Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ubiquitin carboxyl-terminal hydrolase 4

Gene

USP4

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

Functioni

Hydrolase that deubiquitinates target proteins such as the receptor ADORA2A, PDPK1 and TRIM21. Deubiquitination of ADORA2A increases the amount of functional receptor at the cell surface. May regulate mRNA splicing through deubiquitination of the U4 spliceosomal protein PRPF3. This may prevent its recognition by the U5 component PRPF8 thereby destabilizing interactions within the U4/U6.U5 snRNP. May also play a role in the regulation of quality control in the ER.5 Publications

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 sitei311 – 3111Nucleophile
Metal bindingi461 – 4611Zinc
Metal bindingi464 – 4641Zinc
Metal bindingi799 – 7991Zinc
Metal bindingi802 – 8021Zinc
Active sitei881 – 8811Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

  1. adenosine receptor binding Source: UniProtKB
  2. cysteine-type endopeptidase activity Source: GO_Central
  3. identical protein binding Source: IntAct
  4. metal ion binding Source: UniProtKB-KW
  5. ubiquitin-specific protease activity Source: UniProtKB
  6. ubiquitin thiolesterase activity Source: UniProtKB

GO - Biological processi

  1. negative regulation of protein ubiquitination Source: UniProtKB
  2. proteasome-mediated ubiquitin-dependent protein catabolic process Source: GO_Central
  3. protein deubiquitination Source: UniProtKB
  4. protein localization to cell surface Source: UniProtKB
  5. regulation of proteasomal protein catabolic process Source: GO_Central
  6. regulation of protein stability Source: UniProtKB
  7. spliceosomal tri-snRNP complex assembly Source: UniProtKB
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

MEROPSiC19.010.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin carboxyl-terminal hydrolase 4 (EC:3.4.19.12)
Alternative name(s):
Deubiquitinating enzyme 4
Ubiquitin thioesterase 4
Ubiquitin-specific-processing protease 4
Ubiquitous nuclear protein homolog
Gene namesi
Name:USP4
Synonyms:UNP, UNPH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:12627. USP4.

Subcellular locationi

Cytoplasm 2 Publications. Nucleus 2 Publications
Note: Shuttles between the nucleus and cytoplasm. Exported to the cytoplasm in a CRM1-dependent manner and recycled back to the nucleus via the importin alpha/beta heterodimeric import receptor. The relative amounts found in the nucleus and cytoplasm vary according to the cell type.2 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. lysosome Source: ProtInc
  3. nucleus Source: UniProtKB
  4. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi311 – 3111C → A: Loss of activity. Its ubiquitination by TRIM21 is enhanced. 2 Publications
Mutagenesisi459 – 4635LVCPE → AVRPH: Reduces the interaction with RB1. 1 Publication
Mutagenesisi463 – 4631E → Q: Reduces the interaction with RB1. 1 Publication

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA37252.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 963963Ubiquitin carboxyl-terminal hydrolase 4PRO_0000080621Add
BLAST

Post-translational modificationi

Monoubiquitinated by TRIM21. Ubiquitination does not lead to its proteasomal degradation. Autodeubiquitinated.2 Publications

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiQ13107.
PaxDbiQ13107.
PRIDEiQ13107.

PTM databases

PhosphoSiteiQ13107.

Expressioni

Tissue specificityi

Overexpressed in small cell tumors and adenocarcinomas of the lung compared to wild-type lung (at protein level). Expressed in the hippocampal neurons.2 Publications

Gene expression databases

BgeeiQ13107.
CleanExiHS_USP4.
ExpressionAtlasiQ13107. baseline and differential.
GenevestigatoriQ13107.

Organism-specific databases

HPAiHPA018499.

Interactioni

Subunit structurei

Interacts with RB1 (both dephosphorylated and hypophosphorylated forms). Interacts with RBL1 and RBL2. Interacts with ADORA2A (via cytoplasmic C-terminus); the interaction is direct. Interacts with SART3; recruits USP4 to its substrate PRPF3.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-723290,EBI-723290
ADORA2AP292744EBI-723290,EBI-2902702
HUWE1Q7Z6Z74EBI-723290,EBI-625934
RIPK1Q135464EBI-723290,EBI-358507
TRIM21P194743EBI-723305,EBI-81290

Protein-protein interaction databases

BioGridi113221. 79 interactions.
IntActiQ13107. 32 interactions.
MINTiMINT-3027027.
STRINGi9606.ENSP00000265560.

Structurei

Secondary structure

1
963
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi311 – 32111Combined sources
Helixi324 – 3318Combined sources
Helixi335 – 3384Combined sources
Helixi350 – 36213Combined sources
Beta strandi364 – 3663Combined sources
Beta strandi368 – 3703Combined sources
Helixi373 – 38210Combined sources
Helixi384 – 3863Combined sources
Beta strandi388 – 3903Combined sources
Helixi394 – 40815Combined sources
Helixi428 – 44215Combined sources
Helixi446 – 4516Combined sources
Beta strandi453 – 4608Combined sources
Turni462 – 4643Combined sources
Beta strandi467 – 48014Combined sources
Helixi778 – 7858Combined sources
Beta strandi797 – 7993Combined sources
Turni800 – 8034Combined sources
Beta strandi804 – 8063Combined sources
Beta strandi809 – 8168Combined sources
Beta strandi819 – 8268Combined sources
Beta strandi828 – 8303Combined sources
Beta strandi835 – 8373Combined sources
Helixi852 – 8543Combined sources
Beta strandi858 – 8603Combined sources
Beta strandi864 – 87411Combined sources
Beta strandi876 – 8794Combined sources
Beta strandi881 – 8877Combined sources
Turni889 – 8913Combined sources
Beta strandi894 – 8985Combined sources
Beta strandi901 – 9044Combined sources
Helixi907 – 9093Combined sources
Beta strandi915 – 9228Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Y6EX-ray2.40A/B/C/D/E/F296-490[»]
A/B/C/D/E/F765-932[»]
ProteinModelPortaliQ13107.
SMRiQ13107. Positions 8-226, 297-483, 740-930.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13107.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 122112DUSPPROSITE-ProRule annotationAdd
BLAST
Domaini142 – 22685Ubiquitin-like 1Add
BLAST
Domaini302 – 923622USPAdd
BLAST
Domaini483 – 57189Ubiquitin-like 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni27 – 216190Necessary for interaction with SART31 PublicationAdd
BLAST
Regioni405 – 4073Necessary for interaction with RBL2By similarity
Regioni459 – 4635Necessary for interaction with RB1 and RBL2By similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi133 – 1419Nuclear export signalBy similarity
Motifi767 – 7726Nuclear localization signalBy similarity

Domaini

The Ubiquitin-like domain 2 inserts into the catalytic domain and competes with the ubiquitin substrate, partially inhibiting DUB activity.1 Publication

Sequence similaritiesi

Belongs to the peptidase C19 family. USP4 subfamily.Curated
Contains 1 DUSP domain.PROSITE-ProRule annotation
Contains 2 ubiquitin-like domains.Curated
Contains 1 USP domain.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5560.
GeneTreeiENSGT00670000097750.
HOGENOMiHOG000264375.
HOVERGENiHBG000864.
InParanoidiQ13107.
KOiK11835.
OMAiHCRPTQY.
PhylomeDBiQ13107.
TreeFamiTF106276.

Family and domain databases

Gene3Di3.30.2230.10. 1 hit.
InterProiIPR006615. Pept_C19_DUSP.
IPR001394. Peptidase_C19_UCH.
IPR028135. Ub_USP-typ.
IPR028134. USP.
IPR018200. USP_CS.
IPR028889. USP_dom.
[Graphical view]
PANTHERiPTHR24006:SF360. PTHR24006:SF360. 1 hit.
PfamiPF06337. DUSP. 1 hit.
PF14836. Ubiquitin_3. 1 hit.
PF00443. UCH. 1 hit.
[Graphical view]
SMARTiSM00695. DUSP. 1 hit.
[Graphical view]
SUPFAMiSSF143791. SSF143791. 1 hit.
PROSITEiPS51283. DUSP. 1 hit.
PS00972. 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: Q13107-1) [UniParc]FASTAAdd to Basket

Also known as: UnpEL

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
MAEGGGCRER PDAETQKSEL GPLMRTTLQR GAQWYLIDSR WFKQWKKYVG
60 70 80 90 100
FDSWDMYNVG EHNLFPGPID NSGLFSDPES QTLKEHLIDE LDYVLVPTEA
110 120 130 140 150
WNKLLNWYGC VEGQQPIVRK VVEHGLFVKH CKVEVYLLEL KLCENSDPTN
160 170 180 190 200
VLSCHFSKAD TIATIEKEMR KLFNIPAERE TRLWNKYMSN TYEQLSKLDN
210 220 230 240 250
TVQDAGLYQG QVLVIEPQNE DGTWPRQTLQ SKSSTAPSRN FTTSPKSSAS
260 270 280 290 300
PYSSVSASLI ANGDSTSTCG MHSSGVSRGG SGFSASYNCQ EPPSSHIQPG
310 320 330 340 350
LCGLGNLGNT CFMNSALQCL SNTAPLTDYF LKDEYEAEIN RDNPLGMKGE
360 370 380 390 400
IAEAYAELIK QMWSGRDAHV APRMFKTQVG RFAPQFSGYQ QQDSQELLAF
410 420 430 440 450
LLDGLHEDLN RVKKKPYLEL KDANGRPDAV VAKEAWENHR LRNDSVIVDT
460 470 480 490 500
FHGLFKSTLV CPECAKVSVT FDPFCYLTLP LPLKKDRVME VFLVPADPHC
510 520 530 540 550
RPTQYRVTVP LMGAVSDLCE ALSRLSGIAA ENMVVADVYN HRFHKIFQMD
560 570 580 590 600
EGLNHIMPRD DIFVYEVCST SVDGSECVTL PVYFRERKSR PSSTSSASAL
610 620 630 640 650
YGQPLLLSVP KHKLTLESLY QAVCDRISRY VKQPLPDEFG SSPLEPGACN
660 670 680 690 700
GSRNSCEGED EEEMEHQEEG KEQLSETEGS GEDEPGNDPS ETTQKKIKGQ
710 720 730 740 750
PCPKRLFTFS LVNSYGTADI NSLAADGKLL KLNSRSTLAM DWDSETRRLY
760 770 780 790 800
YDEQESEAYE KHVSMLQPQK KKKTTVALRD CIELFTTMET LGEHDPWYCP
810 820 830 840 850
NCKKHQQATK KFDLWSLPKI LVVHLKRFSY NRYWRDKLDT VVEFPIRGLN
860 870 880 890 900
MSEFVCNLSA RPYVYDLIAV SNHYGAMGVG HYTAYAKNKL NGKWYYFDDS
910 920 930 940 950
NVSLASEDQI VTKAAYVLFY QRRDDEFYKT PSLSSSGSSD GGTRPSSSQQ
960
GFGDDEACSM DTN
Length:963
Mass (Da):108,565
Last modified:October 17, 2006 - v3
Checksum:i63055C9ADFE36713
GO
Isoform 2 (identifier: Q13107-2) [UniParc]FASTAAdd to Basket

Also known as: UnpES

The sequence of this isoform differs from the canonical sequence as follows:
     232-279: KSSTAPSRNFTTSPKSSASPYSSVSASLIANGDSTSTCGMHSSGVSRG → N

Show »
Length:916
Mass (Da):103,958
Checksum:i86CBBDE6AA2AB04E
GO
Isoform 3 (identifier: Q13107-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     233-313: SSTAPSRNFT...LGNLGNTCFM → VSFFLPRLEC...LLPQPPEWLG
     314-963: Missing.

Note: No experimental confirmation available.

Show »
Length:313
Mass (Da):35,661
Checksum:i7B2258A3A64AC0EB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti373 – 3731R → S in AAB72237. (PubMed:7784062)Curated
Sequence conflicti744 – 7441S → R in AAB72237. (PubMed:7784062)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti620 – 6201Y → C.
Corresponds to variant rs9311440 [ dbSNP | Ensembl ].
VAR_028180

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei232 – 27948KSSTA…GVSRG → N in isoform 2. 1 PublicationVSP_005258Add
BLAST
Alternative sequencei233 – 31381SSTAP…NTCFM → VSFFLPRLECNGAILAHCNF CLPGSSNSPASASRVAPSHL ANFFFFEMESHSVTKLECGG AVSAYSRVQVMLLPQPPEWL G in isoform 3. 1 PublicationVSP_044814Add
BLAST
Alternative sequencei314 – 963650Missing in isoform 3. 1 PublicationVSP_044815Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20657 mRNA. Translation: AAB72237.1.
AF017305 mRNA. Translation: AAC27355.1.
AF017306 mRNA. Translation: AAC27356.1.
AK291795 mRNA. Translation: BAF84484.1.
AC121247 Genomic DNA. No translation available.
BC068017 mRNA. No translation available.
BC125130 mRNA. Translation: AAI25131.1.
CCDSiCCDS2793.1. [Q13107-1]
CCDS2794.1. [Q13107-2]
CCDS58832.1. [Q13107-3]
PIRiT09478.
RefSeqiNP_001238806.1. NM_001251877.1. [Q13107-3]
NP_003354.2. NM_003363.3. [Q13107-1]
NP_955475.1. NM_199443.2. [Q13107-2]
UniGeneiHs.403828.
Hs.77500.

Genome annotation databases

EnsembliENST00000265560; ENSP00000265560; ENSG00000114316. [Q13107-1]
ENST00000351842; ENSP00000341028; ENSG00000114316. [Q13107-2]
ENST00000416417; ENSP00000400623; ENSG00000114316. [Q13107-3]
GeneIDi7375.
KEGGihsa:7375.
UCSCiuc003cwp.2. human. [Q13107-1]
uc003cwr.2. human. [Q13107-2]

Polymorphism databases

DMDMi116242839.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20657 mRNA. Translation: AAB72237.1.
AF017305 mRNA. Translation: AAC27355.1.
AF017306 mRNA. Translation: AAC27356.1.
AK291795 mRNA. Translation: BAF84484.1.
AC121247 Genomic DNA. No translation available.
BC068017 mRNA. No translation available.
BC125130 mRNA. Translation: AAI25131.1.
CCDSiCCDS2793.1. [Q13107-1]
CCDS2794.1. [Q13107-2]
CCDS58832.1. [Q13107-3]
PIRiT09478.
RefSeqiNP_001238806.1. NM_001251877.1. [Q13107-3]
NP_003354.2. NM_003363.3. [Q13107-1]
NP_955475.1. NM_199443.2. [Q13107-2]
UniGeneiHs.403828.
Hs.77500.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Y6EX-ray2.40A/B/C/D/E/F296-490[»]
A/B/C/D/E/F765-932[»]
ProteinModelPortaliQ13107.
SMRiQ13107. Positions 8-226, 297-483, 740-930.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113221. 79 interactions.
IntActiQ13107. 32 interactions.
MINTiMINT-3027027.
STRINGi9606.ENSP00000265560.

Chemistry

BindingDBiQ13107.
ChEMBLiCHEMBL2406900.

Protein family/group databases

MEROPSiC19.010.

PTM databases

PhosphoSiteiQ13107.

Polymorphism databases

DMDMi116242839.

Proteomic databases

MaxQBiQ13107.
PaxDbiQ13107.
PRIDEiQ13107.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265560; ENSP00000265560; ENSG00000114316. [Q13107-1]
ENST00000351842; ENSP00000341028; ENSG00000114316. [Q13107-2]
ENST00000416417; ENSP00000400623; ENSG00000114316. [Q13107-3]
GeneIDi7375.
KEGGihsa:7375.
UCSCiuc003cwp.2. human. [Q13107-1]
uc003cwr.2. human. [Q13107-2]

Organism-specific databases

CTDi7375.
GeneCardsiGC03M049315.
HGNCiHGNC:12627. USP4.
HPAiHPA018499.
MIMi603486. gene.
neXtProtiNX_Q13107.
PharmGKBiPA37252.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5560.
GeneTreeiENSGT00670000097750.
HOGENOMiHOG000264375.
HOVERGENiHBG000864.
InParanoidiQ13107.
KOiK11835.
OMAiHCRPTQY.
PhylomeDBiQ13107.
TreeFamiTF106276.

Miscellaneous databases

ChiTaRSiUSP4. human.
EvolutionaryTraceiQ13107.
GeneWikiiUSP4.
GenomeRNAii7375.
NextBioi28880.
PROiQ13107.
SOURCEiSearch...

Gene expression databases

BgeeiQ13107.
CleanExiHS_USP4.
ExpressionAtlasiQ13107. baseline and differential.
GenevestigatoriQ13107.

Family and domain databases

Gene3Di3.30.2230.10. 1 hit.
InterProiIPR006615. Pept_C19_DUSP.
IPR001394. Peptidase_C19_UCH.
IPR028135. Ub_USP-typ.
IPR028134. USP.
IPR018200. USP_CS.
IPR028889. USP_dom.
[Graphical view]
PANTHERiPTHR24006:SF360. PTHR24006:SF360. 1 hit.
PfamiPF06337. DUSP. 1 hit.
PF14836. Ubiquitin_3. 1 hit.
PF00443. UCH. 1 hit.
[Graphical view]
SMARTiSM00695. DUSP. 1 hit.
[Graphical view]
SUPFAMiSSF143791. SSF143791. 1 hit.
PROSITEiPS51283. DUSP. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Elevated expression of Unph, a proto-oncogene at 3p21.3, in human lung tumors."
    Gray D.A., Inazawa J., Gupta K., Wong A., Ueda R., Takahashi T.
    Oncogene 10:2179-2183(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
    Tissue: Brain cortex.
  2. Gray D.A.
    Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "The human UNP locus at 3p21.31 encodes two tissue-selective, cytoplasmic isoforms with deubiquitinating activity that have reduced expression in small cell lung carcinoma cell lines."
    Frederick A., Rolfe M., Chiu M.I.
    Oncogene 16:153-165(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING.
    Tissue: B-cell and T-cell.
  4. "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: Placenta.
  5. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    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 1 AND 3).
    Tissue: Leukocyte.
  7. "The de-ubiquitinating enzyme Unp interacts with the retinoblastoma protein."
    DeSalle L.M., Latres E., Lin D., Graner E., Montagnoli A., Baker R.T., Pagano M., Loda M.
    Oncogene 20:5538-5542(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RB1, MUTAGENESIS OF GLU-463 AND 459-LEU--GLU-463.
  8. "Oncogenic protein UnpEL/Usp4 deubiquitinates Ro52 by its isopeptidase activity."
    Wada K., Tanji K., Kamitani T.
    Biochem. Biophys. Res. Commun. 339:731-736(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-311.
  9. "UnpEL/Usp4 is ubiquitinated by Ro52 and deubiquitinated by itself."
    Wada K., Kamitani T.
    Biochem. Biophys. Res. Commun. 342:253-258(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, AUTODEUBIQUITINATION, UBIQUITINATION BY TRIM21, MUTAGENESIS OF CYS-311.
  10. "The ubiquitin-specific protease Usp4 regulates the cell surface level of the A2A receptor."
    Milojevic T., Reiterer V., Stefan E., Korkhov V.M., Dorostkar M.M., Ducza E., Ogris E., Boehm S., Freissmuth M., Nanoff C.
    Mol. Pharmacol. 69:1083-1094(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ADORA2A, TISSUE SPECIFICITY.
  11. "The Prp19 complex and the Usp4Sart3 deubiquitinating enzyme control reversible ubiquitination at the spliceosome."
    Song E.J., Werner S.L., Neubauer J., Stegmeier F., Aspden J., Rio D., Harper J.W., Elledge S.J., Kirschner M.W., Rape M.
    Genes Dev. 24:1434-1447(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SART3, SUBCELLULAR LOCATION.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Ubiquitin-specific protease 4 inhibits mono-ubiquitination of the master growth factor signaling kinase PDK1."
    Uras I.Z., List T., Nijman S.M.
    PLoS ONE 7:E31003-E31003(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEUBIQUITINATION OF PDPK1.
  14. "Ubiquitin-specific protease 4 is inhibited by its ubiquitin-like domain."
    Luna-Vargas M.P., Faesen A.C., van Dijk W.J., Rape M., Fish A., Sixma T.K.
    EMBO Rep. 12:365-372(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 296-932, DOMAINS UBIQUITIN-LIKE, ZINC-BINDING SITES.

Entry informationi

Entry nameiUBP4_HUMAN
AccessioniPrimary (citable) accession number: Q13107
Secondary accession number(s): A8K6Y0
, C9IY91, O43452, O43453, Q08AK8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 17, 2006
Last modified: February 4, 2015
This is version 143 of the entry and version 3 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 3
    Human chromosome 3: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.