Reviewed, UniProtKB/Swiss-Prot Q9JMA1 (UBP14_MOUSE)

Names and origin

Protein names

Recommended name:
    Ubiquitin carboxyl-terminal hydrolase 14
    EC=3.1.2.15
Alternative name(s):
    Ubiquitin thioesterase 14
    Ubiquitin-specific-processing protease 14
    Deubiquitinating enzyme 14

Gene names

Name:

Usp14

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

Protein attributes

Sequence length	493 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Ubiquitin C-terminal thioester + H2O = ubiquitin + a thiol.
Subunit structure	Homodimer Potential.
Sequence similarities	Belongs to the peptidase C19 family. Contains 1 ubiquitin-like domain.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Molecular function	Hydrolase Protease Thiol protease
PTM	Acetylation Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	synaptic transmission Inferred from mutant phenotype. Source: MGI ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	soluble fraction Inferred from direct assay. Source: MGI synaptosome Inferred from direct assay. Source: MGI
Molecular function	cysteine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin thiolesterase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 493

492

Ubiquitin carboxyl-terminal hydrolase 14

PRO_0000080637

Regions

Domain

4 – 80

77

Ubiquitin-like

Sites

Active site

114

1

By similarity

Active site

425

1

By similarity

Active site

434

1

By similarity

Amino acid modifications

Modified residue

136

1

Phosphotyrosine Ref.4

Modified residue

143

1

Phosphoserine Ref.4

Modified residue

222

1

Phosphoserine Ref.4

Modified residue

291

1

N6-acetyllysine By similarity

Modified residue

313

1

N6-acetyllysine By similarity

Modified residue

448

1

N6-acetyllysine By similarity

Experimental info

Sequence conflict

185

1

Q → R in BAA93551. Ref.1

Sequence conflict

310

1

L → S in BAA93551. Ref.1

Sequence conflict

385

1

Q → E in BAB27544. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

493

Helix Strand Turn

Details...

Beta strand

4 – 10

7

Beta strand

13 – 24

12

Helix

26 – 36

11

Turn

41 – 43

3

Beta strand

68 – 70

3

Sequences

	Sequence		Length	Mass (Da)
	Q9JMA1-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 4E5F5DCB86057FF9	FASTA	493	56,002
	10 20 30 40 50 60 MPLYSVTVKW GKEKFEGVEL NTDEPPMVFK AQLFALTGVQ PARQKVMVKG GTLKDDDWGN 70 80 90 100 110 120 IKMKNGMTVL MMGSADALPE EPSAKTVFVE DMTEEQLATA MELPCGLTNL GNTCYMNATV 130 140 150 160 170 180 QCIRSVPELK DALKRYAGAL RASGEMASAQ YITAALRDLF DSMDKTSSSI PPIILLQFLH 190 200 210 220 230 240 MAFPQFAEKG EQGQYLQQDA NECWIQMMRV LQQKLEAIED DSGRETDSSS APAVTPSKKK 250 260 270 280 290 300 SLIDQYFGVE FETTMKCTES EEEEVTKGKE NQLQLSCFIN QEVKYLFTGL KLRLQEEITK 310 320 330 340 350 360 QSPTLQRNAL YIKSSKISRL PAYLTIQMVR FFYKEKESVN AKVLKDVKFP LMLDVYELCT 370 380 390 400 410 420 PELQEKMVSF RSKFKDLEDK KVNQQPNAND KNSPPKEIKY EPFSFADDIG SNNCGYYDLQ 430 440 450 460 470 480 AVLTHQGRSS SSGHYVSWVR RKQDEWIKFD DDKVSIVTPE DILRLSGGGD WHIAYVLLYG 490 PRRVEIMEEE SEQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mouse deubiquitinating enzyme-type TGT." Hidaka T., Morishita T. Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: 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]. Strain: C57BL/6J. Tissue: Corpora quadrigemina, Embryo and Testis.
[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].
[4]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-136; SER-143 AND SER-222, MASS SPECTROMETRY. Tissue: Liver.
[5]	"Solution structure of the N-terminal ubiquitin-like domain of mouse ubiquitin specific protease 14 (usp14)." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2004) to the PDB data bank Cited for: STRUCTURE BY NMR OF 4-86.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB034633 mRNA. Translation: BAA93551.1.
AK011322 mRNA. Translation: BAB27544.1.
AK029977 mRNA. Translation: BAC26713.1.
AK045909 mRNA. Translation: BAC32528.1.
BC005571 mRNA. Translation: AAH05571.1.

IPI

IPI00270877.

RefSeq

NP_067497.2.

UniGene

Mm.219648
Mm.329277
Mm.447089

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WGG	NMR	-	A	4-85	[»]

SMR

Q9JMA1. Positions 98-482.

ModBase

Search...

Protein-protein interaction databases

STRING

Q9JMA1.

Protein family/group databases

MEROPS

C19.015.

PTM databases

PhosphoSite

Q9JMA1.

Proteomic databases

PRIDE

Q9JMA1.

Genome annotation databases

Ensembl

ENSMUST00000092096; ENSMUSP00000089728; ENSMUSG00000047879; Mus musculus. [Genome view]

GeneID

59025.

UCSC

uc008ean.1. mouse.

Organism-specific databases

CTD

59025.

MGI

MGI:1928898. Usp14.

Phylogenomic databases

HOVERGEN

Q9JMA1.

OMA

ITHKGRS.

PhylomeDB

Q9JMA1.

Enzyme and pathway databases

BRENDA

3.1.2.15. 244.

Gene expression databases

ArrayExpress

Q9JMA1.

Bgee

Q9JMA1.

CleanEx

MM_USP14.

Genevestigator

Q9JMA1.

GermOnline

ENSMUSG00000047879. Mus musculus.

Family and domain databases

InterPro

IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19.
IPR000626. Ubiquitin.
IPR019954. Ubiquitin_CS.
IPR019955. Ubiquitin_supergroup.
[Graphical view]

Pfam

PF00443. UCH. 1 hit.
[Graphical view]

SMART

SM00213. UBQ. 1 hit.
[Graphical view]

PROSITE

PS00299. UBIQUITIN_1. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
PS00972. UCH_2_1. 1 hit.
PS00973. UCH_2_2. 1 hit.
PS50235. UCH_2_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

314596.

SOURCE

Search...

Entry information

Entry name

UBP14_MOUSE

Accession

Primary (citable) accession number: Q9JMA1
Secondary accession number(s): Q543U5, Q923F2, Q9D0L0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 16, 2002
Last sequence update:	January 23, 2007
Last modified:	January 19, 2010
This is version 89 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)