dbPTM

TEX10_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TEX10_HUMAN
UniProt AC	Q9NXF1
Protein Name	Testis-expressed protein 10
Gene Name	TEX10
Organism	Homo sapiens (Human).
Sequence Length	929
Subcellular Localization	Nucleus, nucleoplasm . Cytoplasm . Nucleus, nucleolus . Mainly found in the nucleoplasm, with low levels detected in the cytoplasmic and chromatin fractions.
Protein Description	Functions as a component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes. [PubMed: 22872859 Component of the PELP1 complex involved in the nucleolar steps of 28S rRNA maturation and the subsequent nucleoplasmic transit of the pre-60S ribosomal subunit]
Protein Sequence	MTKKRKRQHDFQKVKLKVGKKKPKLQNATPTNFKTKTIHLPEQLKEDGTLPTNNRKLNIKDLLSQMHHYNAGVKQSALLGLKDLLSQYPFIIDAHLSNILSEVTAVFTDKDANVRLAAVQLLQFLAPKIRAEQISPFFPLVSAHLSSAMTHITEGIQEDSLKVLDILLEQYPALITGRSSILLKNFVELISHQQLSKGLINRDRSQSWILSVNPNRRLTSQQWRLKVLVRLSKFLQALADGSSRLRESEGLQEQKENPHATSNSIFINWKEHANDQQHIQVYENGGSQPNVSSQFRLRYLVGGLSGVDEGLSSTENLKGFIEIIIPLLIECWVEAVPPQLATPVGNGIEREPLQVMQQVLNIISLLWKLSKQQDETHKLESWLRKNYLIDFKHHFMSRFPYVLKEITKHKRKEPNKSIKHCTVLSNNIDHLLLNLTLSDIMVSLANASTLQKDCSWIEMIRKFVTETLEDGSRLNSKQLNRLLGVSWRLMQIQPNREDTETLIKAVYTLYQQRGLILPVRTLLLKFFSKIYQTEELRSCRFRYRSKVLSRWLAGLPLQLAHLGSRNPELSTQLIDIIHTAAARANKELLKSLQATALRIYDPQEGAVVVLPADSQQRLVQLVYFLPSLPADLLSRLSRCCIMGRLSSSLAAMLIGILHMRSSFSGWKYSAKDWLMSDVDYFSFLFSTLTGFSKEELTWLQSLRGVPHVIQTQLSPVLLYLTDLDQFLHHWDVTEAVFHSLLVIPARSQNFDILQSAISKHLVGLTVIPDSTAGCVFGVICKLLDHTCVVSETLLPFLASCCYSLLYFLLTIEKGEAEHLRKRDKLWGVCVSILALLPRVLRLMLQSLRVNRVGPEELPVVGQLLRLLLQHAPLRTHMLTNAILVQQIIKNITTLKSGSVQEQWLTDLHYCFNVYITGHPQGPSALATVY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
20	Acetylation	KVKLKVGKKKPKLQN HCCCCCCCCCCCCCC	61.69	26051181
21	Acetylation	VKLKVGKKKPKLQNA CCCCCCCCCCCCCCC	69.27	26051181
24	Acetylation	KVGKKKPKLQNATPT CCCCCCCCCCCCCCC	72.14	26051181
29	Phosphorylation	KPKLQNATPTNFKTK CCCCCCCCCCCCCCC	37.89	29255136
31	O-linked_Glycosylation	KLQNATPTNFKTKTI CCCCCCCCCCCCCEE	49.27	30379171
31	Phosphorylation	KLQNATPTNFKTKTI CCCCCCCCCCCCCEE	49.27	19664994
34	Ubiquitination	NATPTNFKTKTIHLP CCCCCCCCCCEECCC	51.70	-
34	Methylation	NATPTNFKTKTIHLP CCCCCCCCCCEECCC	51.70	115980007
36	Methylation	TPTNFKTKTIHLPEQ CCCCCCCCEECCCHH	46.18	115980013
36	Ubiquitination	TPTNFKTKTIHLPEQ CCCCCCCCEECCCHH	46.18	-
37	Phosphorylation	PTNFKTKTIHLPEQL CCCCCCCEECCCHHH	20.89	28555341
45	Ubiquitination	IHLPEQLKEDGTLPT ECCCHHHCCCCCCCC	54.15	-
45	Acetylation	IHLPEQLKEDGTLPT ECCCHHHCCCCCCCC	54.15	26051181
49	Phosphorylation	EQLKEDGTLPTNNRK HHHCCCCCCCCCCCC	41.72	25159151
52	Phosphorylation	KEDGTLPTNNRKLNI CCCCCCCCCCCCCCH	48.52	25159151
64	Phosphorylation	LNIKDLLSQMHHYNA CCHHHHHHHHHHHCH	32.52	23401153
76	Phosphorylation	YNAGVKQSALLGLKD HCHHHHHHHHHCHHH	18.37	21406692
196	Phosphorylation	LISHQQLSKGLINRD HHCHHHHHCCCCCCC	21.97	-
197	Acetylation	ISHQQLSKGLINRDR HCHHHHHCCCCCCCC	67.35	26051181
197	Ubiquitination	ISHQQLSKGLINRDR HCHHHHHCCCCCCCC	67.35	21890473
200	Ubiquitination	QQLSKGLINRDRSQS HHHHCCCCCCCCCCC	5.61	21890473
205	Phosphorylation	GLINRDRSQSWILSV CCCCCCCCCCEEEEE	32.62	22210691
207	Phosphorylation	INRDRSQSWILSVNP CCCCCCCCEEEEECC	19.82	28555341
220	Phosphorylation	NPNRRLTSQQWRLKV CCCCCCCCHHHHHHH	25.60	22210691
233	Acetylation	KVLVRLSKFLQALAD HHHHHHHHHHHHHHH	55.47	26051181
305	Phosphorylation	RYLVGGLSGVDEGLS HHHHCCCCCCCCCCC	39.79	-
312	Phosphorylation	SGVDEGLSSTENLKG CCCCCCCCCCCCHHH	46.18	-
378	Ubiquitination	KQQDETHKLESWLRK HCCCCHHHHHHHHHH	62.46	-
385	Acetylation	KLESWLRKNYLIDFK HHHHHHHHCCCHHHH	48.01	26051181
385	Malonylation	KLESWLRKNYLIDFK HHHHHHHHCCCHHHH	48.01	26320211
392	Acetylation	KNYLIDFKHHFMSRF HCCCHHHHHHHHHHC	32.21	25953088
404	Ubiquitination	SRFPYVLKEITKHKR HHCHHHHHHHHHCCC	36.71	-
462	Acetylation	SWIEMIRKFVTETLE HHHHHHHHHHHHHCC	33.01	26051181
462	Ubiquitination	SWIEMIRKFVTETLE HHHHHHHHHHHHHCC	33.01	-
525	Acetylation	PVRTLLLKFFSKIYQ HHHHHHHHHHHHHHC	44.31	26051181
529	Acetylation	LLLKFFSKIYQTEEL HHHHHHHHHHCCHHH	40.03	25825284
529	Ubiquitination	LLLKFFSKIYQTEEL HHHHHHHHHHCCHHH	40.03	-
531	Phosphorylation	LKFFSKIYQTEELRS HHHHHHHHCCHHHHH	17.08	25690035
533	Phosphorylation	FFSKIYQTEELRSCR HHHHHHCCHHHHHCC	17.92	25690035
590	Ubiquitination	RANKELLKSLQATAL HCCHHHHHHHHHHHH	62.84	21890473
623	Phosphorylation	QRLVQLVYFLPSLPA HHHHHHHHHCCCCCH	14.16	22817900
846	Phosphorylation	VLRLMLQSLRVNRVG HHHHHHHHHCCCCCC	17.74	21406692
873	Acetylation	LLLQHAPLRTHMLTN HHHHCCCHHHHHHHH	11.64	19608861
889	Acetylation	ILVQQIIKNITTLKS HHHHHHHHHCCCCCC	43.88	19608861

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 TEX10_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TEX10_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 TEX10_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GNL3_HUMAN	GNL3	physical	26344197
NOL9_HUMAN	NOL9	physical	26344197
PELP1_HUMAN	PELP1	physical	26344197
SENP3_HUMAN	SENP3	physical	26344197

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 TEX10_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-889, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-29, AND MASSSPECTROMETRY.	19413330 [Abstract]
"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 THR-29, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31, AND MASSSPECTROMETRY.	19007248 [Abstract]