Q9D9M2 (UBP12_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin carboxyl-terminal hydrolase 12
EC=3.4.19.12

Alternative name(s):
Deubiquitinating enzyme 12
Ubiquitin thioesterase 12
Ubiquitin-hydrolyzing enzyme 1
Ubiquitin-specific-processing protease 12

Gene names

Name:	Usp12
Synonyms:	Ubh1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	370 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Deubiquitinating enzyme. Has almost no deubiquitinating activity by itself and requires the interaction with WDR48 to have a high activity. Not involved in deubiquitination of monoubiquitinated FANCD2 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 WDR48 By similarity.
Sequence similarities	Belongs to the peptidase C19 family. USP12/USP46 subfamily.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Coding sequence diversity	Alternative splicing
Molecular function	Hydrolase Protease Thiol protease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein deubiquitination Inferred from sequence or structural similarity. Source: UniProtKB ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	cysteine-type endopeptidase activity Inferred from sequence or structural similarity. Source: UniProtKB ubiquitin thiolesterase activity Inferred from sequence or structural similarity. Source: UniProtKB ubiquitin-specific protease activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9D9M2-1)

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: Q9D9M2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-120: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 370	370	Ubiquitin carboxyl-terminal hydrolase 12		PRO_0000260312
Sites
	Active site	48	1	Nucleophile By similarity
	Active site	317	1	Proton acceptor By similarity
Natural variations
	Alternative sequence	1 – 120	120	Missing in isoform 2.		VSP_037617

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 5, 2004. Version 2. Checksum: B11AC16D9B12EBB8	FASTA	370	42,914
	10 20 30 40 50 60 MEILMTVSKF ASICTMGANA SALEKEIGPE QFPVNEHYFG LVNFGNTCYC NSVLQALYFC 70 80 90 100 110 120 RPFREKVLAY KSQPRKKENL LTCLADLFHS IATQKKKVGV IPPKKFITRL RKENELFDNY 130 140 150 160 170 180 MQQDAHEFLN YLLNTIADIL QEERKQEKQN GRLRNGDVDN EDNNSTPDPT WVHEIFQGTL 190 200 210 220 230 240 TNETRCLTCE TISSKDEDFL DLSVDVEQNT SITHCLRGFS NTETLCSEYK YYCEECRSKQ 250 260 270 280 290 300 EAHKRMKVKK LPLILALHLK RFKYMDQLHR YTKLSYRVVF PLELRLFNTS GDATNPDRMY 310 320 330 340 350 360 DLVAVVVHCG SGPNRGHYIA IVKSHDFWLL FDDDIVEKID AQAIEEFYGL TSDISKNSES 370 GYILFYQSRD
	Isoform 2 [UniParc]. Checksum: 4FBC07CA0DABD050	FASTA	250	29,157
	10 20 30 40 50 60 MQQDAHEFLN YLLNTIADIL QEERKQEKQN GRLRNGDVDN EDNNSTPDPT WVHEIFQGTL 70 80 90 100 110 120 TNETRCLTCE TISSKDEDFL DLSVDVEQNT SITHCLRGFS NTETLCSEYK YYCEECRSKQ 130 140 150 160 170 180 EAHKRMKVKK LPLILALHLK RFKYMDQLHR YTKLSYRVVF PLELRLFNTS GDATNPDRMY 190 200 210 220 230 240 DLVAVVVHCG SGPNRGHYIA IVKSHDFWLL FDDDIVEKID AQAIEEFYGL TSDISKNSES 250 GYILFYQSRD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: C57BL/6J. Tissue: Testis and Urinary bladder.
[2]	"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] (ISOFORMS 1 AND 2). Strain: C57BL/6 and FVB/N. Tissue: Brain and Liver.
[3]	"Molecular cloning and complete cDNA sequence of UBH1 in mouse testis." Baek K.-H., Park K.-H., Kim Y.-S., Kim M.-S., Choi H.-K. DNA Seq. 13:145-148(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-370 (ISOFORM 1). Strain: C57BL/6J. Tissue: Testis.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK006739 mRNA. Translation: BAB24720.2. AK035629 mRNA. Translation: BAC29129.1. AK167153 mRNA. Translation: BAE39295.1. BC049274 mRNA. Translation: AAH49274.1. BC055398 mRNA. Translation: AAH55398.1. BC068136 mRNA. Translation: AAH68136.1. AF441835 mRNA. Translation: AAL86740.1.
IPI	IPI00228375. IPI00938515.
RefSeq	NP_035799.1. NM_011669.3.
UniGene	Mm.167971.
3D structure databases
HSSP	HSSP built from PDB template 1NBF based on UniProtKB Q93009.
ProteinModelPortal	Q9D9M2.
SMR	Q9D9M2. Positions 40-369.
ModBase	Search...
Protein family/group databases
MEROPS	C19.020.
PTM databases
PhosphoSite	Q9D9M2.
Proteomic databases
PaxDb	Q9D9M2.
PRIDE	Q9D9M2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000085614; ENSMUSP00000082754; ENSMUSG00000029640.
GeneID	22217.
KEGG	mmu:22217.
UCSC	uc008xtg.1. mouse.
Organism-specific databases
CTD	219333.
MGI	MGI:1270128. Usp12.
Phylogenomic databases
eggNOG	COG5077.
GeneTree	ENSGT00650000093027.
HOGENOM	HOG000231498.
HOVERGEN	HBG054038.
InParanoid	Q80Y43.
KO	K11842.
OMA	SKFASFC.
OrthoDB	EOG42Z4Q8.
Gene expression databases
Bgee	Q9D9M2.
CleanEx	MM_USP12.
Genevestigator	Q9D9M2.
GermOnline	ENSMUSG00000029640. Mus musculus.
Family and domain databases
InterPro	IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. [Graphical view]
Pfam	PF00443. UCH. 1 hit. [Graphical view]
PROSITE	PS00972. UCH_2_1. 1 hit. PS00973. UCH_2_2. 1 hit. PS50235. UCH_2_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	302225.
SOURCE	Search...

Entry information

Entry name

UBP12_MOUSE

Accession

Primary (citable) accession number: Q9D9M2
Secondary accession number(s): Q790B0 , Q7TNV4, Q80Y43, Q8CBN8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	July 5, 2004
Last modified:	May 1, 2013
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program