RILP_HUMAN - dbPTM
RILP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RILP_HUMAN
UniProt AC Q96NA2
Protein Name Rab-interacting lysosomal protein
Gene Name RILP
Organism Homo sapiens (Human).
Sequence Length 401
Subcellular Localization Late endosome membrane . Lysosome membrane . Cytoplasmic vesicle, phagosome membrane . Associated with late endosomal, lysosomal and phagosomal membranes. The interaction with RAB7A is necessary for its recruitment to phagosomes.
Protein Description Rab effector playing a role in late endocytic transport to degradative compartments. Involved in the regulation of lysosomal morphology and distribution. Induces recruitment of dynein-dynactin motor complexes to Rab7A-containing late endosome and lysosome compartments. Promotes centripetal migration of phagosomes and the fusion of phagosomes with the late endosomes and lysosomes..
Protein Sequence MEPRRAAPGVPGWGSREAAGSASAAELVYHLAGALGTELQDLARRFGPEAAAGLVPLVVRALELLEQAAVGPAPDSLQVSAQPAEQELRRLREENERLRRELRAGPQEERALLRQLKEVTDRQRDELRAHNRDLRQRGQETEALQEQLQRLLLVNAELRHKLAAMQTQLRAAQDRERERQQPGEAATPQAKERARGQAGRPGHQHGQEPEWATAGAGAPGNPEDPAEAAQQLGRPSEAGQCRFSREEFEQILQERNELKAKVFLLKEELAYFQRELLTDHRVPGLLLEAMKVAVRKQRKKIKAKMLGTPEEAESSEDEAGPWILLSDDKGDHPPPPESKIQSFFGLWYRGKAESSEDETSSPAPSKLGGEEEAQPQSPAPDPPCSALHEHLCLGASAAPEA
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
187PhosphorylationQQPGEAATPQAKERA
CCCCCCCCHHHHHHH
24.0025262027
308PhosphorylationIKAKMLGTPEEAESS
HHHHHCCCHHHHHCC
24.4620068231
314PhosphorylationGTPEEAESSEDEAGP
CCHHHHHCCCCCCCC
46.1825159151
315PhosphorylationTPEEAESSEDEAGPW
CHHHHHCCCCCCCCE
40.3415933719
326PhosphorylationAGPWILLSDDKGDHP
CCCEEEEECCCCCCC
40.0820068231
338PhosphorylationDHPPPPESKIQSFFG
CCCCCCHHHHHHHHH
40.6120068231
354PhosphorylationWYRGKAESSEDETSS
HHCCCCCCCCCCCCC
43.8425159151
355PhosphorylationYRGKAESSEDETSSP
HCCCCCCCCCCCCCC
40.3425159151
359PhosphorylationAESSEDETSSPAPSK
CCCCCCCCCCCCCHH
46.9929396449
360PhosphorylationESSEDETSSPAPSKL
CCCCCCCCCCCCHHC
32.0729396449
361PhosphorylationSSEDETSSPAPSKLG
CCCCCCCCCCCHHCC
32.2825627689
365PhosphorylationETSSPAPSKLGGEEE
CCCCCCCHHCCCCCC
42.49-
377PhosphorylationEEEAQPQSPAPDPPC
CCCCCCCCCCCCCCC
29.7030576142

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 RILP_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RILP_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 RILP_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAB7A_HUMANRAB7Aphysical
11448994
VPS36_HUMANVPS36physical
17010938
SNF8_HUMANSNF8physical
17010938
RAB7A_HUMANRAB7Aphysical
18552835
RAB7B_HUMANRAB7Bphysical
18552835
VPS11_HUMANVPS11physical
25445562
VPS16_HUMANVPS16physical
25445562
VPS18_HUMANVPS18physical
25445562
VPS39_HUMANVPS39physical
25445562
VPS41_HUMANVPS41physical
25445562
RAB7A_HUMANRAB7Aphysical
25445562
RAB7A_HUMANRAB7Aphysical
26911690
RAB7A_HUMANRAB7Aphysical
25080504

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 RILP_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314 AND SER-315, ANDMASS SPECTROMETRY.

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