SETLP_HUMAN - dbPTM
SETLP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SETLP_HUMAN
UniProt AC P0DME0
Protein Name Protein SETSIP
Gene Name SETSIP
Organism Homo sapiens (Human).
Sequence Length 302
Subcellular Localization Cytoplasm . Nucleus . Translocated from the cytoplasm to the nucleus in protein-induced pluripotent stem (PiPS) endothelial cells.
Protein Description Plays a role as a transcriptional activator involved in the early stage of somatic cell reprogramming. Promotes the differentiation of protein-induced pluripotent stem (PiPS) cells into endothelial cells and the formation of vascular-like tubes (in vitro). Involved in the transcription induction of vascular endothelial-cadherin (VE-cadherin) expression. Associates to the VE-cadherin gene promoter..
Protein Sequence MVWFLDFPNSMAPKRQSPLPLQKKKPRPPPALGLEETSASAGLPKKGEKEQQEAIEHIDEVQNEIDRLNEQDSEEILKVEQKYNKLRQPFFQKRSELIAKIPNFGVTTFVNHPQVSSLLGEEDEEALHYLTKVEVTEFEDIKSGYRIDFYFDENPYFENKVFSKEFHLNESGDPSSKSTKIKWKSGKDVTKRSSQTQNKASRKRQHEEPESFFTWFTDHSDAGADELEEVIKDDIWPNPLQYYLVPDMDDEEGGEDDDDDDDDGDEGEEELEDIDEGDEDEGEEDEDDDEGEEGEEDEGEDD
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
17PhosphorylationSMAPKRQSPLPLQKK
CCCCCCCCCCCCCCC
30622161
40PhosphorylationGLEETSASAGLPKKG
CCCCCCHHCCCCCCC
22817900
49AcetylationGLPKKGEKEQQEAIE
CCCCCCHHHHHHHHH
26051181
78UbiquitinationQDSEEILKVEQKYNK
HCHHHHHHHHHHHHH
22817900
82SuccinylationEILKVEQKYNKLRQP
HHHHHHHHHHHHHCC
23954790
82UbiquitinationEILKVEQKYNKLRQP
HHHHHHHHHHHHHCC
22817900
82AcetylationEILKVEQKYNKLRQP
HHHHHHHHHHHHHCC
23749302
85NeddylationKVEQKYNKLRQPFFQ
HHHHHHHHHHCCHHH
32015554
93MethylationLRQPFFQKRSELIAK
HHCCHHHHHHHHHHC
127455561
93UbiquitinationLRQPFFQKRSELIAK
HHCCHHHHHHHHHHC
23000965
93AcetylationLRQPFFQKRSELIAK
HHCCHHHHHHHHHHC
23954790
136PhosphorylationYLTKVEVTEFEDIKS
HHEEEEEEEEECCCC
23403867
142AcetylationVTEFEDIKSGYRIDF
EEEEECCCCCEEEEE
23954790
142MalonylationVTEFEDIKSGYRIDF
EEEEECCCCCEEEEE
26320211
142UbiquitinationVTEFEDIKSGYRIDF
EEEEECCCCCEEEEE
23000965
142MethylationVTEFEDIKSGYRIDF
EEEEECCCCCEEEEE
80475811
143PhosphorylationTEFEDIKSGYRIDFY
EEEECCCCCEEEEEE
22167270
145PhosphorylationFEDIKSGYRIDFYFD
EECCCCCEEEEEEEC
23403867
150PhosphorylationSGYRIDFYFDENPYF
CCEEEEEEECCCCCC
27259358
156PhosphorylationFYFDENPYFENKVFS
EEECCCCCCCCCEEC
25884760
171PhosphorylationKEFHLNESGDPSSKS
EEECCCCCCCCCCCC
30266825
175PhosphorylationLNESGDPSSKSTKIK
CCCCCCCCCCCCCCE
30266825
176PhosphorylationNESGDPSSKSTKIKW
CCCCCCCCCCCCCEE
30266825
194PhosphorylationKDVTKRSSQTQNKAS
CCCHHHCHHHCCHHH
-
199UbiquitinationRSSQTQNKASRKRQH
HCHHHCCHHHHHHHH
-
201PhosphorylationSQTQNKASRKRQHEE
HHHCCHHHHHHHHCC
-
211PhosphorylationRQHEEPESFFTWFTD
HHHCCCHHHHHHHCC
22468782
217PhosphorylationESFFTWFTDHSDAGA
HHHHHHHCCCCCCCH
22468782
220PhosphorylationFTWFTDHSDAGADEL
HHHHCCCCCCCHHHH
22468782

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 SETLP_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SETLP_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 SETLP_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
P3H1_HUMANP3H1physical
22863883
NRDC_HUMANNRD1physical
22863883
PFD1_HUMANPFDN1physical
22863883
TSN_HUMANTSNphysical
22863883
VAT1_HUMANVAT1physical
22863883

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

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Related Literatures of Post-Translational Modification

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