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P45974

- UBP5_HUMAN

UniProt

P45974 - UBP5_HUMAN

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Protein

Ubiquitin carboxyl-terminal hydrolase 5

Gene

USP5

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

Functioni

Cleaves linear and branched multiubiquitin polymers with a marked preference for branched polymers. Involved in unanchored 'Lys-48'-linked polyubiquitin disassembly. Binds linear and 'Lys-63'-linked polyubiquitin with a lower affinity. Knock-down of USP5 causes the accumulation of p53/TP53 and an increase in p53/TP53 transcriptional activity because the unanchored polyubiquitin that accumulates is able to compete with ubiquitinated p53/TP53 but not with MDM2 for proteasomal recognition.1 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).

Cofactori

Zn2+Note: Binds 1 zinc ion.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi199 – 1991Zinc
Metal bindingi202 – 2021Zinc
Binding sitei209 – 2091Substrate
Metal bindingi219 – 2191Zinc
Metal bindingi232 – 2321Zinc
Binding sitei259 – 2591Substrate
Binding sitei261 – 2611Substrate; via carbonyl oxygen
Binding sitei264 – 2641Substrate
Active sitei335 – 3351Nucleophile
Active sitei818 – 8181Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri197 – 26973UBP-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: ProtInc
  2. omega peptidase activity Source: InterPro
  3. ubiquitin thiolesterase activity Source: ProtInc
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  2. protein K48-linked deubiquitination Source: UniProtKB
  3. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiC19.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin carboxyl-terminal hydrolase 5 (EC:3.4.19.12)
Alternative name(s):
Deubiquitinating enzyme 5
Isopeptidase T
Ubiquitin thioesterase 5
Ubiquitin-specific-processing protease 5
Gene namesi
Name:USP5
Synonyms:ISOT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:12628. USP5.

Subcellular locationi

GO - Cellular componenti

  1. lysosome Source: ProtInc
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi199 – 1991C → A: Decreased rate of activity and decreased zinc binding. 1 Publication
Mutagenesisi202 – 2021C → A: Decreased rate of activity. 1 Publication
Mutagenesisi219 – 2191C → A: Decreased rate of activity. 1 Publication
Mutagenesisi221 – 2233RRY → KWF: Loss of polyubiquitin binding and subsequent activation. 1 Publication
Mutagenesisi221 – 2211R → A: Loss of polyubiquitin hydrolysis. Loss of ubiquitin binding; when associated with A-335. 1 Publication
Mutagenesisi232 – 2321H → A: Decreased rate of activity. 1 Publication
Mutagenesisi261 – 2611Y → F: Loss of polyubiquitin binding. 1 Publication
Mutagenesisi335 – 3351C → A: Loss of activity. Loss of ubiquitin binding; when associated with A-221. Lower affinity for triubiquitin and tetraubiquitin, but no effect on affinity for diubiquitin; when associated with E-666. Lower affinity for diubiquitin, triubiquitin and tetraubiquitin; when associated with E-734. 1 Publication
Mutagenesisi435 – 4351D → A: Loss of polyubiquitin binding and hydrolysis. 1 Publication
Mutagenesisi666 – 6661M → E: Lower affinity for triubiquitin and tetraubiquitin, but no effect on affinity for diubiquitin; when associated with A-335. No effect on activity; when associated with E-734. 1 Publication
Mutagenesisi734 – 7341M → E: Lower affinity for diubiquitin, triubiquitin and tetraubiquitin; when associated with A-335. No effect on activity; when associated with E-666. 1 Publication

Organism-specific databases

PharmGKBiPA37253.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 858857Ubiquitin carboxyl-terminal hydrolase 5PRO_0000080623Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Disulfide bondi195 ↔ 8161 Publication
Modified residuei623 – 6231PhosphothreonineBy similarity
Modified residuei783 – 7831Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiP45974.
PaxDbiP45974.
PRIDEiP45974.

2D gel databases

REPRODUCTION-2DPAGEIPI00375145.

PTM databases

PhosphoSiteiP45974.

Miscellaneous databases

PMAP-CutDBP45974.

Expressioni

Gene expression databases

BgeeiP45974.
CleanExiHS_USP5.
ExpressionAtlasiP45974. baseline and differential.
GenevestigatoriP45974.

Organism-specific databases

HPAiHPA006756.

Interactioni

Subunit structurei

Interacts with TRIML1.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
RAD23BP547272EBI-741277,EBI-954531
TADA3O755282EBI-741277,EBI-473249

Protein-protein interaction databases

BioGridi113751. 61 interactions.
DIPiDIP-34459N.
IntActiP45974. 6 interactions.
MINTiMINT-5001006.
STRINGi9606.ENSP00000229268.

Structurei

Secondary structure

1
858
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 117Combined sources
Helixi12 – 154Combined sources
Beta strandi31 – 344Combined sources
Beta strandi43 – 464Combined sources
Turni47 – 493Combined sources
Turni55 – 573Combined sources
Helixi58 – 658Combined sources
Beta strandi69 – 757Combined sources
Beta strandi118 – 1247Combined sources
Turni125 – 1284Combined sources
Beta strandi129 – 1313Combined sources
Helixi141 – 15414Combined sources
Turni178 – 1825Combined sources
Beta strandi200 – 2034Combined sources
Beta strandi206 – 2116Combined sources
Turni212 – 2143Combined sources
Beta strandi217 – 2193Combined sources
Helixi232 – 2409Combined sources
Beta strandi244 – 2474Combined sources
Beta strandi258 – 2603Combined sources
Turni261 – 2644Combined sources
Beta strandi265 – 2684Combined sources
Helixi272 – 2776Combined sources
Turni278 – 2803Combined sources
Turni283 – 2853Combined sources
Helixi335 – 34410Combined sources
Helixi348 – 3547Combined sources
Turni355 – 3573Combined sources
Helixi358 – 3647Combined sources
Helixi369 – 3713Combined sources
Helixi373 – 38513Combined sources
Helixi415 – 4217Combined sources
Turni422 – 4243Combined sources
Turni426 – 4294Combined sources
Beta strandi430 – 4323Combined sources
Helixi436 – 44914Combined sources
Helixi457 – 4604Combined sources
Beta strandi463 – 4719Combined sources
Turni472 – 4754Combined sources
Beta strandi476 – 48914Combined sources
Helixi493 – 4953Combined sources
Helixi499 – 51416Combined sources
Helixi529 – 5379Combined sources
Beta strandi540 – 5478Combined sources
Turni548 – 5514Combined sources
Beta strandi552 – 56413Combined sources
Beta strandi567 – 5737Combined sources
Beta strandi576 – 5783Combined sources
Helixi580 – 5823Combined sources
Beta strandi584 – 5863Combined sources
Beta strandi595 – 5984Combined sources
Helixi600 – 6023Combined sources
Helixi658 – 6669Combined sources
Helixi670 – 67910Combined sources
Helixi685 – 69511Combined sources
Helixi700 – 7023Combined sources
Helixi725 – 7328Combined sources
Turni733 – 7353Combined sources
Helixi738 – 74710Combined sources
Turni748 – 7503Combined sources
Helixi752 – 77019Combined sources
Beta strandi799 – 81214Combined sources
Beta strandi818 – 8258Combined sources
Beta strandi828 – 8336Combined sources
Beta strandi836 – 8394Combined sources
Beta strandi849 – 8557Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DAGNMR-A655-715[»]
2DAKNMR-A723-772[»]
2G43X-ray2.09A/B163-291[»]
2G45X-ray1.99A/D163-291[»]
3IHPX-ray2.80A/B1-858[»]
ProteinModelPortaliP45974.
SMRiP45974. Positions 1-858.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP45974.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini326 – 856531USPAdd
BLAST
Domaini654 – 69542UBA 1PROSITE-ProRule annotationAdd
BLAST
Domaini722 – 76241UBA 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni221 – 2244Substrate binding

Domaini

The UBP-type zinc finger domain interacts selectively with an unmodified C-terminus of the proximal ubiquitin. Both UBA domains are involved in polyubiquitin recognition.

Sequence similaritiesi

Belongs to the peptidase C19 family.Curated
Contains 2 UBA domains.PROSITE-ProRule annotation
Contains 1 UBP-type zinc finger.PROSITE-ProRule annotation
Contains 1 USP domain.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri197 – 26973UBP-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5207.
GeneTreeiENSGT00390000000874.
HOGENOMiHOG000162311.
HOVERGENiHBG002833.
InParanoidiP45974.
KOiK11836.
OMAiDDMVEDP.
PhylomeDBiP45974.
TreeFamiTF300576.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000449. UBA/Ts_N.
IPR016652. Ubiquitinyl_hydrolase.
IPR028889. UCH/PAN2.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view]
PfamiPF00627. UBA. 2 hits.
PF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]
PIRSFiPIRSF016308. UBP. 1 hit.
SMARTiSM00165. UBA. 2 hits.
SM00290. ZnF_UBP. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
PROSITEiPS50030. UBA. 2 hits.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform Long (identifier: P45974-1) [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
MAELSEEALL SVLPTIRVPK AGDRVHKDEC AFSFDTPESE GGLYICMNTF
60 70 80 90 100
LGFGKQYVER HFNKTGQRVY LHLRRTRRPK EEDPATGTGD PPRKKPTRLA
110 120 130 140 150
IGVEGGFDLS EEKFELDEDV KIVILPDYLE IARDGLGGLP DIVRDRVTSA
160 170 180 190 200
VEALLSADSA SRKQEVQAWD GEVRQVSKHA FSLKQLDNPA RIPPCGWKCS
210 220 230 240 250
KCDMRENLWL NLTDGSILCG RRYFDGSGGN NHAVEHYRET GYPLAVKLGT
260 270 280 290 300
ITPDGADVYS YDEDDMVLDP SLAEHLSHFG IDMLKMQKTD KTMTELEIDM
310 320 330 340 350
NQRIGEWELI QESGVPLKPL FGPGYTGIRN LGNSCYLNSV VQVLFSIPDF
360 370 380 390 400
QRKYVDKLEK IFQNAPTDPT QDFSTQVAKL GHGLLSGEYS KPVPESGDGE
410 420 430 440 450
RVPEQKEVQD GIAPRMFKAL IGKGHPEFST NRQQDAQEFF LHLINMVERN
460 470 480 490 500
CRSSENPNEV FRFLVEEKIK CLATEKVKYT QRVDYIMQLP VPMDAALNKE
510 520 530 540 550
ELLEYEEKKR QAEEEKMALP ELVRAQVPFS SCLEAYGAPE QVDDFWSTAL
560 570 580 590 600
QAKSVAVKTT RFASFPDYLV IQIKKFTFGL DWVPKKLDVS IEMPEELDIS
610 620 630 640 650
QLRGTGLQPG EEELPDIAPP LVTPDEPKGS LGFYGNEDED SFCSPHFSSP
660 670 680 690 700
TSPMLDESVI IQLVEMGFPM DACRKAVYYT GNSGAEAAMN WVMSHMDDPD
710 720 730 740 750
FANPLILPGS SGPGSTSAAA DPPPEDCVTT IVSMGFSRDQ ALKALRATNN
760 770 780 790 800
SLERAVDWIF SHIDDLDAEA AMDISEGRSA ADSISESVPV GPKVRDGPGK
810 820 830 840 850
YQLFAFISHM GTSTMCGHYV CHIKKEGRWV IYNDQKVCAS EKPPKDLGYI

YFYQRVAS
Length:858
Mass (Da):95,786
Last modified:October 1, 1996 - v2
Checksum:iE99CB7CDFA682C65
GO
Isoform Short (identifier: P45974-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     629-652: GSLGFYGNEDEDSFCSPHFSSPTS → A

Show »
Length:835
Mass (Da):93,308
Checksum:i227CB29B11C7DAEA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 42EL → DV in CAA62690. (PubMed:7498549)Curated
Sequence conflicti45 – 451I → V in CAA62690. (PubMed:7498549)Curated
Sequence conflicti468 – 4681K → R in AAA78934. 1 PublicationCurated
Sequence conflicti681 – 6811G → D in AAA78934. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei629 – 65224GSLGF…SSPTS → A in isoform Short. 1 PublicationVSP_005259Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91349 mRNA. Translation: CAA62690.1.
U47927 mRNA. Translation: AAC50465.1.
U47924 Genomic DNA. Translation: AAB51314.1.
U47924 Genomic DNA. Translation: AAB51315.1.
U35116 mRNA. Translation: AAA78934.1.
CH471116 Genomic DNA. Translation: EAW88724.1.
CH471116 Genomic DNA. Translation: EAW88725.1.
CH471116 Genomic DNA. Translation: EAW88726.1.
CH471116 Genomic DNA. Translation: EAW88727.1.
BC004889 mRNA. Translation: AAH04889.1.
BC005139 mRNA. Translation: AAH05139.1.
CCDSiCCDS31733.1. [P45974-2]
CCDS41743.1. [P45974-1]
PIRiS68227.
RefSeqiNP_001092006.1. NM_001098536.1. [P45974-1]
NP_003472.2. NM_003481.2. [P45974-2]
UniGeneiHs.631661.

Genome annotation databases

EnsembliENST00000229268; ENSP00000229268; ENSG00000111667. [P45974-1]
ENST00000389231; ENSP00000373883; ENSG00000111667. [P45974-2]
GeneIDi8078.
KEGGihsa:8078.
UCSCiuc001qrh.4. human. [P45974-2]
uc001qri.4. human. [P45974-1]

Polymorphism databases

DMDMi1717869.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91349 mRNA. Translation: CAA62690.1 .
U47927 mRNA. Translation: AAC50465.1 .
U47924 Genomic DNA. Translation: AAB51314.1 .
U47924 Genomic DNA. Translation: AAB51315.1 .
U35116 mRNA. Translation: AAA78934.1 .
CH471116 Genomic DNA. Translation: EAW88724.1 .
CH471116 Genomic DNA. Translation: EAW88725.1 .
CH471116 Genomic DNA. Translation: EAW88726.1 .
CH471116 Genomic DNA. Translation: EAW88727.1 .
BC004889 mRNA. Translation: AAH04889.1 .
BC005139 mRNA. Translation: AAH05139.1 .
CCDSi CCDS31733.1. [P45974-2 ]
CCDS41743.1. [P45974-1 ]
PIRi S68227.
RefSeqi NP_001092006.1. NM_001098536.1. [P45974-1 ]
NP_003472.2. NM_003481.2. [P45974-2 ]
UniGenei Hs.631661.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DAG NMR - A 655-715 [» ]
2DAK NMR - A 723-772 [» ]
2G43 X-ray 2.09 A/B 163-291 [» ]
2G45 X-ray 1.99 A/D 163-291 [» ]
3IHP X-ray 2.80 A/B 1-858 [» ]
ProteinModelPortali P45974.
SMRi P45974. Positions 1-858.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113751. 61 interactions.
DIPi DIP-34459N.
IntActi P45974. 6 interactions.
MINTi MINT-5001006.
STRINGi 9606.ENSP00000229268.

Chemistry

BindingDBi P45974.
ChEMBLi CHEMBL6158.

Protein family/group databases

MEROPSi C19.001.

PTM databases

PhosphoSitei P45974.

Polymorphism databases

DMDMi 1717869.

2D gel databases

REPRODUCTION-2DPAGE IPI00375145.

Proteomic databases

MaxQBi P45974.
PaxDbi P45974.
PRIDEi P45974.

Protocols and materials databases

DNASUi 8078.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000229268 ; ENSP00000229268 ; ENSG00000111667 . [P45974-1 ]
ENST00000389231 ; ENSP00000373883 ; ENSG00000111667 . [P45974-2 ]
GeneIDi 8078.
KEGGi hsa:8078.
UCSCi uc001qrh.4. human. [P45974-2 ]
uc001qri.4. human. [P45974-1 ]

Organism-specific databases

CTDi 8078.
GeneCardsi GC12P007137.
HGNCi HGNC:12628. USP5.
HPAi HPA006756.
MIMi 601447. gene.
neXtProti NX_P45974.
PharmGKBi PA37253.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5207.
GeneTreei ENSGT00390000000874.
HOGENOMi HOG000162311.
HOVERGENi HBG002833.
InParanoidi P45974.
KOi K11836.
OMAi DDMVEDP.
PhylomeDBi P45974.
TreeFami TF300576.

Miscellaneous databases

ChiTaRSi USP5. human.
EvolutionaryTracei P45974.
GeneWikii USP5.
GenomeRNAii 8078.
NextBioi 30687.
PMAP-CutDB P45974.
PROi P45974.
SOURCEi Search...

Gene expression databases

Bgeei P45974.
CleanExi HS_USP5.
ExpressionAtlasi P45974. baseline and differential.
Genevestigatori P45974.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000449. UBA/Ts_N.
IPR016652. Ubiquitinyl_hydrolase.
IPR028889. UCH/PAN2.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view ]
Pfami PF00627. UBA. 2 hits.
PF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view ]
PIRSFi PIRSF016308. UBP. 1 hit.
SMARTi SM00165. UBA. 2 hits.
SM00290. ZnF_UBP. 1 hit.
[Graphical view ]
SUPFAMi SSF46934. SSF46934. 1 hit.
PROSITEi PS50030. UBA. 2 hits.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning of a human 100 kDa de-ubiquitinating enzyme: the 100 kDa human de-ubiquitinase belongs to the ubiquitin C-terminal hydrolase family 2 (UCH2)."
    Falquet L., Paquet N., Frutiger S., Hughes G.J., Hoang-Van K., Jaton J.-C.
    FEBS Lett. 376:233-237(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
  2. "A gene-rich cluster between the CD4 and triosephosphate isomerase genes at human chromosome 12p13."
    Ansari-Lari M.A., Muzny D.M., Lu J., Lu F., Lilley C.E., Spanos S., Malley T., Gibbs R.A.
    Genome Res. 6:314-326(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  3. "Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination."
    Ansari-Lari M.A., Shen Y., Muzny D.M., Lee W., Gibbs R.A.
    Genome Res. 7:268-280(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. Tashayev V.L., O'Connor L.B., Larsen C.N., Kasperek E., Pickart C.M.
    Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. 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] (ISOFORMS LONG AND SHORT).
    Tissue: Kidney and Lung.
  7. "A human de-ubiquitinating enzyme with both isopeptidase and peptidase activities in vitro."
    Falquet L., Paquet N., Frutiger S., Hughes G.J., Hoang-Van K., Jaton J.-C.
    FEBS Lett. 359:73-77(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Recognition of polyubiquitin isoforms by the multiple ubiquitin binding modules of isopeptidase T."
    Reyes-Turcu F.E., Shanks J.R., Komander D., Wilkinson K.D.
    J. Biol. Chem. 283:19581-19592(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ARG-221; CYS-335; ASP-435; MET-666 AND MET-734, POLYUBIQUITIN BINDING.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  12. "Suppression of the deubiquitinating enzyme USP5 causes the accumulation of unanchored polyubiquitin and the activation of p53."
    Dayal S., Sparks A., Jacob J., Allende-Vega N., Lane D.P., Saville M.K.
    J. Biol. Chem. 284:5030-5041(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "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-783, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Domain analysis reveals that a deubiquitinating enzyme USP13 performs non-activating catalysis for Lys63-linked polyubiquitin."
    Zhang Y.H., Zhou C.J., Zhou Z.R., Song A.X., Hu H.Y.
    PLoS ONE 6:E29362-E29362(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF 221-ARG--TYR-223 AND TYR-261.
  17. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "The ubiquitin binding domain ZnF UBP recognizes the C-terminal diglycine motif of unanchored ubiquitin."
    Reyes-Turcu F.E., Horton J.R., Mullally J.E., Heroux A., Cheng X., Wilkinson K.D.
    Cell 124:1197-1208(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 163-291 IN COMPLEX WITH UBIQUITIN, ZINC-BINDING, MUTAGENESIS OF CYS-199; CYS-202; CYS-219 AND HIS-232.
  20. "Solution structure of the first and second UBA domains in the human ubiquitin specific protease 5 (isopeptidase 5)."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JUN-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 655-772.
  21. "Covalent ubiquitin-USP5 complex."
    Walker J.R., Avvakumov G.V., Xue S., Butler-Cole C., Weigelt J., Bountra C., Arrowsmith C.H., Edwards A.M., Bochkarev A., Dhe-Paganon S.
    Submitted (DEC-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-858 IN COMPLEX WITH UBIQUITIN, DISULFIDE BOND, ZINC-BINDING.

Entry informationi

Entry nameiUBP5_HUMAN
AccessioniPrimary (citable) accession number: P45974
Secondary accession number(s): D3DUS7, D3DUS8, Q96J22
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: October 1, 1996
Last modified: November 26, 2014
This is version 152 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

Miscellaneous

The UBP-type zinc finger domain crystallizes as a dimer linked by a disulfide bond between the Cys-195 residues of both molecules, but there is no evidence that the full-length USP5 exists as a dimer.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families

External Data

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