Q3UJD6 (UBP19_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin carboxyl-terminal hydrolase 19
EC=3.4.19.12

Alternative name(s):
Deubiquitinating enzyme 19
Ubiquitin thiolesterase 19
Ubiquitin-specific-processing protease 19

Gene names

Name:	Usp19
Synonyms:	Kiaa0891

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1360 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
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.
Subcellular location	Endoplasmic reticulum membrane; Single-pass membrane protein By similarity.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR By similarity.
Sequence similarities	Contains 2 CS domains. Contains 1 MYND-type zinc finger.
Sequence caution	The sequence BAC65678.4 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing
Domain	Repeat Transmembrane Transmembrane helix Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Protease Thiol protease
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	ER-associated protein catabolic process Inferred from sequence or structural similarity. 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 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 component	cytosol Inferred from direct assay. Source: UniProtKB endoplasmic reticulum membrane Inferred from sequence or structural similarity. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ubiquitin thiolesterase activity Inferred from electronic annotation. Source: InterPro ubiquitin-specific protease activity Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1360	1360	Ubiquitin carboxyl-terminal hydrolase 19		PRO_0000295157
Regions
	Topological domain	1 – 1333	1333	Cytoplasmic Potential
	Transmembrane	1334 – 1354	21	Helical; Potential
	Topological domain	1355 – 1360	6	Lumenal Potential
	Domain	51 – 140	90	CS 1
	Domain	322 – 424	103	CS 2
	Zinc finger	833 – 875	43	MYND-type
	Compositional bias	524 – 530	7	Poly-Glu
Sites
	Active site	548	1	Nucleophile By similarity
	Active site	1207	1	Proton acceptor By similarity
Amino acid modifications
	Modified residue	1284	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	1286 – 1340	55	ASRIW…LGTVA → GLGPGQAPEVAPTRTAPERF APPVDRPAPTYSNMEEVD in isoform 2.		VSP_026769
	Alternative sequence	1341 – 1360	20	Missing in isoform 2.		VSP_026770
Experimental info
	Sequence conflict	140	1	L → LK in BAE42739. Ref.2
	Sequence conflict	142	1	P → S in AAH60613. Ref.3
	Sequence conflict	430 – 431	2	Missing in BAE42739. Ref.2
	Sequence conflict	669	1	A → T in BAE42739. Ref.2
	Sequence conflict	1058	1	D → E in BAE42739. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 11, 2005. Version 1. Checksum: FE9C3020D2CD9AED	FASTA	1,360	150,549
	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
	Isoform 2 [UniParc]. Checksum: 73E85AA9778738F7	FASTA	1,323	146,283
	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 AAASQGLGPG QAPEVAPTRT APERFAPPVD RPAPTYSNME EVD

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: 12693553] [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. , 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: 16141072] [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: 15489334] [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.
+	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.
IPI	IPI00420483. IPI00457619.
RefSeq	NP_001161843.1. NM_001168371.2. NP_001161844.1. NM_001168372.2. NP_001161845.1. NM_001168373.2. NP_082080.3. NM_027804.4. NP_663382.2. NM_145407.3.
UniGene	Mm.289706.
3D structure databases
HSSP	HSSP built from PDB template 2GFO based on UniProtKB P40818.
ProteinModelPortal	Q3UJD6.
SMR	Q3UJD6. Positions 306-444, 532-722.
ModBase	Search...
Protein-protein interaction databases
STRING	Q3UJD6.
Protein family/group databases
MEROPS	C19.024.
PTM databases
PhosphoSite	Q3UJD6.
Proteomic databases
PRIDE	Q3UJD6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000006854; ENSMUSP00000006854; ENSMUSG00000006676. ENSMUST00000085044; ENSMUSP00000082119; ENSMUSG00000006676.
GeneID	71472.
KEGG	mmu:71472.
UCSC	uc009rpt.2. mouse. uc009rpu.2. mouse.
Organism-specific databases
CTD	10869.
MGI	MGI:1918722. Usp19.
Rouge	Search...
Phylogenomic databases
eggNOG	roNOG11044.
GeneTree	ENSGT00600000084034.
HOVERGEN	HBG061889.
OrthoDB	EOG4NVZJG.
PhylomeDB	Q3UJD6.
Gene expression databases
ArrayExpress	Q3UJD6.
Bgee	Q3UJD6.
CleanEx	MM_USP19.
Genevestigator	Q3UJD6.
Family and domain databases
InterPro	IPR007052. CS-like_domain. IPR017447. CS_domain. IPR015054. DUF1872. IPR008978. HSP20-like_chaperone. IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. IPR002893. Znf_MYND. [Graphical view]
KO	K11847.
Pfam	PF04969. CS. 1 hit. PF08959. DUF1872. 1 hit. PF00443. UCH. 1 hit. PF01753. zf-MYND. 1 hit. [Graphical view]
SUPFAM	SSF49764. HSP20_chap. 2 hits.
PROSITE	PS51203. CS. 2 hits. PS00972. UCH_2_1. 1 hit. PS00973. UCH_2_2. 1 hit. PS50235. UCH_2_3. 1 hit. PS01360. ZF_MYND_1. 1 hit. PS50865. ZF_MYND_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	333851.
SOURCE	Search...

Entry information

Entry name

UBP19_MOUSE

Accession

Primary (citable) accession number: Q3UJD6
Secondary accession number(s): Q3TAC9 , Q3TUE6, Q6P9T0, Q80TP5, Q80ZW5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 10, 2007
Last sequence update:	October 11, 2005
Last modified:	November 16, 2011
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program