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Q76LT8 (UBP48_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin carboxyl-terminal hydrolase 48

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 48
Synaptic ubiquitin-specific protease
Short name=synUSP
Ubiquitin thioesterase 48
Ubiquitin-specific-processing protease 48
Gene names
Name:Usp48
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1036 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins. May be involved in the regulation of NF-kappa-B activation by TNF receptor superfamily via its interactions with RELA and TRAF2. May also play a regulatory role at postsynaptic sites. Ref.1

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). Ref.1

Subunit structure

Interacts with TRAF2 and RELA By similarity.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Note: In neuronal cells, it localizes to dendrites, as well as somas. Ref.1

Tissue specificity

Present in the brain, in particular in the postsynaptic density and the dendritic lipid raft fractions (at protein level). Ref.1

Sequence similarities

Belongs to the peptidase C19 family.

Contains 3 DUSP domains.

Contains 1 ubiquitin-like domain.

Contains 1 USP domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10361036Ubiquitin carboxyl-terminal hydrolase 48
PRO_0000249525

Regions

Domain89 – 421333USP
Domain460 – 55495DUSP 1
Domain569 – 692124DUSP 2
Domain712 – 825114DUSP 3
Domain930 – 101081Ubiquitin-like

Sites

Active site981Nucleophile By similarity
Active site3531Proton acceptor By similarity

Amino acid modifications

Modified residue8871Phosphoserine By similarity
Modified residue8881Phosphoserine By similarity
Modified residue8891Phosphoserine By similarity
Modified residue9571N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q76LT8 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: EEC407C21D4BC539

FASTA1,036118,787
        10         20         30         40         50         60 
MAPRLQLEKA AWRWAETVRP EEVSQEHIET AYRIWLEPCI RGVCRRNCRG NPNCLVGIGE 

        70         80         90        100        110        120 
HIWLGEIDEN SFHNIDDPNC ERRKKNSFVG LTNLGASCYV NTFLQVWFLN LELRQALYLC 

       130        140        150        160        170        180 
PSTCSDYTKG DGIRGGKDYE PQTICEHLQY LFALLQNSNR RYIDPSGFVK ALGLDTGQQQ 

       190        200        210        220        230        240 
DAQESSKLFM SLLEDTLSKQ KNPDVRNVVQ QQFCGEYAYV TVCSQCGRES KLVSKFYELE 

       250        260        270        280        290        300 
LNIQGHKQLT DCISEFLKEE RLEGDNRYFC ENCQSKQNAT RKIRLLSLPC TLNLQLMRFV 

       310        320        330        340        350        360 
FDRQTGHKKK LNAYIGFSES LDMEPYVEHK GGSFVYELSA VLIHRGVSAY SGHYIAHVKD 

       370        380        390        400        410        420 
PQSGDWYKFN DEDIEKMEGK KLQLGIEEDL TEPSKSQTRK PKCGKGTHCS RNAYMLVYRL 

       430        440        450        460        470        480 
QTQEKNHTMV QVPAFLQELV DRDNSKFEEW CVEMAEMRRQ SVDKGRAKHE EVKELYQRLP 

       490        500        510        520        530        540 
AGAEPYEFVS LEWLQKWLDE STPTKPIDNN ACLCSHDKLH PDKISIMKRI SEYAADIFYS 

       550        560        570        580        590        600 
RYGGGPRLTV KALCKDCVVE RCRILRLKNQ LNEDYKTVNN LLKATMKGSD GFWVGKSSLR 

       610        620        630        640        650        660 
SWRQLALEQL DEQDGEAEQS NGKINGSPFS KDESKEEKKE EEEELNFNED ILCPHGELSI 

       670        680        690        700        710        720 
SENERRLVSQ EAWSKLQQYF PKAPEFPSYK ECCSQCKILE REGEENEALH KMIAKEQKTS 

       730        740        750        760        770        780 
LPNLFQDKNR PCLSNWPEDT DALYIVSHFF LDEWRKFVRK PARSTPVSSV GNAALLCPHG 

       790        800        810        820        830        840 
GLMFTFPSLT KEDSKLIALI WPSEWQMIQK LFVVDKVIKI TRIEVGDVNP SQTQYISEPN 

       850        860        870        880        890        900 
LCPDCREGLL CQQQKDLREY TQATIYVHKV VDNKKVMKDS APELNVSSSE TEEDKEEAKP 

       910        920        930        940        950        960 
DGEKDPDFNQ SNGGTKRQKT SQQGYVAYQK QVIRRSTRHR KVRGEKALLV SANQTLKELK 

       970        980        990       1000       1010       1020 
IQIMHAFSVA PFDQNLSIDG KILNDDCATL GTLGVIPESV ILLKADEPIA DYAAMDDVMQ 

      1030 
VCMPEEGFKG TGLLGH 

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References

[1]"A novel ubiquitin-specific protease, synUSP, is localized at the post-synaptic density and post-synaptic lipid raft."
Tian Q.B., Okano A., Nakayama K., Miyazawa S., Endo S., Suzuki T.
J. Neurochem. 87:665-675(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB073880 mRNA. Translation: BAD00009.1.
RefSeqNP_942080.1. NM_198785.1.
UniGeneRn.100022.

3D structure databases

ProteinModelPortalQ76LT8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid263601. 1 interaction.
STRING10116.ENSRNOP00000052796.

Protein family/group databases

MEROPSC19.068.

PTM databases

PhosphoSiteQ76LT8.

Proteomic databases

PRIDEQ76LT8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID362636.
KEGGrno:362636.
UCSCRGD:735213. rat.

Organism-specific databases

CTD84196.
RGD735213. Usp48.

Phylogenomic databases

eggNOGCOG5077.
HOGENOMHOG000231639.
HOVERGENHBG080368.
KOK11858.
PhylomeDBQ76LT8.

Gene expression databases

GenevestigatorQ76LT8.

Family and domain databases

InterProIPR006615. Pept_C19_DUSP.
IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR028889. UCH/PAN2.
[Graphical view]
PfamPF00443. UCH. 1 hit.
[Graphical view]
SUPFAMSSF143791. SSF143791. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEPS51283. DUSP. 3 hits.
PS50053. UBIQUITIN_2. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio680703.
PROQ76LT8.

Entry information

Entry nameUBP48_RAT
AccessionPrimary (citable) accession number: Q76LT8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: July 5, 2004
Last modified: June 11, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries