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Q6J1Y9 (UBP19_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 19

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 19
Ubiquitin thioesterase 19
Ubiquitin-specific-processing protease 19
Gene names
Name:Usp19
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1357 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Deubiquitinating enzyme that regulates the degradation of various proteins. Deubiquitinates and prevents proteasomal degradation of RNF123 which in turn stimulates CDKN1B ubiquitin-dependent degradation thereby playing a role in cell proliferation. Involved in decreased protein synthesis in atrophying skeletal muscle. Modulates transcription of major myofibrillar proteins. Also involved in turnover of endoplasmic-reticulum-associated degradation (ERAD) substrates. Regulates the stability of BIRC2/c-IAP1 and BIRC3/c-IAP2 by preventing thier ubiquitination. Required for cells to mount an appropriate response to hypoxia and rescues HIF1A from degradation in a non-catalytic manner. Plays an important role in 17 beta-estradiol (E2)-inhibited myogenesis. Decreases the levels of ubiquitinated proteins during skeletal muscle formation and acts to repress myogenesis. Exhibits a preference towards 'Lys-63'-linked Ubiquitin chains By similarity. Ref.3 Ref.4

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).

Subunit structure

Interacts with and stabilizes RNF123. Interacts with BIRC2/c-IAP1, BIRC3/c-IAP2 and XIAP/BIRC4. Interacts with HIF1A (via N-terminus) By similarity. Ref.4

Subcellular location

Endoplasmic reticulum membrane; Single-pass membrane protein Ref.4.

Tissue specificity

Expressed in testis, heart, kidney and skeletal muscle. Low levels of expression are detectable in all other tissues screened. Ref.1

Induction

By streptozotocin and fasting in skeletal muscle. Ref.1

Sequence similarities

Contains 2 CS domains.

Contains 1 MYND-type zinc finger.

Contains 1 USP domain.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentEndoplasmic reticulum
Membrane
   DomainRepeat
Transmembrane
Transmembrane helix
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Protease
Thiol protease
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processER-associated ubiquitin-dependent protein catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of skeletal muscle tissue development

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell cycle process

Inferred from mutant phenotype Ref.4. Source: UniProtKB

protein deubiquitination

Inferred from mutant phenotype Ref.1. Source: UniProtKB

regulation of cellular response to hypoxia

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of protein stability

Inferred from direct assay Ref.4. Source: UniProtKB

response to endoplasmic reticulum stress

Inferred from sequence or structural similarity. Source: UniProtKB

skeletal muscle atrophy

Inferred from expression pattern Ref.3. Source: UniProtKB

   Cellular_componentendoplasmic reticulum membrane

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

ubiquitin-specific protease activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13571357Ubiquitin carboxyl-terminal hydrolase 19
PRO_0000295158

Regions

Topological domain1 – 13301330Cytoplasmic Potential
Transmembrane1331 – 135121Helical; Potential
Topological domain1352 – 13576Lumenal Potential
Domain51 – 14090CS 1
Domain321 – 423103CS 2
Domain536 – 1253718USP
Zinc finger830 – 87243MYND-type

Sites

Active site5451Nucleophile By similarity
Active site12041Proton acceptor By similarity

Experimental info

Mutagenesis5451C → A: Has a destabilizing effect on RNF123. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q6J1Y9 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: E2CE888D61EC3C81

FASTA1,357150,302
        10         20         30         40         50         60 
MSAGTSATGP RRGPPGLEEA TSKKKQKDRA NQESKDGDPR RVSMPRKEPT KDELLLDWRQ 

        70         80         90        100        110        120 
SSDKVVVKLR VGTGPICLEE VDAAFTDTDC VVRLPDGRQW GGVFFAKIQS SCTKVQTRKG 

       130        140        150        160        170        180 
GLLQLALPKK VPLLTWPSLL KKPLGTQELV PGLRCQENGQ ELSPIALEPG SEPRRAKQEA 

       190        200        210        220        230        240 
RNQKRAQGRG EVGSGASPGA QAGPSAKRAV HLCRGPEGEG SMDGPGPQGD APSFLSDSAT 

       250        260        270        280        290        300 
QVEAEEQLHV PPVNPQTSLL GSEKNLALLT VEKTVSPRSD SVSPVMIRNR DPEKDDHFKE 

       310        320        330        340        350        360 
EMAVGADPAA LADEPESMVN LAFVKNDSYE KGPDSVVVHV YVKESRRDTS RVLFREQDFT 

       370        380        390        400        410        420 
LIFQTRDGNF LRLHPGCGPH TIFRWQVKLR NLIEPEQCTF CFTASRIDIC LRKRQSQRWG 

       430        440        450        460        470        480 
GLEAPATRVG GAKVAVPTGP TPLDSTPPGG GPLPLTGQEE ARAVEKEKPK ARSEDSGLDG 

       490        500        510        520        530        540 
VVARTPLEHV TPKPEPHLAS PKPTCMVPPM PHSPVSGDSV EEDEEEEKKV CLPGFTGLVN 

       550        560        570        580        590        600 
LGNTCFMNSV IQSLSNTREL RDFFHDRSFE AEINYNNPLG TGGRLAIGFA VLLRALWKGT 

       610        620        630        640        650        660 
HQAFQPSKLK AIVASKASQF TGYAQHDAQE FMAFLLDGLH EDLNRIQNKP YTETVDSDGR 

       670        680        690        700        710        720 
PDEVVAEEAW QRHKMRNDSF IVDLFQGQYK SKLVCPVCAK VSITFDPFLY LPVPLPQKQK 

       730        740        750        760        770        780 
VLPIYYFARE PHSKPIKFLV SVSKENSSAS EVLESLSQSV HVKPESLRLA EVIKNRFHRV 

       790        800        810        820        830        840 
FLPSHSLDAV SPTDVLLCFE LLSPELAKER VVVLEVQQRP QVPSIPISKC AACQRKQQSE 

       850        860        870        880        890        900 
DEKLKRCTRC YRVGYCNQFC QKTHWPDHKG LCRPENIGYP FLVSVPASRL TYARLAQLLE 

       910        920        930        940        950        960 
GYARYSVSVF QPPFQPGRMA LESQSPGCTT LLSTSSLEAG DSEREPIQPS ELQLVTPVAE 

       970        980        990       1000       1010       1020 
GDTGAHRMWP PADRGPVPST SGISSEMLAS GPMEGCSLLA GERVSRPEAA VPGYQHSRES 

      1030       1040       1050       1060       1070       1080 
VSAHTPQFFI YKIDASSREQ RLEDKGDTPL ELGDDCSLAL VWRNNERLQE FVLVASKELE 

      1090       1100       1110       1120       1130       1140 
CAEDPGSAGE AARAGHFTLD QCLNLFTRPE VLAPEEAWYC PQCKQHREAS KQLLLWRLPN 

      1150       1160       1170       1180       1190       1200 
VLIVQLKRFS FRSFIWRDKI NDLVEFPVRN LDLSKFCIGQ KEEQLPSYDL YAVINHYGGM 

      1210       1220       1230       1240       1250       1260 
IGGHYTACAR LPSDRSSQRS DVGWRLFDDS TVTTVDESQV VTRYAYVLFY RRRNSPVERP 

      1270       1280       1290       1300       1310       1320 
PRAAHAEHHP DLGPAAEAAA SQASRIWQEL EAEEEMVPEG PGPLGPWGPQ DWVGPPPRGP 

      1330       1340       1350 
TTSDEGCLRY FVLGTVAALV ALVLNVFYPL VSQSRWR 

« Hide

References

[1]"USP19 is a ubiquitin-specific protease regulated in rat skeletal muscle during catabolic states."
Combaret L., Adegoke O.A.J., Bedard N., Baracos V., Attaix D., Wing S.S.
Am. J. Physiol. 288:E693-E700(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
Strain: Sprague-Dawley.
Tissue: Testis.
[2]Lubec G., Kang S.U., Lubec S.
Submitted (SEP-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-11; 60-76 AND 837-845, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain.
[3]"USP19-deubiquitinating enzyme regulates levels of major myofibrillar proteins in L6 muscle cells."
Sundaram P., Pang Z., Miao M., Yu L., Wing S.S.
Am. J. Physiol. 297:E1283-E1290(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[4]"USP19 deubiquitinating enzyme supports cell proliferation by stabilizing KPC1, a ubiquitin ligase for p27Kip1."
Lu Y., Adegoke O.A.J., Nepveu A., Nakayama K.I., Bedard N., Cheng D., Peng J., Wing S.S.
Mol. Cell. Biol. 29:547-558(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RNF123, MUTAGENESIS OF CYS-545.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY605065 mRNA. Translation: AAT35219.1.
RefSeqNP_001001516.1. NM_001001516.2.
UniGeneRn.13484.

3D structure databases

ProteinModelPortalQ6J1Y9.
SMRQ6J1Y9. Positions 305-441.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC19.024.

PTM databases

PhosphoSiteQ6J1Y9.

Proteomic databases

PRIDEQ6J1Y9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID361190.
KEGGrno:361190.

Organism-specific databases

CTD10869.
RGD1303276. Usp19.

Phylogenomic databases

HOVERGENHBG061889.
KOK11847.
PhylomeDBQ6J1Y9.

Gene expression databases

GenevestigatorQ6J1Y9.

Family and domain databases

Gene3D2.60.40.790. 2 hits.
InterProIPR007052. CS_dom.
IPR008978. HSP20-like_chaperone.
IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR002893. Znf_MYND.
[Graphical view]
PfamPF04969. CS. 2 hits.
PF00443. UCH. 1 hit.
PF01753. zf-MYND. 1 hit.
[Graphical view]
SUPFAMSSF49764. SSF49764. 2 hits.
PROSITEPS51203. CS. 2 hits.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
PS01360. ZF_MYND_1. 1 hit.
PS50865. ZF_MYND_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio675485.
PROQ6J1Y9.

Entry information

Entry nameUBP19_RAT
AccessionPrimary (citable) accession number: Q6J1Y9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 66 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