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Q9UK80

- UBP21_HUMAN

UniProt

Q9UK80 - UBP21_HUMAN

Protein

Ubiquitin carboxyl-terminal hydrolase 21

Gene

USP21

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Deubiquitinates histone H2A, a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Deubiquitination of histone H2A releaves the repression of di- and trimethylation of histone H3 at 'Lys-4', resulting in regulation of transcriptional initiation. Regulates gene expression via histone H2A deubiquitination By similarity. Also capable of removing NEDD8 from NEDD8 conjugates but has no effect on Sentrin-1 conjugates.By similarity1 Publication

    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 sitei221 – 2211Nucleophile
    Metal bindingi384 – 3841Zinc
    Metal bindingi387 – 3871Zinc
    Metal bindingi437 – 4371Zinc
    Metal bindingi440 – 4401Zinc
    Active sitei518 – 5181Proton acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. cysteine-type peptidase activity Source: UniProtKB
    2. metal ion binding Source: UniProtKB-KW
    3. NEDD8-specific protease activity Source: UniProtKB
    4. transcription coactivator activity Source: UniProtKB
    5. ubiquitin-specific protease activity Source: UniProtKB
    6. ubiquitin thiolesterase activity Source: UniProtKB

    GO - Biological processi

    1. histone deubiquitination Source: UniProtKB
    2. positive regulation of transcription, DNA-templated Source: UniProtKB
    3. transcription, DNA-templated Source: UniProtKB-KW
    4. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Activator, Chromatin regulator, Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Transcription, Transcription regulation, Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi3.1.2.15. 2681.

    Protein family/group databases

    MEROPSiC19.034.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin carboxyl-terminal hydrolase 21 (EC:3.4.19.12)
    Alternative name(s):
    Deubiquitinating enzyme 21
    Ubiquitin thioesterase 21
    Ubiquitin-specific-processing protease 21
    Gene namesi
    Name:USP21
    Synonyms:USP23
    ORF Names:PP1490
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:12620. USP21.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. nucleus Source: HPA
    3. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi221 – 2211C → A: Abolishes ubiquitin thioesterase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA37246.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 565565Ubiquitin carboxyl-terminal hydrolase 21PRO_0000080648Add
    BLAST

    Proteomic databases

    PaxDbiQ9UK80.
    PRIDEiQ9UK80.

    PTM databases

    PhosphoSiteiQ9UK80.

    Miscellaneous databases

    PMAP-CutDBQ9UK80.

    Expressioni

    Tissue specificityi

    Highly expressed in heart, pancreas and skeletal muscle. Also expressed in brain, placenta, liver and kidney, and at very low level in lung.1 Publication

    Gene expression databases

    BgeeiQ9UK80.
    CleanExiHS_USP21.
    GenevestigatoriQ9UK80.

    Organism-specific databases

    HPAiHPA028397.

    Interactioni

    Protein-protein interaction databases

    BioGridi117950. 69 interactions.
    DIPiDIP-31255N.
    IntActiQ9UK80. 19 interactions.
    MINTiMINT-7970258.
    STRINGi9606.ENSP00000289865.

    Structurei

    Secondary structure

    1
    565
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi217 – 2193
    Helixi221 – 23111
    Helixi234 – 2429
    Helixi245 – 2484
    Helixi257 – 26812
    Helixi281 – 29010
    Helixi292 – 2943
    Helixi302 – 31716
    Helixi351 – 36515
    Helixi369 – 3746
    Beta strandi376 – 3849
    Turni385 – 3873
    Beta strandi390 – 40213
    Helixi416 – 4249
    Beta strandi427 – 4293
    Helixi431 – 4333
    Beta strandi438 – 4403
    Beta strandi446 – 4549
    Beta strandi457 – 4637
    Beta strandi466 – 4716
    Beta strandi473 – 4753
    Helixi490 – 4923
    Beta strandi501 – 51313
    Beta strandi516 – 52510
    Beta strandi528 – 5336
    Beta strandi536 – 5405
    Helixi542 – 5465
    Beta strandi551 – 5577

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2Y5BX-ray2.70A/E196-565[»]
    3I3TX-ray2.59A/C/E/G209-563[»]
    3MTNX-ray2.70A/C209-562[»]
    ProteinModelPortaliQ9UK80.
    SMRiQ9UK80. Positions 202-559.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UK80.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini212 – 558347USPAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi134 – 15219Nuclear export signalAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase C19 family. USP21 subfamily.Curated
    Contains 1 USP domain.Curated

    Phylogenomic databases

    eggNOGiCOG5533.
    HOVERGENiHBG011164.
    KOiK11833.
    OMAiNVQPRVG.
    OrthoDBiEOG7FR7GN.
    PhylomeDBiQ9UK80.
    TreeFamiTF106277.

    Family and domain databases

    InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR028889. UCH/PAN2.
    [Graphical view]
    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.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UK80-1) [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

    MPQASEHRLG RTREPPVNIQ PRVGSKLPFA PRARSKERRN PASGPNPMLR    50
    PLPPRPGLPD ERLKKLELGR GRTSGPRPRG PLRADHGVPL PGSPPPTVAL 100
    PLPSRTNLAR SKSVSSGDLR PMGIALGGHR GTGELGAALS RLALRPEPPT 150
    LRRSTSLRRL GGFPGPPTLF SIRTEPPASH GSFHMISARS SEPFYSDDKM 200
    AHHTLLLGSG HVGLRNLGNT CFLNAVLQCL SSTRPLRDFC LRRDFRQEVP 250
    GGGRAQELTE AFADVIGALW HPDSCEAVNP TRFRAVFQKY VPSFSGYSQQ 300
    DAQEFLKLLM ERLHLEINRR GRRAPPILAN GPVPSPPRRG GALLEEPELS 350
    DDDRANLMWK RYLEREDSKI VDLFVGQLKS CLKCQACGYR STTFEVFCDL 400
    SLPIPKKGFA GGKVSLRDCF NLFTKEEELE SENAPVCDRC RQKTRSTKKL 450
    TVQRFPRILV LHLNRFSASR GSIKKSSVGV DFPLQRLSLG DFASDKAGSP 500
    VYQLYALCNH SGSVHYGHYT ALCRCQTGWH VYNDSRVSPV SENQVASSEG 550
    YVLFYQLMQE PPRCL 565
    Length:565
    Mass (Da):62,656
    Last modified:May 1, 2000 - v1
    Checksum:i8A13ED34C03B2330
    GO
    Isoform 2 (identifier: Q9UK80-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         372-382: DLFVGQLKSCL → GMEWGKAMREN
         383-565: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:382
    Mass (Da):42,171
    Checksum:i750D5FE7DBA5F9BF
    GO
    Isoform 3 (identifier: Q9UK80-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         498-511: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:551
    Mass (Da):61,122
    Checksum:i9F04C052E111F030
    GO

    Sequence cautioni

    The sequence AAF61308.1 differs from that shown. Reason: Frameshift at positions 90 and 132.
    The sequence AAG17222.1 differs from that shown. Reason: Frameshift at positions 188, 214 and 228.
    The sequence BAD92136.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti42 – 421A → G in AAH90946. (PubMed:15489334)Curated
    Sequence conflicti272 – 2721P → L in AAF61308. (PubMed:10799498)Curated
    Sequence conflicti415 – 4151S → F in AAF61308. (PubMed:10799498)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti91 – 911P → S.
    Corresponds to variant rs34779722 [ dbSNP | Ensembl ].
    VAR_051531
    Natural varianti321 – 3211G → D.
    Corresponds to variant rs17356051 [ dbSNP | Ensembl ].
    VAR_051532
    Natural varianti336 – 3361P → T.
    Corresponds to variant rs1127525 [ dbSNP | Ensembl ].
    VAR_051533

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei372 – 38211DLFVGQLKSCL → GMEWGKAMREN in isoform 2. 1 PublicationVSP_036717Add
    BLAST
    Alternative sequencei383 – 565183Missing in isoform 2. 1 PublicationVSP_036718Add
    BLAST
    Alternative sequencei498 – 51114Missing in isoform 3. 1 PublicationVSP_036719Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF177758 mRNA. Translation: AAD54321.1.
    AF233442 mRNA. Translation: AAF61308.1. Frameshift.
    AK292319 mRNA. Translation: BAF85008.1.
    AF217979 mRNA. Translation: AAG17222.1. Frameshift.
    AB208899 mRNA. Translation: BAD92136.1. Different initiation.
    AL590714 Genomic DNA. Translation: CAH72142.1.
    AL590714 Genomic DNA. Translation: CAH72143.1.
    CH471121 Genomic DNA. Translation: EAW52644.1.
    BC003130 mRNA. Translation: AAH03130.2.
    BC090946 mRNA. Translation: AAH90946.1.
    BC136291 mRNA. Translation: AAI36292.1.
    CCDSiCCDS30920.1. [Q9UK80-1]
    RefSeqiNP_001014443.1. NM_001014443.2. [Q9UK80-1]
    NP_036607.3. NM_012475.4. [Q9UK80-1]
    UniGeneiHs.8015.

    Genome annotation databases

    EnsembliENST00000289865; ENSP00000289865; ENSG00000143258. [Q9UK80-1]
    ENST00000368001; ENSP00000356980; ENSG00000143258. [Q9UK80-3]
    ENST00000368002; ENSP00000356981; ENSG00000143258. [Q9UK80-1]
    GeneIDi27005.
    KEGGihsa:27005.
    UCSCiuc010pkc.2. human. [Q9UK80-1]

    Polymorphism databases

    DMDMi10720334.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF177758 mRNA. Translation: AAD54321.1 .
    AF233442 mRNA. Translation: AAF61308.1 . Frameshift.
    AK292319 mRNA. Translation: BAF85008.1 .
    AF217979 mRNA. Translation: AAG17222.1 . Frameshift.
    AB208899 mRNA. Translation: BAD92136.1 . Different initiation.
    AL590714 Genomic DNA. Translation: CAH72142.1 .
    AL590714 Genomic DNA. Translation: CAH72143.1 .
    CH471121 Genomic DNA. Translation: EAW52644.1 .
    BC003130 mRNA. Translation: AAH03130.2 .
    BC090946 mRNA. Translation: AAH90946.1 .
    BC136291 mRNA. Translation: AAI36292.1 .
    CCDSi CCDS30920.1. [Q9UK80-1 ]
    RefSeqi NP_001014443.1. NM_001014443.2. [Q9UK80-1 ]
    NP_036607.3. NM_012475.4. [Q9UK80-1 ]
    UniGenei Hs.8015.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2Y5B X-ray 2.70 A/E 196-565 [» ]
    3I3T X-ray 2.59 A/C/E/G 209-563 [» ]
    3MTN X-ray 2.70 A/C 209-562 [» ]
    ProteinModelPortali Q9UK80.
    SMRi Q9UK80. Positions 202-559.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117950. 69 interactions.
    DIPi DIP-31255N.
    IntActi Q9UK80. 19 interactions.
    MINTi MINT-7970258.
    STRINGi 9606.ENSP00000289865.

    Chemistry

    ChEMBLi CHEMBL2157852.

    Protein family/group databases

    MEROPSi C19.034.

    PTM databases

    PhosphoSitei Q9UK80.

    Polymorphism databases

    DMDMi 10720334.

    Proteomic databases

    PaxDbi Q9UK80.
    PRIDEi Q9UK80.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000289865 ; ENSP00000289865 ; ENSG00000143258 . [Q9UK80-1 ]
    ENST00000368001 ; ENSP00000356980 ; ENSG00000143258 . [Q9UK80-3 ]
    ENST00000368002 ; ENSP00000356981 ; ENSG00000143258 . [Q9UK80-1 ]
    GeneIDi 27005.
    KEGGi hsa:27005.
    UCSCi uc010pkc.2. human. [Q9UK80-1 ]

    Organism-specific databases

    CTDi 27005.
    GeneCardsi GC01P161129.
    HGNCi HGNC:12620. USP21.
    HPAi HPA028397.
    MIMi 604729. gene.
    neXtProti NX_Q9UK80.
    PharmGKBi PA37246.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5533.
    HOVERGENi HBG011164.
    KOi K11833.
    OMAi NVQPRVG.
    OrthoDBi EOG7FR7GN.
    PhylomeDBi Q9UK80.
    TreeFami TF106277.

    Enzyme and pathway databases

    BRENDAi 3.1.2.15. 2681.

    Miscellaneous databases

    EvolutionaryTracei Q9UK80.
    GenomeRNAii 27005.
    NextBioi 49506.
    PMAP-CutDB Q9UK80.
    PROi Q9UK80.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9UK80.
    CleanExi HS_USP21.
    Genevestigatori Q9UK80.

    Family and domain databases

    InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR028889. UCH/PAN2.
    [Graphical view ]
    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

    1. "Sequencing, tissue distribution and chromosomal assignment of a novel ubiquitin-specific protease USP23."
      Smith T.S., Southan C.
      Biochim. Biophys. Acta 1490:184-188(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Identification of a novel isopeptidase with dual specificity for ubiquitin- and NEDD8-conjugated proteins."
      Gong L., Kamitani T., Millas S., Yeh E.T.H.
      J. Biol. Chem. 275:14212-14216(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-221.
      Tissue: Placenta.
    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] (ISOFORM 1).
      Tissue: Testis.
    4. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
      Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
      , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
      Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    5. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    6. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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).
      Tissue: Kidney, Lung and Testis.
    9. "A global survey of CRM1-dependent nuclear export sequences in the human deubiquitinase family."
      Garcia-Santisteban I., Banuelos S., Rodriguez J.A.
      Biochem. J. 441:209-217(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, NUCLEAR EXPORT SIGNAL.
    10. "Polyubiquitin binding and cross-reactivity in the USP domain deubiquitinase USP21."
      Ye Y., Akutsu M., Reyes-Turcu F., Enchev R.I., Wilkinson K.D., Komander D.
      EMBO Rep. 12:350-357(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 1-75 IN COMPLEX WITH USP21.

    Entry informationi

    Entry nameiUBP21_HUMAN
    AccessioniPrimary (citable) accession number: Q9UK80
    Secondary accession number(s): Q59H60
    , Q5BKT5, Q5VTW9, Q5VTX0, Q9BTV1, Q9HBS2, Q9NYN4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 133 of the entry and version 1 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3