Q14694 (UBP10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin carboxyl-terminal hydrolase 10
EC=3.4.19.12

Alternative name(s):
Deubiquitinating enzyme 10
Ubiquitin thioesterase 10
Ubiquitin-specific-processing protease 10

Gene names

Name:	USP10
Synonyms:	KIAA0190

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	798 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.1 Ref.11 Ref.14 Ref.16 Ref.19
Catalytic activity	Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal). Ref.16
Enzyme regulation	Specifically inhibited by spautin-1 (specific and potent autophagy inhibitor-1), a derivative of MBCQ that binds to USP10 and inhibits deubiquitinase activity. Regulated by PIK3C3/VPS34-containing complexes. Ref.19
Subunit structure	Interacts with G3BP, which may regulate its function. Interacts with p53/TP53, SNX3 and CFTR. Ref.1 Ref.11 Ref.14 Ref.16
Subcellular location	Cytoplasm. Nucleus. Early endosome. Note: Cytoplasmic in normal conditions. After DNA damage, translocates to the nucleus following phosphorylation by ATM. Ref.14 Ref.16
Tissue specificity	Widely expressed. Ref.1
Induction	Following DNA damage. Down-regulated in renal cell carcinomas. Ref.16 Ref.19
Post-translational modification	Phosphorylated by ATM following DNA damage, leading to stablization and translocation it to the nucleus. Ref.16 Ubiquitinated. Deubiquitinated by USP13. Ref.19
Sequence similarities	Belongs to the peptidase C19 family. USP10 subfamily.
Sequence caution	The sequence CAD97644.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Autophagy DNA damage DNA repair Ubl conjugation pathway
Cellular component	Cytoplasm Endosome Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Hydrolase Protease Thiol protease
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA damage response, signal transduction by p53 class mediator Inferred from mutant phenotype Ref.16. Source: UniProtKB DNA repair Inferred from electronic annotation. Source: UniProtKB-KW autophagy Inferred from electronic annotation. Source: UniProtKB-KW protein deubiquitination Inferred from direct assay Ref.16. Source: UniProtKB regulation of autophagy Inferred from direct assay Ref.19. Source: UniProtKB ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	early endosome Inferred from direct assay Ref.14. Source: UniProtKB intermediate filament cytoskeleton Inferred from direct assay. Source: HPA nucleus Inferred from direct assay Ref.16. Source: UniProtKB
Molecular_function	cysteine-type endopeptidase activity Inferred from mutant phenotype Ref.19. Source: UniProtKB ion channel binding Inferred from direct assay Ref.14. Source: UniProtKB ubiquitin thiolesterase activity Inferred from direct assay Ref.19. Source: UniProtKB ubiquitin-specific protease activity Inferred from direct assay Ref.16Ref.19. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q14694-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q14694-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MCSKDTVLSVCALYWRKGIQSHTPLIGAWRRGKQREQPEDRGVPMKRAA

Isoform 3 (identifier: Q14694-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: MALHSP → MPWLPSPGIG

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.17
	Chain	2 – 798	797	Ubiquitin carboxyl-terminal hydrolase 10		PRO_0000080629
Regions
	Region	2 – 100	99	Interaction with p53/TP53
Sites
	Active site	424	1	Nucleophile
	Active site	749	1	Proton acceptor By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.17
	Modified residue	24	1	Phosphothreonine Ref.17
	Modified residue	42	1	Phosphothreonine; by ATM Ref.16
	Modified residue	100	1	Phosphothreonine Ref.12
	Modified residue	208	1	Phosphothreonine By similarity
	Modified residue	226	1	Phosphoserine Ref.12
	Modified residue	337	1	Phosphoserine; by ATM Ref.16
	Modified residue	365	1	Phosphoserine Ref.8 Ref.17
	Modified residue	370	1	Phosphoserine Ref.8 Ref.12 Ref.17
	Modified residue	563	1	Phosphoserine Ref.15
	Modified residue	576	1	Phosphoserine Ref.7 Ref.9 Ref.10 Ref.13 Ref.15 Ref.17 Ref.20
Natural variations
	Alternative sequence	1 – 6	6	MALHSP → MPWLPSPGIG in isoform 3.		VSP_038868
	Alternative sequence	1	1	M → MCSKDTVLSVCALYWRKGIQ SHTPLIGAWRRGKQREQPED RGVPMKRAA in isoform 2.		VSP_038869
	Natural variant	200	1	M → V. Ref.4 Corresponds to variant rs1862792 [ dbSNP | Ensembl ].		VAR_015859
	Natural variant	203	1	S → P. Ref.6 Corresponds to variant rs2326391 [ dbSNP | Ensembl ].		VAR_015860
	Natural variant	204	1	V → L. Ref.6 Corresponds to variant rs1812061 [ dbSNP | Ensembl ].		VAR_015861
Experimental info
	Mutagenesis	42	1	T → A: Abolishes phosphorylation by ATM; when associated with A-337. Ref.16
	Mutagenesis	42	1	T → E: Phospho-mimetic mutant that translocates to the nucleus in absence of genotoxic stress; when associated with D-337. Ref.16
	Mutagenesis	337	1	S → A: Abolishes phosphorylation by ATM; when associated with A-42. Ref.16
	Mutagenesis	337	1	S → D: Phospho-mimetic mutant that translocates to the nucleus in absence of genotoxic stress; when associated with E-42. Ref.16
	Mutagenesis	424	1	C → A: Abolishes de-ubiquitinating activity. Ref.1 Ref.14 Ref.19
	Sequence conflict	108	1	A → V in BAG61546. Ref.3
	Sequence conflict	263	1	T → A in BAG61546. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: E6BA77E2B5CE2B3F	FASTA	798	87,134
	10 20 30 40 50 60 MALHSPQYIF GDFSPDEFNQ FFVTPRSSVE LPPYSGTVLC GTQAVDKLPD GQEYQRIEFG 70 80 90 100 110 120 VDEVIEPSDT LPRTPSYSIS STLNPQAPEF ILGCTASKIT PDGITKEASY GSIDCQYPGS 130 140 150 160 170 180 ALALDGSSNV EAEVLENDGV SGGLGQRERK KKKKRPPGYY SYLKDGGDDS ISTEALVNGH 190 200 210 220 230 240 ANSAVPNSVS AEDAEFMGDM PPSVTPRTCN SPQNSTDSVS DIVPDSPFPG ALGSDTRTAG 250 260 270 280 290 300 QPEGGPGADF GQSCFPAEAG RDTLSRTAGA QPCVGTDTTE NLGVANGQIL ESSGEGTATN 310 320 330 340 350 360 GVELHTTESI DLDPTKPESA SPPADGTGSA SGTLPVSQPK SWASLFHDSK PSSSSPVAYV 370 380 390 400 410 420 ETKYSPPAIS PLVSEKQVEV KEGLVPVSED PVAIKIAELL ENVTLIHKPV SLQPRGLINK 430 440 450 460 470 480 GNWCYINATL QALVACPPMY HLMKFIPLYS KVQRPCTSTP MIDSFVRLMN EFTNMPVPPK 490 500 510 520 530 540 PRQALGDKIV RDIRPGAAFE PTYIYRLLTV NKSSLSEKGR QEDAEEYLGF ILNGLHEEML 550 560 570 580 590 600 NLKKLLSPSN EKLTISNGPK NHSVNEEEQE EQGEGSEDEW EQVGPRNKTS VTRQADFVQT 610 620 630 640 650 660 PITGIFGGHI RSVVYQQSSK ESATLQPFFT LQLDIQSDKI RTVQDALESL VARESVQGYT 670 680 690 700 710 720 TKTKQEVEIS RRVTLEKLPP VLVLHLKRFV YEKTGGCQKL IKNIEYPVDL EISKELLSPG 730 740 750 760 770 780 VKNKNFKCHR TYRLFAVVYH HGNSATGGHY TTDVFQIGLN GWLRIDDQTV KVINQYQVVK 790 PTAERTAYLL YYRRVDLL
	Isoform 2 [UniParc]. Checksum: 01C2CD6FC3709AE4	FASTA	846	92,597
	10 20 30 40 50 60 MCSKDTVLSV CALYWRKGIQ SHTPLIGAWR RGKQREQPED RGVPMKRAAA LHSPQYIFGD 70 80 90 100 110 120 FSPDEFNQFF VTPRSSVELP PYSGTVLCGT QAVDKLPDGQ EYQRIEFGVD EVIEPSDTLP 130 140 150 160 170 180 RTPSYSISST LNPQAPEFIL GCTASKITPD GITKEASYGS IDCQYPGSAL ALDGSSNVEA 190 200 210 220 230 240 EVLENDGVSG GLGQRERKKK KKRPPGYYSY LKDGGDDSIS TEALVNGHAN SAVPNSVSAE 250 260 270 280 290 300 DAEFMGDMPP SVTPRTCNSP QNSTDSVSDI VPDSPFPGAL GSDTRTAGQP EGGPGADFGQ 310 320 330 340 350 360 SCFPAEAGRD TLSRTAGAQP CVGTDTTENL GVANGQILES SGEGTATNGV ELHTTESIDL 370 380 390 400 410 420 DPTKPESASP PADGTGSASG TLPVSQPKSW ASLFHDSKPS SSSPVAYVET KYSPPAISPL 430 440 450 460 470 480 VSEKQVEVKE GLVPVSEDPV AIKIAELLEN VTLIHKPVSL QPRGLINKGN WCYINATLQA 490 500 510 520 530 540 LVACPPMYHL MKFIPLYSKV QRPCTSTPMI DSFVRLMNEF TNMPVPPKPR QALGDKIVRD 550 560 570 580 590 600 IRPGAAFEPT YIYRLLTVNK SSLSEKGRQE DAEEYLGFIL NGLHEEMLNL KKLLSPSNEK 610 620 630 640 650 660 LTISNGPKNH SVNEEEQEEQ GEGSEDEWEQ VGPRNKTSVT RQADFVQTPI TGIFGGHIRS 670 680 690 700 710 720 VVYQQSSKES ATLQPFFTLQ LDIQSDKIRT VQDALESLVA RESVQGYTTK TKQEVEISRR 730 740 750 760 770 780 VTLEKLPPVL VLHLKRFVYE KTGGCQKLIK NIEYPVDLEI SKELLSPGVK NKNFKCHRTY 790 800 810 820 830 840 RLFAVVYHHG NSATGGHYTT DVFQIGLNGW LRIDDQTVKV INQYQVVKPT AERTAYLLYY RRVDLL
	Isoform 3 [UniParc]. Checksum: CBA33D0F268AEF5A	FASTA	802	87,533
	10 20 30 40 50 60 MPWLPSPGIG QYIFGDFSPD EFNQFFVTPR SSVELPPYSG TVLCGTQAVD KLPDGQEYQR 70 80 90 100 110 120 IEFGVDEVIE PSDTLPRTPS YSISSTLNPQ APEFILGCTA SKITPDGITK EASYGSIDCQ 130 140 150 160 170 180 YPGSALALDG SSNVEAEVLE NDGVSGGLGQ RERKKKKKRP PGYYSYLKDG GDDSISTEAL 190 200 210 220 230 240 VNGHANSAVP NSVSAEDAEF MGDMPPSVTP RTCNSPQNST DSVSDIVPDS PFPGALGSDT 250 260 270 280 290 300 RTAGQPEGGP GADFGQSCFP AEAGRDTLSR TAGAQPCVGT DTTENLGVAN GQILESSGEG 310 320 330 340 350 360 TATNGVELHT TESIDLDPTK PESASPPADG TGSASGTLPV SQPKSWASLF HDSKPSSSSP 370 380 390 400 410 420 VAYVETKYSP PAISPLVSEK QVEVKEGLVP VSEDPVAIKI AELLENVTLI HKPVSLQPRG 430 440 450 460 470 480 LINKGNWCYI NATLQALVAC PPMYHLMKFI PLYSKVQRPC TSTPMIDSFV RLMNEFTNMP 490 500 510 520 530 540 VPPKPRQALG DKIVRDIRPG AAFEPTYIYR LLTVNKSSLS EKGRQEDAEE YLGFILNGLH 550 560 570 580 590 600 EEMLNLKKLL SPSNEKLTIS NGPKNHSVNE EEQEEQGEGS EDEWEQVGPR NKTSVTRQAD 610 620 630 640 650 660 FVQTPITGIF GGHIRSVVYQ QSSKESATLQ PFFTLQLDIQ SDKIRTVQDA LESLVARESV 670 680 690 700 710 720 QGYTTKTKQE VEISRRVTLE KLPPVLVLHL KRFVYEKTGG CQKLIKNIEY PVDLEISKEL 730 740 750 760 770 780 LSPGVKNKNF KCHRTYRLFA VVYHHGNSAT GGHYTTDVFQ IGLNGWLRID DQTVKVINQY 790 800 QVVKPTAERT AYLLYYRRVD LL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Ras-GAP SH3 domain binding protein (G3BP) is a modulator of USP10, a novel human ubiquitin specific protease." Soncini C., Berdo I., Draetta G. Oncogene 20:3869-3879(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH G3BP, MUTAGENESIS OF CYS-424.
[2]	"Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1." Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N. DNA Res. 3:17-24(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Bone marrow.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). Tissue: Brain and Placenta.
[4]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT VAL-200. Tissue: Melanoma and Retina.
[5]	"The sequence and analysis of duplication-rich human chromosome 16." Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A. Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS PRO-203 AND LEU-204. Tissue: Brain.
[7]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365 AND SER-370, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line." Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S. Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, MASS SPECTROMETRY. Tissue: Prostate cancer.
[10]	"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt 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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[11]	"Vasopressin-inducible ubiquitin-specific protease 10 increases ENaC cell surface expression by deubiquitylating and stabilizing sorting nexin 3." Boulkroun S., Ruffieux-Daidie D., Vitagliano J.J., Poirot O., Charles R.P., Lagnaz D., Firsov D., Kellenberger S., Staub O. Am. J. Physiol. 295:F889-F900(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SNX3.
[12]	"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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-100; SER-226 AND SER-370, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange 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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, MASS SPECTROMETRY. Tissue: Liver.
[14]	"The deubiquitinating enzyme USP10 regulates the post-endocytic sorting of cystic fibrosis transmembrane conductance regulator in airway epithelial cells." Bomberger J.M., Barnaby R.L., Stanton B.A. J. Biol. Chem. 284:18778-18789(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CFTR, MUTAGENESIS OF CYS-424.
[15]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-563 AND SER-576, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[16]	"USP10 regulates p53 localization and stability by deubiquitinating p53." Yuan J., Luo K., Zhang L., Cheville J.C., Lou Z. Cell 140:384-396(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INDUCTION, INTERACTION WITH TP53, PHOSPHORYLATION AT THR-42; SER-337 AND CYS-424, MUTAGENESIS OF THR-42 AND SER-337.
[17]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-24; SER-365; SER-370 AND SER-576, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE. Tissue: Cervix carcinoma.
[18]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]	"Beclin1 controls the levels of p53 by regulating the deubiquitination activity of USP10 and USP13." Liu J., Xia H., Kim M., Xu L., Li Y., Zhang L., Cai Y., Norberg H.V., Zhang T., Furuya T., Jin M., Zhu Z., Wang H., Yu J., Li Y., Hao Y., Choi A., Ke H., Ma D., Yuan J. Cell 147:223-234(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ENZYME REGULATION, UBIQUITINATION, MUTAGENESIS OF CYS-424.
[20]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D80012 mRNA. Translation: BAA11507.1. AK299618 mRNA. Translation: BAG61546.1. AK315570 mRNA. Translation: BAG37945.1. AL162049 mRNA. Translation: CAB82392.2. BX537402 mRNA. Translation: CAD97644.1. Different initiation. AC009116 Genomic DNA. No translation available. AC025280 Genomic DNA. No translation available. BC000263 mRNA. Translation: AAH00263.1.
IPI	IPI00291946. IPI00941385. IPI00955965.
RefSeq	NP_001259004.1. NM_001272075.1. NP_005144.2. NM_005153.2.
UniGene	Hs.136778.
3D structure databases
ProteinModelPortal	Q14694.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q14694. 9 interactions.
MINT	MINT-3030173.
STRING	9606.ENSP00000219473.
Protein family/group databases
MEROPS	C19.018.
PTM databases
PhosphoSite	Q14694.
Polymorphism databases
DMDM	2501458.
Proteomic databases
PaxDb	Q14694.
PRIDE	Q14694.
Protocols and materials databases
DNASU	9100.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000219473; ENSP00000219473; ENSG00000103194. ENST00000570191; ENSP00000457411; ENSG00000103194.
GeneID	9100.
KEGG	hsa:9100.
UCSC	uc002fii.3. human. uc010voe.2. human.
Organism-specific databases
CTD	9100.
GeneCards	GC16P084734.
H-InvDB	HIX0173245.
HGNC	HGNC:12608. USP10.
HPA	HPA006731. HPA006749.
MIM	609818. gene.
neXtProt	NX_Q14694.
PharmGKB	PA37234.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5533.
HOGENOM	HOG000285959.
HOVERGEN	HBG059823.
InParanoid	Q14694.
KO	K11841.
OMA	GQEYQRI.
OrthoDB	EOG4FN4H7.
Gene expression databases
ArrayExpress	Q14694.
Bgee	Q14694.
CleanEx	HS_USP10.
Genevestigator	Q14694.
GermOnline	ENSG00000103194. Homo sapiens.
Family and domain databases
InterPro	IPR009818. Ataxin-2_C. IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. [Graphical view]
Pfam	PF07145. PAM2. 1 hit. PF00443. UCH. 1 hit. [Graphical view]
PROSITE	PS00972. UCH_2_1. 1 hit. PS00973. UCH_2_2. 1 hit. PS50235. UCH_2_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	USP10. human.
GenomeRNAi	9100.
NextBio	34113.
SOURCE	Search...

Entry information

Entry name

UBP10_HUMAN

Accession

Primary (citable) accession number: Q14694
Secondary accession number(s): B2RDJ8 , B4DS84, Q9BWG7, Q9NSL7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	May 29, 2013
This is version 128 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.