ATE1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ATE1_HUMAN
• UniProt AC: O95260
• Protein Name: Arginyl-tRNA--protein transferase 1
• Gene Name: ATE1
• Organism: Homo sapiens (Human).
• Sequence Length: 518
• Subcellular Localization: Isoform ATE1-1: Nucleus . Cytoplasm .; Isoform ATE1-2: Cytoplasm .
• Protein Description: Involved in the post-translational conjugation of arginine to the N-terminal aspartate or glutamate of a protein. This arginylation is required for degradation of the protein via the ubiquitin pathway. Does not arginylate cysteine residues (By similarity)..
• Protein Sequence: MAFWAGGSPSVVDYFPSEDFYRCGYCKNESGSRSNGMWAHSMTVQDYQDLIDRGWRRSGKYVYKPVMNQTCCPQYTIRCRPLQFQPSKSHKKVLKKMLKFLAKGEVPKGSCEDEPMDSTMDDAVAGDFALINKLDIQCDLKTLSDDIKESLESEGKNSKKEEPQELLQSQDFVGEKLGSGEPSHSVKVHTVPKPGKGADLSKPPCRKAKEIRKERKRLKLMQQNPAGELEGFQAQGHPPSLFPPKAKSNQPKSLEDLIFESLPENASHKLEVRVVRSSPPSSQFKATLLESYQVYKRYQMVIHKNPPDTPTESQFTRFLCSSPLEAETPPNGPDCGYGSFHQQYWLDGKIIAVGVIDILPNCVSSVYLYYDPDYSFLSLGVYSALREIAFTRQLHEKTSQLSYYYMGFYIHSCPKMKYKGQYRPSDLLCPETYVWVPIEQCLPSLENSKYCRFNQDPEAVDEDRSTEPDRLQVFHKRAIMPYGVYKKQQKDPSEEAAVLQYASLVGQKCSERMLLFRN

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
10	Phosphorylation	FWAGGSPSVVDYFPS CCCCCCCCHHHCCCC	36.15	28348404
25	Phosphorylation	EDFYRCGYCKNESGS CCCCCCCCCCCCCCC	12.13	22210691
32	Phosphorylation	YCKNESGSRSNGMWA CCCCCCCCCCCCEEC	41.64	22210691
34	Phosphorylation	KNESGSRSNGMWAHS CCCCCCCCCCEECEE	39.16	22210691
43	Phosphorylation	GMWAHSMTVQDYQDL CEECEEEEHHHHHHH	20.31	22210691
61	Phosphorylation	GWRRSGKYVYKPVMN HCHHCCCEEEECCCC	16.73	-
63	Phosphorylation	RRSGKYVYKPVMNQT HHCCCEEEECCCCCC	13.39	18083107
75	Phosphorylation	NQTCCPQYTIRCRPL CCCCCCCCEEEECCC	6.84	26434776
76	Phosphorylation	QTCCPQYTIRCRPLQ CCCCCCCEEEECCCC	9.19	24719451
103	Ubiquitination	KMLKFLAKGEVPKGS HHHHHHHCCCCCCCC	58.72	-
110	Phosphorylation	KGEVPKGSCEDEPMD CCCCCCCCCCCCCCC	22.06	28270605
118	Phosphorylation	CEDEPMDSTMDDAVA CCCCCCCCCCCHHHH	21.27	28270605
119	Phosphorylation	EDEPMDSTMDDAVAG CCCCCCCCCCHHHHH	21.98	27690223
141	Ubiquitination	LDIQCDLKTLSDDIK CCEEEEHHHCCHHHH	33.88	-
142	Phosphorylation	DIQCDLKTLSDDIKE CEEEEHHHCCHHHHH	38.50	23312004
144	Phosphorylation	QCDLKTLSDDIKESL EEEHHHCCHHHHHHH	38.17	23312004
148	Ubiquitination	KTLSDDIKESLESEG HHCCHHHHHHHHHCC	48.52	-
150	Phosphorylation	LSDDIKESLESEGKN CCHHHHHHHHHCCCC	32.22	22817901
160	Ubiquitination	SEGKNSKKEEPQELL HCCCCCCCCCHHHHH	68.10	-
169	Phosphorylation	EPQELLQSQDFVGEK CHHHHHHCCCCCCCC	31.52	17525332
169 (in isoform 2)	Phosphorylation	-	31.52	-
176	Ubiquitination	SQDFVGEKLGSGEPS CCCCCCCCCCCCCCC	52.82	-
179	Phosphorylation	FVGEKLGSGEPSHSV CCCCCCCCCCCCCEE	50.88	25159151
179	O-linked_Glycosylation	FVGEKLGSGEPSHSV CCCCCCCCCCCCCEE	50.88	29351928
183	O-linked_Glycosylation	KLGSGEPSHSVKVHT CCCCCCCCCEEEEEE	24.88	29351928
185	Phosphorylation	GSGEPSHSVKVHTVP CCCCCCCEEEEEECC	28.15	28857561
202	Acetylation	GKGADLSKPPCRKAK CCCCCCCCCCCHHHH	61.34	26822725
240 (in isoform 2)	Phosphorylation	-	47.28	-
240	Phosphorylation	QAQGHPPSLFPPKAK HHCCCCCCCCCCCCC	47.28	20068231
252	Ubiquitination	KAKSNQPKSLEDLIF CCCCCCCCCHHHHHH	58.89	-
261	Phosphorylation	LEDLIFESLPENASH HHHHHHHHCCCCCCC	38.18	25921289
267	Phosphorylation	ESLPENASHKLEVRV HHCCCCCCCCEEEEE	32.51	25921289
269 (in isoform 1)	Ubiquitination	-	43.79	21906983
269 (in isoform 2)	Ubiquitination	-	43.79	21906983
269	Ubiquitination	LPENASHKLEVRVVR CCCCCCCCEEEEEEE	43.79	2190698
277	Phosphorylation	LEVRVVRSSPPSSQF EEEEEEECCCCHHHH	35.27	24719451
278	Phosphorylation	EVRVVRSSPPSSQFK EEEEEECCCCHHHHH	30.20	28192239
285	Methylation	SPPSSQFKATLLESY CCCHHHHHHHHHHHH	32.59	-
287	Phosphorylation	PSSQFKATLLESYQV CHHHHHHHHHHHHHH	32.25	28192239
291	Phosphorylation	FKATLLESYQVYKRY HHHHHHHHHHHHHHE	22.34	28192239
292	Phosphorylation	KATLLESYQVYKRYQ HHHHHHHHHHHHHEE	7.82	28192239
311	Phosphorylation	KNPPDTPTESQFTRF CCCCCCCCHHHHHHH	50.81	29759185
316	Phosphorylation	TPTESQFTRFLCSSP CCCHHHHHHHHHCCC	16.93	29759185
422	Phosphorylation	KMKYKGQYRPSDLLC CCCCCCCCCHHHCCC	32.91	-
433	Phosphorylation	DLLCPETYVWVPIEQ HCCCCCCEEEEEHHH	7.22	-
464	Methylation	PEAVDEDRSTEPDRL HHHCCCCCCCCCCHH	43.35	-
482	Phosphorylation	HKRAIMPYGVYKKQQ HHHHHHCCCCCCCCC	11.22	24719451
485	Phosphorylation	AIMPYGVYKKQQKDP HHHCCCCCCCCCCCC	14.22	18083107
490	Ubiquitination	GVYKKQQKDPSEEAA CCCCCCCCCCCHHHH	69.94	-
501	Phosphorylation	EEAAVLQYASLVGQK HHHHHHHHHHHHCHH	8.26	27642862
508	Ubiquitination	YASLVGQKCSERMLL HHHHHCHHHHHHHHH	33.52	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of ATE1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ATE1_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 ATE1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SUV91_HUMAN	SUV39H1	physical	23455924

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169, AND MASSSPECTROMETRY.
PubMed: 17525332