PPIL3_HUMAN - dbPTM
PPIL3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PPIL3_HUMAN
UniProt AC Q9H2H8
Protein Name Peptidyl-prolyl cis-trans isomerase-like 3
Gene Name PPIL3
Organism Homo sapiens (Human).
Sequence Length 161
Subcellular Localization
Protein Description PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be involved in pre-mRNA splicing..
Protein Sequence MSVTLHTDVGDIKIEVFCERTPKTCENFLALCASNYYNGCIFHRNIKGFMVQTGDPTGTGRGGNSIWGKKFEDEYSEYLKHNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVNEKTYRPLNDVHIKDITIHANPFAQ
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
2Acetylation------MSVTLHTDV
------CCEEEEECC
24.6522223895
7Phosphorylation-MSVTLHTDVGDIKI
-CCEEEEECCCCEEE
35.1821060948
47 (in isoform 1)Ubiquitination-50.0421890473
47UbiquitinationCIFHRNIKGFMVQTG
EEEECCCCEEEEEEC
50.0421890473
50SulfoxidationHRNIKGFMVQTGDPT
ECCCCEEEEEECCCC
2.7321406390
53PhosphorylationIKGFMVQTGDPTGTG
CCEEEEEECCCCCCC
31.9420068231
61MethylationGDPTGTGRGGNSIWG
CCCCCCCCCCCCCCC
50.0830988933
69AcetylationGGNSIWGKKFEDEYS
CCCCCCCCCCHHHHH
39.0123749302
70UbiquitinationGNSIWGKKFEDEYSE
CCCCCCCCCHHHHHH
50.47-
75PhosphorylationGKKFEDEYSEYLKHN
CCCCHHHHHHHHHHH
21.0829978859
76PhosphorylationKKFEDEYSEYLKHNV
CCCHHHHHHHHHHHH
20.0929978859
78PhosphorylationFEDEYSEYLKHNVRG
CHHHHHHHHHHHHCC
18.3429978859
80UbiquitinationDEYSEYLKHNVRGVV
HHHHHHHHHHHCCEE
32.03-
120UbiquitinationMKYTVFGKVIDGLET
CEEEECCEEECCCCC
25.26-
127PhosphorylationKVIDGLETLDELEKL
EEECCCCCHHHHHCC
44.55-
133UbiquitinationETLDELEKLPVNEKT
CCHHHHHCCCCCCCC
71.382190698
133 (in isoform 1)Ubiquitination-71.3821890473
137 (in isoform 2)Ubiquitination-43.0121906983
139AcetylationEKLPVNEKTYRPLND
HCCCCCCCCCCCCCC
45.7326051181
139UbiquitinationEKLPVNEKTYRPLND
HCCCCCCCCCCCCCC
45.73-
142MethylationPVNEKTYRPLNDVHI
CCCCCCCCCCCCCEE
34.17115368667

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 PPIL3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PPIL3_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 PPIL3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SPS1_HUMANSEPHS1physical
22939629
SUMO1_HUMANSUMO1physical
22939629
PSA1_HUMANPSMA1physical
22939629
SLD5_HUMANGINS4physical
22939629
SAHH2_HUMANAHCYL1physical
22939629
TMOD3_HUMANTMOD3physical
22939629
RD23B_HUMANRAD23Bphysical
22939629
SC24C_HUMANSEC24Cphysical
22939629
RCN1_HUMANRCN1physical
22939629
RPAP1_HUMANRPAP1physical
22939629
SGT1_HUMANSUGT1physical
22939629
SLU7_HUMANSLU7physical
22365833
PCBP1_HUMANPCBP1physical
22365833
BAG1_HUMANBAG1physical
26344197
TAGL2_HUMANTAGLN2physical
26344197

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 PPIL3_HUMAN

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Related Literatures of Post-Translational Modification

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