Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q9D9M2 (UBP12_MOUSE)

Last modified November 3, 2009. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Ubiquitin carboxyl-terminal hydrolase 12
    EC=3.1.2.15
Alternative name(s):
    Ubiquitin thioesterase 12
    Ubiquitin-specific-processing protease 12
    Deubiquitinating enzyme 12
    Ubiquitin-hydrolyzing enzyme 1
Gene names
Name: Usp12
Synonyms: Ubh1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length370 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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

Ubiquitin C-terminal thioester + H2O = ubiquitin + a thiol.

Subunit structure

Interacts with WDR48 By similarity.

Sequence similarities

Belongs to the peptidase C19 family. USP12/USP46 subfamily.

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

Sites

Active site481 By similarity
Active site3081 By similarity
Active site3171 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.

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: 16141072] [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: 15489334] [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: 12391724] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-370 (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Testis.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
IPIIPI00228375.
IPI00938515.
RefSeqNP_035799.1.
UniGeneMm.167971

3D structure databases

HSSPHSSP built from PDB template 1NBF based on UniProtKB Q93009.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9D9M2.

Protein family/group databases

MEROPSC19.020.

Proteomic databases

PRIDEQ9D9M2.

Genome annotation databases

EnsemblENSMUST00000085614; ENSMUSP00000082754; ENSMUSG00000029640; Mus musculus. [Genome view]
GeneID22217.
KEGGmmu:22217.
UCSCuc009anj.1. mouse.

Organism-specific databases

CTD22217.
MGIMGI:1270128. Usp12.

Phylogenomic databases

HOVERGENQ9D9M2.
OMAQPRRKEN.

Enzyme and pathway databases

BRENDA3.1.2.15. 244.

Gene expression databases

ArrayExpressQ9D9M2.
BgeeQ9D9M2.
CleanExMM_USP12.
GenevestigatorQ9D9M2.
GermOnlineENSMUSG00000029640. Mus musculus.

Family and domain databases

InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19.
[Graphical view]
PfamPF00443. UCH. 1 hit.
[Graphical view]
PROSITEPS00972. UCH_2_1. 1 hit.
PS00973. UCH_2_2. 1 hit.
PS50235. UCH_2_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio302225.
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: November 3, 2009
This is version 60 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents