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Q9UHP3

- UBP25_HUMAN

UniProt

Q9UHP3 - UBP25_HUMAN

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Protein

Ubiquitin carboxyl-terminal hydrolase 25

Gene

USP25

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

Functioni

Deubiquitinating enzyme that hydrolyzes ubiquitin moieties conjugated to substrates and thus, functions to process newly synthesized Ubiquitin, to recycle ubiquitin molecules or to edit polyubiquitin chains and prevents proteasomal degradation of substrates. Hydrolyzes both 'Lys-48'- and 'Lys-63'-linked tetraubiquitin chains.
The muscle-specific isoform (USP25m) may have a role in the regulation of muscular differentiation and function.

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).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei178 – 17811 Publication
Active sitei599 – 5991By similarity
Active sitei607 – 6071By similarity

GO - Molecular functioni

  1. peptidase activity Source: ProtInc
  2. SUMO binding Source: UniProtKB
  3. ubiquitin-specific protease activity Source: UniProtKB

GO - Biological processi

  1. cellular protein modification process Source: ProtInc
  2. protein K48-linked deubiquitination Source: UniProtKB
  3. protein K63-linked deubiquitination Source: UniProtKB
  4. proteolysis Source: ProtInc
  5. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Protein family/group databases

MEROPSiC19.041.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin carboxyl-terminal hydrolase 25 (EC:3.4.19.12)
Alternative name(s):
Deubiquitinating enzyme 25
USP on chromosome 21
Ubiquitin thioesterase 25
Ubiquitin-specific-processing protease 25
Gene namesi
Name:USP25
Synonyms:USP21
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 21

Organism-specific databases

HGNCiHGNC:12624. USP25.

Subcellular locationi

Cytoplasm 2 Publications
Isoform USP25m : Cytoplasm By similarity. Nucleus By similarity
Note: Some transient punctuate nuclear location in myotubes during myocyte development.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi91 – 911V → A: No interaction with SUMO3; when associated with A-92. 1 Publication
Mutagenesisi92 – 921I → A: No interaction with SUMO3; when associated with A-91. 1 Publication
Mutagenesisi99 – 991K → R: Abolishes sumoylation. Decreased enzymatic activity. 2 Publications
Mutagenesisi178 – 1781C → S: Abrogates deubiquitinating activity. No effect on homo- or oligomerization. 1 Publication
Mutagenesisi740 – 7401Y → F: No effect on interaction with SYK. 1 Publication
Mutagenesisi878 – 8781T → I: No effect on interaction with SYK. 1 Publication
Mutagenesisi880 – 8801Y → F: No effect on interaction with SYK. 1 Publication
Mutagenesisi883 – 8831I → S: No effect on interaction with SYK. 1 Publication

Organism-specific databases

PharmGKBiPA37249.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10551055Ubiquitin carboxyl-terminal hydrolase 25PRO_0000080653Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki99 – 99Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross-linki99 – 99Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residuei740 – 7401Phosphotyrosine1 Publication

Post-translational modificationi

Acetylated.1 Publication
Sumoylation impairs binding to and hydrolysis of ubiquitin chains. Sumoylated preferentially with SUMO2 or SUMO3. Desumoylated by SENP1. Regulated by ubiquitination on the same residue.1 Publication
Preferentially monoubiquitinated but can also be polyubiquitinated. Autodeubiquitinated. Ubiquitination activates the enzymatic activity either by preventing sumoylation or by allowing novel interactions.1 Publication
Phosphorylation in the C-terminal by SYK regulates USP25 cellular levels.2 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9UHP3.
PaxDbiQ9UHP3.
PRIDEiQ9UHP3.

PTM databases

PhosphoSiteiQ9UHP3.

Expressioni

Tissue specificityi

Isoform USB25a is found in most adult and fetal tissues; expression is moderately high in testis, pancreas, kidney, skeletal muscle, liver, lung, placenta, brain, heart, but very low in peripheral blood, colon, small intestine, ovary, prostate, thymus and spleen. Isoform USB25b is found in all tissues except heart and skeletal muscle. Isoform USB25m is heart and skeletal muscle specific.2 Publications

Inductioni

The muscle-specific isoform (USP25m) is up-regulated during myocyte differentiation. Levels increase up to 100-fold towards completion of differentiation.1 Publication

Gene expression databases

BgeeiQ9UHP3.
CleanExiHS_USP21.
HS_USP25.
ExpressionAtlasiQ9UHP3. baseline and differential.
GenevestigatoriQ9UHP3.

Organism-specific databases

HPAiHPA018297.
HPA024142.

Interactioni

Subunit structurei

Homodimer or oligomer. Interacts with ACTA1 (via its C-terminus); the interaction occurs for all isoforms but is strongest for isoform USP25m in muscle differentiating cells. Interacts (isoform USP25m only) with MYBPC1; the interaction prevents proteasomal degradation of MYBPC1. Interacts (isoform USP25m only) with FLNC (via filament repeats 17-18, 20-21 and 24). Interacts with GAPDH. Interacts with SUMO3; the interaction sumoylates efficiently USP25. Interacts with SUMO2; the interaction sumoylates efficiently USP25. Interacts with SUMO1; the interaction only weakly sumoylates USP25. Interacts with SYK; phosphorylates USP25 and regulates USP25 intracellular levels.4 Publications

Protein-protein interaction databases

BioGridi118895. 35 interactions.
IntActiQ9UHP3. 18 interactions.
MINTiMINT-1188384.
STRINGi9606.ENSP00000285679.

Structurei

3D structure databases

ProteinModelPortaliQ9UHP3.
SMRiQ9UHP3. Positions 1-138, 140-411, 591-676.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 5744UBA-likeAdd
BLAST
Repeati97 – 11620UIM 1Add
BLAST
Repeati123 – 14018UIM 2Add
BLAST
Domaini169 – 657489USPAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni77 – 10226SUMO interaction domain (SIM)Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili541 – 57838Sequence AnalysisAdd
BLAST
Coiled coili684 – 71734Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi89 – 957Required for SUMO paralog-specific binding

Sequence similaritiesi

Belongs to the peptidase C19 family.Curated
Contains 1 UBA-like domain.Curated
Contains 2 UIM (ubiquitin-interacting motif) repeats.PROSITE-ProRule annotation
Contains 1 USP domain.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiCOG5077.
GeneTreeiENSGT00390000016082.
HOGENOMiHOG000007956.
HOVERGENiHBG056030.
InParanoidiQ9UHP3.
KOiK11849.
OMAiSRSVIHK.
OrthoDBiEOG761BSZ.
PhylomeDBiQ9UHP3.
TreeFamiTF329035.

Family and domain databases

InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR009060. UBA-like.
IPR003903. Ubiquitin-int_motif.
IPR028889. UCH/PAN2.
[Graphical view]
PfamiPF00443. UCH. 1 hit.
PF02809. UIM. 2 hits.
[Graphical view]
SMARTiSM00726. UIM. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
PROSITEiPS50330. UIM. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform USP25a (identifier: Q9UHP3-2) [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

        10         20         30         40         50
MTVEQNVLQQ SAAQKHQQTF LNQLREITGI NDTQILQQAL KDSNGNLELA
60 70 80 90 100
VAFLTAKNAK TPQQEETTYY QTALPGNDRY ISVGSQADTN VIDLTGDDKD
110 120 130 140 150
DLQRAIALSL AESNRAFRET GITDEEQAIS RVLEASIAEN KACLKRTPTE
160 170 180 190 200
VWRDSRNPYD RKRQDKAPVG LKNVGNTCWF SAVIQSLFNL LEFRRLVLNY
210 220 230 240 250
KPPSNAQDLP RNQKEHRNLP FMRELRYLFA LLVGTKRKYV DPSRAVEILK
260 270 280 290 300
DAFKSNDSQQ QDVSEFTHKL LDWLEDAFQM KAEEETDEEK PKNPMVELFY
310 320 330 340 350
GRFLAVGVLE GKKFENTEMF GQYPLQVNGF KDLHECLEAA MIEGEIESLH
360 370 380 390 400
SENSGKSGQE HWFTELPPVL TFELSRFEFN QALGRPEKIH NKLEFPQVLY
410 420 430 440 450
LDRYMHRNRE ITRIKREEIK RLKDYLTVLQ QRLERYLSYG SGPKRFPLVD
460 470 480 490 500
VLQYALEFAS SKPVCTSPVD DIDASSPPSG SIPSQTLPST TEQQGALSSE
510 520 530 540 550
LPSTSPSSVA AISSRSVIHK PFTQSRIPPD LPMHPAPRHI TEEELSVLES
560 570 580 590 600
CLHRWRTEIE NDTRDLQESI SRIHRTIELM YSDKSMIQVP YRLHAVLVHE
610 620 630 640 650
GQANAGHYWA YIFDHRESRW MKYNDIAVTK SSWEELVRDS FGGYRNASAY
660 670 680 690 700
CLMYINDKAQ FLIQEEFNKE TGQPLVGIET LPPDLRDFVE EDNQRFEKEL
710 720 730 740 750
EEWDAQLAQK ALQEKLLASQ KLRESETSVT TAQAAGDPEY LEQPSRSDFS
760 770 780 790 800
KHLKEETIQI ITKASHEHED KSPETVLQSA IKLEYARLVK LAQEDTPPET
810 820 830 840 850
DYRLHHVVVY FIQNQAPKKI IEKTLLEQFG DRNLSFDERC HNIMKVAQAK
860 870 880 890 900
LEMIKPEEVN LEEYEEWHQD YRKFRETTMY LIIGLENFQR ESYIDSLLFL
910 920 930 940 950
ICAYQNNKEL LSKGLYRGHD EELISHYRRE CLLKLNEQAA ELFESGEDRE
960 970 980 990 1000
VNNGLIIMNE FIVPFLPLLL VDEMEEKDIL AVEDMRNRWC SYLGQEMEPH
1010 1020 1030 1040 1050
LQEKLTDFLP KLLDCSMEIK SFHEPPKLPS YSTHELCERF ARIMLSLSRT

PADGR
Length:1,055
Mass (Da):122,218
Last modified:August 10, 2010 - v4
Checksum:i0B9CECDCAD619CF2
GO
Isoform USP25b (identifier: Q9UHP3-1) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     779-779: S → SIMMTPNMQGIIMAIGKSRSVYDRCGPEAGFFK

Show »
Length:1,087
Mass (Da):125,750
Checksum:i8F852D91651B2C6E
GO
Isoform USP25m (identifier: Q9UHP3-3) [UniParc]FASTAAdd to Basket

Also known as: Muscle-specific isoform

The sequence of this isoform differs from the canonical sequence as follows:
     779-779: S → SKPENTTSQPLSNQRVVEVAIPHVGKFMIESKEGGYDDEIMMTPNMQGIIMAIGKSRSVYDRCGPEAGFFK

Show »
Length:1,125
Mass (Da):129,963
Checksum:i85236A294FFEFD60
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti544 – 5441E → K in AAF32263. (PubMed:10644437)Curated
Sequence conflicti544 – 5441E → K in ACN76567. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei779 – 7791S → SIMMTPNMQGIIMAIGKSRS VYDRCGPEAGFFK in isoform USP25b. 1 PublicationVSP_039632
Alternative sequencei779 – 7791S → SKPENTTSQPLSNQRVVEVA IPHVGKFMIESKEGGYDDEI MMTPNMQGIIMAIGKSRSVY DRCGPEAGFFK in isoform USP25m. 1 PublicationVSP_039631

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF170562 mRNA. Translation: AAF32263.1.
AF134213 mRNA. Translation: AAF24998.1.
FJ763652 mRNA. Translation: ACN76567.1.
CH471079 Genomic DNA. Translation: EAX10041.1.
BC075792 mRNA. Translation: AAH75792.1.
AK022574 mRNA. Translation: BAB14107.1.
CCDSiCCDS33515.1. [Q9UHP3-2]
CCDS63336.1. [Q9UHP3-3]
CCDS63337.1. [Q9UHP3-1]
RefSeqiNP_001269970.1. NM_001283041.1. [Q9UHP3-3]
NP_001269971.1. NM_001283042.1. [Q9UHP3-1]
NP_037528.3. NM_013396.4. [Q9UHP3-2]
UniGeneiHs.743994.

Genome annotation databases

EnsembliENST00000285679; ENSP00000285679; ENSG00000155313. [Q9UHP3-2]
ENST00000285681; ENSP00000285681; ENSG00000155313. [Q9UHP3-1]
ENST00000400183; ENSP00000383044; ENSG00000155313. [Q9UHP3-3]
GeneIDi29761.
KEGGihsa:29761.
UCSCiuc002yjy.1. human. [Q9UHP3-2]
uc002yjz.1. human. [Q9UHP3-1]
uc011aby.1. human. [Q9UHP3-3]

Polymorphism databases

DMDMi302393833.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF170562 mRNA. Translation: AAF32263.1 .
AF134213 mRNA. Translation: AAF24998.1 .
FJ763652 mRNA. Translation: ACN76567.1 .
CH471079 Genomic DNA. Translation: EAX10041.1 .
BC075792 mRNA. Translation: AAH75792.1 .
AK022574 mRNA. Translation: BAB14107.1 .
CCDSi CCDS33515.1. [Q9UHP3-2 ]
CCDS63336.1. [Q9UHP3-3 ]
CCDS63337.1. [Q9UHP3-1 ]
RefSeqi NP_001269970.1. NM_001283041.1. [Q9UHP3-3 ]
NP_001269971.1. NM_001283042.1. [Q9UHP3-1 ]
NP_037528.3. NM_013396.4. [Q9UHP3-2 ]
UniGenei Hs.743994.

3D structure databases

ProteinModelPortali Q9UHP3.
SMRi Q9UHP3. Positions 1-138, 140-411, 591-676.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 118895. 35 interactions.
IntActi Q9UHP3. 18 interactions.
MINTi MINT-1188384.
STRINGi 9606.ENSP00000285679.

Protein family/group databases

MEROPSi C19.041.

PTM databases

PhosphoSitei Q9UHP3.

Polymorphism databases

DMDMi 302393833.

Proteomic databases

MaxQBi Q9UHP3.
PaxDbi Q9UHP3.
PRIDEi Q9UHP3.

Protocols and materials databases

DNASUi 29761.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000285679 ; ENSP00000285679 ; ENSG00000155313 . [Q9UHP3-2 ]
ENST00000285681 ; ENSP00000285681 ; ENSG00000155313 . [Q9UHP3-1 ]
ENST00000400183 ; ENSP00000383044 ; ENSG00000155313 . [Q9UHP3-3 ]
GeneIDi 29761.
KEGGi hsa:29761.
UCSCi uc002yjy.1. human. [Q9UHP3-2 ]
uc002yjz.1. human. [Q9UHP3-1 ]
uc011aby.1. human. [Q9UHP3-3 ]

Organism-specific databases

CTDi 29761.
GeneCardsi GC21P017102.
HGNCi HGNC:12624. USP25.
HPAi HPA018297.
HPA024142.
MIMi 604736. gene.
neXtProti NX_Q9UHP3.
PharmGKBi PA37249.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5077.
GeneTreei ENSGT00390000016082.
HOGENOMi HOG000007956.
HOVERGENi HBG056030.
InParanoidi Q9UHP3.
KOi K11849.
OMAi SRSVIHK.
OrthoDBi EOG761BSZ.
PhylomeDBi Q9UHP3.
TreeFami TF329035.

Miscellaneous databases

ChiTaRSi USP25. human.
GenomeRNAii 29761.
NextBioi 52254.
PROi Q9UHP3.
SOURCEi Search...

Gene expression databases

Bgeei Q9UHP3.
CleanExi HS_USP21.
HS_USP25.
ExpressionAtlasi Q9UHP3. baseline and differential.
Genevestigatori Q9UHP3.

Family and domain databases

InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR009060. UBA-like.
IPR003903. Ubiquitin-int_motif.
IPR028889. UCH/PAN2.
[Graphical view ]
Pfami PF00443. UCH. 1 hit.
PF02809. UIM. 2 hits.
[Graphical view ]
SMARTi SM00726. UIM. 1 hit.
[Graphical view ]
SUPFAMi SSF46934. SSF46934. 1 hit.
PROSITEi PS50330. UIM. 1 hit.
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. "USP25, a novel gene encoding a deubiquitinating enzyme, is located in the gene-poor region 21q11.2."
    Valero R., Marfany G., Gonzalez-Angulo O., Gonzalez-Gonzalez G., Puelles L., Gonzalez-Duarte R.
    Genomics 62:395-405(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS USP25A AND USP25B), TISSUE SPECIFICITY.
    Tissue: Fetal brain.
  2. "Narrowing of the region of allelic loss in 21q11-21 in squamous non-small cell lung carcinoma and cloning of a novel ubiquitin-specific protease gene from the deleted segment."
    Groet J., Ives J.H., Jones T.A., Danton M., Flomen R.H., Sheer D., Hrascan R., Pavelic K., Nizetic D.
    Genes Chromosomes Cancer 27:153-161(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM USP25A), FUNCTION.
  3. Valero R., Bosch-Comas A., Denuc A., Gonzalez-Duarte R., Marfany G.
    Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM USP25M).
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 USP25A).
    Tissue: Placenta.
  6. "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] OF 319-1055 (ISOFORM USP25A).
  7. "Characterization of alternatively spliced products and tissue-specific isoforms of USP28 and USP25."
    Valero R., Bayes M., Francisca Sanchez-Font M., Gonzalez-Angulo O., Gonzalez-Duarte R., Marfany G.
    Genome Biol. 2:RESEARCH0043.1-RESEARCH0043.10(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING, FUNCTION, TISSUE SPECIFICITY.
  8. "The ubiquitin-specific protease USP25 interacts with three sarcomeric proteins."
    Bosch-Comas A., Lindsten K., Gonzalez-Duarte R., Masucci M.G., Marfany G.
    Cell. Mol. Life Sci. 63:723-734(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING, INTERACTION WITH ACTA1; FLNC; GAPDH AND MYBPC1, INDUCTION, SUBCELLULAR LOCATION, POSSIBLE FUNCTION.
  9. "Mechanism and consequences for paralog-specific sumoylation of ubiquitin-specific protease 25."
    Meulmeester E., Kunze M., Hsiao H.H., Urlaub H., Melchior F.
    Mol. Cell 30:610-619(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-99, FUNCTION, INTERACTION WITH SUMO1; SUMO3 AND UBIQUITIN, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF VAL-91; ILE-92 AND LYS-99.
  10. "The UBA-UIM domains of the USP25 regulate the enzyme ubiquitination state and modulate substrate recognition."
    Denuc A., Bosch-Comas A., Gonzalez-Duarte R., Marfany G.
    PLoS ONE 4:E5571-E5571(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-99, DEUBIQUITINATION, ACTIVE SITE CYS-178, ACETYLATION, PHOSPHORYLATION, SUMOYLATION, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF LYS-99 AND CYS-178.
  11. "Functional interaction between the ubiquitin-specific protease 25 and the SYK tyrosine kinase."
    Cholay M., Reverdy C., Benarous R., Colland F., Daviet L.
    Exp. Cell Res. 316:667-675(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SYK, PHOSPHORYLATION AT TYR-740, MUTAGENESIS OF TYR-740; THR-878; TYR-880 AND ILE-883.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiUBP25_HUMAN
AccessioniPrimary (citable) accession number: Q9UHP3
Secondary accession number(s): C0LSZ0, Q6DHZ9, Q9H9W1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 10, 2010
Last modified: October 29, 2014
This is version 143 of the entry and version 4 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 21
    Human chromosome 21: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3