; A55055; A55055.
DR RefSeq; NP_001119522.1; NM_001126050.1.
DR RefSeq; NP_001119523.1; NM_001126051.1.
DR RefSeq; NP_004485.1; NM_004494.2.
DR UniGene; Hs.743948; -.
DR PDB; 1RI0; NMR; -; A=1-100.
DR PDB; 2NLU; NMR; -; A/B=1-100.
DR PDBsum; 1RI0; -.
DR PDBsum; 2NLU; -.
DR ProteinModelPortal; P51858; -.
DR SMR; P51858; 1-100.
DR IntAct; P51858; 111.
DR MINT; MINT-5003673; -.
DR STRING; 9606.ENSP00000357189; -.
DR PhosphoSite; P51858; -.
DR DMDM; 1708157; -.
DR PaxDb; P51858; -.
DR PeptideAtlas; P51858; -.
DR PRIDE; P51858; -.
DR DNASU; 3068; -.
DR Ensembl; ENST00000357325; ENSP00000349878; ENSG00000143321.
DR Ensembl; ENST00000368206; ENSP00000357189; ENSG00000143321.
DR Ensembl; ENST00000368209; ENSP00000357192; ENSG00000143321.
DR Ensembl; ENST00000537739; ENSP00000443120; ENSG00000143321.
DR GeneID; 3068; -.
DR KEGG; hsa:3068; -.
DR UCSC; uc001fpy.4; human.
DR CTD; 3068; -.
DR GeneCards; GC01M156711; -.
DR HGNC; HGNC:4856; HDGF.
DR HPA; CAB026035; -.
DR MIM; 600339; gene.
DR neXtProt; NX_P51858; -.
DR PharmGKB; PA29234; -.
DR eggNOG; NOG240243; -.
DR HOGENOM; HOG000112874; -.
DR HOVERGEN; HBG010574; -.
DR KO; K16641; -.
DR OMA; EDSPKRL; -.
DR OrthoDB; EOG7NKKMQ; -.
DR PhylomeDB; P51858; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR ChiTaRS; HDGF; human.
DR EvolutionaryTrace; P51858; -.
DR GeneWiki; Hepatoma-derived_growth_factor; -.
DR GenomeRNAi; 3068; -.
DR NextBio; 12137; -.
DR PRO; PR:P51858; -.
DR ArrayExpress; P51858; -.
DR Bgee; P51858; -.
DR CleanEx; HS_HDGF; -.
DR Genevestigator; P51858; -.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0017053; C:transcriptional repressor complex; IDA:BHF-UCL.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008201; F:heparin binding; TAS:ProtInc.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0001106; F:RNA polymerase II transcription corepressor activity; IDA:BHF-UCL.
DR GO; GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; TAS:Reactome.
DR GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
DR GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
DR GO; GO:0034504; P:protein localization to nucleus; IEA:Ensembl.
DR InterPro; IPR000313; PWWP_dom.
DR Pfam; PF00855; PWWP; 1.
DR SMART; SM00293; PWWP; 1.
DR PROSITE; PS50812; PWWP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Direct protein sequencing; DNA-binding; Growth factor;
KW Heparin-binding; Isopeptide bond; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1 240 Hepatoma-derived growth factor.
FT /FTId=PRO_0000191700.
FT DOMAIN 12 69 PWWP.
FT MOTIF 75 80 Nuclear localization signal.
FT MOTIF 155 170 Bipartite nuclear localization signal.
FT COMPBIAS 110 230 Glu-rich.
FT BINDING 19 19 Heparin (Probable).
FT BINDING 21 21 Heparin (Probable).
FT BINDING 72 72 Heparin (Probable).
FT BINDING 75 75 Heparin (Probable).
FT BINDING 79 79 Heparin (Probable).
FT BINDING 80 80 Heparin (Probable).
FT MOD_RES 44 44 N6-acetyllysine.
FT MOD_RES 132 132 Phosphoserine.
FT MOD_RES 133 133 Phosphoserine.
FT MOD_RES 165 165 Phosphoserine.
FT MOD_RES 200 200 Phosphothreonine.
FT MOD_RES 206 206 Phosphoserine.
FT MOD_RES 239 239 Phosphoserine.
FT CROSSLNK 80 80 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in SUMO).
FT VAR_SEQ 1 29 MSRSNRQKEYKCGDLVFAKMKGYPHWPAR -> MEQRAGGN
FT RVQTSTLNCAGAAV (in isoform 2).
FT /FTId=VSP_045620.
FT VAR_SEQ 1 29 MSRSNRQKEYKCGDLVFAKMKGYPHWPAR -> MHPEGGQF
FT VPQLLGHLLATKLKRFLLSKGGRRAQIPDVSRATPHT (in
FT isoform 3).
FT /FTId=VSP_047328.
FT VARIANT 201 201 P -> L (in dbSNP:rs4399146).
FT /FTId=VAR_061209.
FT CONFLICT 206 206 S -> P (in Ref. 2; BAG53283).
FT STRAND 7 9
FT STRAND 15 20
FT STRAND 23 31
FT STRAND 35 38
FT STRAND 45 49
FT TURN 50 53
FT STRAND 54 58
FT HELIX 60 62
FT HELIX 66 72
FT HELIX 80 90
SQ SEQUENCE 240 AA; 26788 MW; DD60D9203BDD4B34 CRC64;
MSRSNRQKEY KCGDLVFAKM KGYPHWPARI DEMPEAAVKS TANKYQVFFF GTHETAFLGP
KDLFPYEESK EKFGKPNKRK GFSEGLWEIE NNPTVKASGY QSSQKKSCVE EPEPEPEAAE
GDGDKKGNAE GSSDEEGKLV IDEPAKEKNE KGALKRRAGD LLEDSPKRPK EAENPEGEEK
EAATLEVERP LPMEVEKNST PSEPGSGRGP PQEEEEEEDE EEEATKEDAE APGIRDHESL
//
MIM
600339
*RECORD*
*FIELD* NO
600339
*FIELD* TI
*600339 HEPATOMA-DERIVED GROWTH FACTOR; HDGF
*FIELD* TX
CLONING
Nakamura et al. (1994) purified a novel hepatoma-derived growth factor
read morefrom the conditioned medium of human hepatoma-derived cell line HuH-7.
Molecular cloning of a cDNA from the cDNA library of the same cell line
was done on the basis of the N-terminal amino acid sequence. The cDNA
was 2.4 kb long and the deduced amino acid sequence contained 240 amino
acids without a signal peptide-like N-terminal hydrophobic sequence. The
primary sequence shared homology with the high mobility group-1 protein
(163905); they showed 23.4% amino acid identity and 35.6% amino acid
similarity.
GENE FUNCTION
By immunofluorescence study, Nakamura et al. (1994) showed that HDGF is
localized in the cytoplasm of hepatoma cells and northern blots showed
that it is expressed ubiquitously in normal tissues and tumor cell
lines. Nakamura et al. (1994) suggested that it is a novel
heparin-binding protein with mitogenic activity for fibroblasts.
MAPPING
By PCR screening of a commercial monochromosomal hybrid panel, Wanschura
et al. (1996) mapped HDGF to the X chromosome. By FISH, they refined the
localization to Xq25. Subsequently, however, the International Radiation
Hybrid Mapping Consortium mapped the HDGF gene to chromosome 1 (TMAP
SHGC-132090). Amberger (2007) refined the localization to 1q21 based on
an alignment of the HDGF sequence (GenBank GENBANK D16431) with the
genomic sequence (build 36.2).
*FIELD* RF
1. Amberger, J. S.: Personal Communication. Baltimore, Md. 12/11/2007.
2. Nakamura, H.; Izumoto, Y.; Kambe, H.; Kuroda, T.; Mori, T.; Kawamura,
K.; Yamamoto, H.; Kishimoto, T.: Molecular cloning of complementary
DNA for a novel human hepatoma-derived growth factor: its homology
with high mobility group-1 protein. J. Biol. Chem. 269: 25143-25149,
1994.
3. Wanschura, S.; Schoenmakers, E. F. P. M.; Huysmans, C.; Bartnitzke,
S.; Van de Ven, W. J. M.; Bullerdiek, J.: Mapping of the gene encoding
the human hepatoma-derived growth factor (HDGF) with homology to the
high-mobility group (HMG)-1 protein to Xq25. Genomics 32: 298-300,
1996.
*FIELD* CN
Joanna S. Amberger - updated: 12/11/2007
*FIELD* CD
Victor A. McKusick: 1/24/1995
*FIELD* ED
carol: 12/12/2007
carol: 12/11/2007
joanna: 12/11/2007
mark: 3/25/1996
terry: 3/14/1996
carol: 1/24/1995
*RECORD*
*FIELD* NO
600339
*FIELD* TI
*600339 HEPATOMA-DERIVED GROWTH FACTOR; HDGF
*FIELD* TX
CLONING
Nakamura et al. (1994) purified a novel hepatoma-derived growth factor
read morefrom the conditioned medium of human hepatoma-derived cell line HuH-7.
Molecular cloning of a cDNA from the cDNA library of the same cell line
was done on the basis of the N-terminal amino acid sequence. The cDNA
was 2.4 kb long and the deduced amino acid sequence contained 240 amino
acids without a signal peptide-like N-terminal hydrophobic sequence. The
primary sequence shared homology with the high mobility group-1 protein
(163905); they showed 23.4% amino acid identity and 35.6% amino acid
similarity.
GENE FUNCTION
By immunofluorescence study, Nakamura et al. (1994) showed that HDGF is
localized in the cytoplasm of hepatoma cells and northern blots showed
that it is expressed ubiquitously in normal tissues and tumor cell
lines. Nakamura et al. (1994) suggested that it is a novel
heparin-binding protein with mitogenic activity for fibroblasts.
MAPPING
By PCR screening of a commercial monochromosomal hybrid panel, Wanschura
et al. (1996) mapped HDGF to the X chromosome. By FISH, they refined the
localization to Xq25. Subsequently, however, the International Radiation
Hybrid Mapping Consortium mapped the HDGF gene to chromosome 1 (TMAP
SHGC-132090). Amberger (2007) refined the localization to 1q21 based on
an alignment of the HDGF sequence (GenBank GENBANK D16431) with the
genomic sequence (build 36.2).
*FIELD* RF
1. Amberger, J. S.: Personal Communication. Baltimore, Md. 12/11/2007.
2. Nakamura, H.; Izumoto, Y.; Kambe, H.; Kuroda, T.; Mori, T.; Kawamura,
K.; Yamamoto, H.; Kishimoto, T.: Molecular cloning of complementary
DNA for a novel human hepatoma-derived growth factor: its homology
with high mobility group-1 protein. J. Biol. Chem. 269: 25143-25149,
1994.
3. Wanschura, S.; Schoenmakers, E. F. P. M.; Huysmans, C.; Bartnitzke,
S.; Van de Ven, W. J. M.; Bullerdiek, J.: Mapping of the gene encoding
the human hepatoma-derived growth factor (HDGF) with homology to the
high-mobility group (HMG)-1 protein to Xq25. Genomics 32: 298-300,
1996.
*FIELD* CN
Joanna S. Amberger - updated: 12/11/2007
*FIELD* CD
Victor A. McKusick: 1/24/1995
*FIELD* ED
carol: 12/12/2007
carol: 12/11/2007
joanna: 12/11/2007
mark: 3/25/1996
terry: 3/14/1996
carol: 1/24/1995