U119A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: U119A_HUMAN
• UniProt AC: Q13432
• Protein Name: Protein unc-119 homolog A
• Gene Name: UNC119
• Organism: Homo sapiens (Human).
• Sequence Length: 240
• Subcellular Localization: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, spindle pole . Cytoplasm, cytoskeleton, spindle . Localizes to the centrosome in interphase cells and begins to translocate from the spindle pole to the spi
• Protein Description: Involved in synaptic functions in photoreceptor cells, the signal transduction in immune cells as a Src family kinase activator, endosome recycling, the uptake of bacteria and endocytosis, protein trafficking in sensory neurons and as lipid-binding chaperone with specificity for a diverse subset of myristoylated proteins. Specifically binds the myristoyl moiety of a subset of N-terminally myristoylated proteins and is required for their localization. Binds myristoylated GNAT1 and is required for G-protein localization and trafficking in sensory neurons. Probably plays a role in trafficking proteins in photoreceptor cells. Plays important roles in mediating Src family kinase signals for the completion of cytokinesis via RAB11A..
• Protein Sequence: MKVKKGGGGAGTATESAPGPSGQSVAPIPQPPAESESGSESEPDAGPGPRPGPLQRKQPIGPEDVLGLQRITGDYLCSPEENIYKIDFVRFKIRDMDSGTVLFEIKKPPVSERLPINRRDLDPNAGRFVRYQFTPAFLRLRQVGATVEFTVGDKPVNNFRMIERHYFRNQLLKSFDFHFGFCIPSSKNTCEHIYDFPPLSEELISEMIRHPYETQSDSFYFVDDRLVMHNKADYSYSGTP

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
12	Phosphorylation	KGGGGAGTATESAPG CCCCCCCCCCCCCCC	29.85	30177828
14	Phosphorylation	GGGAGTATESAPGPS CCCCCCCCCCCCCCC	30.25	30177828
16	Phosphorylation	GAGTATESAPGPSGQ CCCCCCCCCCCCCCC	35.09	30177828
21	Phosphorylation	TESAPGPSGQSVAPI CCCCCCCCCCCCCCC	56.21	29449344
24	Phosphorylation	APGPSGQSVAPIPQP CCCCCCCCCCCCCCC	24.62	29449344
35	Phosphorylation	IPQPPAESESGSESE CCCCCCCCCCCCCCC	38.89	20363803
37	Phosphorylation	QPPAESESGSESEPD CCCCCCCCCCCCCCC	57.82	20363803
39	Phosphorylation	PAESESGSESEPDAG CCCCCCCCCCCCCCC	47.42	20363803
41	Phosphorylation	ESESGSESEPDAGPG CCCCCCCCCCCCCCC	57.01	20363803
57	Ubiquitination	RPGPLQRKQPIGPED CCCCCCCCCCCCHHH	47.68	-
75	Phosphorylation	LQRITGDYLCSPEEN CEEECCCEEECCCCC	15.79	29496907
78	Phosphorylation	ITGDYLCSPEENIYK ECCCEEECCCCCEEE	32.52	25159151
84	Phosphorylation	CSPEENIYKIDFVRF ECCCCCEEECEEEEE	17.30	29496907
85	Ubiquitination	SPEENIYKIDFVRFK CCCCCEEECEEEEEE	31.81	-
98	Phosphorylation	FKIRDMDSGTVLFEI EEEEECCCCEEEEEE	29.71	20068231
100	Phosphorylation	IRDMDSGTVLFEIKK EEECCCCEEEEEEEC	20.28	20068231
111	Phosphorylation	EIKKPPVSERLPINR EEECCCHHHCCCCCC	23.83	20068231
146	Phosphorylation	RLRQVGATVEFTVGD HHHCCCCEEEEEECC	18.03	-
150	Phosphorylation	VGATVEFTVGDKPVN CCCEEEEEECCCCCC	15.29	-
194	Phosphorylation	KNTCEHIYDFPPLSE CCCCCEECCCCCCCH	17.28	-
228	Sulfoxidation	FVDDRLVMHNKADYS EECCEEEEECCCCCC	3.22	30846556
234	Phosphorylation	VMHNKADYSYSGTP- EEECCCCCCCCCCC-	17.86	-
236	Phosphorylation	HNKADYSYSGTP--- ECCCCCCCCCCC---	12.61	-

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
37	S	Phosphorylation	Kinase	CK2	-	Uniprot
39	S	Phosphorylation	Kinase	CK2	-	Uniprot
41	S	Phosphorylation	Kinase	CK2	-	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of U119A_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of U119A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CP074_HUMAN	C16orf74	physical	16189514
CD3Z_HUMAN	CD247	physical	14757743
CD4_HUMAN	CD4	physical	14757743
FYN_HUMAN	FYN	physical	14757743
LCK_HUMAN	LCK	physical	14757743
LYN_HUMAN	LYN	physical	12496276
HCK_HUMAN	HCK	physical	12496276
ARL2_HUMAN	ARL2	physical	12527357
AMOT_HUMAN	AMOT	physical	25416956
CP074_HUMAN	C16orf74	physical	25416956
PALD_HUMAN	PALD1	physical	26186194
PDE9A_HUMAN	PDE9A	physical	26186194
NPHP3_HUMAN	NPHP3	physical	26186194
OCC1_HUMAN	C12orf75	physical	26186194
PDE8A_HUMAN	PDE8A	physical	26186194
LIMK2_HUMAN	LIMK2	physical	26186194
CE030_HUMAN	C5orf30	physical	26186194
KGP2_HUMAN	PRKG2	physical	26186194
RFTN1_HUMAN	RFTN1	physical	26186194
ARL3_HUMAN	ARL3	physical	26186194
RNF34_HUMAN	RNF34	physical	26186194
RSPRY_HUMAN	RSPRY1	physical	26186194
NPHP3_HUMAN	NPHP3	physical	28514442
KGP2_HUMAN	PRKG2	physical	28514442
PALD_HUMAN	PALD1	physical	28514442
PDE9A_HUMAN	PDE9A	physical	28514442
PDE8A_HUMAN	PDE8A	physical	28514442
RNF34_HUMAN	RNF34	physical	28514442
LIMK2_HUMAN	LIMK2	physical	28514442
CE030_HUMAN	C5orf30	physical	28514442
LZTS1_HUMAN	LZTS1	physical	28514442
LZTS2_HUMAN	LZTS2	physical	28514442
OCC1_HUMAN	C12orf75	physical	28514442
RFTN1_HUMAN	RFTN1	physical	28514442
RSPRY_HUMAN	RSPRY1	physical	28514442
CAN15_HUMAN	CAPN15	physical	28514442
U119B_HUMAN	UNC119B	physical	28514442
KPSH1_HUMAN	PSKH1	physical	28514442
NOCT_HUMAN	CCRN4L	physical	28514442
FMNL2_HUMAN	FMNL2	physical	28514442
ARL3_HUMAN	ARL3	physical	28514442
NISCH_HUMAN	NISCH	physical	28514442

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• from 40 year old, the patient suffered from poor night vision, defective color vision and light-sensitivity. At 57 year old, she displayed reduced visual acuity, myopa, macular atrophy and pericentral ring scotomas. The disease was caused by a heterozygous mutation causing premature termination and truncated UNC119 protein with dominant-negative effect.: Note=Defects in UNC119 may be a cause of cone-rod dystrophy. A mutation was found in a 57-year-old woman with late-onset cone-rod dystrophy
• 615518:
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.