SP7_HUMAN - dbPTM
SP7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SP7_HUMAN
UniProt AC Q8TDD2
Protein Name Transcription factor Sp7
Gene Name SP7
Organism Homo sapiens (Human).
Sequence Length 431
Subcellular Localization Nucleus .
Protein Description Transcriptional activator essential for osteoblast differentiation. [PubMed: 23457570 Binds to SP1 and EKLF consensus sequences and to other G/C-rich sequences (By similarity; Transcriptional activator essential for osteoblast differentiation. Binds to SP1 and EKLF consensus sequences and to other G/C-rich sequences.]
Protein Sequence MASSLLEEEVHYGSSPLAMLTAACSKFGGSSPLRDSTTLGKAGTKKPYSVGSDLSASKTMGDAYPAPFTSTNGLLSPAGSPPAPTSGYANDYPPFSHSFPGPTGTQDPGLLVPKGHSSSDCLPSVYTSLDMTHPYGSWYKAGIHAGISPGPGNTPTPWWDMHPGGNWLGGGQGQGDGLQGTLPTGPAQPPLNPQLPTYPSDFAPLNPAPYPAPHLLQPGPQHVLPQDVYKPKAVGNSGQLEGSGGAKPPRGASTGGSGGYGGSGAGRSSCDCPNCQELERLGAAAAGLRKKPIHSCHIPGCGKVYGKASHLKAHLRWHTGERPFVCNWLFCGKRFTRSDELERHVRTHTREKKFTCLLCSKRFTRSDHLSKHQRTHGEPGPGPPPSGPKELGEGRSTGEEEASQTPRPSASPATPEKAPGGSPEQSNLLEI
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
3Phosphorylation-----MASSLLEEEV
-----CCCCHHHCHH
21.8829759185
4Phosphorylation----MASSLLEEEVH
----CCCCHHHCHHH
27.6929759185
30PhosphorylationACSKFGGSSPLRDST
HHHHHCCCCCCCCCC
29.21-
31PhosphorylationCSKFGGSSPLRDSTT
HHHHCCCCCCCCCCC
31.09-
37PhosphorylationSSPLRDSTTLGKAGT
CCCCCCCCCCCCCCC
30.26-
38PhosphorylationSPLRDSTTLGKAGTK
CCCCCCCCCCCCCCC
37.15-
41UbiquitinationRDSTTLGKAGTKKPY
CCCCCCCCCCCCCCC
46.91-
41PropionylationRDSTTLGKAGTKKPY
CCCCCCCCCCCCCCC
46.91-
45PropionylationTLGKAGTKKPYSVGS
CCCCCCCCCCCCCCC
51.32-
49PhosphorylationAGTKKPYSVGSDLSA
CCCCCCCCCCCCCCC
28.64-
52PhosphorylationKKPYSVGSDLSASKT
CCCCCCCCCCCCCCC
32.9724719451
58UbiquitinationGSDLSASKTMGDAYP
CCCCCCCCCCCCCCC
42.10-
76PhosphorylationTSTNGLLSPAGSPPA
CCCCCCCCCCCCCCC
20.11-
80PhosphorylationGLLSPAGSPPAPTSG
CCCCCCCCCCCCCCC
29.80-
230UbiquitinationVLPQDVYKPKAVGNS
CCCCCCCCCCCCCCC
39.63-
237PhosphorylationKPKAVGNSGQLEGSG
CCCCCCCCCCCCCCC
23.22-
307AcetylationGCGKVYGKASHLKAH
CCCCEEEEHHHHHHH
29.09113429599
312AcetylationYGKASHLKAHLRWHT
EEEHHHHHHHHHHCC
28.47113429601
319PhosphorylationKAHLRWHTGERPFVC
HHHHHHCCCCCCEEE
33.50-
338PhosphorylationCGKRFTRSDELERHV
ECCCCCCHHHHHHHH
32.1725159151
361PropionylationFTCLLCSKRFTRSDH
EEEEEECCCCCCHHH
51.00-
364PhosphorylationLLCSKRFTRSDHLSK
EEECCCCCCHHHHHH
33.04-
366PhosphorylationCSKRFTRSDHLSKHQ
ECCCCCCHHHHHHHH
26.73-
370PhosphorylationFTRSDHLSKHQRTHG
CCCHHHHHHHHHHCC
25.36-
371PropionylationTRSDHLSKHQRTHGE
CCHHHHHHHHHHCCC
50.55-
396PhosphorylationKELGEGRSTGEEEAS
CCCCCCCCCCHHHHH
52.17-
397PhosphorylationELGEGRSTGEEEASQ
CCCCCCCCCHHHHHC
47.45-

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 SP7_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SP7_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 SP7_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CHIP_HUMANSTUB1physical
25818514
CBL_HUMANCBLphysical
25744063
CBLB_HUMANCBLBphysical
25744063

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SP7_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP