RBL2B_HUMAN - dbPTM
RBL2B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RBL2B_HUMAN
UniProt AC Q9UNT1
Protein Name Rab-like protein 2B
Gene Name RABL2B
Organism Homo sapiens (Human).
Sequence Length 228
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole . Cytoplasm, cytoskeleton, cilium basal body . Cytoplasm . Localizes on the mother centriole. Localizes slightly apical to the subdistal appendage, but below the distal app
Protein Description Small GTPase required for ciliation. Activated in a guanine nucleotide exchange factor (GEF)-independent manner via its intrinsic GDP for GTP nucleotide exchange ability. [PubMed: 28625565 Involved in ciliary assembly by binding the intraflagellar transport (IFT) complex B from the large pool pre-docked at the base of the cilium and thus triggers its entry into the cilia]
Protein Sequence MAEDKTKPSELDQGKYDADDNVKIICLGDSAVGKSKLMERFLMDGFQPQQLSTYALTLYKHTATVDGRTILVDFWDTAGQERFQSMHASYYHKAHACIMVFDVQRKVTYRNLSTWYTELREFRPEIPCIVVANKIDDINVTQKSFNFAKKFSLPLYFVSAADGTNVVKLFNDAIRLAVSYKQNSQDFMDEIFQELENFSLEQEEEDVPDQEQSSSIETPSEEAASPHS
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
23UbiquitinationYDADDNVKIICLGDS
CCCCCCEEEEEECCC
32.38-
23AcetylationYDADDNVKIICLGDS
CCCCCCEEEEEECCC
32.38-
26S-nitrosylationDDNVKIICLGDSAVG
CCCEEEEEECCCHHC
3.8624105792
30PhosphorylationKIICLGDSAVGKSKL
EEEEECCCHHCHHHH
24.0530622161
34AcetylationLGDSAVGKSKLMERF
ECCCHHCHHHHHHHH
37.51-
34UbiquitinationLGDSAVGKSKLMERF
ECCCHHCHHHHHHHH
37.51-
35AcetylationGDSAVGKSKLMERFL
CCCHHCHHHHHHHHH
25.70-
52PhosphorylationGFQPQQLSTYALTLY
CCCHHHHHHHHHEEE
18.29-
57PhosphorylationQLSTYALTLYKHTAT
HHHHHHHEEEEEEEE
21.62-
59PhosphorylationSTYALTLYKHTATVD
HHHHHEEEEEEEEEC
8.76-
85PhosphorylationAGQERFQSMHASYYH
HCHHHHHHHHHHHHH
15.1523663014
89PhosphorylationRFQSMHASYYHKAHA
HHHHHHHHHHHHCCE
16.1423663014
90PhosphorylationFQSMHASYYHKAHAC
HHHHHHHHHHHCCEE
15.4623663014
91PhosphorylationQSMHASYYHKAHACI
HHHHHHHHHHCCEEE
8.3723663014
108PhosphorylationFDVQRKVTYRNLSTW
EEEECHHCCCCHHHH
21.5724719451
141PhosphorylationKIDDINVTQKSFNFA
CCCCCCCCHHHCCHH
26.2820058876
143UbiquitinationDDINVTQKSFNFAKK
CCCCCCHHHCCHHHH
47.88-
144PhosphorylationDINVTQKSFNFAKKF
CCCCCHHHCCHHHHC
18.66-
144 (in isoform 2)Ubiquitination-18.6621890473
149UbiquitinationQKSFNFAKKFSLPLY
HHHCCHHHHCCCCEE
50.65-
150UbiquitinationKSFNFAKKFSLPLYF
HHCCHHHHCCCCEEE
36.43-
150 (in isoform 1)Ubiquitination-36.4321890473
151 (in isoform 2)Ubiquitination-10.0021890473

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 RBL2B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RBL2B_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 RBL2B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CEP19_HUMANCEP19physical
16189514
RASEF_HUMANRASEFphysical
26186194
IDI2_HUMANIDI2physical
26186194
RASEF_HUMANRASEFphysical
28514442
IDI2_HUMANIDI2physical
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 RBL2B_HUMAN

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Related Literatures of Post-Translational Modification

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