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Q3UJD6 (UBP19_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 79. 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·Alt products·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
Synonyms:Kiaa0891
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1360 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 By similarity. 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. Exhibits a preference towards 'Lys-63'-linked Ubiquitin chains By similarity. 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. 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 By similarity. Interacts with BIRC2/c-IAP1, BIRC3/c-IAP2 and XIAP/BIRC4. Interacts with HIF1A (via N-terminus) By similarity.

Subcellular location

Endoplasmic reticulum membrane; Single-pass membrane protein By similarity.

Induction

Up-regulated by ESR1 in the presence of 17 beta-estradiol (E2). Ref.4

Sequence similarities

Contains 2 CS domains.

Contains 1 MYND-type zinc finger.

Contains 1 USP domain.

Sequence caution

The sequence BAC65678.4 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
Transmembrane
Transmembrane helix
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Protease
Thiol protease
   Technical termComplete proteome
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 mutant phenotype Ref.4. Source: UniProtKB

positive regulation of cell cycle process

Inferred from sequence or structural similarity. Source: UniProtKB

protein deubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cellular response to hypoxia

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of protein stability

Inferred from sequence or structural similarity. Source: UniProtKB

response to endoplasmic reticulum stress

Inferred from sequence or structural similarity. Source: UniProtKB

skeletal muscle atrophy

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytosol

Inferred from direct assay PubMed 19015242. Source: UniProtKB

endoplasmic 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 mutant phenotype Ref.4. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q3UJD6-1)

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 2 (identifier: Q3UJD6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1286-1340: ASRIWQELEA...LRYFVLGTVA → GLGPGQAPEV...PTYSNMEEVD
     1341-1360: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13601360Ubiquitin carboxyl-terminal hydrolase 19
PRO_0000295157

Regions

Topological domain1 – 13331333Cytoplasmic Potential
Transmembrane1334 – 135421Helical; Potential
Topological domain1355 – 13606Lumenal Potential
Domain51 – 14090CS 1
Domain322 – 424103CS 2
Domain539 – 1256718USP
Zinc finger833 – 87543MYND-type
Compositional bias524 – 5307Poly-Glu

Sites

Active site5481Nucleophile By similarity
Active site12071Proton acceptor By similarity

Natural variations

Alternative sequence1286 – 134055ASRIW…LGTVA → GLGPGQAPEVAPTRTAPERF APPVDRPAPTYSNMEEVD in isoform 2.
VSP_026769
Alternative sequence1341 – 136020Missing in isoform 2.
VSP_026770

Experimental info

Sequence conflict1401L → LK in BAE42739. Ref.2
Sequence conflict1421P → S in AAH60613. Ref.3
Sequence conflict430 – 4312Missing in BAE42739. Ref.2
Sequence conflict6691A → T in BAE42739. Ref.2
Sequence conflict10581D → E in BAE42739. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: FE9C3020D2CD9AED

FASTA1,360150,549
        10         20         30         40         50         60 
MSAGASATGP RRGPPGLEEA TSKKKQKDRA NLESKDGDAR RVSLPRKEPT KDELLLDWRQ 

        70         80         90        100        110        120 
SADEVIVKLR VGTGPVRLED VDAAFTDTDC VVRLPDGRQW GGVFFAEIQS SCTKVQARKG 

       130        140        150        160        170        180 
GLLQLVLPKK VPLLTWPSLL KPLGTQELVP GLQCQENGQE LSPIALEPGS EPRRAKQEAR 

       190        200        210        220        230        240 
NQKRAQGRGE VGSGAGPGTQ AGPSAKRAVH LRRGPEGEGS MDGPGPQGDA PSFLSDSATQ 

       250        260        270        280        290        300 
VEAEEKLCAP PMNTQTSLLS SEKSLALLTV EKTVSPRNDP VAPVMVQDRD PEPEQEDQVK 

       310        320        330        340        350        360 
EEMALGADPT ALVEEPESMV NLAFVKNDSY EKGPDSVVVH VYVKEIRRDS SRVLFREQDF 

       370        380        390        400        410        420 
TLIFQTRDGN FLRLHPGCGP HTIFRWQVKL RNLIEPEQCT FCFTASRIDI CLRKRQSQRW 

       430        440        450        460        470        480 
GGLEAPATRG AVGGAKVAVP TGPTPLDSTP PGGGPHPLTG QEEARAVEKE KPKARSEDSG 

       490        500        510        520        530        540 
LDGVVARTPL EHVAPKPDPH LASPKPTCMV PPMPHSPVSG DSVEEDEEEE KKVCLPGFTG 

       550        560        570        580        590        600 
LVNLGNTCFM NSVIQSLSNT RELRDFFHDR SFEAEINYNN PLGTGGRLAI GFAVLLRALW 

       610        620        630        640        650        660 
KGTHQAFQPS KLKAIVASKA SQFTGYAQHD AQEFMAFLLD GLHEDLNRIQ NKPYTETVDS 

       670        680        690        700        710        720 
DGRPDEVVAE EAWQRHKMRN DSFIVDLFQG QYKSKLVCPV CAKVSITFDP FLYLPVPLPQ 

       730        740        750        760        770        780 
KQKVLPIFYF AREPHSKPIK FLVSVSKENS SASEVLDSLS QSVHVKPENL RLAEVIKNRF 

       790        800        810        820        830        840 
HRVFLPSHSL DAVSPTDVLL CFELLSPELA KERVVVLEVQ QRPQVPSIPI SKCAACQRKQ 

       850        860        870        880        890        900 
QSEEEKLKRC TRCYRVGYCN QFCQKTHWPD HKGLCRPENI GYPFLVSVPA SRLTYARLAQ 

       910        920        930        940        950        960 
LLEGYARYSV SVFQPPFQPG RMALESQSPG CTTLLSTSSL EAGDSEREPI QPSELQLVTP 

       970        980        990       1000       1010       1020 
VAEGDTGAHR VWPPADRGPV PSTSGLSSEM LASGPIEGCP LLAGERVSRP EAAVPGYQHS 

      1030       1040       1050       1060       1070       1080 
SESVNTHTPQ FFIYKIDASN REQRLEDKGE TPLELGDDCS LALVWRNNER LQEFVLVASK 

      1090       1100       1110       1120       1130       1140 
ELECAEDPGS AGEAARAGHF TLDQCLNLFT RPEVLAPEEA WYCPQCKQHR EASKQLLLWR 

      1150       1160       1170       1180       1190       1200 
LPNVLIVQLK RFSFRSFIWR DKINDLVEFP VRNLDLSKFC IGQKEEQLPS YDLYAVINHY 

      1210       1220       1230       1240       1250       1260 
GGMIGGHYTA CARLPNDRSS QRSDVGWRLF DDSTVTTVDE SQVVTRYAYV LFYRRRNSPV 

      1270       1280       1290       1300       1310       1320 
ERPPRASHSE HHPDLGPAAE AAASQASRIW QELEAEEEMV PEGPGPLGPW GPQDWVGPPP 

      1330       1340       1350       1360 
RGPTTPDEGC LRYFVLGTVA ALVALVLNVF YPLVSQSRWR 

« Hide

Isoform 2 [UniParc].

Checksum: 73E85AA9778738F7
Show »

FASTA1,323146,283

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Fetal brain.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J and NOD.
Tissue: Head, Kidney and Spleen.
[3]"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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 395-1360 (ISOFORM 2).
Strain: C57BL/6.
Tissue: Brain.
[4]"17beta-estradiol represses myogenic differentiation by increasing ubiquitin-specific peptidase 19 through estrogen receptor alpha."
Ogawa M., Yamaji R., Higashimura Y., Harada N., Ashida H., Nakano Y., Inui H.
J. Biol. Chem. 286:41455-41465(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK122396 mRNA. Translation: BAC65678.4. Different initiation.
AK146504 mRNA. Translation: BAE27219.1.
AK160807 mRNA. Translation: BAE36025.1.
AK171942 mRNA. Translation: BAE42739.1.
BC046824 mRNA. Translation: AAH46824.1.
BC060613 mRNA. Translation: AAH60613.1.
CCDSCCDS23529.1. [Q3UJD6-1]
CCDS52924.1. [Q3UJD6-2]
RefSeqNP_001161843.1. NM_001168371.2.
NP_001161844.1. NM_001168372.2. [Q3UJD6-2]
NP_001161845.1. NM_001168373.2.
NP_082080.3. NM_027804.4. [Q3UJD6-1]
NP_663382.2. NM_145407.3.
UniGeneMm.289706.

3D structure databases

ProteinModelPortalQ3UJD6.
SMRQ3UJD6. Positions 306-444, 536-719, 1038-1257.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid214730. 1 interaction.

Protein family/group databases

MEROPSC19.024.

PTM databases

PhosphoSiteQ3UJD6.

Proteomic databases

MaxQBQ3UJD6.
PaxDbQ3UJD6.
PRIDEQ3UJD6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000006854; ENSMUSP00000006854; ENSMUSG00000006676. [Q3UJD6-1]
ENSMUST00000085044; ENSMUSP00000082119; ENSMUSG00000006676. [Q3UJD6-2]
GeneID71472.
KEGGmmu:71472.
UCSCuc009rpt.2. mouse. [Q3UJD6-1]
uc009rpu.2. mouse. [Q3UJD6-2]

Organism-specific databases

CTD10869.
MGIMGI:1918722. Usp19.
RougeSearch...

Phylogenomic databases

eggNOGCOG5560.
GeneTreeENSGT00670000097750.
HOGENOMHOG000074206.
HOVERGENHBG061889.
KOK11847.
OMAPQCKQHR.
PhylomeDBQ3UJD6.
TreeFamTF106276.

Gene expression databases

ArrayExpressQ3UJD6.
BgeeQ3UJD6.
CleanExMM_USP19.
GenevestigatorQ3UJD6.

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

ChiTaRSUSP19. mouse.
NextBio333851.
PROQ3UJD6.
SOURCESearch...

Entry information

Entry nameUBP19_MOUSE
AccessionPrimary (citable) accession number: Q3UJD6
Secondary accession number(s): Q3TAC9 expand/collapse secondary AC list , Q3TUE6, Q6P9T0, Q80TP5, Q80ZW5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: October 11, 2005
Last modified: July 9, 2014
This is version 79 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot