RIPL1_HUMAN - dbPTM
RIPL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RIPL1_HUMAN
UniProt AC Q5EBL4
Protein Name RILP-like protein 1
Gene Name RILPL1
Organism Homo sapiens (Human).
Sequence Length 403
Subcellular Localization Cytoplasm, cytosol . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cell projection, cilium.
Protein Description Plays a role in the regulation of cell shape and polarity. Plays a role in cellular protein transport, including protein transport away from primary cilia. Neuroprotective protein, which acts by sequestring GAPDH in the cytosol and prevent the apoptotic function of GAPDH in the nucleus. Competes with SIAH1 for binding GAPDH (By similarity). Does not regulate lysosomal morphology and distribution..
Protein Sequence MEEERGSALAAESALEKNVAELTVMDVYDIASLVGHEFERVIDQHGCEAIARLMPKVVRVLEILEVLVSRHHVAPELDELRLELDRLRLERMDRIEKERKHQKELELVEDVWRGEAQDLLSQIAQLQEENKQLMTNLSHKDVNFSEEEFQKHEGMSERERQVMKKLKEVVDKQRDEIRAKDRELGLKNEDVEALQQQQTRLMKINHDLRHRVTVVEAQGKALIEQKVELEADLQTKEQEMGSLRAELGKLRERLQGEHSQNGEEEPETEPVGEESISDAEKVAMDLKDPNRPRFTLQELRDVLHERNELKSKVFLLQEELAYYKSEEMEEENRIPQPPPIAHPRTSPQPESGIKRLFSFFSRDKKRLANTQRNVHIQESFGQWANTHRDDGYTEQGQEALQHL
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
7Phosphorylation-MEEERGSALAAESA
-CHHHHHHHHHHHHH
26.74-
47S-nitrosylationRVIDQHGCEAIARLM
HHHHHHHHHHHHHHH
2.75-
47S-nitrosocysteineRVIDQHGCEAIARLM
HHHHHHHHHHHHHHH
2.75-
103UbiquitinationEKERKHQKELELVED
HHHHHHHHHHHHHHH
65.08-
145PhosphorylationSHKDVNFSEEEFQKH
CCCCCCCCHHHHHHH
38.6022199227
151UbiquitinationFSEEEFQKHEGMSER
CCHHHHHHHCCCCHH
49.28-
235PhosphorylationELEADLQTKEQEMGS
HHHCHHHHHHHHHHH
43.7920068231
242PhosphorylationTKEQEMGSLRAELGK
HHHHHHHHHHHHHHH
17.2426270265
249UbiquitinationSLRAELGKLRERLQG
HHHHHHHHHHHHHCC
57.93-
259PhosphorylationERLQGEHSQNGEEEP
HHHCCCCCCCCCCCC
22.4925159151
268PhosphorylationNGEEEPETEPVGEES
CCCCCCCCCCCCCCC
57.2023403867
275PhosphorylationTEPVGEESISDAEKV
CCCCCCCCCCHHHHH
24.0823403867
277PhosphorylationPVGEESISDAEKVAM
CCCCCCCCHHHHHHH
39.7923403867
287UbiquitinationEKVAMDLKDPNRPRF
HHHHHCCCCCCCCCC
67.86-
311PhosphorylationHERNELKSKVFLLQE
HHHHHHHHHHHHHHH
46.83-
322PhosphorylationLLQEELAYYKSEEME
HHHHHHHHHCCHHHH
24.85-
323PhosphorylationLQEELAYYKSEEMEE
HHHHHHHHCCHHHHH
11.48-
345PhosphorylationPPIAHPRTSPQPESG
CCCCCCCCCCCCCCH
49.5728176443
346PhosphorylationPIAHPRTSPQPESGI
CCCCCCCCCCCCCHH
23.8725159151
351PhosphorylationRTSPQPESGIKRLFS
CCCCCCCCHHHHHHH
53.1323403867
354UbiquitinationPQPESGIKRLFSFFS
CCCCCHHHHHHHHHH
46.72-
358PhosphorylationSGIKRLFSFFSRDKK
CHHHHHHHHHHHCHH
29.9429514088
361PhosphorylationKRLFSFFSRDKKRLA
HHHHHHHHHCHHHHH
37.2429978859
379PhosphorylationRNVHIQESFGQWANT
CCHHHHHHCHHHHHH
20.5027251275
392PhosphorylationNTHRDDGYTEQGQEA
HHCCCCCCCHHHHHH
17.6927642862

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 RIPL1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RIPL1_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 RIPL1_HUMAN !!

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

Oops, there are no PPI records of RIPL1_HUMAN !!

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 RIPL1_HUMAN

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Related Literatures of Post-Translational Modification

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