U119B_HUMAN - dbPTM
U119B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID U119B_HUMAN
UniProt AC A6NIH7
Protein Name Protein unc-119 homolog B
Gene Name UNC119B
Organism Homo sapiens (Human).
Sequence Length 251
Subcellular Localization Cell projection, cilium . Enriched at the transition zone and extended into the proximal end of the cilium.
Protein Description Myristoyl-binding protein that acts as a cargo adapter: specifically binds the myristoyl moiety of a subset of N-terminally myristoylated proteins and is required for their localization. Binds myristoylated NPHP3 and plays a key role in localization of NPHP3 to the primary cilium membrane. Does not bind all myristoylated proteins. Probably plays a role in trafficking proteins in photoreceptor cells..
Protein Sequence MSGSNPKAAAAASAAGPGGLVAGKEEKKKAGGGVLNRLKARRQAPHHAADDGVGAAVTEQELLALDTIRPEHVLRLSRVTENYLCKPEDNIYSIDFTRFKIRDLETGTVLFEIAKPCVSDQEEDEEEGGGDVDISAGRFVRYQFTPAFLRLRTVGATVEFTVGDKPVSNFRMIERHYFREHLLKNFDFDFGFCIPSSRNTCEHIYEFPQLSEDVIRLMIENPYETRSDSFYFVDNKLIMHNKADYAYNGGQ
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
2Acetylation------MSGSNPKAA
------CCCCCHHHH
51.4322814378
24AcetylationPGGLVAGKEEKKKAG
CCCEECCHHHHHHCC
53.6219608861
27AcetylationLVAGKEEKKKAGGGV
EECCHHHHHHCCCHH
61.7418585049
29UbiquitinationAGKEEKKKAGGGVLN
CCHHHHHHCCCHHHH
64.43-
86UbiquitinationVTENYLCKPEDNIYS
CCCCEEECCCCCEEE
49.17-
92PhosphorylationCKPEDNIYSIDFTRF
ECCCCCEEEEECEEE
13.0627642862
106PhosphorylationFKIRDLETGTVLFEI
EEEEECCCCCEEEEE
45.5128122231
108PhosphorylationIRDLETGTVLFEIAK
EEECCCCCEEEEEEC
22.8128122231
119PhosphorylationEIAKPCVSDQEEDEE
EEECCCCCCCCHHHH
40.0528464451
205PhosphorylationRNTCEHIYEFPQLSE
CCCCHHHHCCCCCCH
17.2727642862
229PhosphorylationPYETRSDSFYFVDNK
CCCCCCCCEEEECCE
24.0827499020
242UbiquitinationNKLIMHNKADYAYNG
CEEEEECCCCCCCCC
28.14-
245PhosphorylationIMHNKADYAYNGGQ-
EEECCCCCCCCCCC-
18.8229496907
247PhosphorylationHNKADYAYNGGQ---
ECCCCCCCCCCC---
14.2229496907

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 U119B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of U119B_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 U119B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBAC1_HUMANUBAC1physical
22939629

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 U119B_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-24, AND MASS SPECTROMETRY.

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