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Q9D9M2 (UBP12_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length370 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Contains 1 USP domain.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 370370Ubiquitin carboxyl-terminal hydrolase 12
PRO_0000260312

Regions

Domain39 – 369331USP

Sites

Active site481Nucleophile By similarity
Active site3171Proton acceptor By similarity

Natural variations

Alternative sequence1 – 120120Missing in isoform 2.
VSP_037617

Sequences

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

Last modified July 5, 2004. Version 2.
Checksum: B11AC16D9B12EBB8

FASTA37042,914
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 4FBC07CA0DABD050
Show »

FASTA25029,157

References

« Hide '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. 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] (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.
RefSeqNP_035799.1. NM_011669.3.
XP_006504880.1. XM_006504817.1.
XP_006504881.1. XM_006504818.1.
UniGeneMm.167971.

3D structure databases

ProteinModelPortalQ9D9M2.
SMRQ9D9M2. Positions 40-369.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9D9M2. 1 interaction.
MINTMINT-4127824.

Protein family/group databases

MEROPSC19.020.

PTM databases

PhosphoSiteQ9D9M2.

Proteomic databases

PaxDbQ9D9M2.
PRIDEQ9D9M2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000085614; ENSMUSP00000082754; ENSMUSG00000029640. [Q9D9M2-1]
GeneID22217.
KEGGmmu:22217.
UCSCuc009anj.1. mouse. [Q9D9M2-1]

Organism-specific databases

CTD219333.
MGIMGI:1270128. Usp12.

Phylogenomic databases

eggNOGCOG5077.
GeneTreeENSGT00650000093027.
HOGENOMHOG000231498.
HOVERGENHBG054038.
InParanoidQ80Y43.
KOK11842.
OMASKFASFC.
OrthoDBEOG7RBZ8G.
PhylomeDBQ9D9M2.
TreeFamTF314144.

Gene expression databases

BgeeQ9D9M2.
CleanExMM_USP12.
GenevestigatorQ9D9M2.

Family and domain databases

InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
[Graphical view]
PfamPF00443. UCH. 1 hit.
[Graphical view]
PROSITEPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio302225.
PROQ9D9M2.
SOURCESearch...

Entry information

Entry nameUBP12_MOUSE
AccessionPrimary (citable) accession number: Q9D9M2
Secondary accession number(s): Q790B0 expand/collapse secondary AC list , Q7TNV4, Q80Y43, Q8CBN8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 93 of the entry and version 2 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

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

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