P51858 (HDGF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Hepatoma-derived growth factor
Short name=HDGF

Alternative name(s):
High mobility group protein 1-like 2
Short name=HMG-1L2

Gene names

Name:	HDGF
Synonyms:	HMG1L2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	240 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Heparin-binding protein, with mitogenic activity for fibroblasts. Acts as a transcriptional repressor. Ref.11
Subunit structure	Monomer, and domain-swapped homodimer. Ref.25
Subcellular location	Cytoplasm. Nucleus Ref.6 Ref.11.
Tissue specificity	Ubiquitous.
Domain	The PWWP domain harbors the heparin-binding sites and is responsible for DNA-binding, while the C-terminal region is essentially unstructured.
Post-translational modification	Sumoylated with SUMO1. Sumoylation prevents binding to chromatin. Ref.13
Sequence similarities	Belongs to the HDGF family. Contains 1 PWWP domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	DNA-binding Heparin-binding Nucleotide-binding
Molecular function	Growth factor Repressor
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	activation of signaling protein activity involved in unfolded protein response Traceable author statement. Source: Reactome cell proliferation Traceable author statement Ref.1. Source: ProtInc
Cellular_component	cytoplasm Traceable author statement Ref.1. Source: ProtInc extracellular space Inferred from direct assay PubMed 20551380. Source: BHF-UCL transcriptional repressor complex Inferred from direct assay PubMed 19162039. Source: BHF-UCL
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW RNA polymerase II transcription corepressor activity Inferred from direct assay PubMed 19162039. Source: BHF-UCL heparin binding Traceable author statement Ref.1. Source: ProtInc nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P51858-1)

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.

Isoform 2 (identifier: P51858-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 240

240

Hepatoma-derived growth factor

PRO_0000191700

Regions

Domain

12 – 69

58

PWWP

Motif

75 – 80

6

Nuclear localization signal Ref.6

Motif

155 – 170

16

Bipartite nuclear localization signal

Compositional bias

110 – 230

121

Glu-rich

Sites

Binding site

19

1

Heparin Probable

Binding site

21

1

Heparin Probable

Binding site

72

1

Heparin Probable

Binding site

75

1

Heparin Probable

Binding site

79

1

Heparin Probable

Binding site

80

1

Heparin Probable

Amino acid modifications

Modified residue

44

1

N6-acetyllysine Ref.21

Modified residue

132

1

Phosphoserine Ref.8 Ref.10 Ref.12 Ref.14 Ref.15 Ref.18 Ref.20

Modified residue

133

1

Phosphoserine Ref.8 Ref.10 Ref.12 Ref.14 Ref.15 Ref.18 Ref.20 Ref.22

Modified residue

165

1

Phosphoserine Ref.7 Ref.8 Ref.9 Ref.14 Ref.16 Ref.18 Ref.19 Ref.20 Ref.22 Ref.24

Modified residue

199

1

Phosphoserine By similarity

Modified residue

200

1

Phosphothreonine Ref.9 Ref.17 Ref.22

Modified residue

202

1

Phosphoserine By similarity

Modified residue

206

1

Phosphoserine Ref.17

Modified residue

239

1

Phosphoserine Ref.17 Ref.22

Cross-link

80

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.13

Natural variations

Alternative sequence

1 – 29

29

MSRSN…HWPAR → MEQRAGGNRVQTSTLNCAGA AV in isoform 2.

VSP_045620

Natural variant

201

1

P → L. Ref.2
Corresponds to variant rs4399146 [ dbSNP | Ensembl ].

VAR_061209

Experimental info

Sequence conflict

206

1

S → P in BAG53283. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

240

Helix Strand Turn

Details...

Beta strand

7 – 9

3

Beta strand

15 – 20

6

Beta strand

23 – 31

9

Beta strand

35 – 38

4

Beta strand

45 – 49

5

Turn

50 – 53

4

Beta strand

54 – 58

5

Helix

60 – 62

3

Helix

66 – 72

7

Helix

80 – 90

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: DD60D9203BDD4B34	FASTA	240	26,788
	10 20 30 40 50 60 MSRSNRQKEY KCGDLVFAKM KGYPHWPARI DEMPEAAVKS TANKYQVFFF GTHETAFLGP 70 80 90 100 110 120 KDLFPYEESK EKFGKPNKRK GFSEGLWEIE NNPTVKASGY QSSQKKSCVE EPEPEPEAAE 130 140 150 160 170 180 GDGDKKGNAE GSSDEEGKLV IDEPAKEKNE KGALKRRAGD LLEDSPKRPK EAENPEGEEK 190 200 210 220 230 240 EAATLEVERP LPMEVEKNST PSEPGSGRGP PQEEEEEEDE EEEATKEDAE APGIRDHESL
	Isoform 2 [UniParc]. Checksum: 629AFF8900895888	FASTA	233	25,538
	10 20 30 40 50 60 MEQRAGGNRV QTSTLNCAGA AVIDEMPEAA VKSTANKYQV FFFGTHETAF LGPKDLFPYE 70 80 90 100 110 120 ESKEKFGKPN KRKGFSEGLW EIENNPTVKA SGYQSSQKKS CVEEPEPEPE AAEGDGDKKG 130 140 150 160 170 180 NAEGSSDEEG KLVIDEPAKE KNEKGALKRR AGDLLEDSPK RPKEAENPEG EEKEAATLEV 190 200 210 220 230 ERPLPMEVEK NSTPSEPGSG RGPPQEEEEE EDEEEEATKE DAEAPGIRDH ESL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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 MOTIF.
[7]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Phosphoproteomic analysis of the human pituitary." Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F. Pituitary 9:109-120(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-133, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: T-cell.
[15]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-133, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-200; SER-206 AND SER-239, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Liver.
[19]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, MASS SPECTROMETRY.
[20]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[21]	"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, MASS SPECTROMETRY.
[22]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]	"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, MASS SPECTROMETRY.
[25]	"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.
[26]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D16431 mRNA. Translation: BAA03903.1.
AK096411 mRNA. Translation: BAG53283.1.
AL590666 Genomic DNA. Translation: CAI16347.1.
AL590666 Genomic DNA. Translation: CAI16348.1.
CH471121 Genomic DNA. Translation: EAW52910.1.
CH471121 Genomic DNA. Translation: EAW52911.1.
CH471121 Genomic DNA. Translation: EAW52912.1.
BC018991 mRNA. Translation: AAH18991.1.

IPI

IPI00020956.
IPI00514330.

PIR

A55055.

RefSeq

NP_001119522.1. NM_001126050.1.
NP_001119523.1. NM_001126051.1.
NP_004485.1. NM_004494.2.

UniGene

Hs.741151.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1RI0	NMR	-	A	1-100	[»]
2NLU	NMR	-	A/B	1-100	[»]

ProteinModelPortal

P51858.

ModBase

Search...

Protein-protein interaction databases

IntAct

P51858. 111 interactions.

STRING

9606.ENSP00000357189.

PTM databases

PhosphoSite

P51858.

Polymorphism databases

DMDM

1708157.

Proteomic databases

PaxDb

P51858.

PeptideAtlas

P51858.

PRIDE

P51858.

Protocols and materials databases

DNASU

3068.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000357325; ENSP00000349878; ENSG00000143321.
ENST00000368209; ENSP00000357192; ENSG00000143321.
ENST00000537739; ENSP00000443120; ENSG00000143321.

GeneID

3068.

KEGG

hsa:3068.

UCSC

uc001fpy.4. human.

Organism-specific databases

CTD

3068.

GeneCards

GC01M156711.

HGNC

HGNC:4856. HDGF.

HPA

CAB026035.

MIM

600339. gene.

neXtProt

NX_P51858.

PharmGKB

PA29234.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG240243.

HOGENOM

HOG000112874.

HOVERGEN

HBG010574.

KO

K16641.

OrthoDB

EOG4PK28W.

PhylomeDB

P51858.

Enzyme and pathway databases

Reactome

REACT_116125. Disease.

Gene expression databases

ArrayExpress

P51858.

Bgee

P51858.

CleanEx

HS_HDGF.

Genevestigator

P51858.

GermOnline

ENSG00000143321. Homo sapiens.

Family and domain databases

InterPro

IPR000313. PWWP.
[Graphical view]

Pfam

PF00855. PWWP. 1 hit.
[Graphical view]

SMART

SM00293. PWWP. 1 hit.
[Graphical view]

PROSITE

PS50812. PWWP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

HDGF. human.

EvolutionaryTrace

P51858.

GenomeRNAi

3068.

NextBio

12137.

SOURCE

Search...

Entry information

Entry name

HDGF_HUMAN

Accession

Primary (citable) accession number: P51858
Secondary accession number(s): B3KU21 , D3DVC9, Q5SZ08, Q5SZ09

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 121 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.