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Protein

Hepatoma-derived growth factor

Gene

Hdgf

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Heparin-binding protein, with mitogenic activity for fibroblasts. Acts as a transcriptional repressor (By similarity).By similarity

Sites

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Growth factor, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Heparin-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Hepatoma-derived growth factor
Short name:
HDGF
Gene namesi
Name:Hdgf
Synonyms:Tdrm1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1194494. Hdgf.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • extracellular space Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
  • transcriptional repressor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 237237Hepatoma-derived growth factorPRO_0000191701Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei44 – 441N6-acetyllysineBy similarity
Cross-linki80 – 80Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki80 – 80Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei128 – 1281PhosphoserineCombined sources
Modified residuei132 – 1321PhosphoserineCombined sources
Modified residuei133 – 1331PhosphoserineCombined sources
Modified residuei165 – 1651PhosphoserineCombined sources
Modified residuei199 – 1991PhosphoserineBy similarity
Modified residuei200 – 2001PhosphothreonineBy similarity
Modified residuei202 – 2021PhosphoserineCombined sources
Modified residuei206 – 2061PhosphoserineCombined sources
Modified residuei236 – 2361PhosphoserineBy similarity

Post-translational modificationi

Sumoylated with SUMO1. Sumoylation prevents binding to chromatin (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP51859.
MaxQBiP51859.
PaxDbiP51859.
PRIDEiP51859.
TopDownProteomicsiP51859.

PTM databases

iPTMnetiP51859.
PhosphoSiteiP51859.
SwissPalmiP51859.

Miscellaneous databases

PMAP-CutDBP51859.

Expressioni

Tissue specificityi

Expressed predominantly in testis and skeletal muscle, to intermediate extents in heart, brain, lung, liver, and kidney, and to a minimal extent in spleen.

Gene expression databases

BgeeiP51859.
CleanExiMM_HDGF.
ExpressionAtlasiP51859. baseline and differential.
GenevisibleiP51859. MM.

Interactioni

Subunit structurei

Monomer, and domain-swapped homodimer.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Q3UMU9-14EBI-2943087,EBI-7627862
Q3UMU9-34EBI-2943087,EBI-7627932
Hdgfrp2Q3UMU94EBI-2943087,EBI-7627961

GO - Molecular functioni

Protein-protein interaction databases

BioGridi200265. 2 interactions.
IntActiP51859. 8 interactions.
MINTiMINT-4097326.
STRINGi10090.ENSMUSP00000005017.

Structurei

3D structure databases

ProteinModelPortaliP51859.
SMRiP51859. Positions 1-109.
ModBaseiSearch...
MobiDBiSearch...

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 signalBy similarity
Motifi155 – 17016Bipartite nuclear localization signalBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi111 – 227117Glu-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.By similarity

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG410IMJ5. Eukaryota.
ENOG4111IFT. LUCA.
GeneTreeiENSGT00530000063013.
HOGENOMiHOG000112874.
HOVERGENiHBG010574.
InParanoidiP51859.
KOiK16641.
OMAiEDSPKRL.
OrthoDBiEOG7NKKMQ.
PhylomeDBiP51859.
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]

Sequencei

Sequence statusi: Complete.

P51859-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRSNRQKEY KCGDLVFAKM KGYPHWPARI DEMPEAAVKS TANKYQVFFF
60 70 80 90 100
GTHETAFLGP KDLFPYEESK EKFGKPNKRK GFSEGLWEIE NNPTVKASGY
110 120 130 140 150
QSSQKKSCAA EPEVEPEAHE GDGDKKGSAE GSSDEEGKLV IDEPAKEKNE
160 170 180 190 200
KGTLKRRAGD VLEDSPKRPK ESGDHEEEDK EIAALEGERP LPVEVEKNST
210 220 230
PSEPDSGQGP PAEEEEGEEE AAKEEAEAQG VRDHESL
Length:237
Mass (Da):26,269
Last modified:August 13, 2002 - v2
Checksum:iAAE4CF574DA4733F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti118 – 1181A → D in BAB30979 (PubMed:16141072).Curated
Sequence conflicti190 – 1901P → H in BAA09838 (PubMed:9299445).Curated
Sequence conflicti229 – 2291Q → E in BAC36126 (PubMed:16141072).Curated
Sequence conflicti229 – 2291Q → P in BAA09838 (PubMed:9299445).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D63707 mRNA. Translation: BAA09838.1.
AF251787 mRNA. Translation: AAF65469.1.
AK017863 mRNA. Translation: BAB30979.1.
AK029475 mRNA. Translation: BAC26466.1.
AK076021 mRNA. Translation: BAC36126.1.
BC005713 mRNA. Translation: AAH05713.1.
BC021654 mRNA. Translation: AAH21654.1.
CCDSiCCDS17457.1.
PIRiJC5660.
RefSeqiNP_032257.3. NM_008231.4.
UniGeneiMm.292208.

Genome annotation databases

EnsembliENSMUST00000005017; ENSMUSP00000005017; ENSMUSG00000004897.
GeneIDi15191.
KEGGimmu:15191.
UCSCiuc008ptc.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D63707 mRNA. Translation: BAA09838.1.
AF251787 mRNA. Translation: AAF65469.1.
AK017863 mRNA. Translation: BAB30979.1.
AK029475 mRNA. Translation: BAC26466.1.
AK076021 mRNA. Translation: BAC36126.1.
BC005713 mRNA. Translation: AAH05713.1.
BC021654 mRNA. Translation: AAH21654.1.
CCDSiCCDS17457.1.
PIRiJC5660.
RefSeqiNP_032257.3. NM_008231.4.
UniGeneiMm.292208.

3D structure databases

ProteinModelPortaliP51859.
SMRiP51859. Positions 1-109.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200265. 2 interactions.
IntActiP51859. 8 interactions.
MINTiMINT-4097326.
STRINGi10090.ENSMUSP00000005017.

PTM databases

iPTMnetiP51859.
PhosphoSiteiP51859.
SwissPalmiP51859.

Proteomic databases

EPDiP51859.
MaxQBiP51859.
PaxDbiP51859.
PRIDEiP51859.
TopDownProteomicsiP51859.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000005017; ENSMUSP00000005017; ENSMUSG00000004897.
GeneIDi15191.
KEGGimmu:15191.
UCSCiuc008ptc.2. mouse.

Organism-specific databases

CTDi3068.
MGIiMGI:1194494. Hdgf.

Phylogenomic databases

eggNOGiENOG410IMJ5. Eukaryota.
ENOG4111IFT. LUCA.
GeneTreeiENSGT00530000063013.
HOGENOMiHOG000112874.
HOVERGENiHBG010574.
InParanoidiP51859.
KOiK16641.
OMAiEDSPKRL.
OrthoDBiEOG7NKKMQ.
PhylomeDBiP51859.
TreeFamiTF105385.

Miscellaneous databases

ChiTaRSiHdgf. mouse.
NextBioi287715.
PMAP-CutDBP51859.
PROiP51859.
SOURCEiSearch...

Gene expression databases

BgeeiP51859.
CleanExiMM_HDGF.
ExpressionAtlasiP51859. baseline and differential.
GenevisibleiP51859. MM.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Hepatoma-derived growth factor belongs to a gene family in mice showing significant homology in the amino terminus."
    Izumoto Y., Kuroda T., Harada H., Kishimoto T., Nakamura H.
    Biochem. Biophys. Res. Commun. 238:26-32(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ.
    Tissue: Testis.
  2. "Cloning of novel gene related to thymus development."
    Zhao Y., Chen W., Wang Y.
    Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ.
    Tissue: Thymus.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo and Head.
  4. "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].
    Tissue: Liver and Mammary gland.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  6. "A differential phosphoproteomic analysis of retinoic acid-treated P19 cells."
    Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.
    J. Proteome Res. 6:3174-3186(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Teratocarcinoma.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128; SER-132; SER-133 AND SER-165, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-133, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128; SER-132; SER-133; SER-165; SER-202 AND SER-206, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiHDGF_MOUSE
AccessioniPrimary (citable) accession number: P51859
Secondary accession number(s): Q8BPG7, Q9CYA4, Q9JK87
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: August 13, 2002
Last modified: March 16, 2016
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.