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P51858

- HDGF_HUMAN

UniProt

P51858 - HDGF_HUMAN

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Protein

Hepatoma-derived growth factor

Gene
HDGF, HMG1L2
Organism
Homo sapiens (Human)
Status
Reviewed - 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.1 Publication

Sites

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

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
Complete GO annotation...

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

Cytoplasm. Nucleus 2 Publications

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
Complete GO annotation...

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)1 Publication
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.

Miscellaneous databases

EvolutionaryTraceiP51858.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 6958PWWPAdd
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.
Contains 1 PWWP domain.

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

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. VSP_045620Add
BLAST
Alternative sequencei1 – 2929MSRSN…HWPAR → MHPEGGQFVPQLLGHLLATK LKRFLLSKGGRRAQIPDVSR ATPHT in isoform 3. VSP_047328Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti206 – 2061S → P in BAG53283. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 135 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

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