dbPTM

UBP8_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UBP8_HUMAN
UniProt AC	P40818
Protein Name	Ubiquitin carboxyl-terminal hydrolase 8
Gene Name	USP8
Organism	Homo sapiens (Human).
Sequence Length	1118
Subcellular Localization	Cytoplasm . Nucleus . Endosome membrane Peripheral membrane protein . Cell membrane Peripheral membrane protein .
Protein Description	Hydrolase that can remove conjugated ubiquitin from proteins and therefore plays an important regulatory role at the level of protein turnover by preventing degradation. Converts both 'Lys-48' an 'Lys-63'-linked ubiquitin chains. Catalytic activity is enhanced in the M phase. Involved in cell proliferation. Required to enter into S phase in response to serum stimulation. May regulate T-cell anergy mediated by RNF128 via the formation of a complex containing RNF128 and OTUB1. Probably regulates the stability of STAM2 and RASGRF1. Regulates endosomal ubiquitin dynamics, cargo sorting, membrane traffic at early endosomes, and maintenance of ESCRT-0 stability. The level of protein ubiquitination on endosomes is essential for maintaining the morphology of the organelle. Deubiquitinates EPS15 and controles tyrosine kinase stability. Removes conjugated ubiquitin from EGFR thus regulating EGFR degradation and downstream MAPK signaling. Involved in acrosome biogenesis through interaction with the spermatid ESCRT-0 complex and microtubules. Deubiquitinates BIRC6/bruce and KIF23/MKLP1..
Protein Sequence	MPAVASVPKELYLSSSLKDLNKKTEVKPEKISTKSYVHSALKIFKTAEECRLDRDEERAYVLYMKYVTVYNLIKKRPDFKQQQDYFHSILGPGNIKKAVEEAERLSESLKLRYEEAEVRKKLEEKDRQEEAQRLQQKRQETGREDGGTLAKGSLENVLDSKDKTQKSNGEKNEKCETKEKGAITAKELYTMMTDKNISLIIMDARRMQDYQDSCILHSLSVPEEAISPGVTASWIEAHLPDDSKDTWKKRGNVEYVVLLDWFSSAKDLQIGTTLRSLKDALFKWESKTVLRNEPLVLEGGYENWLLCYPQYTTNAKVTPPPRRQNEEVSISLDFTYPSLEESIPSKPAAQTPPASIEVDENIELISGQNERMGPLNISTPVEPVAASKSDVSPIIQPVPSIKNVPQIDRTKKPAVKLPEEHRIKSESTNHEQQSPQSGKVIPDRSTKPVVFSPTLMLTDEEKARIHAETALLMEKNKQEKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAKEEMEKKESEQAKKEDKETSAKRGKEITGVKRQSKSEHETSDAKKSVEDRGKRCPTPEIQKKSTGDVPHTSVTGDSGSGKPFKIKGQPESGILRTGTFREDTDDTERNKAQREPLTRARSEEMGRIVPGLPSGWAKFLDPITGTFRYYHSPTNTVHMYPPEMAPSSAPPSTPPTHKAKPQIPAERDREPSKLKRSYSSPDITQAIQEEEKRKPTVTPTVNRENKPTCYPKAEISRLSASQIRNLNPVFGGSGPALTGLRNLGNTCYMNSILQCLCNAPHLADYFNRNCYQDDINRSNLLGHKGEVAEEFGIIMKALWTGQYRYISPKDFKITIGKINDQFAGYSQQDSQELLLFLMDGLHEDLNKADNRKRYKEENNDHLDDFKAAEHAWQKHKQLNESIIVALFQGQFKSTVQCLTCHKKSRTFEAFMYLSLPLASTSKCTLQDCLRLFSKEEKLTDNNRFYCSHCRARRDSLKKIEIWKLPPVLLVHLKRFSYDGRWKQKLQTSVDFPLENLDLSQYVIGPKNNLKKYNLFSVSNHYGGLDGGHYTAYCKNAARQRWFKFDDHEVSDISVSSVKSSAAYILFYTSLGPRVTDVAT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MPAVASVPKELYL --CCCCCCCCHHHHH	32.14	24719451
12	Phosphorylation	ASVPKELYLSSSLKD CCCCHHHHHCCCHHH	12.96	20068231
14	Phosphorylation	VPKELYLSSSLKDLN CCHHHHHCCCHHHHH	12.34	25690035
15	Phosphorylation	PKELYLSSSLKDLNK CHHHHHCCCHHHHHH	36.77	28348404
16	Phosphorylation	KELYLSSSLKDLNKK HHHHHCCCHHHHHHC	35.74	28348404
32	Phosphorylation	EVKPEKISTKSYVHS CCCHHHCCCHHHHHH	40.63	30631047
33	Phosphorylation	VKPEKISTKSYVHSA CCHHHCCCHHHHHHH	27.73	30631047
42	Acetylation	SYVHSALKIFKTAEE HHHHHHHHHHHCHHH	45.90	26051181
51	Methylation	FKTAEECRLDRDEER HHCHHHHCCCCCHHH	42.79	115919681
54	Methylation	AEECRLDRDEERAYV HHHHCCCCCHHHHHH	58.81	115919685
66	Phosphorylation	AYVLYMKYVTVYNLI HHHHHHHHHHHHHHH	5.71	28258704
70	Phosphorylation	YMKYVTVYNLIKKRP HHHHHHHHHHHHHCC	8.55	28258704
108	Phosphorylation	EAERLSESLKLRYEE HHHHHHHHHHHHHHH	27.68	20068231
113	Phosphorylation	SESLKLRYEEAEVRK HHHHHHHHHHHHHHH	28.67	-
153	Phosphorylation	GGTLAKGSLENVLDS CCCCCCCCHHHHHCC	31.63	20363803
160	Phosphorylation	SLENVLDSKDKTQKS CHHHHHCCCCHHCCC	38.30	23927012
164	O-linked_Glycosylation	VLDSKDKTQKSNGEK HHCCCCHHCCCCCCC	51.90	30379171
167	O-linked_Glycosylation	SKDKTQKSNGEKNEK CCCHHCCCCCCCCCC	40.00	30379171
189	Phosphorylation	AITAKELYTMMTDKN CEEHHHHHHHHCCCC	8.15	29759185
193	Phosphorylation	KELYTMMTDKNISLI HHHHHHHCCCCEEEE	32.76	29759185
288	Phosphorylation	LFKWESKTVLRNEPL HHHCCCCCCCCCCCE	33.77	24719451
312	Phosphorylation	LLCYPQYTTNAKVTP EEECCCCCCCCCCCC	14.34	27251275
313	Phosphorylation	LCYPQYTTNAKVTPP EECCCCCCCCCCCCC	28.39	27251275
318	Phosphorylation	YTTNAKVTPPPRRQN CCCCCCCCCCCCCCC	29.39	27251275
335	Phosphorylation	VSISLDFTYPSLEES EEEEEECCCCCHHHC	33.90	26074081
336	Phosphorylation	SISLDFTYPSLEESI EEEEECCCCCHHHCC	7.27	26074081
338	Phosphorylation	SLDFTYPSLEESIPS EEECCCCCHHHCCCC	37.69	26074081
342	Phosphorylation	TYPSLEESIPSKPAA CCCCHHHCCCCCCCC	30.35	26074081
345	Phosphorylation	SLEESIPSKPAAQTP CHHHCCCCCCCCCCC	49.99	26074081
351	Phosphorylation	PSKPAAQTPPASIEV CCCCCCCCCCCEEEC	26.89	25159151
355	Phosphorylation	AAQTPPASIEVDENI CCCCCCCEEECCCCE	25.67	26074081
378	Phosphorylation	RMGPLNISTPVEPVA CCCCCCCCCCCCCCC	26.11	25159151
379	Phosphorylation	MGPLNISTPVEPVAA CCCCCCCCCCCCCCC	27.79	25159151
387	Phosphorylation	PVEPVAASKSDVSPI CCCCCCCCCCCCCCC	23.97	20068231
389	Phosphorylation	EPVAASKSDVSPIIQ CCCCCCCCCCCCCCC	40.52	30266825
392	Phosphorylation	AASKSDVSPIIQPVP CCCCCCCCCCCCCCC	18.51	29255136
400	Phosphorylation	PIIQPVPSIKNVPQI CCCCCCCCCCCCCCC	46.56	23403867
410	Phosphorylation	NVPQIDRTKKPAVKL CCCCCCCCCCCCCCC	39.41	-
425	Phosphorylation	PEEHRIKSESTNHEQ CHHHCCCCCCCCCCC	34.11	28857561
427	Phosphorylation	EHRIKSESTNHEQQS HHCCCCCCCCCCCCC	41.42	29083192
428	Phosphorylation	HRIKSESTNHEQQSP HCCCCCCCCCCCCCC	36.22	29396449
434	Phosphorylation	STNHEQQSPQSGKVI CCCCCCCCCCCCCCC	25.30	26055452
437	Phosphorylation	HEQQSPQSGKVIPDR CCCCCCCCCCCCCCC	43.92	29083192
445	Phosphorylation	GKVIPDRSTKPVVFS CCCCCCCCCCCEEEC	48.43	30108239
446	Phosphorylation	KVIPDRSTKPVVFSP CCCCCCCCCCEEECC	40.02	30108239
452	Phosphorylation	STKPVVFSPTLMLTD CCCCEEECCEEECCH	12.83	25159151
454	Phosphorylation	KPVVFSPTLMLTDEE CCEEECCEEECCHHH	24.49	21712546
456	Sulfoxidation	VVFSPTLMLTDEEKA EEECCEEECCHHHHH	4.10	21406390
458	Phosphorylation	FSPTLMLTDEEKARI ECCEEECCHHHHHHH	27.65	30108239
538	Acetylation	EQAKKEDKETSAKRG HHHHHHHHHHHHHHC	65.07	20167786
552	Acetylation	GKEITGVKRQSKSEH CCCCCCCCCCCCCCC	46.17	25953088
566	Ubiquitination	HETSDAKKSVEDRGK CCCHHHHHHHHHCCC	62.55	-
577	Phosphorylation	DRGKRCPTPEIQKKS HCCCCCCCHHHHHCC	36.86	19664994
585	Phosphorylation	PEIQKKSTGDVPHTS HHHHHCCCCCCCCCE	46.40	28555341
594	Phosphorylation	DVPHTSVTGDSGSGK CCCCCEEECCCCCCC	34.73	26270265
597	Phosphorylation	HTSVTGDSGSGKPFK CCEEECCCCCCCCEE	35.88	25159151
599	Phosphorylation	SVTGDSGSGKPFKIK EEECCCCCCCCEEEC	47.82	25159151
601	Acetylation	TGDSGSGKPFKIKGQ ECCCCCCCCEEECCC	49.32	23954790
611	Phosphorylation	KIKGQPESGILRTGT EECCCCCCCEECCCC	37.50	-
616	Phosphorylation	PESGILRTGTFREDT CCCCEECCCCCCCCC	36.81	23186163
618	Phosphorylation	SGILRTGTFREDTDD CCEECCCCCCCCCCH	20.93	23312004
623	Phosphorylation	TGTFREDTDDTERNK CCCCCCCCCHHHHHH	30.90	23186163
641	Phosphorylation	EPLTRARSEEMGRIV CCHHHHHHHHHHCCC	36.60	25884760
653	Phosphorylation	RIVPGLPSGWAKFLD CCCCCCCCHHHHHHC	52.59	20068231
663	Phosphorylation	AKFLDPITGTFRYYH HHHHCCCCCEEEEEE	35.24	28857561
665	Phosphorylation	FLDPITGTFRYYHSP HHCCCCCEEEEEECC	9.04	28857561
668	Phosphorylation	PITGTFRYYHSPTNT CCCCEEEEEECCCCC	11.01	20068231
669	Phosphorylation	ITGTFRYYHSPTNTV CCCEEEEEECCCCCE	7.49	20068231
671	Phosphorylation	GTFRYYHSPTNTVHM CEEEEEECCCCCEEE	19.80	25159151
673	Phosphorylation	FRYYHSPTNTVHMYP EEEEECCCCCEEECC	46.68	20068231
675	Phosphorylation	YYHSPTNTVHMYPPE EEECCCCCEEECCCH	17.80	20068231
679	Phosphorylation	PTNTVHMYPPEMAPS CCCCEEECCCHHCCC	10.76	30576142
686	Phosphorylation	YPPEMAPSSAPPSTP CCCHHCCCCCCCCCC	29.60	21712546
687	Phosphorylation	PPEMAPSSAPPSTPP CCHHCCCCCCCCCCC	43.68	30576142
691	Phosphorylation	APSSAPPSTPPTHKA CCCCCCCCCCCCCCC	53.11	25159151
692	Phosphorylation	PSSAPPSTPPTHKAK CCCCCCCCCCCCCCC	38.78	25159151
695	Phosphorylation	APPSTPPTHKAKPQI CCCCCCCCCCCCCCC	36.89	25159151
711	Phosphorylation	AERDREPSKLKRSYS CCCCCCCHHHCCCCC	45.96	21712546
716	Phosphorylation	EPSKLKRSYSSPDIT CCHHHCCCCCCCHHH	27.98	22167270
717	Phosphorylation	PSKLKRSYSSPDITQ CHHHCCCCCCCHHHH	19.73	22167270
718	Phosphorylation	SKLKRSYSSPDITQA HHHCCCCCCCHHHHH	36.32	19664994
719	Phosphorylation	KLKRSYSSPDITQAI HHCCCCCCCHHHHHH	20.54	29255136
723	Phosphorylation	SYSSPDITQAIQEEE CCCCCHHHHHHHHHH	21.23	23927012
735	Phosphorylation	EEEKRKPTVTPTVNR HHHHCCCCCCCCCCC	39.79	23312004
737	Phosphorylation	EKRKPTVTPTVNREN HHCCCCCCCCCCCCC	18.73	25159151
739	Phosphorylation	RKPTVTPTVNRENKP CCCCCCCCCCCCCCC	22.50	23312004
747	Phosphorylation	VNRENKPTCYPKAEI CCCCCCCCCCCHHHH	26.70	30257219
758	Phosphorylation	KAEISRLSASQIRNL HHHHHHCCHHHHCCC	25.43	28555341
760	Phosphorylation	EISRLSASQIRNLNP HHHHCCHHHHCCCCC	23.82	28555341
777	Phosphorylation	GGSGPALTGLRNLGN CCCCHHHHCHHHHCC	35.95	24719451
810	Phosphorylation	DYFNRNCYQDDINRS HHHCCCCCCCCCCCC	20.65	25884760
842	Phosphorylation	KALWTGQYRYISPKD HHHHHCCCEECCHHH	13.51	25884760
846	Phosphorylation	TGQYRYISPKDFKIT HCCCEECCHHHEEEE	19.57	24719451
905	Ubiquitination	NDHLDDFKAAEHAWQ CCCHHHHHHHHHHHH	54.40	-
933	Phosphorylation	FQGQFKSTVQCLTCH HCCCCHHHEEHHHCC	18.39	30576142
938	Phosphorylation	KSTVQCLTCHKKSRT HHHEEHHHCCCCCCE	21.86	30576142
941	Acetylation	VQCLTCHKKSRTFEA EEHHHCCCCCCEEEE	55.37	25953088
945	Phosphorylation	TCHKKSRTFEAFMYL HCCCCCCEEEEHHHH	32.68	-
951	Phosphorylation	RTFEAFMYLSLPLAS CEEEEHHHHHCCCCC	6.15	24260401
958	Phosphorylation	YLSLPLASTSKCTLQ HHHCCCCCCCCCCHH	40.68	24260401
959	Phosphorylation	LSLPLASTSKCTLQD HHCCCCCCCCCCHHH	26.97	24260401
972	Phosphorylation	QDCLRLFSKEEKLTD HHHHHHHCCHHHCCC	43.69	24719451
1012	Methylation	PVLLVHLKRFSYDGR CEEEEEEEECCCCCC	36.20	-
1015	Phosphorylation	LVHLKRFSYDGRWKQ EEEEEECCCCCCHHH	26.75	24719451
1016	Phosphorylation	VHLKRFSYDGRWKQK EEEEECCCCCCHHHH	21.50	-
1051	Phosphorylation	PKNNLKKYNLFSVSN CCCCCCCCCEEEEEC	18.60	28270605
1055	Phosphorylation	LKKYNLFSVSNHYGG CCCCCEEEEECCCCC	28.00	28270605
1057	Phosphorylation	KYNLFSVSNHYGGLD CCCEEEEECCCCCCC	19.38	28270605
1060	Phosphorylation	LFSVSNHYGGLDGGH EEEEECCCCCCCCCC	19.69	28270605
1068	Phosphorylation	GGLDGGHYTAYCKNA CCCCCCCHHHHCCCH	9.06	28270605
1069	Phosphorylation	GLDGGHYTAYCKNAA CCCCCCHHHHCCCHH	12.89	28270605
1071	Phosphorylation	DGGHYTAYCKNAARQ CCCCHHHHCCCHHHH	8.99	22210691
1089	Phosphorylation	KFDDHEVSDISVSSV CCCCCCCCCCCHHHH	26.66	27732954
1092	Phosphorylation	DHEVSDISVSSVKSS CCCCCCCCHHHHHHC	22.42	27732954
1094	Phosphorylation	EVSDISVSSVKSSAA CCCCCCHHHHHHCCH	23.71	27732954
1095	Phosphorylation	VSDISVSSVKSSAAY CCCCCHHHHHHCCHH	31.26	27732954
1106	Phosphorylation	SAAYILFYTSLGPRV CCHHHHHHHCCCCCC	7.62	25884760

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
717	Y	Phosphorylation	Kinase	EGFR	P00533	PSP
810	Y	Phosphorylation	Kinase	EGFR	P00533	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
718	S	Phosphorylation	18669648
Phosphorylation of Ser-718 is essential for interaction with YWHAE and for cytosol localization.
718	S	Phosphorylation	18669648
Undergoes dephosphorylation at Ser-718 in the M phase.

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 UBP8_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
OTUB1_HUMAN	OTUB1	physical	14661020
RN128_HUMAN	RNF128	physical	14661020
STAM2_HUMAN	STAM2	physical	10982817
STAM1_HUMAN	STAM	physical	10982817
GRB2_HUMAN	GRB2	physical	10982817
KIF23_HUMAN	KIF23	physical	18329369
BIRC6_HUMAN	BIRC6	physical	18329369
K1H1_HUMAN	KRT31	physical	19615732
KRT85_HUMAN	KRT85	physical	19615732
KRT36_HUMAN	KRT36	physical	19615732
UBP22_HUMAN	USP22	physical	19615732
AKT1_HUMAN	AKT1	physical	17210635
CHM1B_HUMAN	CHMP1B	physical	17711858
CHM1A_HUMAN	CHMP1A	physical	17711858
CHM4C_HUMAN	CHMP4C	physical	17711858
CHMP7_HUMAN	CHMP7	physical	17711858
KCNN4_HUMAN	KCNN4	physical	21828287
STAM1_HUMAN	STAM	physical	20736164
STAM2_HUMAN	STAM2	physical	20736164
STAM1_HUMAN	STAM	physical	16520378
NBR1_HUMAN	NBR1	physical	19427866
UBP8_HUMAN	USP8	physical	17035239
RNF41_HUMAN	RNF41	physical	17035239
UBC_HUMAN	UBC	physical	22195557
CHM1A_HUMAN	CHMP1A	physical	19302785
CHM1B_HUMAN	CHMP1B	physical	19302785
CHM2A_HUMAN	CHMP2A	physical	19302785
CHM2B_HUMAN	CHMP2B	physical	19302785
CHM4C_HUMAN	CHMP4C	physical	19302785
GRAP2_HUMAN	GRAP2	physical	12176364
VPS4B_HUMAN	VPS4B	physical	22939629
EGFR_HUMAN	EGFR	physical	23153581
ERBB4_HUMAN	ERBB4	physical	23153581
UBC_HUMAN	UBC	physical	23287719
HD_HUMAN	HTT	physical	22863883
DPOD3_HUMAN	POLD3	physical	22863883
STAT6_HUMAN	STAT6	physical	22863883
PTEN_HUMAN	PTEN	physical	24270891
TADBP_HUMAN	TARDBP	physical	24825905
PA2GA_HUMAN	PLA2G2A	physical	22118674
UBC_HUMAN	UBC	physical	17711858
SCNNB_HUMAN	SCNN1B	physical	23297398
SCNNG_HUMAN	SCNN1G	physical	23297398
EPS15_HUMAN	EPS15	physical	16771824
RGRF1_MOUSE	Rasgrf1	physical	11500497
BIRC6_HUMAN	BIRC6	physical	25733871
MCPH1_HUMAN	MCPH1	physical	25733871
UBC_HUMAN	UBC	physical	25527291
THIM_HUMAN	ACAA2	physical	26344197
TATD1_HUMAN	TATDN1	physical	26344197
UB2E1_HUMAN	UBE2E1	physical	26344197
1433E_HUMAN	YWHAE	physical	25485838
UBC_HUMAN	UBC	physical	25485838
EGFR_HUMAN	EGFR	physical	25485838
H2A2C_HUMAN	HIST2H2AC	physical	26507658
H2B2E_HUMAN	HIST2H2BE	physical	26507658
EGFR_HUMAN	EGFR	physical	25853104
GRAP2_HUMAN	GRAP2	physical	26214742
1433B_HUMAN	YWHAB	physical	26214742
BACE1_HUMAN	BACE1	physical	27302062
SYUA_HUMAN	SNCA	physical	27444016
CFLAR_HUMAN	CFLAR	physical	27321185

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 UBP8_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-718, AND MASSSPECTROMETRY.	19690332 [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 SER-452, AND MASSSPECTROMETRY.	19413330 [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 SER-452; SER-718 ANDSER-719, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434, AND MASSSPECTROMETRY.	17924679 [Abstract]

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