RAB7L_HUMAN - dbPTM
RAB7L_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RAB7L_HUMAN
UniProt AC O14966
Protein Name Ras-related protein Rab-7L1
Gene Name RAB29
Organism Homo sapiens (Human).
Sequence Length 203
Subcellular Localization Cell membrane
Lipid-anchor
Cytoplasmic side . Cytoplasm . Cytoplasm, perinuclear region . Golgi apparatus . Golgi apparatus, trans-Golgi network . Vacuole . Cytoplasm, cytoskeleton . Colocalizes with LRRK2 along tubular structures emerging from G
Protein Description Rab GTPase key regulator in vesicle trafficking. Essential for maintaining the integrity of the endosome-trans-Golgi network structure. Together with LRRK2, plays a role in the retrograde trafficking pathway for recycling proteins, such as mannose 6 phosphate receptor (M6PR), between lysosomes and the Golgi apparatus in a retromer-dependent manner. Regulates neuronal process morphology in the intact central nervous system (CNS). May play a role in the formation of typhoid toxin transport intermediates during Salmonella enterica serovar Typhi (S.Typhi) epithelial cell infection..
Protein Sequence MGSRDHLFKVLVVGDAAVGKTSLVQRYSQDSFSKHYKSTVGVDFALKVLQWSDYEIVRLQLWDIAGQERFTSMTRLYYRDASACVIMFDVTNATTFSNSQRWKQDLDSKLTLPNGEPVPCLLLANKCDLSPWAVSRDQIDRFSKENGFTGWTETSVKENKNINEAMRVLIEKMMRNSTEDIMSLSTQGDYINLQTKSSSWSCC
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
20UbiquitinationVGDAAVGKTSLVQRY
ECCCCCCCHHHHHHH		28.48-
31PhosphorylationVQRYSQDSFSKHYKS
HHHHCCCCHHHHHHH		24.6324719451
34UbiquitinationYSQDSFSKHYKSTVG
HCCCCHHHHHHHHHC		49.28-
36 (in isoform 2)Phosphorylation-15.4624719451
36PhosphorylationQDSFSKHYKSTVGVD
CCCHHHHHHHHHCHH		15.4624719451
38PhosphorylationSFSKHYKSTVGVDFA
CHHHHHHHHHCHHHH		22.5924719451
38 (in isoform 2)Phosphorylation-22.5924719451
39PhosphorylationFSKHYKSTVGVDFAL
HHHHHHHHHCHHHHH		19.68-
52PhosphorylationALKVLQWSDYEIVRL
HHHHHCCCCCEEEEE		19.8428796482
54PhosphorylationKVLQWSDYEIVRLQL
HHHCCCCCEEEEEEE		11.3128796482
71PhosphorylationIAGQERFTSMTRLYY
HHCCCCCCCCCEEEE		24.6629212815
72PhosphorylationAGQERFTSMTRLYYR
HCCCCCCCCCEEEEC		18.5529212815
74PhosphorylationQERFTSMTRLYYRDA
CCCCCCCCEEEECCC		19.7929978859
103UbiquitinationFSNSQRWKQDLDSKL
CCCCHHHHHHCCCCC		35.80-
126UbiquitinationPCLLLANKCDLSPWA
CEEEEECCCCCCCCC		24.42-
130PhosphorylationLANKCDLSPWAVSRD
EECCCCCCCCCCCHH		12.73-
135PhosphorylationDLSPWAVSRDQIDRF
CCCCCCCCHHHHHHH		23.5327251275
144UbiquitinationDQIDRFSKENGFTGW
HHHHHHHHHHCCCCC		53.11-
149PhosphorylationFSKENGFTGWTETSV
HHHHHCCCCCCCCCH		32.96-
154PhosphorylationGFTGWTETSVKENKN
CCCCCCCCCHHHCCC		31.29-
155PhosphorylationFTGWTETSVKENKNI
CCCCCCCCHHHCCCH		25.59-
157UbiquitinationGWTETSVKENKNINE
CCCCCCHHHCCCHHH		56.17-
160UbiquitinationETSVKENKNINEAMR
CCCHHHCCCHHHHHH		61.36-
172UbiquitinationAMRVLIEKMMRNSTE
HHHHHHHHHHCCCHH		30.88-
177PhosphorylationIEKMMRNSTEDIMSL
HHHHHCCCHHHHHHH		23.8627251275
178PhosphorylationEKMMRNSTEDIMSLS
HHHHCCCHHHHHHHH		41.0227251275
183PhosphorylationNSTEDIMSLSTQGDY
CCHHHHHHHHCCCCE		21.3630108239
185PhosphorylationTEDIMSLSTQGDYIN
HHHHHHHHCCCCEEE		16.0430278072
186O-linked_GlycosylationEDIMSLSTQGDYINL
HHHHHHHCCCCEEEE		41.69OGP
186PhosphorylationEDIMSLSTQGDYINL
HHHHHHHCCCCEEEE		41.6930278072
190PhosphorylationSLSTQGDYINLQTKS
HHHCCCCEEEEEECC		9.8728796482
202GeranylgeranylationTKSSSWSCC------
ECCCCCCCC------		2.31-
203GeranylgeranylationKSSSWSCC-------
CCCCCCCC-------		5.36-
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
71TPhosphorylationKinaseLRRK2Q5S007
Uniprot
72SPhosphorylationKinaseLRRK2Q5S007
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RAB7L_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 RAB7L_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LDOC1_HUMANLDOC1physical
25416956
CK049_HUMANC11orf49physical
25416956
BEND7_HUMANBEND7physical
25416956
ITPR3_HUMANITPR3physical
28514442
ITPR2_HUMANITPR2physical
28514442
ITPR1_HUMANITPR1physical
28514442
ATP7A_HUMANATP7Aphysical
28514442
PGTA_HUMANRABGGTAphysical
28514442
RAE1_HUMANCHMphysical
28514442
RAE2_HUMANCHMLphysical
28514442
ARL8B_HUMANARL8Bphysical
28514442
CNO6L_HUMANCNOT6Lphysical
28514442
STRP1_HUMANSTRIP1physical
28514442
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 RAB7L_HUMAN

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Related Literatures of Post-Translational Modification

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