Q9GZP0 (PDGFD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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:

1. Platelet-derived growth factor D, latent form
   Short name=PDGFD latent form
2. Platelet-derived growth factor D, receptor-binding form
   Short name=PDGFD receptor-binding form

Gene names

Name:	PDGFD
Synonyms:	IEGF, SCDGFB
ORF Names:	MSTP036, UNQ1899/PRO4345

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	370 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.2 Ref.14
Subunit structure	Homodimer; disulfide-linked. Interacts with PDGFRB homodimers, and with heterodimers formed by PDGFRA and PDGFRB. Ref.2 Ref.3
Subcellular location	Secreted. Note: Released by platelets upon wounding. Ref.3
Tissue specificity	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. Ref.2 Ref.3 Ref.10 Ref.11 Ref.12 Ref.13 Ref.16
Developmental stage	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. Ref.10
Post-translational modification	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.
Sequence similarities	Belongs to the PDGF/VEGF growth factor family. Contains 1 CUB domain.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Proto-oncogene
Domain	Signal
Molecular function	Developmental protein Growth factor Mitogen
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to amino acid stimulus Inferred from electronic annotation. Source: Compara multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of cell division Inferred from electronic annotation. Source: UniProtKB-KW regulation of peptidyl-tyrosine phosphorylation Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi membrane Traceable author statement. Source: Reactome endoplasmic reticulum lumen Traceable author statement. Source: Reactome extracellular region Traceable author statement. Source: Reactome
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q9GZP0-1)

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.

Isoform 2 (identifier: Q9GZP0-2)

Also known as: Short; SCDGF-B-S;

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18	Potential
	Chain	19 – 370	352	Platelet-derived growth factor D, latent form		PRO_0000250188
	Chain	250 – 370	121	Platelet-derived growth factor D, receptor-binding form Potential		PRO_0000250189
Regions
	Domain	52 – 170	119	CUB
Sites
	Site	247 – 248	2	Cleavage Potential
	Site	249 – 250	2	Cleavage Potential
Amino acid modifications
	Glycosylation	276	1	N-linked (GlcNAc...) Potential
	Disulfide bond	109 ↔ 131		By similarity
	Disulfide bond	296		Interchain By similarity
	Disulfide bond	302 ↔ 360		By similarity
	Disulfide bond	306 ↔ 362		By similarity
Natural variations
	Alternative sequence	42 – 47	6	Missing in isoform 2.		VSP_020615
	Natural variant	190	1	I → V. Corresponds to variant rs35045740 [ dbSNP | Ensembl ].		VAR_051563
	Natural variant	202	1	D → Y in a colorectal cancer sample; somatic mutation. Ref.18		VAR_036418
Experimental info
	Mutagenesis	247	1	R → A: Abolishes cleavage into active form; when associated with A-249. Ref.16
	Mutagenesis	249	1	R → A: Abolishes cleavage into active form; when associated with A-247. Ref.16

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Long) (SCDGF-B-L) [UniParc]. Last modified March 1, 2001. Version 1. Checksum: D387F485E7BB7674	FASTA	370	42,848
	10 20 30 40 50 60 MHRLIFVYTL ICANFCSCRD TSATPQSASI KALRNANLRR DESNHLTDLY RRDETIQVKG 70 80 90 100 110 120 NGYVQSPRFP NSYPRNLLLT WRLHSQENTR IQLVFDNQFG LEEAENDICR YDFVEVEDIS 130 140 150 160 170 180 ETSTIIRGRW CGHKEVPPRI KSRTNQIKIT FKSDDYFVAK PGFKIYYSLL EDFQPAAASE 190 200 210 220 230 240 TNWESVTSSI SGVSYNSPSV TDPTLIADAL DKKIAEFDTV EDLLKYFNPE SWQEDLENMY 250 260 270 280 290 300 LDTPRYRGRS YHDRKSKVDL DRLNDDAKRY SCTPRNYSVN IREELKLANV VFFPRCLLVQ 310 320 330 340 350 360 RCGGNCGCGT VNWRSCTCNS GKTVKKYHEV LQFEPGHIKR RGRAKTMALV DIQLDHHERC 370 DCICSSRPPR
	Isoform 2 (Short) (SCDGF-B-S) [UniParc]. Checksum: 245C53E8DDEA9EAC	FASTA	364	42,167
	10 20 30 40 50 60 MHRLIFVYTL ICANFCSCRD TSATPQSASI KALRNANLRR DDLYRRDETI QVKGNGYVQS 70 80 90 100 110 120 PRFPNSYPRN LLLTWRLHSQ ENTRIQLVFD NQFGLEEAEN DICRYDFVEV EDISETSTII 130 140 150 160 170 180 RGRWCGHKEV PPRIKSRTNQ IKITFKSDDY FVAKPGFKIY YSLLEDFQPA AASETNWESV 190 200 210 220 230 240 TSSISGVSYN SPSVTDPTLI ADALDKKIAE FDTVEDLLKY FNPESWQEDL ENMYLDTPRY 250 260 270 280 290 300 RGRSYHDRKS KVDLDRLNDD AKRYSCTPRN YSVNIREELK LANVVFFPRC LLVQRCGGNC 310 320 330 340 350 360 GCGTVNWRSC TCNSGKTVKK YHEVLQFEPG HIKRRGRAKT MALVDIQLDH HERCDCICSS RPPR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"PDGF D, a novel protease-activated growth factor." LaRochelle W.J., Jeffers M., McDonald W.F., Chillakuru R.A., Giese N.A., Lokker N.A., Sullivan C., Boldog F.L., Yang M., Vernet C., Burgess C.E., Fernandez E., Deegler L.L., Rittman B., Shimkets J., Shimkets R.A., Rothberg J.M., Lichenstein H.S. Nat. Cell Biol. 3:517-521(2001) [PubMed] [Europe PMC] [Abstract] 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]	Liu B., Liu Y.Q., Wang X.Y., Zhao B., Sheng H., Zhao X.W., Liu S., Xu Y.Y., Ye J., Song L., Gao Y., Zhang C.L., Zhang J., Wei Y.J., Cao H.Q., Zhao Y., Liu L.S., Ding J.F. , Gao R.L., Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S., Hui R.T. Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Aorta.
[6]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract] 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]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases 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]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] TYR-202.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00011865. IPI00018822.
PIR	JC7591.
RefSeq	NP_079484.1. NM_025208.4. NP_149126.1. NM_033135.3.
UniGene	Hs.352298.
3D structure databases
HSSP	HSSP built from PDB template 1NT0 based on UniProtKB Q9QX89.
ProteinModelPortal	Q9GZP0.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000376865.
PTM databases
PhosphoSite	Q9GZP0.
Polymorphism databases
DMDM	74717921.
Proteomic databases
PaxDb	Q9GZP0.
PRIDE	Q9GZP0.
Protocols and materials databases
DNASU	80310.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000302251; ENSP00000302193; ENSG00000170962. ENST00000393158; ENSP00000376865; ENSG00000170962.
GeneID	80310.
KEGG	hsa:80310.
UCSC	uc001php.3. human. uc001phq.3. human.
Organism-specific databases
CTD	80310.
GeneCards	GC11M103777.
HGNC	HGNC:30620. PDGFD.
MIM	609673. gene.
neXtProt	NX_Q9GZP0.
PharmGKB	PA134892327.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG148355.
HOGENOM	HOG000261610.
HOVERGEN	HBG057324.
InParanoid	Q9GZP0.
KO	K05450.
OMA	LYLDTPH.
OrthoDB	EOG4NKBVN.
Enzyme and pathway databases
Pathway_Interaction_DB	pdgfrbpathway. PDGFR-beta signaling pathway.
Reactome	REACT_111102. Signal Transduction.
Gene expression databases
ArrayExpress	Q9GZP0.
Bgee	Q9GZP0.
CleanEx	HS_PDGFD.
Genevestigator	Q9GZP0.
GermOnline	ENSG00000170962. Homo sapiens.
Family and domain databases
Gene3D	2.60.120.290. 1 hit.
InterPro	IPR000859. CUB_dom. IPR000072. PD_growth_factor. IPR027123. PDGFD. [Graphical view]
PANTHER	PTHR10127:SF13. PTHR10127:SF13. 1 hit.
Pfam	PF00431. CUB. 1 hit. PF00341. PDGF. 1 hit. [Graphical view]
SMART	SM00042. CUB. 1 hit. SM00141. PDGF. 1 hit. [Graphical view]
SUPFAM	SSF49854. CUB. 1 hit.
PROSITE	PS01180. CUB. 1 hit. PS00249. PDGF_1. False negative. PS50278. PDGF_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PDGFD. human.
GenomeRNAi	80310.
NextBio	70792.
PMAP-CutDB	Q9GZP0.
SOURCE	Search...

Entry information

Entry name

PDGFD_HUMAN

Accession

Primary (citable) accession number: Q9GZP0
Secondary accession number(s): A8K9T6, Q9BWV5

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2006
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 90 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.