AR13B_HUMAN - dbPTM
AR13B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AR13B_HUMAN
UniProt AC Q3SXY8
Protein Name ADP-ribosylation factor-like protein 13B
Gene Name ARL13B
Organism Homo sapiens (Human).
Sequence Length 428
Subcellular Localization Cell projection, cilium membrane
Lipid-anchor . Cell projection, cilium . Associates to the cilium membrane via palmitoylation. Localizes to proximal ciliary membranes, to an inversin-like subciliary membrane compartment, excluding the transition z
Protein Description Cilium-specific protein required to control the microtubule-based, ciliary axoneme structure. May act by maintaining the association between IFT subcomplexes A and B. Binds GTP but is not able to hydrolyze it; the GTPase activity remains unclear. Required to pattern the neural tube. Involved in cerebral cortex development: required for the initial formation of a polarized radial glial scaffold, the first step in the construction of the cerebral cortex, by regulating ciliary signaling. Regulates the migration and placement of postmitotic interneurons in the developing cerebral cortex. May regulate endocytic recycling traffic; however, additional evidences are required to confirm these data..
Protein Sequence MFSLMASCCGWFKRWREPVRKVTLLMVGLDNAGKTATAKGIQGEYPEDVAPTVGFSKINLRQGKFEVTIFDLGGGIRIRGIWKNYYAESYGVIFVVDSSDEERMEETKEAMSEMLRHPRISGKPILVLANKQDKEGALGEADVIECLSLEKLVNEHKCLCQIEPCSAISGYGKKIDKSIKKGLYWLLHVIARDFDALNERIQKETTEQRALEEQEKQERAERVRKLREERKQNEQEQAELDGTSGLAELDPEPTNPFQPIASVIIENEGKLEREKKNQKMEKDSDGCHLKHKMEHEQIETQGQVNHNGQKNNEFGLVENYKEALTQQLKNEDETDRPSLESANGKKKTKKLRMKRNHRVEPLNIDDCAPESPTPPPPPPPVGWGTPKVTRLPKLEPLGETHHNDFYRKPLPPLAVPQRPNSDAHDVIS
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
3Phosphorylation-----MFSLMASCCG
-----CCHHHHHHHH		18.8820068231
7Phosphorylation-MFSLMASCCGWFKR
-CCHHHHHHHHHHHH		8.9320068231
8S-palmitoylationMFSLMASCCGWFKRW
CCHHHHHHHHHHHHH		1.48-
9S-palmitoylationFSLMASCCGWFKRWR
CHHHHHHHHHHHHHH		5.11-
23PhosphorylationREPVRKVTLLMVGLD
HHHHHHEEEEEEECC		19.7429514088
32UbiquitinationLMVGLDNAGKTATAK
EEEECCCCCCCCCCC		22.1122817900
35PhosphorylationGLDNAGKTATAKGIQ
ECCCCCCCCCCCCCC		28.4629514088
37PhosphorylationDNAGKTATAKGIQGE
CCCCCCCCCCCCCCC		33.8529514088
39UbiquitinationAGKTATAKGIQGEYP
CCCCCCCCCCCCCCC		52.7923000965
42UbiquitinationTATAKGIQGEYPEDV
CCCCCCCCCCCCCCC		47.5422817900
44UbiquitinationTAKGIQGEYPEDVAP
CCCCCCCCCCCCCCC		41.3529967540
45PhosphorylationAKGIQGEYPEDVAPT
CCCCCCCCCCCCCCC		20.8121945579
45UbiquitinationAKGIQGEYPEDVAPT
CCCCCCCCCCCCCCC		20.8122817900
48UbiquitinationIQGEYPEDVAPTVGF
CCCCCCCCCCCCCCC		37.0629967540
49UbiquitinationQGEYPEDVAPTVGFS
CCCCCCCCCCCCCCE		7.0123000965
50UbiquitinationGEYPEDVAPTVGFSK
CCCCCCCCCCCCCEE		13.3329967540
52UbiquitinationYPEDVAPTVGFSKIN
CCCCCCCCCCCEEEE		24.4323000965
54UbiquitinationEDVAPTVGFSKINLR
CCCCCCCCCEEEEEC		24.4829967540
57UbiquitinationAPTVGFSKINLRQGK
CCCCCCEEEEECCCE		33.0922817900
57 (in isoform 1)Ubiquitination-33.0921906983
64UbiquitinationKINLRQGKFEVTIFD
EEEECCCEEEEEEEE		29.9723000965
136UbiquitinationANKQDKEGALGEADV
EECCCCCCCCCCCCH		31.6629967540
142UbiquitinationEGALGEADVIECLSL
CCCCCCCCHHHHHCH		37.3129967540
148PhosphorylationADVIECLSLEKLVNE
CCHHHHHCHHHHHHC		46.2530576142
151UbiquitinationIECLSLEKLVNEHKC
HHHHCHHHHHHCCCC		64.1329967540
157UbiquitinationEKLVNEHKCLCQIEP
HHHHHCCCCEEEEEC		23.7929967540
178PhosphorylationYGKKIDKSIKKGLYW
CCHHHCHHHHHHHHH		35.57-
184PhosphorylationKSIKKGLYWLLHVIA
HHHHHHHHHHHHHHH		11.59-
214UbiquitinationEQRALEEQEKQERAE
HHHHHHHHHHHHHHH		54.5429967540
218UbiquitinationLEEQEKQERAERVRK
HHHHHHHHHHHHHHH		66.0029967540
306UbiquitinationETQGQVNHNGQKNNE
ECCCCCCCCCCCCCC		40.7229967540
320PhosphorylationEFGLVENYKEALTQQ
CCCHHHHHHHHHHHH		9.1921945579
321UbiquitinationFGLVENYKEALTQQL
CCHHHHHHHHHHHHH		48.3629967540
325PhosphorylationENYKEALTQQLKNED
HHHHHHHHHHHHCCC		22.7129978859
338PhosphorylationEDETDRPSLESANGK
CCCCCCCCHHCCCCC		45.7425159151
341PhosphorylationTDRPSLESANGKKKT
CCCCCHHCCCCCCCC		32.1225159151
371PhosphorylationIDDCAPESPTPPPPP
CCCCCCCCCCCCCCC		32.7725159151
373PhosphorylationDCAPESPTPPPPPPP
CCCCCCCCCCCCCCC		58.6729759185
385PhosphorylationPPPVGWGTPKVTRLP
CCCCCCCCCCCCCCC		17.2725850435
400PhosphorylationKLEPLGETHHNDFYR
CCCCCCCCCCCCCCC		27.0026552605
406PhosphorylationETHHNDFYRKPLPPL
CCCCCCCCCCCCCCC		22.1625884760
421PhosphorylationAVPQRPNSDAHDVIS
CCCCCCCCCCCCCCC		38.5728555341
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 AR13B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AR13B_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 AR13B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TT30A_HUMANTTC30Aphysical
26186194
STK25_HUMANSTK25physical
26186194
IFT56_HUMANTTC26physical
26186194
VAC14_HUMANVAC14physical
26186194
IFT81_HUMANIFT81physical
26186194
IFT46_HUMANIFT46physical
26186194
TTI1_HUMANTTI1physical
26186194
ARV1_HUMANARV1physical
26186194
FAKD1_HUMANFASTKD1physical
26186194
IFT74_HUMANIFT74physical
26186194
IFT52_HUMANIFT52physical
26186194
IPO11_HUMANIPO11physical
26186194
TNPO2_HUMANTNPO2physical
26186194
ANR50_HUMANANKRD50physical
26186194
PDXD1_HUMANPDXDC1physical
26186194
IFT22_HUMANIFT22physical
26186194
RAB18_HUMANRAB18physical
26186194
TT30A_HUMANTTC30Aphysical
28514442
IFT81_HUMANIFT81physical
28514442
IFT46_HUMANIFT46physical
28514442
IFT74_HUMANIFT74physical
28514442
IFT52_HUMANIFT52physical
28514442
IFT22_HUMANIFT22physical
28514442
ANR50_HUMANANKRD50physical
28514442
STK25_HUMANSTK25physical
28514442
PDXD1_HUMANPDXDC1physical
28514442
FAKD1_HUMANFASTKD1physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
612291Joubert syndrome 8 (JBTS8)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AR13B_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory