GDF11_HUMAN - dbPTM
GDF11_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GDF11_HUMAN
UniProt AC O95390
Protein Name Growth/differentiation factor 11 {ECO:0000303|PubMed:10391213}
Gene Name GDF11
Organism Homo sapiens (Human).
Sequence Length 407
Subcellular Localization Secreted .
Protein Description Secreted signal that acts globally to specify positional identity along the anterior/posterior axis during development. May play critical roles in patterning both mesodermal and neural tissues and in establishing the skeletal pattern (By similarity). Signals through activin receptors type-2, ACVR2A and ACVR2B, and activin receptors type-1, ACVR1B, ACVR1C and TGFBR1 leading to the phosphorylation of SMAD2 and SMAD3. [PubMed: 28257634]
Protein Sequence MVLAAPLLLGFLLLALELRPRGEAAEGPAAAAAAAAAAAAAGVGGERSSRPAPSVAPEPDGCPVCVWRQHSRELRLESIKSQILSKLRLKEAPNISREVVKQLLPKAPPLQQILDLHDFQGDALQPEDFLEEDEYHATTETVISMAQETDPAVQTDGSPLCCHFHFSPKVMFTKVLKAQLWVYLRPVPRPATVYLQILRLKPLTGEGTAGGGGGGRRHIRIRSLKIELHSRSGHWQSIDFKQVLHSWFRQPQSNWGIEINAFDPSGTDLAVTSLGPGAEGLHPFMELRVLENTKRSRRNLGLDCDEHSSESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGQCEYMFMQKYPHTHLVQQANPRGSAGPCCTPTKMSPINMLYFNDKQQIIYGKIPGMVVDRCGCS
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
54O-linked_GlycosylationRSSRPAPSVAPEPDG
CCCCCCCCCCCCCCC
32.77OGP
81PhosphorylationLRLESIKSQILSKLR
HHHHHHHHHHHHHHC
22.30-
85PhosphorylationSIKSQILSKLRLKEA
HHHHHHHHHHCCCCC
31.1324719451
94N-linked_GlycosylationLRLKEAPNISREVVK
HCCCCCCCCCHHHHH
52.49UniProtKB CARBOHYD
96PhosphorylationLKEAPNISREVVKQL
CCCCCCCCHHHHHHH
29.0928787133
167PhosphorylationLCCHFHFSPKVMFTK
EEEEEECCCHHHHHH
18.4224719451
232PhosphorylationKIELHSRSGHWQSID
EEEEECCCCCCEEEC
37.7229083192
237PhosphorylationSRSGHWQSIDFKQVL
CCCCCCEEECHHHHH
20.9529083192
246PhosphorylationDFKQVLHSWFRQPQS
CHHHHHHHHHCCCCC
24.6129083192
336PhosphorylationWIIAPKRYKANYCSG
EEECCCCEECCCCCH
22.15-
340PhosphorylationPKRYKANYCSGQCEY
CCCEECCCCCHHCCE
7.89-
342PhosphorylationRYKANYCSGQCEYMF
CEECCCCCHHCCEEE
22.87-
347PhosphorylationYCSGQCEYMFMQKYP
CCCHHCCEEEEECCC
11.86-
367PhosphorylationQQANPRGSAGPCCTP
ECCCCCCCCCCCCCC
31.1922210691
373PhosphorylationGSAGPCCTPTKMSPI
CCCCCCCCCCCCCCC
40.4822210691
375PhosphorylationAGPCCTPTKMSPINM
CCCCCCCCCCCCCEE
22.6422210691
378PhosphorylationCCTPTKMSPINMLYF
CCCCCCCCCCEEEEE
24.9622210691

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 GDF11_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GDF11_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 GDF11_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of GDF11_HUMAN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GDF11_HUMAN

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Related Literatures of Post-Translational Modification

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