GDF9_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: GDF9_HUMAN
• UniProt AC: O60383
• Protein Name: Growth/differentiation factor 9
• Gene Name: GDF9
• Organism: Homo sapiens (Human).
• Sequence Length: 454
• Subcellular Localization: Secreted.
• Protein Description: Required for ovarian folliculogenesis. Promotes primordial follicle development. Stimulates granulosa cell proliferation. Promotes cell transition from G0/G1 to S and G2/M phases, through an increase of CCND1 and CCNE1 expression, and RB1 phosphorylation. It regulates STAR expression and cAMP-dependent progesterone release in granulosa and thecal cells. Attenuates the suppressive effects of activin A on STAR expression and progesterone production by increasing the expression of inhibin B. It suppresses FST and FSTL3 production in granulosa-lutein cells..
• Protein Sequence: MARPNKFLLWFCCFAWLCFPISLGSQASGGEAQIAASAELESGAMPWSLLQHIDERDRAGLLPALFKVLSVGRGGSPRLQPDSRALHYMKKLYKTYATKEGIPKSNRSHLYNTVRLFTPCTRHKQAPGDQVTGILPSVELLFNLDRITTVEHLLKSVLLYNINNSVSFSSAVKCVCNLMIKEPKSSSRTLGRAPYSFTFNSQFEFGKKHKWIQIDVTSLLQPLVASNKRSIHMSINFTCMKDQLEHPSAQNGLFNMTLVSPSLILYLNDTSAQAYHSWYSLHYKRRPSQGPDQERSLSAYPVGEEAAEDGRSSHHRHRRGQETVSSELKKPLGPASFNLSEYFRQFLLPQNECELHDFRLSFSQLKWDNWIVAPHRYNPRYCKGDCPRAVGHRYGSPVHTMVQNIIYEKLDSSVPRPSCVPAKYSPLSVLTIEPDGSIAYKEYEDMIATKCTCR

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
70	Phosphorylation	PALFKVLSVGRGGSP HHHHHHHHCCCCCCC	26.05	23090842
106	N-linked_Glycosylation	KEGIPKSNRSHLYNT CCCCCCCCHHHHHCC	56.45	UniProtKB CARBOHYD
156	Phosphorylation	TVEHLLKSVLLYNIN CHHHHHHHHHHHHCC	20.26	-
163	N-linked_Glycosylation	SVLLYNINNSVSFSS HHHHHHCCCCCCHHH	30.96	UniProtKB CARBOHYD
170	Phosphorylation	NNSVSFSSAVKCVCN CCCCCHHHHHHHHHH	34.76	-
185	Phosphorylation	LMIKEPKSSSRTLGR HHCCCCCCCCCCCCC	44.24	-
186	Phosphorylation	MIKEPKSSSRTLGRA HCCCCCCCCCCCCCC	29.93	-
189	Phosphorylation	EPKSSSRTLGRAPYS CCCCCCCCCCCCCEE	35.20	-
196	Phosphorylation	TLGRAPYSFTFNSQF CCCCCCEEEEECCCC	19.42	-
236	N-linked_Glycosylation	RSIHMSINFTCMKDQ CEEEEEEEEEEEHHH	20.90	UniProtKB CARBOHYD
255	N-linked_Glycosylation	SAQNGLFNMTLVSPS CHHCCCCCCEEECHH	27.80	UniProtKB CARBOHYD
268	N-linked_Glycosylation	PSLILYLNDTSAQAY HHEEEEECCCCHHHH	36.64	UniProtKB CARBOHYD
288	Phosphorylation	LHYKRRPSQGPDQER HEECCCCCCCCCCCC	46.05	-
298	Phosphorylation	PDQERSLSAYPVGEE CCCCCCCCCCCCCHH	27.31	30301811
300	Phosphorylation	QERSLSAYPVGEEAA CCCCCCCCCCCHHHH	8.62	30301811
325	Phosphorylation	RRGQETVSSELKKPL HCCCCCCCHHHCCCC	26.05	17482612
338	N-linked_Glycosylation	PLGPASFNLSEYFRQ CCCCCCCCHHHHHHH	39.91	UniProtKB CARBOHYD
394	Phosphorylation	PRAVGHRYGSPVHTM CCCCCCCCCCHHHHH	19.11	-
407	Phosphorylation	TMVQNIIYEKLDSSV HHHHHHHHHHHCCCC	11.83	-
440	Phosphorylation	EPDGSIAYKEYEDMI CCCCCEECHHHHHHE	11.59	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
325	S	Phosphorylation	Kinase	CK	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
325	S	Phosphorylation	In vitro, can be phosphorylated by CK at Ser-325.	20067794

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of GDF9_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GA45G_HUMAN	GADD45G	physical	15383276
MYH11_HUMAN	MYH11	physical	28514442
AP5B1_HUMAN	AP5B1	physical	28514442
TBA4A_HUMAN	TUBA4A	physical	28514442
ACTBL_HUMAN	ACTBL2	physical	28514442
TBB8_HUMAN	TUBB8	physical	28514442
TBB3_HUMAN	TUBB3	physical	28514442
MED20_HUMAN	MED20	physical	28514442
FBX2_HUMAN	FBXO2	physical	28514442
VWA1_HUMAN	VWA1	physical	28514442
GBB2_HUMAN	GNB2	physical	28514442

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.