Q9UHP3 (UBP25_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin carboxyl-terminal hydrolase 25
EC=3.4.19.12

Alternative name(s):
Deubiquitinating enzyme 25
USP on chromosome 21
Ubiquitin thiolesterase 25
Ubiquitin-specific-processing protease 25

Gene names

Name:	USP25
Synonyms:	USP21

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1055 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.2 Ref.7 Ref.8 Ref.10 Ref.11 The muscle-specific USP25m) may have a role in the regulation of muscular differentiation and function. Ref.2 Ref.7 Ref.8 Ref.10 Ref.11
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).
Subunit structure	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. Ref.8 Ref.10 Ref.11 Ref.12
Subcellular location	Cytoplasm Ref.8 Ref.11. Isoform USP25m: Cytoplasm By similarity. Nucleus By similarity. Note: Some transient punctuate nuclear location in myotubes during myocyte development By similarity. Ref.8 Ref.11
Tissue specificity	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. Ref.1 Ref.7
Induction	The muscle-specific USP25m) is up-regulated during myocyte differentiation. Levels increase up to 100-fold towards completion of differentiation. Ref.8
Post-translational modification	Acetylated. Sumoylation impairs binding to and hydrolysis of ubiquitin chains. Sumoylated preferentially by SUMO2 or SUMO3. Desumoylated by SENP1. Regulated by ubiquitination on the same residue. Ref.10 Ref.11 Preferentially monoubiquitinated but can also be polyubiquitinated. Autodeubiquitinated. Ubiquitination activates the enzymatic activity either by preventing sumoylation or by allowing novel interactions. Phosphorylation in the C-terminal by SYK regulates USP25 cellular levels.
Sequence similarities	Belongs to the peptidase C19 family. Contains 1 UBA-like domain. Contains 2 UIM (ubiquitin-interacting motif) repeats.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Repeat
Molecular function	Hydrolase Protease Thiol protease
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	protein K48-linked deubiquitination Inferred from mutant phenotype Ref.10. Source: UniProtKB protein K63-linked deubiquitination Inferred from mutant phenotype Ref.10. Source: UniProtKB ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	SUMO binding Inferred from direct assay Ref.10. Source: UniProtKB ubiquitin thiolesterase activity Inferred from electronic annotation. Source: InterPro ubiquitin-specific protease activity Inferred from mutant phenotype Ref.10. Source: UniProtKB
Complete GO annotation...

Alternative products

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

Isoform USP25a (identifier: Q9UHP3-2)

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 USP25b (identifier: Q9UHP3-1)

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

Isoform USP25m (identifier: Q9UHP3-3)

Also known as: Muscle-specific isoform;

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1055	1055	Ubiquitin carboxyl-terminal hydrolase 25		PRO_0000080653
Regions
	Domain	14 – 57	44	UBA-like
	Repeat	97 – 116	20	UIM 1
	Repeat	123 – 140	18	UIM 2
	Region	77 – 102	26	SUMO interaction domain (SIM)
	Coiled coil	541 – 578	38	Potential
	Coiled coil	684 – 717	34	Potential
	Motif	89 – 95	7	Required for SUMO paralog-specific binding
Sites
	Active site	178	1	Ref.11
	Active site	599	1	By similarity
	Active site	607	1	By similarity
Amino acid modifications
	Modified residue	916	1	Phosphotyrosine Ref.9
	Cross-link	99		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate Ref.10 Ref.11
	Cross-link	99		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
Natural variations
	Alternative sequence	779	1	S → SIMMTPNMQGIIMAIGKSRS VYDRCGPEAGFFK in isoform USP25b.		VSP_039632
	Alternative sequence	779	1	S → SKPENTTSQPLSNQRVVEVA IPHVGKFMIESKEGGYDDEI MMTPNMQGIIMAIGKSRSVY DRCGPEAGFFK in isoform USP25m.		VSP_039631
Experimental info
	Mutagenesis	91	1	V → A: No interaction with SUMO3; when associated with A-92. Ref.10
	Mutagenesis	92	1	I → A: No interaction with SUMO3; when associated with A-91. Ref.10
	Mutagenesis	99	1	K → R: Abolishes sumoylation. Decreased enzymatic activity. Ref.10 Ref.11
	Mutagenesis	178	1	C → S: Abrogates deubiquitinating activity. No effect on homo- or oligomerization. Ref.11
	Mutagenesis	740	1	Y → F: No effect on interaction with SYK. Ref.12
	Mutagenesis	878	1	T → I: No effect on interaction with SYK. Ref.12
	Mutagenesis	880	1	Y → F: No effect on interaction with SYK. Ref.12
	Mutagenesis	883	1	I → S: No effect on interaction with SYK. Ref.12
	Sequence conflict	544	1	E → K in AAF32263. Ref.1
	Sequence conflict	544	1	E → K in ACN76567. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform USP25a [UniParc]. Last modified August 10, 2010. Version 4. Checksum: 0B9CECDCAD619CF2	FASTA	1,055	122,218
	10 20 30 40 50 60 MTVEQNVLQQ SAAQKHQQTF LNQLREITGI NDTQILQQAL KDSNGNLELA VAFLTAKNAK 70 80 90 100 110 120 TPQQEETTYY QTALPGNDRY ISVGSQADTN VIDLTGDDKD DLQRAIALSL AESNRAFRET 130 140 150 160 170 180 GITDEEQAIS RVLEASIAEN KACLKRTPTE VWRDSRNPYD RKRQDKAPVG LKNVGNTCWF 190 200 210 220 230 240 SAVIQSLFNL LEFRRLVLNY KPPSNAQDLP RNQKEHRNLP FMRELRYLFA LLVGTKRKYV 250 260 270 280 290 300 DPSRAVEILK DAFKSNDSQQ QDVSEFTHKL LDWLEDAFQM KAEEETDEEK PKNPMVELFY 310 320 330 340 350 360 GRFLAVGVLE GKKFENTEMF GQYPLQVNGF KDLHECLEAA MIEGEIESLH SENSGKSGQE 370 380 390 400 410 420 HWFTELPPVL TFELSRFEFN QALGRPEKIH NKLEFPQVLY LDRYMHRNRE ITRIKREEIK 430 440 450 460 470 480 RLKDYLTVLQ QRLERYLSYG SGPKRFPLVD VLQYALEFAS SKPVCTSPVD DIDASSPPSG 490 500 510 520 530 540 SIPSQTLPST TEQQGALSSE LPSTSPSSVA AISSRSVIHK PFTQSRIPPD LPMHPAPRHI 550 560 570 580 590 600 TEEELSVLES CLHRWRTEIE NDTRDLQESI SRIHRTIELM YSDKSMIQVP YRLHAVLVHE 610 620 630 640 650 660 GQANAGHYWA YIFDHRESRW MKYNDIAVTK SSWEELVRDS FGGYRNASAY CLMYINDKAQ 670 680 690 700 710 720 FLIQEEFNKE TGQPLVGIET LPPDLRDFVE EDNQRFEKEL EEWDAQLAQK ALQEKLLASQ 730 740 750 760 770 780 KLRESETSVT TAQAAGDPEY LEQPSRSDFS KHLKEETIQI ITKASHEHED KSPETVLQSA 790 800 810 820 830 840 IKLEYARLVK LAQEDTPPET DYRLHHVVVY FIQNQAPKKI IEKTLLEQFG DRNLSFDERC 850 860 870 880 890 900 HNIMKVAQAK LEMIKPEEVN LEEYEEWHQD YRKFRETTMY LIIGLENFQR ESYIDSLLFL 910 920 930 940 950 960 ICAYQNNKEL LSKGLYRGHD EELISHYRRE CLLKLNEQAA ELFESGEDRE VNNGLIIMNE 970 980 990 1000 1010 1020 FIVPFLPLLL VDEMEEKDIL AVEDMRNRWC SYLGQEMEPH LQEKLTDFLP KLLDCSMEIK 1030 1040 1050 SFHEPPKLPS YSTHELCERF ARIMLSLSRT PADGR
	Isoform USP25b [UniParc]. Checksum: 8F852D91651B2C6E	FASTA	1,087	125,750
	10 20 30 40 50 60 MTVEQNVLQQ SAAQKHQQTF LNQLREITGI NDTQILQQAL KDSNGNLELA VAFLTAKNAK 70 80 90 100 110 120 TPQQEETTYY QTALPGNDRY ISVGSQADTN VIDLTGDDKD DLQRAIALSL AESNRAFRET 130 140 150 160 170 180 GITDEEQAIS RVLEASIAEN KACLKRTPTE VWRDSRNPYD RKRQDKAPVG LKNVGNTCWF 190 200 210 220 230 240 SAVIQSLFNL LEFRRLVLNY KPPSNAQDLP RNQKEHRNLP FMRELRYLFA LLVGTKRKYV 250 260 270 280 290 300 DPSRAVEILK DAFKSNDSQQ QDVSEFTHKL LDWLEDAFQM KAEEETDEEK PKNPMVELFY 310 320 330 340 350 360 GRFLAVGVLE GKKFENTEMF GQYPLQVNGF KDLHECLEAA MIEGEIESLH SENSGKSGQE 370 380 390 400 410 420 HWFTELPPVL TFELSRFEFN QALGRPEKIH NKLEFPQVLY LDRYMHRNRE ITRIKREEIK 430 440 450 460 470 480 RLKDYLTVLQ QRLERYLSYG SGPKRFPLVD VLQYALEFAS SKPVCTSPVD DIDASSPPSG 490 500 510 520 530 540 SIPSQTLPST TEQQGALSSE LPSTSPSSVA AISSRSVIHK PFTQSRIPPD LPMHPAPRHI 550 560 570 580 590 600 TEEELSVLES CLHRWRTEIE NDTRDLQESI SRIHRTIELM YSDKSMIQVP YRLHAVLVHE 610 620 630 640 650 660 GQANAGHYWA YIFDHRESRW MKYNDIAVTK SSWEELVRDS FGGYRNASAY CLMYINDKAQ 670 680 690 700 710 720 FLIQEEFNKE TGQPLVGIET LPPDLRDFVE EDNQRFEKEL EEWDAQLAQK ALQEKLLASQ 730 740 750 760 770 780 KLRESETSVT TAQAAGDPEY LEQPSRSDFS KHLKEETIQI ITKASHEHED KSPETVLQSI 790 800 810 820 830 840 MMTPNMQGII MAIGKSRSVY DRCGPEAGFF KAIKLEYARL VKLAQEDTPP ETDYRLHHVV 850 860 870 880 890 900 VYFIQNQAPK KIIEKTLLEQ FGDRNLSFDE RCHNIMKVAQ AKLEMIKPEE VNLEEYEEWH 910 920 930 940 950 960 QDYRKFRETT MYLIIGLENF QRESYIDSLL FLICAYQNNK ELLSKGLYRG HDEELISHYR 970 980 990 1000 1010 1020 RECLLKLNEQ AAELFESGED REVNNGLIIM NEFIVPFLPL LLVDEMEEKD ILAVEDMRNR 1030 1040 1050 1060 1070 1080 WCSYLGQEME PHLQEKLTDF LPKLLDCSME IKSFHEPPKL PSYSTHELCE RFARIMLSLS RTPADGR
	Isoform USP25m (Muscle-specific isoform) [UniParc]. Checksum: 85236A294FFEFD60	FASTA	1,125	129,963
	10 20 30 40 50 60 MTVEQNVLQQ SAAQKHQQTF LNQLREITGI NDTQILQQAL KDSNGNLELA VAFLTAKNAK 70 80 90 100 110 120 TPQQEETTYY QTALPGNDRY ISVGSQADTN VIDLTGDDKD DLQRAIALSL AESNRAFRET 130 140 150 160 170 180 GITDEEQAIS RVLEASIAEN KACLKRTPTE VWRDSRNPYD RKRQDKAPVG LKNVGNTCWF 190 200 210 220 230 240 SAVIQSLFNL LEFRRLVLNY KPPSNAQDLP RNQKEHRNLP FMRELRYLFA LLVGTKRKYV 250 260 270 280 290 300 DPSRAVEILK DAFKSNDSQQ QDVSEFTHKL LDWLEDAFQM KAEEETDEEK PKNPMVELFY 310 320 330 340 350 360 GRFLAVGVLE GKKFENTEMF GQYPLQVNGF KDLHECLEAA MIEGEIESLH SENSGKSGQE 370 380 390 400 410 420 HWFTELPPVL TFELSRFEFN QALGRPEKIH NKLEFPQVLY LDRYMHRNRE ITRIKREEIK 430 440 450 460 470 480 RLKDYLTVLQ QRLERYLSYG SGPKRFPLVD VLQYALEFAS SKPVCTSPVD DIDASSPPSG 490 500 510 520 530 540 SIPSQTLPST TEQQGALSSE LPSTSPSSVA AISSRSVIHK PFTQSRIPPD LPMHPAPRHI 550 560 570 580 590 600 TEEELSVLES CLHRWRTEIE NDTRDLQESI SRIHRTIELM YSDKSMIQVP YRLHAVLVHE 610 620 630 640 650 660 GQANAGHYWA YIFDHRESRW MKYNDIAVTK SSWEELVRDS FGGYRNASAY CLMYINDKAQ 670 680 690 700 710 720 FLIQEEFNKE TGQPLVGIET LPPDLRDFVE EDNQRFEKEL EEWDAQLAQK ALQEKLLASQ 730 740 750 760 770 780 KLRESETSVT TAQAAGDPEY LEQPSRSDFS KHLKEETIQI ITKASHEHED KSPETVLQSK 790 800 810 820 830 840 PENTTSQPLS NQRVVEVAIP HVGKFMIESK EGGYDDEIMM TPNMQGIIMA IGKSRSVYDR 850 860 870 880 890 900 CGPEAGFFKA IKLEYARLVK LAQEDTPPET DYRLHHVVVY FIQNQAPKKI IEKTLLEQFG 910 920 930 940 950 960 DRNLSFDERC HNIMKVAQAK LEMIKPEEVN LEEYEEWHQD YRKFRETTMY LIIGLENFQR 970 980 990 1000 1010 1020 ESYIDSLLFL ICAYQNNKEL LSKGLYRGHD EELISHYRRE CLLKLNEQAA ELFESGEDRE 1030 1040 1050 1060 1070 1080 VNNGLIIMNE FIVPFLPLLL VDEMEEKDIL AVEDMRNRWC SYLGQEMEPH LQEKLTDFLP 1090 1100 1110 1120 KLLDCSMEIK SFHEPPKLPS YSTHELCERF ARIMLSLSRT PADGR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 10644437] [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: 10612803] [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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [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: 14702039] [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: 11597335] [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: 16501887] [Abstract] Cited for: ALTERNATIVE SPLICING, INTERACTION WITH ACTA1; FLNC; GAPDH AND MYBPC1, INDUCTION, SUBCELLULAR LOCATION, POSSIBLE FUNCTION.
[9]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells 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) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-916, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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: 18538659] [Abstract] Cited for: SUMOYLATION AT LYS-99, FUNCTION, INTERACTION WITH SUMO1; SUMO3 AND UBIQUITIN, MASS SPECTROMETRY, MUTAGENESIS OF VAL-91; ILE-92 AND LYS-99.
[11]	"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: 19440361] [Abstract] Cited for: UBIQUITINATION AT LYS-99, DEUBIQUITINATION, ACTIVE SITE AT CYS-178, ACETYLATION, PHOSPHORYLATION, SUMOYLATION, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF LYS-99 AND CYS-178.
[12]	"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: 19909739] [Abstract] Cited for: INTERACTION WITH SYK, PHOSPHORYLATION AT TYR-740, MUTAGENESIS OF TYR-740; THR-878; TYR-880 AND ILE-883.
[13]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00219886. IPI00300439. IPI00791721.
RefSeq	NP_037528.3. NM_013396.3.
UniGene	Hs.473370.
3D structure databases
ProteinModelPortal	Q9UHP3.
SMR	Q9UHP3. Positions 1-68.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UHP3. 13 interactions.
MINT	MINT-1188384.
STRING	Q9UHP3.
Protein family/group databases
MEROPS	C19.041.
PTM databases
PhosphoSite	Q9UHP3.
Polymorphism databases
DMDM	302393833.
Proteomic databases
PRIDE	Q9UHP3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000285681; ENSP00000285681; ENSG00000155313.
GeneID	29761.
KEGG	hsa:29761.
UCSC	uc002yjy.1. human. uc002yjz.1. human.
Organism-specific databases
CTD	29761.
GeneCards	GC21P017102.
HGNC	HGNC:12624. USP25.
HPA	HPA018297. HPA024142.
MIM	604736. gene.
neXtProt	NX_Q9UHP3.
PharmGKB	PA37249.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00390000016082.
HOGENOM	HBG358355.
HOVERGEN	HBG056030.
InParanoid	Q9UHP3.
OMA	KHQQTFL.
OrthoDB	EOG49S65J.
Gene expression databases
ArrayExpress	Q9UHP3.
Bgee	Q9UHP3.
CleanEx	HS_USP21. HS_USP25.
Genevestigator	Q9UHP3.
GermOnline	ENSG00000155313. Homo sapiens.
Family and domain databases
InterPro	IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. IPR009060. UBA-like. IPR003903. Ubiquitin-int_motif. [Graphical view]
KO	K11849.
Pfam	PF00443. UCH. 1 hit. PF02809. UIM. 2 hits. [Graphical view]
SMART	SM00726. UIM. 1 hit. [Graphical view]
SUPFAM	SSF46934. UBA_like. 1 hit.
PROSITE	PS00972. UCH_2_1. 1 hit. PS00973. UCH_2_2. 1 hit. PS50235. UCH_2_3. 1 hit. PS50330. UIM. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	52254.
SOURCE	Search...

Entry information

Entry name

UBP25_HUMAN

Accession

Primary (citable) accession number: Q9UHP3
Secondary accession number(s): C0LSZ0, Q6DHZ9, Q9H9W1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	August 10, 2010
Last modified:	January 25, 2012
This is version 115 of the entry and version 4 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.