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Q14694

- UBP10_HUMAN

UniProt

Q14694 - UBP10_HUMAN

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Protein

Ubiquitin carboxyl-terminal hydrolase 10

Gene
USP10, KIAA0190
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.5 Publications

Catalytic activityi

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).1 Publication

Enzyme regulationi

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei424 – 4241Nucleophile
Active sitei749 – 7491Proton acceptor By similarity

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: UniProtKB
  2. ion channel binding Source: UniProtKB
  3. p53 binding Source: UniProtKB
  4. poly(A) RNA binding Source: UniProtKB
  5. protein binding Source: UniProtKB
  6. ubiquitin-specific protease activity Source: UniProtKB
  7. ubiquitin thiolesterase activity Source: UniProtKB

GO - Biological processi

  1. autophagy Source: UniProtKB-KW
  2. DNA damage response, signal transduction by p53 class mediator Source: UniProtKB
  3. DNA repair Source: UniProtKB-KW
  4. protein deubiquitination Source: UniProtKB
  5. regulation of autophagy Source: UniProtKB
  6. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Autophagy, DNA damage, DNA repair, Ubl conjugation pathway

Protein family/group databases

MEROPSiC19.018.

Names & Taxonomyi

Protein namesi
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 namesi
Name:USP10
Synonyms:KIAA0190
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:12608. USP10.

Subcellular locationi

Cytoplasm. Nucleus. Early endosome
Note: Cytoplasmic in normal conditions. After DNA damage, translocates to the nucleus following phosphorylation by ATM.2 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. early endosome Source: UniProtKB
  3. intermediate filament cytoskeleton Source: HPA
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi42 – 421T → A: Abolishes phosphorylation by ATM; when associated with A-337. 1 Publication
Mutagenesisi42 – 421T → E: Phospho-mimetic mutant that translocates to the nucleus in absence of genotoxic stress; when associated with D-337. 1 Publication
Mutagenesisi337 – 3371S → A: Abolishes phosphorylation by ATM; when associated with A-42. 1 Publication
Mutagenesisi337 – 3371S → D: Phospho-mimetic mutant that translocates to the nucleus in absence of genotoxic stress; when associated with E-42. 1 Publication
Mutagenesisi424 – 4241C → A: Abolishes de-ubiquitinating activity. 3 Publications

Organism-specific databases

PharmGKBiPA37234.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 798797Ubiquitin carboxyl-terminal hydrolase 10PRO_0000080629Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei24 – 241Phosphothreonine1 Publication
Modified residuei42 – 421Phosphothreonine; by ATM1 Publication
Modified residuei100 – 1001Phosphothreonine1 Publication
Modified residuei226 – 2261Phosphoserine1 Publication
Modified residuei337 – 3371Phosphoserine; by ATM1 Publication
Modified residuei365 – 3651Phosphoserine2 Publications
Modified residuei370 – 3701Phosphoserine3 Publications
Modified residuei563 – 5631Phosphoserine1 Publication
Modified residuei576 – 5761Phosphoserine7 Publications

Post-translational modificationi

Phosphorylated by ATM following DNA damage, leading to stablization and translocation it to the nucleus.1 Publication
Ubiquitinated. Deubiquitinated by USP13.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ14694.
PaxDbiQ14694.
PRIDEiQ14694.

PTM databases

PhosphoSiteiQ14694.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Inductioni

Following DNA damage. Down-regulated in renal cell carcinomas.2 Publications

Gene expression databases

ArrayExpressiQ14694.
BgeeiQ14694.
CleanExiHS_USP10.
GenevestigatoriQ14694.

Organism-specific databases

HPAiHPA006731.
HPA006749.

Interactioni

Subunit structurei

Interacts with G3BP, which may regulate its function. Interacts with p53/TP53, SNX3 and CFTR.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ZC3H12AQ5D1E85EBI-2510389,EBI-747793

Protein-protein interaction databases

BioGridi114554. 33 interactions.
IntActiQ14694. 16 interactions.
MINTiMINT-3030173.
STRINGi9606.ENSP00000219473.

Structurei

3D structure databases

ProteinModelPortaliQ14694.
SMRiQ14694. Positions 416-796.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini415 – 795381USPAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 10099Interaction with p53/TP53Add
BLAST

Sequence similaritiesi

Contains 1 USP domain.

Phylogenomic databases

eggNOGiCOG5533.
HOGENOMiHOG000285959.
HOVERGENiHBG059823.
InParanoidiQ14694.
KOiK11841.
OMAiGQEYQRI.
OrthoDBiEOG7Z69BX.
PhylomeDBiQ14694.
TreeFamiTF323203.

Family and domain databases

InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR028767. USP10.
[Graphical view]
PANTHERiPTHR24006:SF69. PTHR24006:SF69. 1 hit.
PfamiPF00443. UCH. 1 hit.
[Graphical view]
PROSITEiPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q14694-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MALHSPQYIF GDFSPDEFNQ FFVTPRSSVE LPPYSGTVLC GTQAVDKLPD    50
GQEYQRIEFG VDEVIEPSDT LPRTPSYSIS STLNPQAPEF ILGCTASKIT 100
PDGITKEASY GSIDCQYPGS ALALDGSSNV EAEVLENDGV SGGLGQRERK 150
KKKKRPPGYY SYLKDGGDDS ISTEALVNGH ANSAVPNSVS AEDAEFMGDM 200
PPSVTPRTCN SPQNSTDSVS DIVPDSPFPG ALGSDTRTAG QPEGGPGADF 250
GQSCFPAEAG RDTLSRTAGA QPCVGTDTTE NLGVANGQIL ESSGEGTATN 300
GVELHTTESI DLDPTKPESA SPPADGTGSA SGTLPVSQPK SWASLFHDSK 350
PSSSSPVAYV ETKYSPPAIS PLVSEKQVEV KEGLVPVSED PVAIKIAELL 400
ENVTLIHKPV SLQPRGLINK GNWCYINATL QALVACPPMY HLMKFIPLYS 450
KVQRPCTSTP MIDSFVRLMN EFTNMPVPPK PRQALGDKIV RDIRPGAAFE 500
PTYIYRLLTV NKSSLSEKGR QEDAEEYLGF ILNGLHEEML NLKKLLSPSN 550
EKLTISNGPK NHSVNEEEQE EQGEGSEDEW EQVGPRNKTS VTRQADFVQT 600
PITGIFGGHI RSVVYQQSSK ESATLQPFFT LQLDIQSDKI RTVQDALESL 650
VARESVQGYT TKTKQEVEIS RRVTLEKLPP VLVLHLKRFV YEKTGGCQKL 700
IKNIEYPVDL EISKELLSPG VKNKNFKCHR TYRLFAVVYH HGNSATGGHY 750
TTDVFQIGLN GWLRIDDQTV KVINQYQVVK PTAERTAYLL YYRRVDLL 798
Length:798
Mass (Da):87,134
Last modified:November 1, 1997 - v2
Checksum:iE6BA77E2B5CE2B3F
GO
Isoform 2 (identifier: Q14694-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:846
Mass (Da):92,597
Checksum:i01C2CD6FC3709AE4
GO
Isoform 3 (identifier: Q14694-3) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:802
Mass (Da):87,533
Checksum:iCBA33D0F268AEF5A
GO

Sequence cautioni

The sequence CAD97644.1 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti200 – 2001M → V.1 Publication
Corresponds to variant rs1862792 [ dbSNP | Ensembl ].
VAR_015859
Natural varianti203 – 2031S → P.1 Publication
Corresponds to variant rs2326391 [ dbSNP | Ensembl ].
VAR_015860
Natural varianti204 – 2041V → L.1 Publication
Corresponds to variant rs1812061 [ dbSNP | Ensembl ].
VAR_015861

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 66MALHSP → MPWLPSPGIG in isoform 3. VSP_038868
Alternative sequencei1 – 11M → MCSKDTVLSVCALYWRKGIQ SHTPLIGAWRRGKQREQPED RGVPMKRAA in isoform 2. VSP_038869

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti108 – 1081A → V in BAG61546. 1 Publication
Sequence conflicti263 – 2631T → A in BAG61546. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS45537.1. [Q14694-1]
CCDS62004.1. [Q14694-3]
RefSeqiNP_001259004.1. NM_001272075.1. [Q14694-3]
NP_005144.2. NM_005153.2. [Q14694-1]
UniGeneiHs.136778.

Genome annotation databases

EnsembliENST00000219473; ENSP00000219473; ENSG00000103194. [Q14694-1]
ENST00000570191; ENSP00000457411; ENSG00000103194. [Q14694-3]
GeneIDi9100.
KEGGihsa:9100.
UCSCiuc002fii.3. human. [Q14694-1]
uc010voe.2. human. [Q14694-3]

Polymorphism databases

DMDMi2501458.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS45537.1. [Q14694-1 ]
CCDS62004.1. [Q14694-3 ]
RefSeqi NP_001259004.1. NM_001272075.1. [Q14694-3 ]
NP_005144.2. NM_005153.2. [Q14694-1 ]
UniGenei Hs.136778.

3D structure databases

ProteinModelPortali Q14694.
SMRi Q14694. Positions 416-796.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114554. 33 interactions.
IntActi Q14694. 16 interactions.
MINTi MINT-3030173.
STRINGi 9606.ENSP00000219473.

Protein family/group databases

MEROPSi C19.018.

PTM databases

PhosphoSitei Q14694.

Polymorphism databases

DMDMi 2501458.

Proteomic databases

MaxQBi Q14694.
PaxDbi Q14694.
PRIDEi Q14694.

Protocols and materials databases

DNASUi 9100.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000219473 ; ENSP00000219473 ; ENSG00000103194 . [Q14694-1 ]
ENST00000570191 ; ENSP00000457411 ; ENSG00000103194 . [Q14694-3 ]
GeneIDi 9100.
KEGGi hsa:9100.
UCSCi uc002fii.3. human. [Q14694-1 ]
uc010voe.2. human. [Q14694-3 ]

Organism-specific databases

CTDi 9100.
GeneCardsi GC16P084734.
H-InvDB HIX0173245.
HGNCi HGNC:12608. USP10.
HPAi HPA006731.
HPA006749.
MIMi 609818. gene.
neXtProti NX_Q14694.
PharmGKBi PA37234.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5533.
HOGENOMi HOG000285959.
HOVERGENi HBG059823.
InParanoidi Q14694.
KOi K11841.
OMAi GQEYQRI.
OrthoDBi EOG7Z69BX.
PhylomeDBi Q14694.
TreeFami TF323203.

Miscellaneous databases

ChiTaRSi USP10. human.
GeneWikii USP10.
GenomeRNAii 9100.
NextBioi 34113.
PROi Q14694.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q14694.
Bgeei Q14694.
CleanExi HS_USP10.
Genevestigatori Q14694.

Family and domain databases

InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR028767. USP10.
[Graphical view ]
PANTHERi PTHR24006:SF69. PTHR24006:SF69. 1 hit.
Pfami PF00443. UCH. 1 hit.
[Graphical view ]
PROSITEi PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-100; SER-226 AND SER-370, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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.
  16. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  17. "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 AND SER-337, MUTAGENESIS OF THR-42 AND SER-337.
  18. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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.
  21. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiUBP10_HUMAN
AccessioniPrimary (citable) accession number: Q14694
Secondary accession number(s): B2RDJ8
, B4DS84, Q9BWG7, Q9NSL7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: September 3, 2014
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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