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Q9GZP0

- PDGFD_HUMAN

UniProt

Q9GZP0 - PDGFD_HUMAN

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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

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ9GZP0.
CleanExiHS_PDGFD.
ExpressionAtlasiQ9GZP0. baseline and differential.
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.
GeneTreeiENSGT00390000005171.
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

        10         20         30         40         50
MHRLIFVYTL ICANFCSCRD TSATPQSASI KALRNANLRR DESNHLTDLY
60 70 80 90 100
RRDETIQVKG NGYVQSPRFP NSYPRNLLLT WRLHSQENTR IQLVFDNQFG
110 120 130 140 150
LEEAENDICR YDFVEVEDIS ETSTIIRGRW CGHKEVPPRI KSRTNQIKIT
160 170 180 190 200
FKSDDYFVAK PGFKIYYSLL EDFQPAAASE TNWESVTSSI SGVSYNSPSV
210 220 230 240 250
TDPTLIADAL DKKIAEFDTV EDLLKYFNPE SWQEDLENMY LDTPRYRGRS
260 270 280 290 300
YHDRKSKVDL DRLNDDAKRY SCTPRNYSVN IREELKLANV VFFPRCLLVQ
310 320 330 340 350
RCGGNCGCGT VNWRSCTCNS GKTVKKYHEV LQFEPGHIKR RGRAKTMALV
360 370
DIQLDHHERC DCICSSRPPR
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.
GeneTreei ENSGT00390000005171.
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

Bgeei Q9GZP0.
CleanExi HS_PDGFD.
ExpressionAtlasi Q9GZP0. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 106 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