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Protein

Ubiquitin carboxyl-terminal hydrolase 19

Gene

Usp19

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity2 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)DescriptionActionsGraphical viewLength
Active sitei545NucleophilePROSITE-ProRule annotation1
Active sitei1204Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri830 – 872MYND-typePROSITE-ProRule annotationAdd BLAST43

GO - Molecular functioni

GO - Biological processi

  • ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
  • negative regulation of skeletal muscle tissue development Source: UniProtKB
  • positive regulation of cell cycle process Source: UniProtKB
  • protein deubiquitination Source: UniProtKB
  • regulation of cellular response to hypoxia Source: UniProtKB
  • regulation of protein stability Source: UniProtKB
  • response to endoplasmic reticulum stress Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.19.12. 5301.

Protein family/group databases

MEROPSiC19.024.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Usp19
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1303276. Usp19.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 1330CytoplasmicSequence analysisAdd BLAST1330
Transmembranei1331 – 1351HelicalSequence analysisAdd BLAST21
Topological domaini1352 – 1357LumenalSequence analysis6

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi545C → A: Has a destabilizing effect on RNF123. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002951581 – 1357Ubiquitin carboxyl-terminal hydrolase 19Add BLAST1357

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei221PhosphoserineBy similarity1
Modified residuei283PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ6J1Y9.
PRIDEiQ6J1Y9.

PTM databases

iPTMnetiQ6J1Y9.
PhosphoSitePlusiQ6J1Y9.

Expressioni

Tissue specificityi

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

Inductioni

By streptozotocin and fasting in skeletal muscle.1 Publication

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000067744.

Structurei

3D structure databases

ProteinModelPortaliQ6J1Y9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini51 – 140CS 1PROSITE-ProRule annotationAdd BLAST90
Domaini321 – 423CS 2PROSITE-ProRule annotationAdd BLAST103
Domaini536 – 1253USPAdd BLAST718

Sequence similaritiesi

Contains 2 CS domains.PROSITE-ProRule annotation
Contains 1 MYND-type zinc finger.PROSITE-ProRule annotation
Contains 1 USP domain.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri830 – 872MYND-typePROSITE-ProRule annotationAdd BLAST43

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiKOG1870. Eukaryota.
COG5560. LUCA.
HOVERGENiHBG061889.
InParanoidiQ6J1Y9.
KOiK11847.
PhylomeDBiQ6J1Y9.

Family and domain databases

Gene3Di2.60.40.790. 2 hits.
InterProiIPR007052. CS_dom.
IPR008978. HSP20-like_chaperone.
IPR001394. Peptidase_C19_UCH.
IPR018200. USP_CS.
IPR028889. USP_dom.
IPR002893. Znf_MYND.
[Graphical view]
PfamiPF04969. CS. 1 hit.
PF00443. UCH. 1 hit.
PF01753. zf-MYND. 1 hit.
[Graphical view]
SUPFAMiSSF49764. SSF49764. 2 hits.
PROSITEiPS51203. 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]

Sequencei

Sequence statusi: Complete.

Q6J1Y9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAGTSATGP RRGPPGLEEA TSKKKQKDRA NQESKDGDPR RVSMPRKEPT
60 70 80 90 100
KDELLLDWRQ SSDKVVVKLR VGTGPICLEE VDAAFTDTDC VVRLPDGRQW
110 120 130 140 150
GGVFFAKIQS SCTKVQTRKG GLLQLALPKK VPLLTWPSLL KKPLGTQELV
160 170 180 190 200
PGLRCQENGQ ELSPIALEPG SEPRRAKQEA RNQKRAQGRG EVGSGASPGA
210 220 230 240 250
QAGPSAKRAV HLCRGPEGEG SMDGPGPQGD APSFLSDSAT QVEAEEQLHV
260 270 280 290 300
PPVNPQTSLL GSEKNLALLT VEKTVSPRSD SVSPVMIRNR DPEKDDHFKE
310 320 330 340 350
EMAVGADPAA LADEPESMVN LAFVKNDSYE KGPDSVVVHV YVKESRRDTS
360 370 380 390 400
RVLFREQDFT LIFQTRDGNF LRLHPGCGPH TIFRWQVKLR NLIEPEQCTF
410 420 430 440 450
CFTASRIDIC LRKRQSQRWG GLEAPATRVG GAKVAVPTGP TPLDSTPPGG
460 470 480 490 500
GPLPLTGQEE ARAVEKEKPK ARSEDSGLDG VVARTPLEHV TPKPEPHLAS
510 520 530 540 550
PKPTCMVPPM PHSPVSGDSV EEDEEEEKKV CLPGFTGLVN LGNTCFMNSV
560 570 580 590 600
IQSLSNTREL RDFFHDRSFE AEINYNNPLG TGGRLAIGFA VLLRALWKGT
610 620 630 640 650
HQAFQPSKLK AIVASKASQF TGYAQHDAQE FMAFLLDGLH EDLNRIQNKP
660 670 680 690 700
YTETVDSDGR PDEVVAEEAW QRHKMRNDSF IVDLFQGQYK SKLVCPVCAK
710 720 730 740 750
VSITFDPFLY LPVPLPQKQK VLPIYYFARE PHSKPIKFLV SVSKENSSAS
760 770 780 790 800
EVLESLSQSV HVKPESLRLA EVIKNRFHRV FLPSHSLDAV SPTDVLLCFE
810 820 830 840 850
LLSPELAKER VVVLEVQQRP QVPSIPISKC AACQRKQQSE DEKLKRCTRC
860 870 880 890 900
YRVGYCNQFC QKTHWPDHKG LCRPENIGYP FLVSVPASRL TYARLAQLLE
910 920 930 940 950
GYARYSVSVF QPPFQPGRMA LESQSPGCTT LLSTSSLEAG DSEREPIQPS
960 970 980 990 1000
ELQLVTPVAE GDTGAHRMWP PADRGPVPST SGISSEMLAS GPMEGCSLLA
1010 1020 1030 1040 1050
GERVSRPEAA VPGYQHSRES VSAHTPQFFI YKIDASSREQ RLEDKGDTPL
1060 1070 1080 1090 1100
ELGDDCSLAL VWRNNERLQE FVLVASKELE CAEDPGSAGE AARAGHFTLD
1110 1120 1130 1140 1150
QCLNLFTRPE VLAPEEAWYC PQCKQHREAS KQLLLWRLPN VLIVQLKRFS
1160 1170 1180 1190 1200
FRSFIWRDKI NDLVEFPVRN LDLSKFCIGQ KEEQLPSYDL YAVINHYGGM
1210 1220 1230 1240 1250
IGGHYTACAR LPSDRSSQRS DVGWRLFDDS TVTTVDESQV VTRYAYVLFY
1260 1270 1280 1290 1300
RRRNSPVERP PRAAHAEHHP DLGPAAEAAA SQASRIWQEL EAEEEMVPEG
1310 1320 1330 1340 1350
PGPLGPWGPQ DWVGPPPRGP TTSDEGCLRY FVLGTVAALV ALVLNVFYPL

VSQSRWR
Length:1,357
Mass (Da):150,302
Last modified:July 5, 2004 - v1
Checksum:iE2CE888D61EC3C81
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY605065 mRNA. Translation: AAT35219.1.
RefSeqiNP_001001516.1. NM_001001516.2.
UniGeneiRn.13484.

Genome annotation databases

GeneIDi361190.
KEGGirno:361190.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY605065 mRNA. Translation: AAT35219.1.
RefSeqiNP_001001516.1. NM_001001516.2.
UniGeneiRn.13484.

3D structure databases

ProteinModelPortaliQ6J1Y9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000067744.

Protein family/group databases

MEROPSiC19.024.

PTM databases

iPTMnetiQ6J1Y9.
PhosphoSitePlusiQ6J1Y9.

Proteomic databases

PaxDbiQ6J1Y9.
PRIDEiQ6J1Y9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi361190.
KEGGirno:361190.

Organism-specific databases

CTDi10869.
RGDi1303276. Usp19.

Phylogenomic databases

eggNOGiKOG1870. Eukaryota.
COG5560. LUCA.
HOVERGENiHBG061889.
InParanoidiQ6J1Y9.
KOiK11847.
PhylomeDBiQ6J1Y9.

Enzyme and pathway databases

BRENDAi3.4.19.12. 5301.

Miscellaneous databases

PROiQ6J1Y9.

Family and domain databases

Gene3Di2.60.40.790. 2 hits.
InterProiIPR007052. CS_dom.
IPR008978. HSP20-like_chaperone.
IPR001394. Peptidase_C19_UCH.
IPR018200. USP_CS.
IPR028889. USP_dom.
IPR002893. Znf_MYND.
[Graphical view]
PfamiPF04969. CS. 1 hit.
PF00443. UCH. 1 hit.
PF01753. zf-MYND. 1 hit.
[Graphical view]
SUPFAMiSSF49764. SSF49764. 2 hits.
PROSITEiPS51203. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiUBP19_RAT
AccessioniPrimary (citable) accession number: Q6J1Y9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: July 5, 2004
Last modified: November 2, 2016
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.