dbPTM

UBP8_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UBP8_MOUSE
UniProt AC	Q80U87
Protein Name	Ubiquitin carboxyl-terminal hydrolase 8
Gene Name	Usp8
Organism	Mus musculus (Mouse).
Sequence Length	1080
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 (By similarity)..
Protein Sequence	MPAVASVPKELYLSSSLKDLNKKTEVKPEKTSTKNYIHSAQKIFKTAEECRLDRDEERAYVLYMKYVAVYNLIKKRPDFKQQQDYYLSILGPANIKKAIEEAERLSESLKLRYEEAEVRKQLEEKDRREEEQLQQQKRQEMGREDSGAAAKRSVENLLDSKTKTQRINGEKSEGAAAAERGAITAKELYTMMMDKNTSLIIMDARKIQDYQHSCILDSLSVPEEAISPGVTASWIEANLSDDSKDTWKKRGSVDYVVLLDWFSSAKDLLLGTTLRSLKDALFKWESKTVLRHEPLVLEGGYENWLLCYPQFTTNAKVTPPPRSRAEEVSVSLDFTYPSLEEPVPSKLPTQMPPPPIETNEKALLVTDQDEKLRLSTQPALAGPGAAPRAEASPIIQPAPATKSVPQVDRTKKPSVKLPEDHRIKSENTDQSGRVLSDRSTKPVFPSPTTMLTDEEKARIHQETALLMEKNKQEKELWDKQQKEQKEKLRREEQERKAGKTQDADERDSTENQHKAKDGQEKKDSKQTKTEDRELSADGAQEATGTQRQSKSEHEASDAKVPVEGKRCPTSEAQKRPADVSPASVSGELNAGKAQREPLTRARSEEMGRIVPGLPLGWAKFLDPITGTFRYYHSPTNTVHMYPPEMAPSSAPPSTPPTHKVKPQVPAERDREPSKLKRSYSSPDITQALQEEEKRRPAVTPMVNRENKPPCYPKAEISRLSASQIRNLNPVFGGSGPALTGLRNLGNTCYMNSILQCLCNAPHLADYFNRNCYQDDINRSNLLGHKGEVAEEFGIIMKALWTGQYRYISPKDFKVTIGKINDQFAGSSQQDSQELLLFLMDGLHEDLNKADNRKRHKEENNEHLDDLQAAEHAWQKHKQLNESIIVALFQGQFKSTVQCLTCRRRSRTFEAFMYLSLPLASTSKCTLQDCLRLFSKEEKLTDNNRFYCSHCRARRDSLKKIEIWKLPPVLLVHLKRFSYDGRWKQKLQTSVDFPLENLDLSQYVIGPKNSLKKYNLFSVSNHYGGLDGGHYTAYCKNAARQRWFKFDDHEVSDISVSSVRSSAAYILFYTSLGPRITDVAT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
70	Phosphorylation	YMKYVAVYNLIKKRP HHHHHHHHHHHHHCC	8.43	26239621
108	Phosphorylation	EAERLSESLKLRYEE HHHHHHHHHHHHHHH	27.68	23140645
125	Acetylation	VRKQLEEKDRREEEQ HHHHHHHHHHHHHHH	47.35	23864654
146	Phosphorylation	QEMGREDSGAAAKRS HHHHCCCHHHHHHHH	26.11	29899451
153	Phosphorylation	SGAAAKRSVENLLDS HHHHHHHHHHHHHCC	32.83	25521595
160	Phosphorylation	SVENLLDSKTKTQRI HHHHHHCCCCCCCEE	42.04	28066266
162	Phosphorylation	ENLLDSKTKTQRING HHHHCCCCCCCEECC	43.19	25367039
164	Phosphorylation	LLDSKTKTQRINGEK HHCCCCCCCEECCCC	28.45	25367039
273	Phosphorylation	KDLLLGTTLRSLKDA HHHHHHHHHHHHHHH	20.55	30387612
392	Phosphorylation	AAPRAEASPIIQPAP CCCCCCCCCCCCCCC	14.24	26824392
440	Phosphorylation	RVLSDRSTKPVFPSP CCCCCCCCCCCCCCC	40.02	22942356
446	Phosphorylation	STKPVFPSPTTMLTD CCCCCCCCCCCCCCH	24.34	25338131
522	Acetylation	AKDGQEKKDSKQTKT CCCCCCCCCCCCCCH	67.49	7711903
525	Acetylation	GQEKKDSKQTKTEDR CCCCCCCCCCCHHHH	72.60	7711915
528	Acetylation	KKDSKQTKTEDRELS CCCCCCCCHHHHCCC	47.63	7711927
535	Phosphorylation	KTEDRELSADGAQEA CHHHHCCCHHHHHHH	21.40	29899451
549	Phosphorylation	ATGTQRQSKSEHEAS HHCCCCCCCCCHHHC	40.10	25338131
569	Phosphorylation	VEGKRCPTSEAQKRP CCCCCCCCHHHHCCC	42.71	-
580	Phosphorylation	QKRPADVSPASVSGE HCCCCCCCCCHHHCC	18.46	25521595
583	Phosphorylation	PADVSPASVSGELNA CCCCCCCHHHCCCCC	21.87	28066266
585	Phosphorylation	DVSPASVSGELNAGK CCCCCHHHCCCCCCC	24.85	25293948
603	Phosphorylation	EPLTRARSEEMGRIV CCCHHHHHHHHHCCC	36.60	25521595
653	Phosphorylation	APSSAPPSTPPTHKV CCCCCCCCCCCCCCC	53.11	25266776
678	Phosphorylation	EPSKLKRSYSSPDIT CCHHHCCCCCCCHHH	27.98	27087446
679	Phosphorylation	PSKLKRSYSSPDITQ CHHHCCCCCCCHHHH	19.73	24925903
680	Phosphorylation	SKLKRSYSSPDITQA HHHCCCCCCCHHHHH	36.32	24925903
681	Phosphorylation	KLKRSYSSPDITQAL HHCCCCCCCHHHHHH	20.54	25521595
685	Phosphorylation	SYSSPDITQALQEEE CCCCCHHHHHHHHHH	18.37	24925903
711	Phosphorylation	RENKPPCYPKAEISR CCCCCCCCCHHHHHH	17.34	26026062
720	Phosphorylation	KAEISRLSASQIRNL HHHHHHCCHHHHCCC	25.43	16944949
722	Phosphorylation	EISRLSASQIRNLNP HHHHCCHHHHCCCCC	23.82	-
907	Phosphorylation	TCRRRSRTFEAFMYL HCCCCCCCCCCHHHH	27.37	14661020
977	Phosphorylation	LVHLKRFSYDGRWKQ EEEEEECCCCCHHHH	26.75	-
1009	Phosphorylation	YVIGPKNSLKKYNLF EEECCCCCCHHCCEE	47.92	23737553

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
907	T	Phosphorylation	Kinase	AKT1	P31749	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
680	S	Phosphorylation	16944949
Phosphorylation of Ser-680 is essential for interaction with YWHAE and for cytosol localization.
680	S	Phosphorylation	16944949
Undergoes dephosphorylation at Ser-680 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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
1433E_HUMAN	YWHAE	physical	17720156
1433Z_HUMAN	YWHAZ	physical	17720156
1433G_HUMAN	YWHAG	physical	17720156
EGFR_HUMAN	EGFR	physical	16120644
STAM2_MOUSE	Stam2	physical	20130268
EGFR_HUMAN	EGFR	physical	17121848
RGRF1_MOUSE	Rasgrf1	physical	11500497
UBC_MOUSE	Ubc	physical	16810319
UBC_MOUSE	Ubc	physical	24533902

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of UBP8_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-680, AND MASSSPECTROMETRY.	19367708 [Abstract]
"14-3-3-dependent inhibition of the deubiquitinating activity of UBPYand its cancellation in the M phase."; Mizuno E., Kitamura N., Komada M.; Exp. Cell Res. 313:3624-3634(2007). Cited for: FUNCTION, PHOSPHORYLATION AT SER-680, INTERACTION WITH YWHAE; YWHAGAND YWHAZ, MUTAGENESIS OF SER-680, AND SUBCELLULAR LOCATION.	17720156 [Abstract]
"Identification of 14-3-3epsilon substrates from embryonic murinebrain."; Ballif B.A., Cao Z., Schwartz D., Carraway K.L. III, Gygi S.P.; J. Proteome Res. 5:2372-2379(2006). Cited for: PHOSPHORYLATION AT SER-680, INTERACTION WITH YWHAE, MUTAGENESIS OFSER-680, AND SUBCELLULAR LOCATION.	16944949 [Abstract]
"Neuregulin-induced ErbB3 downregulation is mediated by a proteinstability cascade involving the E3 ubiquitin ligase Nrdp1."; Cao Z., Wu X., Yen L., Sweeney C., Carraway K.L. III; Mol. Cell. Biol. 27:2180-2188(2007). Cited for: FUNCTION, PHOSPHORYLATION AT THR-907, AND MUTAGENESIS OF THR-907.	17210635 [Abstract]

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