dbPTM

UBP10_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UBP10_HUMAN
UniProt AC	Q14694
Protein Name	Ubiquitin carboxyl-terminal hydrolase 10
Gene Name	USP10
Organism	Homo sapiens (Human).
Sequence Length	798
Subcellular Localization	Cytoplasm . Nucleus . Early endosome . Cytoplasmic in normal conditions (PubMed:20096447). After DNA damage, translocates to the nucleus following phosphorylation by ATM (PubMed:20096447).
Protein Description	Hydrolase that can remove conjugated ubiquitin from target proteins such as p53/TP53, BECN1, SNX3 and CFTR. Acts as an essential regulator of p53/TP53 stability: in unstressed cells, specifically deubiquitinates p53/TP53 in the cytoplasm, leading to counteract MDM2 action and stabilize p53/TP53. Following DNA damage, translocates to the nucleus and deubiquitinates p53/TP53, leading to regulate the p53/TP53-dependent DNA damage response. Component of a regulatory loop that controls autophagy and p53/TP53 levels: mediates deubiquitination of BECN1, a key regulator of autophagy, leading to stabilize the PIK3C3/VPS34-containing complexes. In turn, PIK3C3/VPS34-containing complexes regulate USP10 stability, suggesting the existence of a regulatory system by which PIK3C3/VPS34-containing complexes regulate p53/TP53 protein levels via USP10 and USP13. Does not deubiquitinate MDM2. Deubiquitinates CFTR in early endosomes, enhancing its endocytic recycling. Involved in a TANK-dependent negative feedback response to attenuate NF-kappaB activation via deubiquitinating IKBKG or TRAF6 in response to interleukin-1-beta (IL1B) stimulation or upon DNA damage. [PubMed: 25861989 Deubiquitinates TBX21 leading to its stabilization]
Protein Sequence	MALHSPQYIFGDFSPDEFNQFFVTPRSSVELPPYSGTVLCGTQAVDKLPDGQEYQRIEFGVDEVIEPSDTLPRTPSYSISSTLNPQAPEFILGCTASKITPDGITKEASYGSIDCQYPGSALALDGSSNVEAEVLENDGVSGGLGQRERKKKKKRPPGYYSYLKDGGDDSISTEALVNGHANSAVPNSVSAEDAEFMGDMPPSVTPRTCNSPQNSTDSVSDIVPDSPFPGALGSDTRTAGQPEGGPGADFGQSCFPAEAGRDTLSRTAGAQPCVGTDTTENLGVANGQILESSGEGTATNGVELHTTESIDLDPTKPESASPPADGTGSASGTLPVSQPKSWASLFHDSKPSSSSPVAYVETKYSPPAISPLVSEKQVEVKEGLVPVSEDPVAIKIAELLENVTLIHKPVSLQPRGLINKGNWCYINATLQALVACPPMYHLMKFIPLYSKVQRPCTSTPMIDSFVRLMNEFTNMPVPPKPRQALGDKIVRDIRPGAAFEPTYIYRLLTVNKSSLSEKGRQEDAEEYLGFILNGLHEEMLNLKKLLSPSNEKLTISNGPKNHSVNEEEQEEQGEGSEDEWEQVGPRNKTSVTRQADFVQTPITGIFGGHIRSVVYQQSSKESATLQPFFTLQLDIQSDKIRTVQDALESLVARESVQGYTTKTKQEVEISRRVTLEKLPPVLVLHLKRFVYEKTGGCQKLIKNIEYPVDLEISKELLSPGVKNKNFKCHRTYRLFAVVYHHGNSATGGHYTTDVFQIGLNGWLRIDDQTVKVINQYQVVKPTAERTAYLLYYRRVDLL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MALHSPQYI ------CCCCCCCEE	17.62	20068231
5	Phosphorylation	---MALHSPQYIFGD ---CCCCCCCEECCC	17.97	25159151
8	Phosphorylation	MALHSPQYIFGDFSP CCCCCCCEECCCCCH	11.12	28450419
14	Phosphorylation	QYIFGDFSPDEFNQF CEECCCCCHHHHHCC	35.86	28464451
24	Phosphorylation	EFNQFFVTPRSSVEL HHHCCEECCCCCCCC	14.08	20068231
27	Phosphorylation	QFFVTPRSSVELPPY CCEECCCCCCCCCCC	39.68	25159151
28	Phosphorylation	FFVTPRSSVELPPYS CEECCCCCCCCCCCC	22.38	25159151
32	Phosphorylation	PRSSVELPPYSGTVL CCCCCCCCCCCCEEE	16.57	27251275
34	Phosphorylation	SSVELPPYSGTVLCG CCCCCCCCCCEEEEC	20.14	27251275
35	Phosphorylation	SVELPPYSGTVLCGT CCCCCCCCCEEEECC	33.49	27251275
37	Phosphorylation	ELPPYSGTVLCGTQA CCCCCCCEEEECCEE	12.36	27251275
42	Phosphorylation	SGTVLCGTQAVDKLP CCEEEECCEEEECCC	16.62	28796482
47	Acetylation	CGTQAVDKLPDGQEY ECCEEEECCCCCCEE	56.15	26051181
54	Phosphorylation	KLPDGQEYQRIEFGV CCCCCCEEEEEECCC	8.66	28796482
68	Phosphorylation	VDEVIEPSDTLPRTP CCCEECCCCCCCCCC	30.36	28387310
70	Phosphorylation	EVIEPSDTLPRTPSY CEECCCCCCCCCCCC	42.89	26074081
74	Phosphorylation	PSDTLPRTPSYSISS CCCCCCCCCCCCCCC	18.04	23401153
76	Phosphorylation	DTLPRTPSYSISSTL CCCCCCCCCCCCCCC	30.79	21945579
77	Phosphorylation	TLPRTPSYSISSTLN CCCCCCCCCCCCCCC	15.95	21945579
78	Phosphorylation	LPRTPSYSISSTLNP CCCCCCCCCCCCCCC	21.97	21945579
80	Phosphorylation	RTPSYSISSTLNPQA CCCCCCCCCCCCCCC	16.01	21945579
81	Phosphorylation	TPSYSISSTLNPQAP CCCCCCCCCCCCCCC	34.93	21945579
82	Phosphorylation	PSYSISSTLNPQAPE CCCCCCCCCCCCCCC	24.62	21945579
94	Glutathionylation	APEFILGCTASKITP CCCEEEEEECCCCCC	2.29	22555962
95	Phosphorylation	PEFILGCTASKITPD CCEEEEEECCCCCCC	31.97	21945579
97	Phosphorylation	FILGCTASKITPDGI EEEEEECCCCCCCCC	13.36	21945579
100	Phosphorylation	GCTASKITPDGITKE EEECCCCCCCCCCCE	21.04	30266825
104	Phosphorylation	SKITPDGITKEASYG CCCCCCCCCCEECCC	6.92	27251275
105	Phosphorylation	KITPDGITKEASYGS CCCCCCCCCEECCCC	28.50	24732914
109	Phosphorylation	DGITKEASYGSIDCQ CCCCCEECCCCCCCC	30.99	28348404
110	Phosphorylation	GITKEASYGSIDCQY CCCCEECCCCCCCCC	23.18	28102081
112	Phosphorylation	TKEASYGSIDCQYPG CCEECCCCCCCCCCC	13.66	28348404
116	Phosphorylation	SYGSIDCQYPGSALA CCCCCCCCCCCCEEE	43.65	27251275
117	Phosphorylation	YGSIDCQYPGSALAL CCCCCCCCCCCEEEE	18.85	28102081
120	Phosphorylation	IDCQYPGSALALDGS CCCCCCCCEEEECCC	18.66	28102081
127	Phosphorylation	SALALDGSSNVEAEV CEEEECCCCCEEEEE	20.57	28348404
128	Phosphorylation	ALALDGSSNVEAEVL EEEECCCCCEEEEEH	50.88	28348404
154	Ubiquitination	RERKKKKKRPPGYYS HHHHCCCCCCCCHHH	78.13	-
159	Phosphorylation	KKKRPPGYYSYLKDG CCCCCCCHHHHCCCC	8.60	21945579
160	Phosphorylation	KKRPPGYYSYLKDGG CCCCCCHHHHCCCCC	9.21	21945579
161	Phosphorylation	KRPPGYYSYLKDGGD CCCCCHHHHCCCCCC	18.59	21945579
162	Phosphorylation	RPPGYYSYLKDGGDD CCCCHHHHCCCCCCC	11.14	21945579
203	Phosphorylation	FMGDMPPSVTPRTCN HHCCCCCCCCCCCCC	32.52	26471730
205	Phosphorylation	GDMPPSVTPRTCNSP CCCCCCCCCCCCCCC	16.05	18669648
208	Phosphorylation	PPSVTPRTCNSPQNS CCCCCCCCCCCCCCC	19.76	29255136
209	Phosphorylation	PSVTPRTCNSPQNST CCCCCCCCCCCCCCC	5.11	27251275
211	Phosphorylation	VTPRTCNSPQNSTDS CCCCCCCCCCCCCCC	29.97	29255136
215	Phosphorylation	TCNSPQNSTDSVSDI CCCCCCCCCCCHHHC	28.48	29255136
216	Phosphorylation	CNSPQNSTDSVSDIV CCCCCCCCCCHHHCC	39.58	23927012
218	Phosphorylation	SPQNSTDSVSDIVPD CCCCCCCCHHHCCCC	24.49	30278072
220	Phosphorylation	QNSTDSVSDIVPDSP CCCCCCHHHCCCCCC	26.10	20201521
222	Phosphorylation	STDSVSDIVPDSPFP CCCCHHHCCCCCCCC	3.64	27251275
224	Phosphorylation	DSVSDIVPDSPFPGA CCHHHCCCCCCCCCC	36.37	27251275
226	Phosphorylation	VSDIVPDSPFPGALG HHHCCCCCCCCCCCC	23.52	23927012
230	Phosphorylation	VPDSPFPGALGSDTR CCCCCCCCCCCCCCC	33.54	27251275
234	Phosphorylation	PFPGALGSDTRTAGQ CCCCCCCCCCCCCCC	36.34	20068231
236	Phosphorylation	PGALGSDTRTAGQPE CCCCCCCCCCCCCCC	31.45	20068231
253	Phosphorylation	PGADFGQSCFPAEAG CCCCCCCCCCCHHCC	20.36	26552605
254	Glutathionylation	GADFGQSCFPAEAGR CCCCCCCCCCHHCCC	3.49	22555962
263	Phosphorylation	PAEAGRDTLSRTAGA CHHCCCCCHHCCCCC	25.85	26552605
265	Phosphorylation	EAGRDTLSRTAGAQP HCCCCCHHCCCCCCC	29.67	26552605
309	Phosphorylation	VELHTTESIDLDPTK EEEEECCEECCCCCC	21.22	22468782
315	Phosphorylation	ESIDLDPTKPESASP CEECCCCCCCCCCCC	59.92	26074081
319	Phosphorylation	LDPTKPESASPPADG CCCCCCCCCCCCCCC	42.44	26074081
321	Phosphorylation	PTKPESASPPADGTG CCCCCCCCCCCCCCC	40.47	27050516
327	Phosphorylation	ASPPADGTGSASGTL CCCCCCCCCCCCCCE	28.63	26074081
329	Phosphorylation	PPADGTGSASGTLPV CCCCCCCCCCCCEEC	21.06	26074081
331	Phosphorylation	ADGTGSASGTLPVSQ CCCCCCCCCCEECCC	33.73	26074081
333	Phosphorylation	GTGSASGTLPVSQPK CCCCCCCCEECCCCC	25.95	26074081
337	Phosphorylation	ASGTLPVSQPKSWAS CCCCEECCCCCCHHH	38.53	26074081
341	Phosphorylation	LPVSQPKSWASLFHD EECCCCCCHHHHCCC	34.26	25159151
344	Phosphorylation	SQPKSWASLFHDSKP CCCCCHHHHCCCCCC	25.88	28464451
349	Phosphorylation	WASLFHDSKPSSSSP HHHHCCCCCCCCCCC	37.59	26074081
350	Acetylation	ASLFHDSKPSSSSPV HHHCCCCCCCCCCCE	55.78	25953088
352	Phosphorylation	LFHDSKPSSSSPVAY HCCCCCCCCCCCEEE	46.73	20068231
353	Phosphorylation	FHDSKPSSSSPVAYV CCCCCCCCCCCEEEE	43.28	25159151
354	Phosphorylation	HDSKPSSSSPVAYVE CCCCCCCCCCEEEEE	42.89	25159151
355	Phosphorylation	DSKPSSSSPVAYVET CCCCCCCCCEEEEEE	25.91	25159151
359	Phosphorylation	SSSSPVAYVETKYSP CCCCCEEEEEECCCC	10.07	22115753
362	Phosphorylation	SPVAYVETKYSPPAI CCEEEEEECCCCCCC	25.82	23898821
363	Acetylation	PVAYVETKYSPPAIS CEEEEEECCCCCCCC	30.17	26051181
364	Phosphorylation	VAYVETKYSPPAISP EEEEEECCCCCCCCC	33.55	19664994
365	Phosphorylation	AYVETKYSPPAISPL EEEEECCCCCCCCCC	26.43	29255136
369	Phosphorylation	TKYSPPAISPLVSEK ECCCCCCCCCCCCCC	5.56	27251275
370	Phosphorylation	KYSPPAISPLVSEKQ CCCCCCCCCCCCCCC	17.81	19664994
374	Phosphorylation	PAISPLVSEKQVEVK CCCCCCCCCCCEEEE	46.92	29255136
376	Acetylation	ISPLVSEKQVEVKEG CCCCCCCCCEEEECC	52.73	25953088
376	Ubiquitination	ISPLVSEKQVEVKEG CCCCCCCCCEEEECC	52.73	-
381	Ubiquitination	SEKQVEVKEGLVPVS CCCCEEEECCCEECC	32.34	-
395	Ubiquitination	SEDPVAIKIAELLEN CCCHHHHHHHHHHHC	26.57	-
408	Acetylation	ENVTLIHKPVSLQPR HCEEEECCCCCCCCC	39.87	26051181
408	Ubiquitination	ENVTLIHKPVSLQPR HCEEEECCCCCCCCC	39.87	21890473
412	Ubiquitination	LIHKPVSLQPRGLIN EECCCCCCCCCCCCC	9.17	21890473
456 (in isoform 2)	Ubiquitination	-	5.24	-
488	Acetylation	PRQALGDKIVRDIRP CCCCCCCHHHHCCCC	41.10	25953088
488	Ubiquitination	PRQALGDKIVRDIRP CCCCCCCHHHHCCCC	41.10	-
503	Phosphorylation	GAAFEPTYIYRLLTV CCCCCCEEEEEEEEE	13.48	-
512	Ubiquitination	YRLLTVNKSSLSEKG EEEEEECHHHCCHHC	36.77	-
513	Phosphorylation	RLLTVNKSSLSEKGR EEEEECHHHCCHHCC	31.16	29978859
514	Phosphorylation	LLTVNKSSLSEKGRQ EEEECHHHCCHHCCH	37.21	29978859
516	Phosphorylation	TVNKSSLSEKGRQED EECHHHCCHHCCHHH	38.93	29978859
518	Acetylation	NKSSLSEKGRQEDAE CHHHCCHHCCHHHHH	56.89	25953088
518	Ubiquitination	NKSSLSEKGRQEDAE CHHHCCHHCCHHHHH	56.89	-
527	Phosphorylation	RQEDAEEYLGFILNG CHHHHHHHHHHHHHH	12.02	-
536 (in isoform 2)	Ubiquitination	-	30.30	-
544	Ubiquitination	EEMLNLKKLLSPSNE HHHHCHHHHHCCCCC	58.80	-
547	Phosphorylation	LNLKKLLSPSNEKLT HCHHHHHCCCCCCCE	36.40	29255136
549	Phosphorylation	LKKLLSPSNEKLTIS HHHHHCCCCCCCEEC	55.00	23401153
551	Phosphorylation	KLLSPSNEKLTISNG HHHCCCCCCCEECCC	54.50	27251275
552	Ubiquitination	LLSPSNEKLTISNGP HHCCCCCCCEECCCC	56.00	-
554	Phosphorylation	SPSNEKLTISNGPKN CCCCCCCEECCCCCC	33.17	26074081
556	Phosphorylation	SNEKLTISNGPKNHS CCCCCEECCCCCCCC	30.42	25159151
563	Phosphorylation	SNGPKNHSVNEEEQE CCCCCCCCCCHHHHH	35.71	23927012
576	Phosphorylation	QEEQGEGSEDEWEQV HHHCCCCCHHHHHHC	37.26	22167270
580	Phosphorylation	GEGSEDEWEQVGPRN CCCCHHHHHHCCCCC	17.40	27251275
600	Phosphorylation	RQADFVQTPITGIFG HHHCCEECCCCCCCC	16.03	27251275
600 (in isoform 2)	Ubiquitination	-	16.03	-
604	Phosphorylation	FVQTPITGIFGGHIR CEECCCCCCCCCEEE	17.59	27251275
615	Nitration	GHIRSVVYQQSSKES CEEEEEEEECCCCCC	9.93	-
659	Phosphorylation	ARESVQGYTTKTKQE HHHHHCCCCCCCCCE	8.31	-
662	Acetylation	SVQGYTTKTKQEVEI HHCCCCCCCCCEEEE	46.02	25953088
662	Ubiquitination	SVQGYTTKTKQEVEI HHCCCCCCCCCEEEE	46.02	-
664	Ubiquitination	QGYTTKTKQEVEISR CCCCCCCCCEEEEEE	46.12	-
670	Phosphorylation	TKQEVEISRRVTLEK CCCEEEEEECCCHHH	10.67	-
674	Phosphorylation	VEISRRVTLEKLPPV EEEEECCCHHHCCCE	27.64	-
677	Acetylation	SRRVTLEKLPPVLVL EECCCHHHCCCEEEE	70.21	26051181
677	Ubiquitination	SRRVTLEKLPPVLVL EECCCHHHCCCEEEE	70.21	-
687	Acetylation	PVLVLHLKRFVYEKT CEEEEEEEEHHHHHC	32.80	25953088
691	Phosphorylation	LHLKRFVYEKTGGCQ EEEEEHHHHHCCCHH	14.70	21214269
693	Acetylation	LKRFVYEKTGGCQKL EEEHHHHHCCCHHHH	34.48	25953088
693	Malonylation	LKRFVYEKTGGCQKL EEEHHHHHCCCHHHH	34.48	26320211
693	Ubiquitination	LKRFVYEKTGGCQKL EEEHHHHHCCCHHHH	34.48	-
694	Phosphorylation	KRFVYEKTGGCQKLI EEHHHHHCCCHHHHH	27.20	21214269
699	Acetylation	EKTGGCQKLIKNIEY HHCCCHHHHHHCCCC	57.14	25953088
699	Ubiquitination	EKTGGCQKLIKNIEY HHCCCHHHHHHCCCC	57.14	-
702	Acetylation	GGCQKLIKNIEYPVD CCHHHHHHCCCCCCC	63.41	26051181
702	Ubiquitination	GGCQKLIKNIEYPVD CCHHHHHHCCCCCCC	63.41	-
710 (in isoform 2)	Ubiquitination	-	6.83	-
712 (in isoform 2)	Ubiquitination	-	10.42	-
713	Phosphorylation	YPVDLEISKELLSPG CCCCHHHCHHHCCCC	15.65	18669648
714	Acetylation	PVDLEISKELLSPGV CCCHHHCHHHCCCCC	59.03	23954790
714	Ubiquitination	PVDLEISKELLSPGV CCCHHHCHHHCCCCC	59.03	-
718	Phosphorylation	EISKELLSPGVKNKN HHCHHHCCCCCCCCC	32.03	30266825
722	Phosphorylation	ELLSPGVKNKNFKCH HHCCCCCCCCCCEEC	69.03	27251275
722	Ubiquitination	ELLSPGVKNKNFKCH HHCCCCCCCCCCEEC	69.03	-
725 (in isoform 2)	Ubiquitination	-	51.51	-
741 (in isoform 2)	Malonylation	-	21.31	26320211
741 (in isoform 2)	Ubiquitination	-	21.31	-
750 (in isoform 2)	Ubiquitination	-	18.01	-
762 (in isoform 2)	Ubiquitination	-	4.96	-
769	Phosphorylation	WLRIDDQTVKVINQY EEEECCCEEEEEEEE	29.32	28258704
771	Acetylation	RIDDQTVKVINQYQV EECCCEEEEEEEEEE	40.56	26051181
780	Acetylation	INQYQVVKPTAERTA EEEEEEECCCHHHEE	37.48	26822725
780	Ubiquitination	INQYQVVKPTAERTA EEEEEEECCCHHHEE	37.48	2190698
786	Phosphorylation	VKPTAERTAYLLYYR ECCCHHHEEEEEEEE	15.91	28152594
788	Phosphorylation	PTAERTAYLLYYRRV CCHHHEEEEEEEEEC	9.16	28152594
791	Phosphorylation	ERTAYLLYYRRVDLL HHEEEEEEEEECCCC	7.73	28176443
792	Phosphorylation	RTAYLLYYRRVDLL- HEEEEEEEEECCCC-	7.60	28176443
828 (in isoform 2)	Malonylation	-		26320211
828 (in isoform 2)	Ubiquitination	-		-

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
42	T	Phosphorylation	Kinase	ATM	Q13315	Uniprot
76	S	Phosphorylation	Kinase	PRKAA1	Q13131	GPS
337	S	Phosphorylation	Kinase	ATM	Q13315	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of UBP10_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 UBP10_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
G3BP1_HUMAN	G3BP1	physical	11439350
SCNNA_HUMAN	SCNN1A	physical	18632802
IF4G1_HUMAN	EIF4G1	physical	19615732
IF4G3_HUMAN	EIF4G3	physical	19615732
G3BP2_HUMAN	G3BP2	physical	19615732
G3BP1_HUMAN	G3BP1	physical	19615732
CELF1_HUMAN	CELF1	physical	19615732
GAR1_HUMAN	GAR1	physical	19615732
P53_HUMAN	TP53	physical	20096447
CFTR_HUMAN	CFTR	physical	20215869
CFTR_HUMAN	CFTR	physical	19398555
UBC_HUMAN	UBC	physical	19398555
ANDR_HUMAN	AR	physical	16368182
WAPL_HUMAN	WAPAL	physical	22939629
ZCH18_HUMAN	ZC3H18	physical	22939629
UBP15_HUMAN	USP15	physical	22939629
ZN281_HUMAN	ZNF281	physical	22939629
UBC_HUMAN	UBC	physical	23287719
PABP1_HUMAN	PABPC1	physical	23230274
G3BP1_HUMAN	G3BP1	physical	23230274
PTEN_HUMAN	PTEN	physical	24270891
ZC12A_HUMAN	ZC3H12A	physical	24270572
NEMO_HUMAN	IKBKG	physical	24270572
UBP10_HUMAN	USP10	physical	24998844
P53_HUMAN	TP53	physical	24998844
G3BP1_HUMAN	G3BP1	physical	24998844
G3BP2_HUMAN	G3BP2	physical	25416956
G3BP1_HUMAN	G3BP1	physical	26344197
SF3B3_HUMAN	SF3B3	physical	26344197
AAPK1_HUMAN	PRKAA1	physical	26876938
AAPK2_HUMAN	PRKAA2	physical	26876938
TANK_HUMAN	TANK	physical	25861989
ZC12A_HUMAN	ZC3H12A	physical	25861989
IF4G1_HUMAN	EIF4G1	physical	27003362
H2A2C_HUMAN	HIST2H2AC	physical	21245042
MSH2_HUMAN	MSH2	physical	26975374
ANR44_HUMAN	ANKRD44	physical	28514442
G3BP2_HUMAN	G3BP2	physical	28514442
ANR52_HUMAN	ANKRD52	physical	28514442
AASD1_HUMAN	AARSD1	physical	28514442
ANR28_HUMAN	ANKRD28	physical	28514442
P4R3A_HUMAN	SMEK1	physical	28514442
GFAP_HUMAN	GFAP	physical	28514442
PP6R2_HUMAN	PPP6R2	physical	28514442
KLDC3_HUMAN	KLHDC3	physical	28514442
G3BP1_HUMAN	G3BP1	physical	28514442
PP6R1_HUMAN	PPP6R1	physical	28514442
PP4R2_HUMAN	PPP4R2	physical	28514442
ZEB1_HUMAN	ZEB1	physical	29119051
PTEN_HUMAN	PTEN	physical	28852924
RN168_HUMAN	RNF168	physical	27558965
G3BP1_HUMAN	G3BP1	physical	27022092
G3BP2_HUMAN	G3BP2	physical	27022092
PABP1_HUMAN	PABPC1	physical	27022092
RS6_HUMAN	RPS6	physical	27022092
IF4G1_HUMAN	EIF4G1	physical	27022092

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 UBP10_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"USP10 regulates p53 localization and stability by deubiquitinatingp53."; Yuan J., Luo K., Zhang L., Cheville J.C., Lou Z.; Cell 140:384-396(2010). Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INDUCTION,INTERACTION WITH TP53, PHOSPHORYLATION AT THR-42; SER-337 AND CYS-424,AND MUTAGENESIS OF THR-42 AND SER-337.	20096447 [Abstract]
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-563 AND SER-576, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, AND MASSSPECTROMETRY.	19369195 [Abstract]
"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-208; SER-365; SER-370;SER-547 AND SER-576, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography."; Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.; Proteomics 8:1346-1361(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, AND MASSSPECTROMETRY.	18318008 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-100; SER-220; SER-226;SER-370; SER-563 AND SER-576, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, AND MASSSPECTROMETRY.	17287340 [Abstract]
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction."; Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.; Mol. Cell. Proteomics 6:1952-1967(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, AND MASSSPECTROMETRY.	17693683 [Abstract]
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline."; Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.; Electrophoresis 28:2027-2034(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, AND MASSSPECTROMETRY.	17487921 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-364; SER-365 ANDSER-370, AND MASS SPECTROMETRY.	16964243 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211 AND SER-576, ANDMASS SPECTROMETRY.	15302935 [Abstract]