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P51858

- HDGF_HUMAN

UniProt

P51858 - HDGF_HUMAN

Protein

Hepatoma-derived growth factor

Gene

HDGF

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Heparin-binding protein, with mitogenic activity for fibroblasts. Acts as a transcriptional repressor.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei19 – 191HeparinCurated
    Binding sitei21 – 211HeparinCurated
    Binding sitei72 – 721HeparinCurated
    Binding sitei75 – 751HeparinCurated
    Binding sitei79 – 791HeparinCurated
    Binding sitei80 – 801HeparinCurated

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. heparin binding Source: ProtInc
    3. nucleotide binding Source: UniProtKB-KW
    4. poly(A) RNA binding Source: UniProtKB
    5. RNA polymerase II transcription corepressor activity Source: BHF-UCL
    6. transcription corepressor binding Source: BHF-UCL

    GO - Biological processi

    1. activation of signaling protein activity involved in unfolded protein response Source: Reactome
    2. cell proliferation Source: ProtInc
    3. cellular protein metabolic process Source: Reactome
    4. endoplasmic reticulum unfolded protein response Source: Reactome
    5. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    6. signal transduction Source: ProtInc

    Keywords - Molecular functioni

    Growth factor, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Heparin-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_18273. XBP1(S) activates chaperone genes.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hepatoma-derived growth factor
    Short name:
    HDGF
    Alternative name(s):
    High mobility group protein 1-like 2
    Short name:
    HMG-1L2
    Gene namesi
    Name:HDGF
    Synonyms:HMG1L2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:4856. HDGF.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: ProtInc
    2. extracellular space Source: BHF-UCL
    3. nucleoplasm Source: Reactome
    4. nucleus Source: HPA
    5. transcriptional repressor complex Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29234.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 240240Hepatoma-derived growth factorPRO_0000191700Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei44 – 441N6-acetyllysine1 Publication
    Cross-linki80 – 80Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei132 – 1321Phosphoserine7 Publications
    Modified residuei133 – 1331Phosphoserine8 Publications
    Modified residuei165 – 1651Phosphoserine10 Publications
    Modified residuei200 – 2001Phosphothreonine3 Publications
    Modified residuei206 – 2061Phosphoserine1 Publication
    Modified residuei239 – 2391Phosphoserine2 Publications

    Post-translational modificationi

    Sumoylated with SUMO1. Sumoylation prevents binding to chromatin.1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP51858.
    PaxDbiP51858.
    PeptideAtlasiP51858.
    PRIDEiP51858.

    PTM databases

    PhosphoSiteiP51858.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiP51858.
    BgeeiP51858.
    CleanExiHS_HDGF.
    GenevestigatoriP51858.

    Organism-specific databases

    HPAiCAB026035.
    HPA048728.
    HPA053422.

    Interactioni

    Subunit structurei

    Monomer, and domain-swapped homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi109318. 207 interactions.
    IntActiP51858. 111 interactions.
    MINTiMINT-5003673.
    STRINGi9606.ENSP00000357189.

    Structurei

    Secondary structure

    1
    240
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 93
    Beta strandi15 – 206
    Beta strandi23 – 319
    Beta strandi35 – 384
    Beta strandi45 – 495
    Turni50 – 534
    Beta strandi54 – 585
    Helixi60 – 623
    Helixi66 – 727
    Helixi80 – 9011

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1RI0NMR-A1-100[»]
    2NLUNMR-A/B1-100[»]
    ProteinModelPortaliP51858.
    SMRiP51858. Positions 1-100.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP51858.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini12 – 6958PWWPPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi75 – 806Nuclear localization signal1 Publication
    Motifi155 – 17016Bipartite nuclear localization signalAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi110 – 230121Glu-richAdd
    BLAST

    Domaini

    The PWWP domain harbors the heparin-binding sites and is responsible for DNA-binding, while the C-terminal region is essentially unstructured.

    Sequence similaritiesi

    Belongs to the HDGF family.Curated
    Contains 1 PWWP domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG240243.
    HOGENOMiHOG000112874.
    HOVERGENiHBG010574.
    KOiK16641.
    OMAiEDSPKRL.
    OrthoDBiEOG7NKKMQ.
    PhylomeDBiP51858.
    TreeFamiTF105385.

    Family and domain databases

    InterProiIPR000313. PWWP_dom.
    [Graphical view]
    PfamiPF00855. PWWP. 1 hit.
    [Graphical view]
    SMARTiSM00293. PWWP. 1 hit.
    [Graphical view]
    PROSITEiPS50812. PWWP. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P51858-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSRSNRQKEY KCGDLVFAKM KGYPHWPARI DEMPEAAVKS TANKYQVFFF    50
    GTHETAFLGP KDLFPYEESK EKFGKPNKRK GFSEGLWEIE NNPTVKASGY 100
    QSSQKKSCVE EPEPEPEAAE GDGDKKGNAE GSSDEEGKLV IDEPAKEKNE 150
    KGALKRRAGD LLEDSPKRPK EAENPEGEEK EAATLEVERP LPMEVEKNST 200
    PSEPGSGRGP PQEEEEEEDE EEEATKEDAE APGIRDHESL 240
    Length:240
    Mass (Da):26,788
    Last modified:October 1, 1996 - v1
    Checksum:iDD60D9203BDD4B34
    GO
    Isoform 2 (identifier: P51858-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-29: MSRSNRQKEYKCGDLVFAKMKGYPHWPAR → MEQRAGGNRVQTSTLNCAGAAV

    Note: No experimental confirmation available.

    Show »
    Length:233
    Mass (Da):25,538
    Checksum:i629AFF8900895888
    GO
    Isoform 3 (identifier: P51858-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-29: MSRSNRQKEYKCGDLVFAKMKGYPHWPAR → MHPEGGQFVPQLLGHLLATKLKRFLLSKGGRRAQIPDVSRATPHT

    Note: Gene prediction based on EST data.

    Show »
    Length:256
    Mass (Da):28,264
    Checksum:iD9D2BC3056553CF9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti206 – 2061S → P in BAG53283. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti201 – 2011P → L.1 Publication
    Corresponds to variant rs4399146 [ dbSNP | Ensembl ].
    VAR_061209

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2929MSRSN…HWPAR → MEQRAGGNRVQTSTLNCAGA AV in isoform 2. 1 PublicationVSP_045620Add
    BLAST
    Alternative sequencei1 – 2929MSRSN…HWPAR → MHPEGGQFVPQLLGHLLATK LKRFLLSKGGRRAQIPDVSR ATPHT in isoform 3. CuratedVSP_047328Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D16431 mRNA. Translation: BAA03903.1.
    AK096411 mRNA. Translation: BAG53283.1.
    AL590666 Genomic DNA. No translation available.
    CH471121 Genomic DNA. Translation: EAW52910.1.
    CH471121 Genomic DNA. Translation: EAW52911.1.
    CH471121 Genomic DNA. Translation: EAW52912.1.
    BC018991 mRNA. Translation: AAH18991.1.
    CCDSiCCDS1156.1. [P51858-1]
    CCDS44247.1. [P51858-3]
    CCDS44248.1. [P51858-2]
    PIRiA55055.
    RefSeqiNP_001119522.1. NM_001126050.1. [P51858-3]
    NP_001119523.1. NM_001126051.1. [P51858-2]
    NP_004485.1. NM_004494.2. [P51858-1]
    UniGeneiHs.743948.

    Genome annotation databases

    EnsembliENST00000357325; ENSP00000349878; ENSG00000143321. [P51858-1]
    ENST00000368206; ENSP00000357189; ENSG00000143321. [P51858-3]
    ENST00000368209; ENSP00000357192; ENSG00000143321. [P51858-2]
    ENST00000537739; ENSP00000443120; ENSG00000143321. [P51858-1]
    GeneIDi3068.
    KEGGihsa:3068.
    UCSCiuc001fpy.4. human. [P51858-1]
    uc001fpz.4. human.

    Polymorphism databases

    DMDMi1708157.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D16431 mRNA. Translation: BAA03903.1 .
    AK096411 mRNA. Translation: BAG53283.1 .
    AL590666 Genomic DNA. No translation available.
    CH471121 Genomic DNA. Translation: EAW52910.1 .
    CH471121 Genomic DNA. Translation: EAW52911.1 .
    CH471121 Genomic DNA. Translation: EAW52912.1 .
    BC018991 mRNA. Translation: AAH18991.1 .
    CCDSi CCDS1156.1. [P51858-1 ]
    CCDS44247.1. [P51858-3 ]
    CCDS44248.1. [P51858-2 ]
    PIRi A55055.
    RefSeqi NP_001119522.1. NM_001126050.1. [P51858-3 ]
    NP_001119523.1. NM_001126051.1. [P51858-2 ]
    NP_004485.1. NM_004494.2. [P51858-1 ]
    UniGenei Hs.743948.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1RI0 NMR - A 1-100 [» ]
    2NLU NMR - A/B 1-100 [» ]
    ProteinModelPortali P51858.
    SMRi P51858. Positions 1-100.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109318. 207 interactions.
    IntActi P51858. 111 interactions.
    MINTi MINT-5003673.
    STRINGi 9606.ENSP00000357189.

    PTM databases

    PhosphoSitei P51858.

    Polymorphism databases

    DMDMi 1708157.

    Proteomic databases

    MaxQBi P51858.
    PaxDbi P51858.
    PeptideAtlasi P51858.
    PRIDEi P51858.

    Protocols and materials databases

    DNASUi 3068.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000357325 ; ENSP00000349878 ; ENSG00000143321 . [P51858-1 ]
    ENST00000368206 ; ENSP00000357189 ; ENSG00000143321 . [P51858-3 ]
    ENST00000368209 ; ENSP00000357192 ; ENSG00000143321 . [P51858-2 ]
    ENST00000537739 ; ENSP00000443120 ; ENSG00000143321 . [P51858-1 ]
    GeneIDi 3068.
    KEGGi hsa:3068.
    UCSCi uc001fpy.4. human. [P51858-1 ]
    uc001fpz.4. human.

    Organism-specific databases

    CTDi 3068.
    GeneCardsi GC01M156711.
    HGNCi HGNC:4856. HDGF.
    HPAi CAB026035.
    HPA048728.
    HPA053422.
    MIMi 600339. gene.
    neXtProti NX_P51858.
    PharmGKBi PA29234.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG240243.
    HOGENOMi HOG000112874.
    HOVERGENi HBG010574.
    KOi K16641.
    OMAi EDSPKRL.
    OrthoDBi EOG7NKKMQ.
    PhylomeDBi P51858.
    TreeFami TF105385.

    Enzyme and pathway databases

    Reactomei REACT_18273. XBP1(S) activates chaperone genes.

    Miscellaneous databases

    ChiTaRSi HDGF. human.
    EvolutionaryTracei P51858.
    GeneWikii Hepatoma-derived_growth_factor.
    GenomeRNAii 3068.
    NextBioi 12137.
    PROi P51858.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P51858.
    Bgeei P51858.
    CleanExi HS_HDGF.
    Genevestigatori P51858.

    Family and domain databases

    InterProi IPR000313. PWWP_dom.
    [Graphical view ]
    Pfami PF00855. PWWP. 1 hit.
    [Graphical view ]
    SMARTi SM00293. PWWP. 1 hit.
    [Graphical view ]
    PROSITEi PS50812. PWWP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of complementary DNA for a novel human hepatoma-derived growth factor. Its homology with high mobility group-1 protein."
      Nakamura H., Izumoto Y., Kambe H., Kuroda T., Mori T., Kawamura K., Yamamoto H., Kishimoto T.
      J. Biol. Chem. 269:25143-25149(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 4-24.
      Tissue: Hepatoma.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT LEU-201.
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    6. "Hepatoma-derived growth factor stimulates cell growth after translocation to the nucleus by nuclear localization signals."
      Kishima Y., Yamamoto H., Izumoto Y., Yoshida K., Enomoto H., Yamamoto M., Kuroda T., Ito H., Yoshizaki K., Nakamura H.
      J. Biol. Chem. 277:10315-10322(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-133 AND SER-165, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165 AND THR-200, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-133, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Pituitary.
    11. "Hepatoma-derived growth factor binds DNA through the N-terminal PWWP domain."
      Yang J., Everett A.D.
      BMC Mol. Biol. 8:101-101(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DNA-BINDING.
    12. "Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
      Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
      Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-133, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Prostate cancer.
    13. "SUMOylation of the hepatoma-derived growth factor negatively influences its binding to chromatin."
      Thakar K., Niedenthal R., Okaz E., Franken S., Jakobs A., Gupta S., Kelm S., Dietz F.
      FEBS J. 275:1411-1426(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-80.
    14. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-133 AND SER-165, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-133, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    16. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-200; SER-206 AND SER-239, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-133 AND SER-165, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    19. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-133 AND SER-165, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    22. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-44, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133; SER-165; THR-200 AND SER-239, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "PWWP module of human hepatoma-derived growth factor forms a domain-swapped dimer with much higher affinity for heparin."
      Sue S.C., Lee W.T., Tien S.C., Lee S.C., Yu J.G., Wu W.J., Wu W.G., Huang T.-H.
      J. Mol. Biol. 367:456-472(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-100, SUBUNIT.
    27. "Solution structure and heparin interaction of human hepatoma-derived growth factor."
      Sue S.C., Chen J.Y., Lee S.C., Wu W.G., Huang T.-H.
      J. Mol. Biol. 343:1365-1377(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-100, HEPARIN-BINDING SITES.

    Entry informationi

    Entry nameiHDGF_HUMAN
    AccessioniPrimary (citable) accession number: P51858
    Secondary accession number(s): B3KU21
    , D3DVC9, Q5SZ07, Q5SZ08, Q5SZ09
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 136 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3