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Q9UK80

- UBP21_HUMAN

UniProt

Q9UK80 - UBP21_HUMAN

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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

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
Complete GO annotation...

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
Complete GO annotation...

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.
ExpressionAtlasiQ9UK80. baseline and differential.
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 – 2193Combined sources
Helixi221 – 23111Combined sources
Helixi234 – 2429Combined sources
Helixi245 – 2484Combined sources
Helixi257 – 26812Combined sources
Helixi281 – 29010Combined sources
Helixi292 – 2943Combined sources
Helixi302 – 31716Combined sources
Helixi351 – 36515Combined sources
Helixi369 – 3746Combined sources
Beta strandi376 – 3849Combined sources
Turni385 – 3873Combined sources
Beta strandi390 – 40213Combined sources
Helixi416 – 4249Combined sources
Beta strandi427 – 4293Combined sources
Helixi431 – 4333Combined sources
Beta strandi438 – 4403Combined sources
Beta strandi446 – 4549Combined sources
Beta strandi457 – 4637Combined sources
Beta strandi466 – 4716Combined sources
Beta strandi473 – 4753Combined sources
Helixi490 – 4923Combined sources
Beta strandi501 – 51313Combined sources
Beta strandi516 – 52510Combined sources
Beta strandi528 – 5336Combined sources
Beta strandi536 – 5405Combined sources
Helixi542 – 5465Combined sources
Beta strandi551 – 5577Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000119208.
HOVERGENiHBG011164.
InParanoidiQ9UK80.
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

        10         20         30         40         50
MPQASEHRLG RTREPPVNIQ PRVGSKLPFA PRARSKERRN PASGPNPMLR
60 70 80 90 100
PLPPRPGLPD ERLKKLELGR GRTSGPRPRG PLRADHGVPL PGSPPPTVAL
110 120 130 140 150
PLPSRTNLAR SKSVSSGDLR PMGIALGGHR GTGELGAALS RLALRPEPPT
160 170 180 190 200
LRRSTSLRRL GGFPGPPTLF SIRTEPPASH GSFHMISARS SEPFYSDDKM
210 220 230 240 250
AHHTLLLGSG HVGLRNLGNT CFLNAVLQCL SSTRPLRDFC LRRDFRQEVP
260 270 280 290 300
GGGRAQELTE AFADVIGALW HPDSCEAVNP TRFRAVFQKY VPSFSGYSQQ
310 320 330 340 350
DAQEFLKLLM ERLHLEINRR GRRAPPILAN GPVPSPPRRG GALLEEPELS
360 370 380 390 400
DDDRANLMWK RYLEREDSKI VDLFVGQLKS CLKCQACGYR STTFEVFCDL
410 420 430 440 450
SLPIPKKGFA GGKVSLRDCF NLFTKEEELE SENAPVCDRC RQKTRSTKKL
460 470 480 490 500
TVQRFPRILV LHLNRFSASR GSIKKSSVGV DFPLQRLSLG DFASDKAGSP
510 520 530 540 550
VYQLYALCNH SGSVHYGHYT ALCRCQTGWH VYNDSRVSPV SENQVASSEG
560
YVLFYQLMQE PPRCL
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. Curated
The sequence AAG17222.1 differs from that shown. Reason: Frameshift at positions 188, 214 and 228. Curated
The sequence BAD92136.1 differs from that shown. Reason: Erroneous initiation. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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

BindingDBi Q9UK80.
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.
GeneTreei ENSGT00760000119208.
HOVERGENi HBG011164.
InParanoidi Q9UK80.
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.
ExpressionAtlasi Q9UK80. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 135 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