P45974 (UBP5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	USP5
Synonyms:	ISOT

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	858 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. 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).
Cofactor	Binds 1 zinc ion.
Subunit structure	Interacts with TRIML1 By similarity.
Domain	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.
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.
Sequence similarities	Belongs to the peptidase C19 family. Contains 2 UBA domains. Contains 1 UBP-type zinc finger.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Coding sequence diversity	Alternative splicing
Domain	Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Protease Thiol protease
PTM	Disulfide bond Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of proteasomal ubiquitin-dependent protein catabolic process Inferred from mutant phenotype Ref.11. Source: UniProtKB protein K48-linked deubiquitination Inferred from mutant phenotype Ref.11. Source: UniProtKB ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	lysosome Traceable author statement PubMed 9827704. Source: ProtInc
Molecular_function	cysteine-type endopeptidase activity Traceable author statement PubMed 7578059. Source: ProtInc omega peptidase activity Inferred from electronic annotation. Source: InterPro ubiquitin thiolesterase activity Traceable author statement PubMed 7578059. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TADA3	O75528	2	EBI-741277,EBI-473249

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Long (identifier: P45974-1)

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 Short (identifier: P45974-2)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 858

858

Ubiquitin carboxyl-terminal hydrolase 5

PRO_0000080623

Regions

Domain

654 – 695

42

UBA 1

Domain

722 – 762

41

UBA 2

Zinc finger

197 – 269

73

UBP-type

Region

221 – 224

4

Substrate binding

Sites

Active site

335

1

Nucleophile

Active site

818

1

Proton acceptor By similarity

Metal binding

199

1

Zinc

Metal binding

202

1

Zinc

Metal binding

219

1

Zinc

Metal binding

232

1

Zinc

Binding site

209

1

Substrate

Binding site

259

1

Substrate

Binding site

261

1

Substrate; via carbonyl oxygen

Binding site

264

1

Substrate

Amino acid modifications

Modified residue

623

1

Phosphothreonine By similarity

Modified residue

783

1

Phosphoserine Ref.12 Ref.13

Disulfide bond

195 ↔ 816

Ref.18

Natural variations

Alternative sequence

629 – 652

24

GSLGF…SSPTS → A in isoform Short.

VSP_005259

Experimental info

Mutagenesis

199

1

C → A: Decreased rate of activity and decreased zinc binding. Ref.16

Mutagenesis

202

1

C → A: Decreased rate of activity. Ref.16

Mutagenesis

219

1

C → A: Decreased rate of activity. Ref.16

Mutagenesis

221 – 223

3

RRY → KWF: Loss of polyubiquitin binding and subsequent activation. Ref.9 Ref.15

Mutagenesis

221

1

R → A: Loss of polyubiquitin hydrolysis. Loss of ubiquitin binding; when associated with A-335. Ref.9

Mutagenesis

232

1

H → A: Decreased rate of activity. Ref.16

Mutagenesis

261

1

Y → F: Loss of polyubiquitin binding. Ref.15

Mutagenesis

335

1

C → 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. Ref.9

Mutagenesis

435

1

D → A: Loss of polyubiquitin binding and hydrolysis. Ref.9

Mutagenesis

666

1

M → 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. Ref.9

Mutagenesis

734

1

M → E: Lower affinity for diubiquitin, triubiquitin and tetraubiquitin; when associated with A-335. No effect on activity; when associated with E-666. Ref.9

Sequence conflict

3 – 4

2

EL → DV in CAA62690. Ref.1

Sequence conflict

45

1

I → V in CAA62690. Ref.1

Sequence conflict

468

1

K → R in AAA78934. Ref.4

Sequence conflict

681

1

G → D in AAA78934. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

858

Helix Strand Turn

Details...

Helix

5 – 11

7

Helix

12 – 15

4

Beta strand

31 – 34

4

Beta strand

43 – 46

4

Turn

47 – 49

3

Turn

55 – 57

3

Helix

58 – 65

8

Beta strand

69 – 75

7

Beta strand

118 – 124

7

Turn

125 – 128

4

Beta strand

129 – 131

3

Helix

141 – 154

14

Turn

178 – 182

5

Beta strand

200 – 203

4

Beta strand

206 – 211

6

Turn

212 – 214

3

Beta strand

217 – 219

3

Helix

232 – 240

9

Beta strand

244 – 247

4

Beta strand

258 – 260

3

Turn

261 – 264

4

Beta strand

265 – 268

4

Helix

272 – 277

6

Turn

278 – 280

3

Turn

283 – 285

3

Helix

335 – 344

10

Helix

348 – 354

7

Turn

355 – 357

3

Helix

358 – 364

7

Helix

369 – 371

3

Helix

373 – 385

13

Helix

415 – 421

7

Turn

422 – 424

3

Turn

426 – 429

4

Beta strand

430 – 432

3

Helix

436 – 449

14

Helix

457 – 460

4

Beta strand

463 – 471

9

Turn

472 – 475

4

Beta strand

476 – 489

14

Helix

493 – 495

3

Helix

499 – 514

16

Helix

529 – 537

9

Beta strand

540 – 547

8

Turn

548 – 551

4

Beta strand

552 – 564

13

Beta strand

567 – 573

7

Beta strand

576 – 578

3

Helix

580 – 582

3

Beta strand

584 – 586

3

Beta strand

595 – 598

4

Helix

600 – 602

3

Helix

658 – 666

9

Helix

670 – 679

10

Helix

685 – 695

11

Helix

700 – 702

3

Helix

725 – 732

8

Turn

733 – 735

3

Helix

738 – 747

10

Turn

748 – 750

3

Helix

752 – 770

19

Beta strand

799 – 812

14

Beta strand

818 – 825

8

Beta strand

828 – 833

6

Beta strand

836 – 839

4

Beta strand

849 – 855

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified October 1, 1996. Version 2. Checksum: E99CB7CDFA682C65	FASTA	858	95,786
	10 20 30 40 50 60 MAELSEEALL SVLPTIRVPK AGDRVHKDEC AFSFDTPESE GGLYICMNTF LGFGKQYVER 70 80 90 100 110 120 HFNKTGQRVY LHLRRTRRPK EEDPATGTGD PPRKKPTRLA IGVEGGFDLS EEKFELDEDV 130 140 150 160 170 180 KIVILPDYLE IARDGLGGLP DIVRDRVTSA VEALLSADSA SRKQEVQAWD GEVRQVSKHA 190 200 210 220 230 240 FSLKQLDNPA RIPPCGWKCS KCDMRENLWL NLTDGSILCG RRYFDGSGGN NHAVEHYRET 250 260 270 280 290 300 GYPLAVKLGT ITPDGADVYS YDEDDMVLDP SLAEHLSHFG IDMLKMQKTD KTMTELEIDM 310 320 330 340 350 360 NQRIGEWELI QESGVPLKPL FGPGYTGIRN LGNSCYLNSV VQVLFSIPDF QRKYVDKLEK 370 380 390 400 410 420 IFQNAPTDPT QDFSTQVAKL GHGLLSGEYS KPVPESGDGE RVPEQKEVQD GIAPRMFKAL 430 440 450 460 470 480 IGKGHPEFST NRQQDAQEFF LHLINMVERN CRSSENPNEV FRFLVEEKIK CLATEKVKYT 490 500 510 520 530 540 QRVDYIMQLP VPMDAALNKE ELLEYEEKKR QAEEEKMALP ELVRAQVPFS SCLEAYGAPE 550 560 570 580 590 600 QVDDFWSTAL QAKSVAVKTT RFASFPDYLV IQIKKFTFGL DWVPKKLDVS IEMPEELDIS 610 620 630 640 650 660 QLRGTGLQPG EEELPDIAPP LVTPDEPKGS LGFYGNEDED SFCSPHFSSP TSPMLDESVI 670 680 690 700 710 720 IQLVEMGFPM DACRKAVYYT GNSGAEAAMN WVMSHMDDPD FANPLILPGS SGPGSTSAAA 730 740 750 760 770 780 DPPPEDCVTT IVSMGFSRDQ ALKALRATNN SLERAVDWIF SHIDDLDAEA AMDISEGRSA 790 800 810 820 830 840 ADSISESVPV GPKVRDGPGK YQLFAFISHM GTSTMCGHYV CHIKKEGRWV IYNDQKVCAS 850 EKPPKDLGYI YFYQRVAS
	Isoform Short [UniParc]. Checksum: 227CB29B11C7DAEA	FASTA	835	93,308
	10 20 30 40 50 60 MAELSEEALL SVLPTIRVPK AGDRVHKDEC AFSFDTPESE GGLYICMNTF LGFGKQYVER 70 80 90 100 110 120 HFNKTGQRVY LHLRRTRRPK EEDPATGTGD PPRKKPTRLA IGVEGGFDLS EEKFELDEDV 130 140 150 160 170 180 KIVILPDYLE IARDGLGGLP DIVRDRVTSA VEALLSADSA SRKQEVQAWD GEVRQVSKHA 190 200 210 220 230 240 FSLKQLDNPA RIPPCGWKCS KCDMRENLWL NLTDGSILCG RRYFDGSGGN NHAVEHYRET 250 260 270 280 290 300 GYPLAVKLGT ITPDGADVYS YDEDDMVLDP SLAEHLSHFG IDMLKMQKTD KTMTELEIDM 310 320 330 340 350 360 NQRIGEWELI QESGVPLKPL FGPGYTGIRN LGNSCYLNSV VQVLFSIPDF QRKYVDKLEK 370 380 390 400 410 420 IFQNAPTDPT QDFSTQVAKL GHGLLSGEYS KPVPESGDGE RVPEQKEVQD GIAPRMFKAL 430 440 450 460 470 480 IGKGHPEFST NRQQDAQEFF LHLINMVERN CRSSENPNEV FRFLVEEKIK CLATEKVKYT 490 500 510 520 530 540 QRVDYIMQLP VPMDAALNKE ELLEYEEKKR QAEEEKMALP ELVRAQVPFS SCLEAYGAPE 550 560 570 580 590 600 QVDDFWSTAL QAKSVAVKTT RFASFPDYLV IQIKKFTFGL DWVPKKLDVS IEMPEELDIS 610 620 630 640 650 660 QLRGTGLQPG EEELPDIAPP LVTPDEPKAP MLDESVIIQL VEMGFPMDAC RKAVYYTGNS 670 680 690 700 710 720 GAEAAMNWVM SHMDDPDFAN PLILPGSSGP GSTSAAADPP PEDCVTTIVS MGFSRDQALK 730 740 750 760 770 780 ALRATNNSLE RAVDWIFSHI DDLDAEAAMD ISEGRSAADS ISESVPVGPK VRDGPGKYQL 790 800 810 820 830 FAFISHMGTS TMCGHYVCHI KKEGRWVIYN DQKVCASEKP PKDLGYIYFY QRVAS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	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].
[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]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[11]	"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.
[12]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[13]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]	"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.
[16]	"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.
[17]	"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.
[18]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00024664.
IPI00375145.

PIR

S68227.

RefSeq

NP_001092006.1. NM_001098536.1.
NP_003472.2. NM_003481.2.

UniGene

Hs.631661.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P45974.

ModBase

Search...

Protein-protein interaction databases

IntAct

P45974. 4 interactions.

MINT

MINT-5001006.

STRING

9606.ENSP00000229268.

Protein family/group databases

MEROPS

C19.001.

PTM databases

PhosphoSite

P45974.

Polymorphism databases

DMDM

1717869.

2D gel databases

REPRODUCTION-2DPAGE

IPI00375145.

Proteomic databases

PaxDb

P45974.

PRIDE

P45974.

Protocols and materials databases

DNASU

8078.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000229268; ENSP00000229268; ENSG00000111667.
ENST00000389231; ENSP00000373883; ENSG00000111667.
ENST00000595281; ENSP00000472079; ENSG00000268462.
ENST00000597018; ENSP00000470388; ENSG00000268462.

GeneID

8078.

KEGG

hsa:8078.

UCSC

uc001qrh.4. human.
uc001qri.4. human.

Organism-specific databases

CTD

8078.

GeneCards

GC12P007024.

HGNC

HGNC:12628. USP5.

HPA

HPA006756.

MIM

601447. gene.

neXtProt

NX_P45974.

PharmGKB

PA37253.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5207.

HOGENOM

HOG000162311.

HOVERGEN

HBG002833.

InParanoid

P45974.

KO

K11836.

OMA

DDMVEDP.

OrthoDB

EOG4229J2.

PhylomeDB

P45974.

Gene expression databases

ArrayExpress

P45974.

Bgee

P45974.

CleanEx

HS_USP5.

Genevestigator

P45974.

GermOnline

ENSG00000111667. Homo sapiens.

Family and domain databases

Gene3D

3.30.40.10. 1 hit.

InterPro

IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19.
IPR009060. UBA-like.
IPR000449. UBA/transl_elong_EF1B_N.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR016652. Ubiquitinyl_hydrolase.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view]

Pfam

PF00627. UBA. 2 hits.
PF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]

PIRSF

PIRSF016308. UBP. 1 hit.

SMART

SM00165. UBA. 2 hits.
SM00290. ZnF_UBP. 1 hit.
[Graphical view]

SUPFAM

SSF46934. UBA_like. 1 hit.

PROSITE

PS50030. UBA. 2 hits.
PS00972. UCH_2_1. 1 hit.
PS00973. UCH_2_2. 1 hit.
PS50235. UCH_2_3. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL6158.

ChiTaRS

USP5. human.

EvolutionaryTrace

P45974.

GenomeRNAi

8078.

NextBio

30687.

PMAP-CutDB

P45974.

SOURCE

Search...

Entry information

Entry name

UBP5_HUMAN

Accession

Primary (citable) accession number: P45974
Secondary accession number(s): D3DUS7, D3DUS8, Q96J22

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 138 of the entry and version 2 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.