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Q9GZP0

- PDGFD_HUMAN

UniProt

Q9GZP0 - PDGFD_HUMAN

Protein

Platelet-derived growth factor D

Gene

PDGFD

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Plays an important role in wound healing. Induces macrophage recruitment, increased interstitial pressure, and blood vessel maturation during angiogenesis. Can initiate events that lead to a mesangial proliferative glomerulonephritis, including influx of monocytes and macrophages and production of extracellular matrix By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei247 – 2482CleavageSequence Analysis
    Sitei249 – 2502CleavageSequence Analysis

    GO - Biological processi

    1. cellular response to amino acid stimulus Source: Ensembl
    2. multicellular organismal development Source: UniProtKB-KW
    3. platelet-derived growth factor receptor signaling pathway Source: InterPro
    4. positive regulation of cell division Source: UniProtKB-KW
    5. regulation of peptidyl-tyrosine phosphorylation Source: Ensembl

    Keywords - Molecular functioni

    Developmental protein, Growth factor, Mitogen

    Enzyme and pathway databases

    ReactomeiREACT_16888. Signaling by PDGF.
    SignaLinkiQ9GZP0.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Platelet-derived growth factor D
    Short name:
    PDGF-D
    Alternative name(s):
    Iris-expressed growth factor
    Spinal cord-derived growth factor B
    Short name:
    SCDGF-B
    Cleaved into the following 2 chains:
    Platelet-derived growth factor D, receptor-binding form
    Short name:
    PDGFD receptor-binding form
    Gene namesi
    Name:PDGFD
    Synonyms:IEGF, SCDGFB
    ORF Names:MSTP036, UNQ1899/PRO4345
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:30620. PDGFD.

    Subcellular locationi

    Secreted 1 Publication
    Note: Released by platelets upon wounding.

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: Reactome
    2. extracellular region Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. Golgi membrane Source: Reactome

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi247 – 2471R → A: Abolishes cleavage into active form; when associated with A-249. 1 Publication
    Mutagenesisi249 – 2491R → A: Abolishes cleavage into active form; when associated with A-247. 1 Publication

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    PharmGKBiPA134892327.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 370352Platelet-derived growth factor D, latent formPRO_0000250188Add
    BLAST
    Chaini250 – 370121Platelet-derived growth factor D, receptor-binding formSequence AnalysisPRO_0000250189Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi109 ↔ 131PROSITE-ProRule annotation
    Glycosylationi276 – 2761N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi296 – 296InterchainPROSITE-ProRule annotation
    Disulfide bondi302 ↔ 360PROSITE-ProRule annotation
    Disulfide bondi306 ↔ 362PROSITE-ProRule annotation

    Post-translational modificationi

    Activated by proteolytic cleavage. Proteolytic removal of the N-terminal CUB domain releasing the core domain is necessary for unmasking the receptor-binding epitopes of the core domain. Cleavage after Arg-247 or Arg-249 by urokinase plasminogen activator gives rise to the active form.

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ9GZP0.
    PRIDEiQ9GZP0.

    PTM databases

    PhosphoSiteiQ9GZP0.

    Miscellaneous databases

    PMAP-CutDBQ9GZP0.

    Expressioni

    Tissue specificityi

    Expressed at high levels in the heart, pancreas, adrenal gland and ovary and at low levels in placenta, liver, kidney, prostate, testis, small intestine, spleen and colon. In the kidney, expressed by the visceral epithelial cells of the glomeruli. A widespread expression is also seen in the medial smooth muscle cells of arteries and arterioles, as well as in smooth muscle cells of vasa rectae in the medullary area. Expressed in the adventitial connective tissue surrounding the suprarenal artery. In chronic obstructive nephropathy, a persistent expression is seen in glomerular visceral epithelial cells and vascular smooth muscle cells, as well as de novo expression by periglomerular interstitial cells and by some neointimal cells of atherosclerotic vessels. Expression in normal prostate is seen preferentially in the mesenchyme of the gland while expression is increased and more profuse in prostate carcinoma. Expressed in many ovarian, lung, renal and brain cancer-derived cell lines.7 Publications

    Developmental stagei

    Not detectable in the earliest stages of glomerulogenesis, and not detected in the metanephric blastema or surrounding cortical interstitial cells. In later stages of glomerulogenesis, localized to epithelial cells transitioning from the early developing nephrons of the comma- and S-shaped stages to the visceral epithelial cells of differentiated glomeruli. In the developing pelvis, expressed at the basement membrane of immature collecting ducts and by presumptive fibroblastic cells in the interstitium.1 Publication

    Gene expression databases

    ArrayExpressiQ9GZP0.
    BgeeiQ9GZP0.
    CleanExiHS_PDGFD.
    GenevestigatoriQ9GZP0.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked. Interacts with PDGFRB homodimers, and with heterodimers formed by PDGFRA and PDGFRB.2 Publications

    Protein-protein interaction databases

    BioGridi123223. 1 interaction.
    STRINGi9606.ENSP00000376865.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9GZP0.
    SMRiQ9GZP0. Positions 61-171.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini52 – 170119CUBPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the PDGF/VEGF growth factor family.Curated
    Contains 1 CUB domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG148355.
    HOGENOMiHOG000261610.
    HOVERGENiHBG057324.
    InParanoidiQ9GZP0.
    KOiK05450.
    OMAiHYRGRSY.
    OrthoDBiEOG7VB2FN.
    PhylomeDBiQ9GZP0.
    TreeFamiTF332130.

    Family and domain databases

    Gene3Di2.10.90.10. 1 hit.
    2.60.120.290. 1 hit.
    InterProiIPR000859. CUB_dom.
    IPR029034. Cystine-knot_cytokine.
    IPR000072. PDGF/VEGF_dom.
    IPR027123. PDGFD.
    [Graphical view]
    PANTHERiPTHR10127:SF13. PTHR10127:SF13. 1 hit.
    PfamiPF00431. CUB. 1 hit.
    PF00341. PDGF. 1 hit.
    [Graphical view]
    SMARTiSM00042. CUB. 1 hit.
    SM00141. PDGF. 1 hit.
    [Graphical view]
    SUPFAMiSSF49854. SSF49854. 1 hit.
    SSF57501. SSF57501. 1 hit.
    PROSITEiPS01180. CUB. 1 hit.
    PS50278. PDGF_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9GZP0-1) [UniParc]FASTAAdd to Basket

    Also known as: Long, SCDGF-B-L

    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

    MHRLIFVYTL ICANFCSCRD TSATPQSASI KALRNANLRR DESNHLTDLY    50
    RRDETIQVKG NGYVQSPRFP NSYPRNLLLT WRLHSQENTR IQLVFDNQFG 100
    LEEAENDICR YDFVEVEDIS ETSTIIRGRW CGHKEVPPRI KSRTNQIKIT 150
    FKSDDYFVAK PGFKIYYSLL EDFQPAAASE TNWESVTSSI SGVSYNSPSV 200
    TDPTLIADAL DKKIAEFDTV EDLLKYFNPE SWQEDLENMY LDTPRYRGRS 250
    YHDRKSKVDL DRLNDDAKRY SCTPRNYSVN IREELKLANV VFFPRCLLVQ 300
    RCGGNCGCGT VNWRSCTCNS GKTVKKYHEV LQFEPGHIKR RGRAKTMALV 350
    DIQLDHHERC DCICSSRPPR 370
    Length:370
    Mass (Da):42,848
    Last modified:March 1, 2001 - v1
    Checksum:iD387F485E7BB7674
    GO
    Isoform 2 (identifier: Q9GZP0-2) [UniParc]FASTAAdd to Basket

    Also known as: Short, SCDGF-B-S

    The sequence of this isoform differs from the canonical sequence as follows:
         42-47: Missing.

    Show »
    Length:364
    Mass (Da):42,167
    Checksum:i245C53E8DDEA9EAC
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti190 – 1901I → V.
    Corresponds to variant rs35045740 [ dbSNP | Ensembl ].
    VAR_051563
    Natural varianti202 – 2021D → Y in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036418

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei42 – 476Missing in isoform 2. 4 PublicationsVSP_020615

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB033832 mRNA. Translation: BAB18903.1.
    AF336376 mRNA. Translation: AAK56136.1.
    AF335584 mRNA. Translation: AAK38840.1.
    AY027517 mRNA. Translation: AAK20081.1.
    AY027518 mRNA. Translation: AAK20082.1.
    AF113216 mRNA. Translation: AAG39287.1.
    AY359116 mRNA. Translation: AAQ89474.1.
    AK292801 mRNA. Translation: BAF85490.1.
    CH471065 Genomic DNA. Translation: EAW67045.1.
    BC030645 mRNA. Translation: AAH30645.1.
    CCDSiCCDS41703.1. [Q9GZP0-1]
    CCDS8326.1. [Q9GZP0-2]
    PIRiJC7591.
    RefSeqiNP_079484.1. NM_025208.4. [Q9GZP0-1]
    NP_149126.1. NM_033135.3. [Q9GZP0-2]
    UniGeneiHs.352298.

    Genome annotation databases

    EnsembliENST00000302251; ENSP00000302193; ENSG00000170962. [Q9GZP0-2]
    ENST00000393158; ENSP00000376865; ENSG00000170962. [Q9GZP0-1]
    GeneIDi80310.
    KEGGihsa:80310.
    UCSCiuc001php.3. human. [Q9GZP0-2]
    uc001phq.3. human. [Q9GZP0-1]

    Polymorphism databases

    DMDMi74717921.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB033832 mRNA. Translation: BAB18903.1 .
    AF336376 mRNA. Translation: AAK56136.1 .
    AF335584 mRNA. Translation: AAK38840.1 .
    AY027517 mRNA. Translation: AAK20081.1 .
    AY027518 mRNA. Translation: AAK20082.1 .
    AF113216 mRNA. Translation: AAG39287.1 .
    AY359116 mRNA. Translation: AAQ89474.1 .
    AK292801 mRNA. Translation: BAF85490.1 .
    CH471065 Genomic DNA. Translation: EAW67045.1 .
    BC030645 mRNA. Translation: AAH30645.1 .
    CCDSi CCDS41703.1. [Q9GZP0-1 ]
    CCDS8326.1. [Q9GZP0-2 ]
    PIRi JC7591.
    RefSeqi NP_079484.1. NM_025208.4. [Q9GZP0-1 ]
    NP_149126.1. NM_033135.3. [Q9GZP0-2 ]
    UniGenei Hs.352298.

    3D structure databases

    ProteinModelPortali Q9GZP0.
    SMRi Q9GZP0. Positions 61-171.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123223. 1 interaction.
    STRINGi 9606.ENSP00000376865.

    PTM databases

    PhosphoSitei Q9GZP0.

    Polymorphism databases

    DMDMi 74717921.

    Proteomic databases

    PaxDbi Q9GZP0.
    PRIDEi Q9GZP0.

    Protocols and materials databases

    DNASUi 80310.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000302251 ; ENSP00000302193 ; ENSG00000170962 . [Q9GZP0-2 ]
    ENST00000393158 ; ENSP00000376865 ; ENSG00000170962 . [Q9GZP0-1 ]
    GeneIDi 80310.
    KEGGi hsa:80310.
    UCSCi uc001php.3. human. [Q9GZP0-2 ]
    uc001phq.3. human. [Q9GZP0-1 ]

    Organism-specific databases

    CTDi 80310.
    GeneCardsi GC11M103777.
    HGNCi HGNC:30620. PDGFD.
    MIMi 609673. gene.
    neXtProti NX_Q9GZP0.
    PharmGKBi PA134892327.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG148355.
    HOGENOMi HOG000261610.
    HOVERGENi HBG057324.
    InParanoidi Q9GZP0.
    KOi K05450.
    OMAi HYRGRSY.
    OrthoDBi EOG7VB2FN.
    PhylomeDBi Q9GZP0.
    TreeFami TF332130.

    Enzyme and pathway databases

    Reactomei REACT_16888. Signaling by PDGF.
    SignaLinki Q9GZP0.

    Miscellaneous databases

    ChiTaRSi PDGFD. human.
    GeneWikii PDGFD.
    GenomeRNAii 80310.
    NextBioi 70792.
    PMAP-CutDB Q9GZP0.
    PROi Q9GZP0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9GZP0.
    Bgeei Q9GZP0.
    CleanExi HS_PDGFD.
    Genevestigatori Q9GZP0.

    Family and domain databases

    Gene3Di 2.10.90.10. 1 hit.
    2.60.120.290. 1 hit.
    InterProi IPR000859. CUB_dom.
    IPR029034. Cystine-knot_cytokine.
    IPR000072. PDGF/VEGF_dom.
    IPR027123. PDGFD.
    [Graphical view ]
    PANTHERi PTHR10127:SF13. PTHR10127:SF13. 1 hit.
    Pfami PF00431. CUB. 1 hit.
    PF00341. PDGF. 1 hit.
    [Graphical view ]
    SMARTi SM00042. CUB. 1 hit.
    SM00141. PDGF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49854. SSF49854. 1 hit.
    SSF57501. SSF57501. 1 hit.
    PROSITEi PS01180. CUB. 1 hit.
    PS50278. PDGF_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of SCDGF-B, a novel growth factor homologous to SCDGF/PDGF-C/fallotein."
      Hamada T., Ui-Tei K., Imaki J., Miyata Y.
      Biochem. Biophys. Res. Commun. 280:733-737(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    2. "PDGF-D is a specific, protease-activated ligand for the PDGF beta-receptor."
      Bergsten E., Uutela M., Li X., Pietras K., Oestman A., Heldin C.-H., Alitalo K., Eriksson U.
      Nat. Cell Biol. 3:512-516(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, TISSUE SPECIFICITY.
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    4. "Expressed sequence tag analysis of adult human iris for the NEIBank project: steroid-response factors and similarities with retinal pigment epithelium."
      Wistow G., Bernstein S.L., Ray S., Wyatt M.K., Behal A., Touchman J.W., Bouffard G., Smith D., Peterson K.
      Mol. Vis. 8:185-195(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
      Tissue: Iris.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Aorta.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    7. "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 1).
      Tissue: Trachea.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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 2).
      Tissue: Testis.
    10. "Platelet-derived growth factor-D expression in developing and mature human kidneys."
      Changsirikulchai S., Hudkins K.L., Goodpaster T.A., Volpone J., Topouzis S., Gilbertson D.G., Alpers C.E.
      Kidney Int. 62:2043-2054(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 64-369, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    11. "Chromosomal location, exon structure, and vascular expression patterns of the human PDGFC and PDGFC genes."
      Uutela M., Lauren J., Bergsten E., Li X., Horelli-Kuitunen N., Eriksson U., Alitalo K.
      Circulation 103:2242-2247(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    12. "Platelet-derived growth factor D: tumorigenicity in mice and dysregulated expression in human cancer."
      LaRochelle W.J., Jeffers M., Corvalan J.R.F., Jia X.-C., Feng X., Vanegas S., Vickroy J.D., Yang X.-D., Chen F., Gazit G., Mayotte J., Macaluso J., Rittman B., Wu F., Dhanabal M., Herrmann J., Lichenstein H.S.
      Cancer Res. 62:2468-2473(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    13. "Obstructive uropathy in mice and humans: potential role for PDGF-D in the progression of tubulointerstitial injury."
      Taneda S., Hudkins K.L., Topouzis S., Gilbertson D.G., Ophascharoensuk V., Truong L., Johnson R.J., Alpers C.E.
      J. Am. Soc. Nephrol. 14:2544-2555(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    14. "PDGF-D induces macrophage recruitment, increased interstitial pressure, and blood vessel maturation during angiogenesis."
      Uutela M., Wirzenius M., Paavonen K., Rajantie I., He Y., Karpanen T., Lohela M., Wiig H., Salven P., Pajusola K., Eriksson U., Alitalo K.
      Blood 104:3198-3204(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "Structural and functional specificities of PDGF-C and PDGF-D, the novel members of the platelet-derived growth factors family."
      Reigstad L.J., Varhaug J.E., Lillehaug J.R.
      FEBS J. 272:5723-5741(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    16. "Platelet-derived growth factor D is activated by urokinase plasminogen activator in prostate carcinoma cells."
      Ustach C.V., Kim H.-R.C.
      Mol. Cell. Biol. 25:6279-6288(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, PTM, MUTAGENESIS OF ARG-247 AND ARG-249.
    17. "Emerging roles of PDGF-D signaling pathway in tumor development and progression."
      Wang Z., Ahmad A., Li Y., Kong D., Azmi A.S., Banerjee S., Sarkar F.H.
      Biochim. Biophys. Acta 1806:122-130(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    18. Cited for: VARIANT [LARGE SCALE ANALYSIS] TYR-202.

    Entry informationi

    Entry nameiPDGFD_HUMAN
    AccessioniPrimary (citable) accession number: Q9GZP0
    Secondary accession number(s): A8K9T6, Q9BWV5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2006
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 105 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3