GDF10_HUMAN - dbPTM
GDF10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GDF10_HUMAN
UniProt AC P55107
Protein Name Growth/differentiation factor 10
Gene Name GDF10 {ECO:0000312|HGNC:HGNC:4215}
Organism Homo sapiens (Human).
Sequence Length 478
Subcellular Localization Secreted .
Protein Description Growth factor involved in osteogenesis and adipogenesis. Plays an inhibitory role in the process of osteoblast differentiation via SMAD2/3 pathway. Plays an inhibitory role in the process of adipogenesis..
Protein Sequence MAHVPARTSPGPGPQLLLLLLPLFLLLLRDVAGSHRAPAWSALPAAADGLQGDRDLQRHPGDAAATLGPSAQDMVAVHMHRLYEKYSRQGARPGGGNTVRSFRARLEVVDQKAVYFFNLTSMQDSEMILTATFHFYSEPPRWPRALEVLCKPRAKNASGRPLPLGPPTRQHLLFRSLSQNTATQGLLRGAMALAPPPRGLWQAKDISPIVKAARRDGELLLSAQLDSEERDPGVPRPSPYAPYILVYANDLAISEPNSVAVTLQRYDPFPAGDPEPRAAPNNSADPRVRRAAQATGPLQDNELPGLDERPPRAHAQHFHKHQLWPSPFRALKPRPGRKDRRKKGQEVFMAASQVLDFDEKTMQKARRKQWDEPRVCSRRYLKVDFADIGWNEWIISPKSFDAYYCAGACEFPMPKIVRPSNHATIQSIVRAVGIIPGIPEPCCVPDKMNSLGVLFLDENRNVVLKVYPNMSVDTCACR
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 Orthologous
Protein Cluster
86PhosphorylationMHRLYEKYSRQGARP
HHHHHHHHHHCCCCC
21082442
87PhosphorylationHRLYEKYSRQGARPG
HHHHHHHHHCCCCCC
21082442
98PhosphorylationARPGGGNTVRSFRAR
CCCCCCCHHHHHHHE
22817900
101PhosphorylationGGGNTVRSFRARLEV
CCCCHHHHHHHEEEE
24719451
118N-linked_GlycosylationQKAVYFFNLTSMQDS
CCEEEEEECCCCCCC
UniProtKB CARBOHYD
156N-linked_GlycosylationLCKPRAKNASGRPLP
HHCCCCCCCCCCCCC
UniProtKB CARBOHYD
176PhosphorylationRQHLLFRSLSQNTAT
HHHHHHHHCCCCHHH
24043423
178PhosphorylationHLLFRSLSQNTATQG
HHHHHHCCCCHHHHH
24043423
181PhosphorylationFRSLSQNTATQGLLR
HHHCCCCHHHHHHHH
24043423
183PhosphorylationSLSQNTATQGLLRGA
HCCCCHHHHHHHHHH
24043423
207PhosphorylationLWQAKDISPIVKAAR
CCCCCCCHHHHHHHH
24719451
281N-linked_GlycosylationPEPRAAPNNSADPRV
CCCCCCCCCCCCHHH
UniProtKB CARBOHYD
283PhosphorylationPRAAPNNSADPRVRR
CCCCCCCCCCHHHHH
-
360AcetylationQVLDFDEKTMQKARR
HHHCCCHHHHHHHHH
11790781
396PhosphorylationGWNEWIISPKSFDAY
CCCCEEECCCCCCCE
24719451
469N-linked_GlycosylationVVLKVYPNMSVDTCA
EEEEEECCCCCCCCC
UniProtKB CARBOHYD

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

Oops, there are no upstream regulatory protein records of GDF10_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GDF10_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of GDF10_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LRP4_HUMANLRP4physical
28514442
MYCB2_HUMANMYCBP2physical
28514442
BANP_HUMANBANPphysical
28514442
ZN507_HUMANZNF507physical
28514442
MTHR_HUMANMTHFRphysical
28514442
FBSP1_HUMANFBXO45physical
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.
Regulatory Network of GDF10_HUMAN

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Related Literatures of Post-Translational Modification

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