dbPTM

TIAR_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TIAR_HUMAN
UniProt AC	Q01085
Protein Name	Nucleolysin TIAR
Gene Name	TIAL1
Organism	Homo sapiens (Human).
Sequence Length	375
Subcellular Localization	Cytoplasm. Nucleus. Cytoplasmic granule. The cytoplasmic granules are stress granules which are a dense aggregation in the cytosol composed of proteins and RNAs that appear when the cell is under stress. Colocalizes with NANOS3 in the stress granules
Protein Description	RNA-binding protein. Possesses nucleolytic activity against cytotoxic lymphocyte target cells. May be involved in apoptosis..
Protein Sequence	MMEDDGQPRTLYVGNLSRDVTEVLILQLFSQIGPCKSCKMITEHTSNDPYCFVEFYEHRDAAAALAAMNGRKILGKEVKVNWATTPSSQKKDTSNHFHVFVGDLSPEITTEDIKSAFAPFGKISDARVVKDMATGKSKGYGFVSFYNKLDAENAIVHMGGQWLGGRQIRTNWATRKPPAPKSTQENNTKQLRFEDVVNQSSPKNCTVYCGGIASGLTDQLMRQTFSPFGQIMEIRVFPEKGYSFVRFSTHESAAHAIVSVNGTTIEGHVVKCYWGKESPDMTKNFQQVDYSQWGQWSQVYGNPQQYGQYMANGWQVPPYGVYGQPWNQQGFGVDQSPSAAWMGGFGAQPPQGQAPPPVIPPPNQAGYGMASYQTQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Phosphorylation	EDDGQPRTLYVGNLS CCCCCCCEEEECCCC	29.17	28152594
12	Phosphorylation	DGQPRTLYVGNLSRD CCCCCEEEECCCCCC	13.00	28152594
17	Phosphorylation	TLYVGNLSRDVTEVL EEEECCCCCCHHHHH	30.36	28152594
39	Acetylation	IGPCKSCKMITEHTS HCCCCCCCEEEECCC	40.19	26051181
50	Phosphorylation	EHTSNDPYCFVEFYE ECCCCCCEEEEEEEC	11.03	19060867
52 (in isoform 2)	Phosphorylation	-	4.94	-
52	Phosphorylation	TSNDPYCFVEFYEHR CCCCCEEEEEEECCH	4.94	-
53	Phosphorylation	SNDPYCFVEFYEHRD CCCCEEEEEEECCHH	4.43	-
53 (in isoform 2)	Phosphorylation	-	4.43	-
57	Phosphorylation	YCFVEFYEHRDAAAA EEEEEEECCHHHHHH	37.45	-
57 (in isoform 2)	Phosphorylation	-	37.45	-
67	Phosphorylation	DAAAALAAMNGRKIL HHHHHHHHHCCCEEC	7.88	-
67 (in isoform 2)	Phosphorylation	-	7.88	15592455
76	Ubiquitination	NGRKILGKEVKVNWA CCCEECCEEEEEEEE	56.75	-
79	Ubiquitination	KILGKEVKVNWATTP EECCEEEEEEEECCC	30.83	-
84	Phosphorylation	EVKVNWATTPSSQKK EEEEEEECCCCCCCC	30.74	28857561
85	Phosphorylation	VKVNWATTPSSQKKD EEEEEECCCCCCCCC	17.27	21815630
87	Phosphorylation	VNWATTPSSQKKDTS EEEECCCCCCCCCCC	43.22	25159151
88	Phosphorylation	NWATTPSSQKKDTSN EEECCCCCCCCCCCC	47.42	25159151
90	Acetylation	ATTPSSQKKDTSNHF ECCCCCCCCCCCCCE	55.34	26051181
90	Ubiquitination	ATTPSSQKKDTSNHF ECCCCCCCCCCCCCE	55.34	-
91	Ubiquitination	TTPSSQKKDTSNHFH CCCCCCCCCCCCCEE	59.61	-
93	Phosphorylation	PSSQKKDTSNHFHVF CCCCCCCCCCCEEEE	40.06	21406692
94	Phosphorylation	SSQKKDTSNHFHVFV CCCCCCCCCCEEEEE	38.14	21406692
101	Phosphorylation	SNHFHVFVGDLSPEI CCCEEEEEECCCCCC	5.92	27251275
102	Phosphorylation	NHFHVFVGDLSPEIT CCEEEEEECCCCCCC	20.76	24719451
105	Phosphorylation	HVFVGDLSPEITTED EEEEECCCCCCCHHH	25.81	20068231
108 (in isoform 2)	Ubiquitination	-	7.02	-
109	Phosphorylation	GDLSPEITTEDIKSA ECCCCCCCHHHHHHH	23.59	20068231
110	Phosphorylation	DLSPEITTEDIKSAF CCCCCCCHHHHHHHC	37.00	21406692
115	Phosphorylation	ITTEDIKSAFAPFGK CCHHHHHHHCCCCCC	29.02	18452278
122	Phosphorylation	SAFAPFGKISDARVV HHCCCCCCCCCCEEE	39.14	-
122	Ubiquitination	SAFAPFGKISDARVV HHCCCCCCCCCCEEE	39.14	19608861
122	Malonylation	SAFAPFGKISDARVV HHCCCCCCCCCCEEE	39.14	26320211
122	Acetylation	SAFAPFGKISDARVV HHCCCCCCCCCCEEE	39.14	19608861
132	Phosphorylation	DARVVKDMATGKSKG CCEEEEECCCCCCCC	2.74	-
134	O-linked_Glycosylation	RVVKDMATGKSKGYG EEEEECCCCCCCCCC	38.21	30379171
134	Phosphorylation	RVVKDMATGKSKGYG EEEEECCCCCCCCCC	38.21	22210691
136	Ubiquitination	VKDMATGKSKGYGFV EEECCCCCCCCCCEE	44.64	-
137	O-linked_Glycosylation	KDMATGKSKGYGFVS EECCCCCCCCCCEEE	32.43	30379171
138	Malonylation	DMATGKSKGYGFVSF ECCCCCCCCCCEEEE	60.69	26320211
139	Ubiquitination	MATGKSKGYGFVSFY CCCCCCCCCCEEEEE	34.58	19608861
139 (in isoform 2)	Ubiquitination	-	34.58	-
139	Ubiquitination	MATGKSKGYGFVSFY CCCCCCCCCCEEEEE	34.58	21890473
139	Acetylation	MATGKSKGYGFVSFY CCCCCCCCCCEEEEE	34.58	19608861
140	Phosphorylation	ATGKSKGYGFVSFYN CCCCCCCCCEEEEEE	15.89	20090780
146	Phosphorylation	GYGFVSFYNKLDAEN CCCEEEEEEECCCCC	12.13	20090780
189	Ubiquitination	STQENNTKQLRFEDV CCCCCCCEEEEHHHH	49.84	-
200	Phosphorylation	FEDVVNQSSPKNCTV HHHHHCCCCCCCCEE	43.32	30266825
201	Phosphorylation	EDVVNQSSPKNCTVY HHHHCCCCCCCCEEE	30.08	30266825
203	Ubiquitination	VVNQSSPKNCTVYCG HHCCCCCCCCEEEEC	67.61	-
206	Phosphorylation	QSSPKNCTVYCGGIA CCCCCCCEEEECHHH	24.73	22210691
208	Phosphorylation	SPKNCTVYCGGIASG CCCCCEEEECHHHHC	2.75	22210691
217	Phosphorylation	GGIASGLTDQLMRQT CHHHHCHHHHHHHHH	25.81	22210691
218	Phosphorylation	GIASGLTDQLMRQTF HHHHCHHHHHHHHHC	44.66	24719451
220 (in isoform 2)	Ubiquitination	-	3.21	-
226	Phosphorylation	QLMRQTFSPFGQIME HHHHHHCCCCCCEEE	23.78	27050516
243	Phosphorylation	VFPEKGYSFVRFSTH ECCCCCCCEEEEECC	26.40	24719451
276	Acetylation	VVKCYWGKESPDMTK EEEEECCCCCCCCCC	40.65	26051181
278	Phosphorylation	KCYWGKESPDMTKNF EEECCCCCCCCCCCC	29.68	21815630
282	Phosphorylation	GKESPDMTKNFQQVD CCCCCCCCCCCEECC	30.16	-
295	Phosphorylation	VDYSQWGQWSQVYGN CCHHHHCCHHHHHCC	33.42	27251275

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 TIAR_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TIAR_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 TIAR_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
VDAC1_HUMAN	VDAC1	physical	22939629
UB2D2_HUMAN	UBE2D2	physical	22939629
TOM40_HUMAN	TOMM40	physical	22939629
UFM1_HUMAN	UFM1	physical	22939629
GA45A_HUMAN	GADD45A	physical	20932473
CCD58_HUMAN	CCDC58	physical	26344197
PCBP1_HUMAN	PCBP1	physical	26344197
PCBP2_HUMAN	PCBP2	physical	26344197
PTRD1_HUMAN	PTRHD1	physical	26344197
FA83H_HUMAN	FAM83H	physical	28514442
TROP_HUMAN	TRO	physical	28514442
AINX_HUMAN	INA	physical	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 TIAR_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-122, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-50, AND MASSSPECTROMETRY.	15592455 [Abstract]