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Q9NRA1

- PDGFC_HUMAN

UniProt

Q9NRA1 - PDGFC_HUMAN

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Protein

Platelet-derived growth factor C

Gene
PDGFC, SCDGF, UNQ174/PRO200
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 and chemoattractant for cells of mesenchymal origin. Required for normal skeleton formation during embryonic development, especially for normal development of the craniofacial skeleton and for normal development of the palate. Required for normal skin morphogenesis during embryonic development. Plays an important role in wound healing, where it appears to be involved in three stages: inflammation, proliferation and remodeling. Plays an important role in angiogenesis and blood vessel development. Involved in fibrotic processes, in which transformation of interstitial fibroblasts into myofibroblasts plus collagen deposition occurs. The CUB domain has mitogenic activity in coronary artery smooth muscle cells, suggesting a role beyond the maintenance of the latency of the PDGF domain. In the nucleus, PDGFC seems to have additional function.12 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei225 – 2262Cleavage
Sitei231 – 2322Cleavage Reviewed prediction
Sitei234 – 2352Cleavage Reviewed prediction

GO - Molecular functioni

  1. platelet-derived growth factor receptor binding Source: BHF-UCL
  2. protein binding Source: IntAct
  3. protein homodimerization activity Source: BHF-UCL

GO - Biological processi

  1. activation of transmembrane receptor protein tyrosine kinase activity Source: Ensembl
  2. cellular response to amino acid stimulus Source: Ensembl
  3. central nervous system development Source: UniProtKB
  4. organ morphogenesis Source: Ensembl
  5. platelet-derived growth factor receptor signaling pathway Source: BHF-UCL
  6. positive regulation of cell division Source: UniProtKB-KW
  7. positive regulation of DNA replication Source: BHF-UCL
  8. positive regulation of fibroblast proliferation Source: BHF-UCL
  9. 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.
SignaLinkiQ9NRA1.

Names & Taxonomyi

Protein namesi
Recommended name:
Platelet-derived growth factor C
Short name:
PDGF-C
Alternative name(s):
Fallotein
Spinal cord-derived growth factor
Short name:
SCDGF
VEGF-E
Cleaved into the following 2 chains:
Platelet-derived growth factor C, receptor-binding form
Short name:
PDGFC receptor-binding form
Gene namesi
Name:PDGFC
Synonyms:SCDGF
ORF Names:UNQ174/PRO200
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:8801. PDGFC.

Subcellular locationi

Cytoplasm. Secreted. Nucleus. Cytoplasmic granule
Note: Sumoylated form is predominant in the nucleus. Stored in alpha granules in platelets. Membrane associated when bound to receptors.7 Publications

GO - Cellular componenti

  1. cell surface Source: BHF-UCL
  2. cytoplasm Source: HPA
  3. endoplasmic reticulum lumen Source: Reactome
  4. extracellular region Source: Reactome
  5. extracellular space Source: BHF-UCL
  6. extracellular vesicular exosome Source: UniProt
  7. Golgi membrane Source: Reactome
  8. nucleus Source: UniProtKB-SubCell
  9. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi124 – 1241C → S: Loss of mitogenic activity of CUB domain in coronary artery smooth muscle cells. 1 Publication
Mutagenesisi231 – 2311R → A: Essential for cleavage by PLAT. 1 Publication
Mutagenesisi232 – 2321K → A: Not essential for cleavage by PLAT. 1 Publication
Mutagenesisi234 – 2341R → A: Not essential for cleavage by PLAT. 1 Publication

Organism-specific databases

PharmGKBiPA33146.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 345Platelet-derived growth factor C, receptor-binding formPRO_0000343872
Signal peptidei1 – 2222 Reviewed predictionAdd
BLAST
Chaini23 – 345323Platelet-derived growth factor C, latent formPRO_0000343871Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi25 – 251N-linked (GlcNAc...) Reviewed prediction
Glycosylationi55 – 551N-linked (GlcNAc...) By similarity
Disulfide bondi104 ↔ 124 By similarity
Disulfide bondi250 ↔ 294 Inferred
Disulfide bondi274 – 274Interchain (with C-286) Inferred
Disulfide bondi280 ↔ 335 Inferred
Disulfide bondi286 – 286Interchain (with C-274) Inferred
Disulfide bondi287 ↔ 337 Inferred

Post-translational modificationi

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 basic residues in the hinge region (region connecting the CUB and growth factor domains) gives rise to the receptor-binding form. Cleaved by PLAT and PLG.
Sumoylated with SUMO1.1 Publication
N-glycosylated.1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9NRA1.
PRIDEiQ9NRA1.

PTM databases

PhosphoSiteiQ9NRA1.

Expressioni

Tissue specificityi

Expressed in the fallopian tube, vascular smooth muscle cells in kidney, breast and colon and in visceral smooth muscle of the gastrointestinal tract. Highly expressed in retinal pigment epithelia. Expressed in medulloblastoma. In the kidney, constitutively expressed in parietal epithelial cells of Bowman's capsule, tubular epithelial cells and in arterial endothelial cells (at protein level). Highly expressed in the platelets, prostate, testis and uterus. Higher expression is observed in uterine leiomyomata. Weaker expression in the spleen, thymus, heart, pancreas, liver, ovary cells and small intestine, and negligible expression in the colon and peripheral blood leukocytes.9 Publications

Developmental stagei

In the fetal kidney, detected in the developing mesangium, ureteric bud epithelium and the undifferentiated mesenchyme (at protein level).1 Publication

Inductioni

Up-regulated by EWS-FLI1 chimeric transcription factor in tumor derived cells. Up-regulated in podocytes and interstitial cells after injury/activation of these cells. FGF2 activates PDGFC transcription via EGR1. Up-regulated by TGFB1 in concert with FGF2.4 Publications

Gene expression databases

ArrayExpressiQ9NRA1.
BgeeiQ9NRA1.
CleanExiHS_PDGFC.
GenevestigatoriQ9NRA1.

Organism-specific databases

HPAiHPA009134.

Interactioni

Subunit structurei

Homodimer; disulfide-linked. Interacts with PDGFRA homodimers, and with heterodimers formed by PDGFRA and PDGFRB. Interacts (via CUB domain) with PLAT (via kringle domain).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PDGFRAP162342EBI-8833587,EBI-2861522

Protein-protein interaction databases

BioGridi121032. 5 interactions.
DIPiDIP-59339N.
IntActiQ9NRA1. 1 interaction.
STRINGi9606.ENSP00000274071.

Structurei

3D structure databases

ProteinModelPortaliQ9NRA1.
SMRiQ9NRA1. Positions 49-198.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 163118CUBAdd
BLAST

Sequence similaritiesi

Contains 1 CUB domain.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG74970.
HOGENOMiHOG000185996.
HOVERGENiHBG057324.
InParanoidiQ9NRA1.
KOiK05450.
OMAiDCVCRGN.
OrthoDBiEOG7VB2FN.
PhylomeDBiQ9NRA1.
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.
[Graphical view]
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 (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NRA1-1) [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

MSLFGLLLLT SALAGQRQGT QAESNLSSKF QFSSNKEQNG VQDPQHERII    50
TVSTNGSIHS PRFPHTYPRN TVLVWRLVAV EENVWIQLTF DERFGLEDPE 100
DDICKYDFVE VEEPSDGTIL GRWCGSGTVP GKQISKGNQI RIRFVSDEYF 150
PSEPGFCIHY NIVMPQFTEA VSPSVLPPSA LPLDLLNNAI TAFSTLEDLI 200
RYLEPERWQL DLEDLYRPTW QLLGKAFVFG RKSRVVDLNL LTEEVRLYSC 250
TPRNFSVSIR EELKRTDTIF WPGCLLVKRC GGNCACCLHN CNECQCVPSK 300
VTKKYHEVLQ LRPKTGVRGL HKSLTDVALE HHEECDCVCR GSTGG 345
Length:345
Mass (Da):39,029
Last modified:July 22, 2008 - v2
Checksum:iCDE9E51F40633E78
GO
Isoform 2 (identifier: Q9NRA1-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     244-306: Missing.

Note: No experimental confirmation available.

Show »
Length:282
Mass (Da):31,808
Checksum:i8426CEB8FF9AA45B
GO
Isoform 3 (identifier: Q9NRA1-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     155-167: GFCIHYNIVMPQF → SNRGGKIIQLHTS
     168-345: Missing.

Note: No experimental confirmation available.

Show »
Length:167
Mass (Da):18,784
Checksum:i60023851D9FE5E65
GO
Isoform 4 (identifier: Q9NRA1-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-163: Missing.

Note: No experimental confirmation available.

Show »
Length:182
Mass (Da):20,609
Checksum:iF5B9733D3794B1B7
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 163163Missing in isoform 4. VSP_047606Add
BLAST
Alternative sequencei155 – 16713GFCIH…VMPQF → SNRGGKIIQLHTS in isoform 3. VSP_034701Add
BLAST
Alternative sequencei168 – 345178Missing in isoform 3. VSP_034702Add
BLAST
Alternative sequencei244 – 30663Missing in isoform 2. VSP_034703Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91L → V in AAF80597. 1 Publication
Sequence conflicti18 – 181Q → R in AAF80597. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF091434 mRNA. Translation: AAF00049.1.
AB033831 mRNA. Translation: BAB03266.1.
AF244813 mRNA. Translation: AAF80597.1.
AF260738 mRNA. Translation: AAK51637.1.
AM922296 mRNA. Translation: CAP58278.1.
AY358493 mRNA. Translation: AAQ88857.1.
AK300480 mRNA. Translation: BAG62196.1.
AC092608 Genomic DNA. Translation: AAY40906.1.
AC093325 Genomic DNA. No translation available.
CH471056 Genomic DNA. Translation: EAX04874.1.
CH471056 Genomic DNA. Translation: EAX04875.1.
BC136662 mRNA. Translation: AAI36663.1.
CCDSiCCDS3795.1. [Q9NRA1-1]
RefSeqiNP_057289.1. NM_016205.2. [Q9NRA1-1]
UniGeneiHs.570855.

Genome annotation databases

EnsembliENST00000422544; ENSP00000410048; ENSG00000145431. [Q9NRA1-2]
ENST00000502773; ENSP00000422464; ENSG00000145431. [Q9NRA1-1]
ENST00000541126; ENSP00000442943; ENSG00000145431. [Q9NRA1-4]
GeneIDi56034.
KEGGihsa:56034.
UCSCiuc003iph.2. human. [Q9NRA1-1]

Polymorphism databases

DMDMi205830662.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF091434 mRNA. Translation: AAF00049.1 .
AB033831 mRNA. Translation: BAB03266.1 .
AF244813 mRNA. Translation: AAF80597.1 .
AF260738 mRNA. Translation: AAK51637.1 .
AM922296 mRNA. Translation: CAP58278.1 .
AY358493 mRNA. Translation: AAQ88857.1 .
AK300480 mRNA. Translation: BAG62196.1 .
AC092608 Genomic DNA. Translation: AAY40906.1 .
AC093325 Genomic DNA. No translation available.
CH471056 Genomic DNA. Translation: EAX04874.1 .
CH471056 Genomic DNA. Translation: EAX04875.1 .
BC136662 mRNA. Translation: AAI36663.1 .
CCDSi CCDS3795.1. [Q9NRA1-1 ]
RefSeqi NP_057289.1. NM_016205.2. [Q9NRA1-1 ]
UniGenei Hs.570855.

3D structure databases

ProteinModelPortali Q9NRA1.
SMRi Q9NRA1. Positions 49-198.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121032. 5 interactions.
DIPi DIP-59339N.
IntActi Q9NRA1. 1 interaction.
STRINGi 9606.ENSP00000274071.

PTM databases

PhosphoSitei Q9NRA1.

Polymorphism databases

DMDMi 205830662.

Proteomic databases

PaxDbi Q9NRA1.
PRIDEi Q9NRA1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000422544 ; ENSP00000410048 ; ENSG00000145431 . [Q9NRA1-2 ]
ENST00000502773 ; ENSP00000422464 ; ENSG00000145431 . [Q9NRA1-1 ]
ENST00000541126 ; ENSP00000442943 ; ENSG00000145431 . [Q9NRA1-4 ]
GeneIDi 56034.
KEGGi hsa:56034.
UCSCi uc003iph.2. human. [Q9NRA1-1 ]

Organism-specific databases

CTDi 56034.
GeneCardsi GC04M157682.
HGNCi HGNC:8801. PDGFC.
HPAi HPA009134.
MIMi 608452. gene.
neXtProti NX_Q9NRA1.
PharmGKBi PA33146.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG74970.
HOGENOMi HOG000185996.
HOVERGENi HBG057324.
InParanoidi Q9NRA1.
KOi K05450.
OMAi DCVCRGN.
OrthoDBi EOG7VB2FN.
PhylomeDBi Q9NRA1.
TreeFami TF332130.

Enzyme and pathway databases

Reactomei REACT_16888. Signaling by PDGF.
SignaLinki Q9NRA1.

Miscellaneous databases

GeneWikii PDGFC.
GenomeRNAii 56034.
NextBioi 35475084.
PROi Q9NRA1.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9NRA1.
Bgeei Q9NRA1.
CleanExi HS_PDGFC.
Genevestigatori Q9NRA1.

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.
[Graphical view ]
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. "Identification of a novel platelet-derived growth factor-like gene, fallotein, in the human reproductive tract."
    Tsai Y.J., Lee R.K., Lin S.P., Chen Y.H.
    Biochim. Biophys. Acta 1492:196-202(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Uterus.
  2. "A novel gene derived from developing spinal cords, SCDGF, is a unique member of the PDGF/VEGF family."
    Hamada T., Ui-Tei K., Miyata Y.
    FEBS Lett. 475:97-102(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION.
    Tissue: Brain.
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    Tissue: Lung.
  4. "Platelet-derived growth factor C (PDGF-C), a novel growth factor that binds to PDGF alpha and beta receptor."
    Gilbertson D.G., Duff M.E., West J.W., Kelly J.D., Sheppard P.O., Hofstrand P.D., Gao Z., Shoemaker K., Bukowski T.R., Moore M., Feldhaus A.L., Humes J.M., Palmer T.E., Hart C.E.
    J. Biol. Chem. 276:27406-27414(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  5. "An N-terminally truncated isoform of human PDGF-C regulates the secretion of full-length PDGF-C and is deregulated in renal cell carcinoma."
    Zhao J., Liu Z., Liu T., Nilsson S., Nister M.
    Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
    Tissue: Fetal brain.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  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 4).
    Tissue: Prostate.
  8. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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: Testis.
  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. "PDGF-C is an EWS/FLI induced transforming growth factor in Ewing family tumors."
    Zwerner J.P., May W.A.
    Oncogene 20:626-633(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  13. "Platelet-derived growth factor-B and -C and active alpha-receptors in medulloblastoma cells."
    Andrae J., Molander C., Smits A., Funa K., Nister M.
    Biochem. Biophys. Res. Commun. 296:604-611(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  14. "Characterization of platelet-derived growth factor-C (PDGF-C): expression in normal and tumor cells, biological activity and chromosomal localization."
    Dijkmans J., Xu J., Masure S., Dhanaraj S., Gosiewska A., Geesin J., Sprengel J., Harris S., Verhasselt P., Gordon R., Yon J.
    Int. J. Biochem. Cell Biol. 34:414-426(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, ALTERNATIVE SPLICING (ISOFORMS 2 AND 3), GLYCOSYLATION, MUTAGENESIS OF CYS-124.
  15. "Dominant negative PDGF-C inhibits growth of Ewing family tumor cell lines."
    Zwerner J.P., May W.A.
    Oncogene 21:3847-3854(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "PDGF-C expression in the developing and normal adult human kidney and in glomerular diseases."
    Eitner F., Ostendorf T., Kretzler M., Cohen C.D., Eriksson U., Grone H.J., Floege J.
    J. Am. Soc. Nephrol. 14:1145-1153(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE, INDUCTION.
  17. "Platelet-derived growth factor (PDGF)-C, a PDGF family member with a vascular endothelial growth factor-like structure."
    Reigstad L.J., Sande H.M., Fluge O., Bruland O., Muga A., Varhaug J.E., Martinez A., Lillehaug J.R.
    J. Biol. Chem. 278:17114-17120(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF SECRETED ACTIVE FORM, SUBUNIT, DISULFIDE BONDS, 3D-STRUCTURE MODELING.
  18. "PDGF C is a selective alpha platelet-derived growth factor receptor agonist that is highly expressed in platelet alpha granules and vascular smooth muscle."
    Fang L., Yan Y., Komuves L.G., Yonkovich S., Sullivan C.M., Stringer B., Galbraith S., Lokker N.A., Hwang S.S., Nurden P., Phillips D.R., Giese N.A.
    Arterioscler. Thromb. Vasc. Biol. 24:787-792(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  19. "Tissue plasminogen activator is a potent activator of PDGF-CC."
    Fredriksson L., Li H., Fieber C., Li X., Eriksson U.
    EMBO J. 23:3793-3802(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PLAT.
  20. "Fibroblast growth factor-2 induction of platelet-derived growth factor-C chain transcription in vascular smooth muscle cells is ERK-dependent but not JNK-dependent and mediated by Egr-1."
    Midgley V.C., Khachigian L.M.
    J. Biol. Chem. 279:40289-40295(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY EGR1.
  21. "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.
  22. "Structural requirements for activation of latent platelet-derived growth factor CC by tissue plasminogen activator."
    Fredriksson L., Ehnman M., Fieber C., Eriksson U.
    J. Biol. Chem. 280:26856-26862(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PLAT, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-231; LYS-232 AND ARG-234.
  23. "Regulation of fibrogenic/fibrolytic genes by platelet-derived growth factor C, a novel growth factor, in human dermal fibroblasts."
    Jinnin M., Ihn H., Mimura Y., Asano Y., Yamane K., Tamaki K.
    J. Cell. Physiol. 202:510-517(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  24. Cited for: FUNCTION.
  25. "Fibroblast growth factor 2 and transforming growth factor beta1 synergism in human bronchial smooth muscle cell proliferation."
    Bosse Y., Thompson C., Stankova J., Rola-Pleszczynski M.
    Am. J. Respir. Cell Mol. Biol. 34:746-753(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  26. "Nuclear localisation of endogenous SUMO-1-modified PDGF-C in human thyroid tissue and cell lines."
    Reigstad L.J., Martinez A., Varhaug J.E., Lillehaug J.R.
    Exp. Cell Res. 312:782-795(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, SUMOYLATION.
  27. "PDGF-C and -D induced proliferation/migration of human RPE is abolished by inflammatory cytokines."
    Li R., Maminishkis A., Wang F.E., Miller S.S.
    Invest. Ophthalmol. Vis. Sci. 48:5722-5732(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  28. "Increased expression of platelet-derived growth factor C messenger ribonucleic acid in uterine leiomyomata."
    Hwu Y.M., Li S.H., Lee R.K., Tsai Y.H., Yeh T.S., Lin S.Y.
    Fertil. Steril. 89:468-471(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  29. "Plasmin is the major protease responsible for processing PDGF-C in the vitreous of patients with proliferative vitreoretinopathy."
    Lei H., Velez G., Hovland P., Hirose T., Kazlauskas A.
    Invest. Ophthalmol. Vis. Sci. 49:42-48(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE BY PLG.

Entry informationi

Entry nameiPDGFC_HUMAN
AccessioniPrimary (citable) accession number: Q9NRA1
Secondary accession number(s): B4DU34
, B9EGR8, Q4W5M9, Q9UL22
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: July 22, 2008
Last modified: September 3, 2014
This is version 97 of the entry and version 2 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

Miscellaneous

A lower molecular weight form (around 43 kDa) is present in patients with papillary thyroid carcinoma.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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