THYN1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: THYN1_HUMAN
• UniProt AC: Q9P016
• Protein Name: Thymocyte nuclear protein 1
• Gene Name: THYN1
• Organism: Homo sapiens (Human).
• Sequence Length: 225
• Subcellular Localization: Nucleus.
• Protein Description: Specifically binds 5-hydroxymethylcytosine (5hmC), suggesting that it acts as a specific reader of 5hmC..
• Protein Sequence: MSRPRKRLAGTSGSDKGLSGKRTKTENSGEALAKVEDSNPQKTSATKNCLKNLSSHWLMKSEPESRLEKGVDVKFSIEDLKAQPKQTTCWDGVRNYQARNFLRAMKLGEEAFFYHSNCKEPGIAGLMKIVKEAYPDHTQFEKNNPHYDPSSKEDNPKWSMVDVQFVRMMKRFIPLAELKSYHQAHKATGGPLKNMVLFTRQRLSIQPLTQEEFDFVLSLEEKEPS

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
11	Phosphorylation	PRKRLAGTSGSDKGL CCCCCCCCCCCCCCC	25.06	23684312
12	Phosphorylation	RKRLAGTSGSDKGLS CCCCCCCCCCCCCCC	35.07	21712546
14	Phosphorylation	RLAGTSGSDKGLSGK CCCCCCCCCCCCCCC	35.60	23401153
16	Acetylation	AGTSGSDKGLSGKRT CCCCCCCCCCCCCCE	64.55	23954790
16	Ubiquitination	AGTSGSDKGLSGKRT CCCCCCCCCCCCCCE	64.55	-
19	Phosphorylation	SGSDKGLSGKRTKTE CCCCCCCCCCCEECC	51.44	23401153
21	Acetylation	SDKGLSGKRTKTENS CCCCCCCCCEECCCC	54.22	25953088
23	Phosphorylation	KGLSGKRTKTENSGE CCCCCCCEECCCCHH	45.89	26074081
24	Sumoylation	GLSGKRTKTENSGEA CCCCCCEECCCCHHH	58.85	-
24	Ubiquitination	GLSGKRTKTENSGEA CCCCCCEECCCCHHH	58.85	-
24	Sumoylation	GLSGKRTKTENSGEA CCCCCCEECCCCHHH	58.85	-
25	Phosphorylation	LSGKRTKTENSGEAL CCCCCEECCCCHHHH	39.52	26074081
28	Phosphorylation	KRTKTENSGEALAKV CCEECCCCHHHHHHC	31.60	25159151
34	Acetylation	NSGEALAKVEDSNPQ CCHHHHHHCCCCCCC	47.19	26051181
34	Ubiquitination	NSGEALAKVEDSNPQ CCHHHHHHCCCCCCC	47.19	-
42	Acetylation	VEDSNPQKTSATKNC CCCCCCCCCHHHHHH	45.78	25953088
42	Ubiquitination	VEDSNPQKTSATKNC CCCCCCCCCHHHHHH	45.78	-
44	Phosphorylation	DSNPQKTSATKNCLK CCCCCCCHHHHHHHH	40.76	25627689
51	Acetylation	SATKNCLKNLSSHWL HHHHHHHHHHHHHCH	59.03	23954790
54	Phosphorylation	KNCLKNLSSHWLMKS HHHHHHHHHHCHHCC	29.56	27251275
55	Phosphorylation	NCLKNLSSHWLMKSE HHHHHHHHHCHHCCC	23.11	27251275
60	Ubiquitination	LSSHWLMKSEPESRL HHHHCHHCCCCHHHH	49.88	-
60	Sumoylation	LSSHWLMKSEPESRL HHHHCHHCCCCHHHH	49.88	-
60	Sumoylation	LSSHWLMKSEPESRL HHHHCHHCCCCHHHH	49.88	-
60	Acetylation	LSSHWLMKSEPESRL HHHHCHHCCCCHHHH	49.88	25953088
61	Phosphorylation	SSHWLMKSEPESRLE HHHCHHCCCCHHHHH	44.40	27251275
65	Phosphorylation	LMKSEPESRLEKGVD HHCCCCHHHHHCCCC	53.53	27251275
69	Acetylation	EPESRLEKGVDVKFS CCHHHHHCCCCEEEE	69.68	25953088
69	Ubiquitination	EPESRLEKGVDVKFS CCHHHHHCCCCEEEE	69.68	-
74	Sumoylation	LEKGVDVKFSIEDLK HHCCCCEEEEHHHHC	29.00	-
74	Sumoylation	LEKGVDVKFSIEDLK HHCCCCEEEEHHHHC	29.00	-
76	O-linked_Glycosylation	KGVDVKFSIEDLKAQ CCCCEEEEHHHHCCC	21.25	28510447
81 (in isoform 2)	Acetylation	-	58.24	-
81	Ubiquitination	KFSIEDLKAQPKQTT EEEHHHHCCCCCCCC	58.24	19608861
81	Acetylation	KFSIEDLKAQPKQTT EEEHHHHCCCCCCCC	58.24	19608861
85	Ubiquitination	EDLKAQPKQTTCWDG HHHCCCCCCCCCCHH	48.47	-
87	Phosphorylation	LKAQPKQTTCWDGVR HCCCCCCCCCCHHHH	30.01	24043423
88	Phosphorylation	KAQPKQTTCWDGVRN CCCCCCCCCCHHHHH	14.76	24043423
106	Acetylation	RNFLRAMKLGEEAFF HHHHHHHHHCCHHEE	52.97	25953088
119	Ubiquitination	FFYHSNCKEPGIAGL EECCCCCCCCCHHHH	71.80	-
119	Acetylation	FFYHSNCKEPGIAGL EECCCCCCCCCHHHH	71.80	25953088
128	Ubiquitination	PGIAGLMKIVKEAYP CCHHHHHHHHHHHCC	49.76	-
128	Acetylation	PGIAGLMKIVKEAYP CCHHHHHHHHHHHCC	49.76	25953088
131	Acetylation	AGLMKIVKEAYPDHT HHHHHHHHHHCCCCC	39.85	26051181
131	Ubiquitination	AGLMKIVKEAYPDHT HHHHHHHHHHCCCCC	39.85	-
142	Ubiquitination	PDHTQFEKNNPHYDP CCCCCHHHCCCCCCC	64.41	-
152	Ubiquitination	PHYDPSSKEDNPKWS CCCCCCCCCCCCCCC	73.71	-
152	Acetylation	PHYDPSSKEDNPKWS CCCCCCCCCCCCCCC	73.71	25953088
179	Ubiquitination	FIPLAELKSYHQAHK HCCHHHHHHHHHHHH	40.24	-
179	Acetylation	FIPLAELKSYHQAHK HCCHHHHHHHHHHHH	40.24	25953088
186	Ubiquitination	KSYHQAHKATGGPLK HHHHHHHHHHCCCHH	51.13	-
188	Phosphorylation	YHQAHKATGGPLKNM HHHHHHHHCCCHHHH	47.69	-
199	Phosphorylation	LKNMVLFTRQRLSIQ HHHHEEEECCCCCCC	23.02	-
204	Phosphorylation	LFTRQRLSIQPLTQE EEECCCCCCCCCCHH	22.74	27251275
209	Phosphorylation	RLSIQPLTQEEFDFV CCCCCCCCHHHCCEE	40.39	-
218	Phosphorylation	EEFDFVLSLEEKEPS HHCCEEEECCCCCCC	28.56	-
225	Phosphorylation	SLEEKEPS------- ECCCCCCC-------	54.68	26714015

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

Oops, there are no upstream regulatory protein records of THYN1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of THYN1_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 THYN1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SHPK_HUMAN	SHPK	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.

Related Literatures of Post-Translational Modification

Acetylation

"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-81, AND MASS SPECTROMETRY.
PubMed: 19608861