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Q9D9M2

- UBP12_MOUSE

UniProt

Q9D9M2 - UBP12_MOUSE

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Protein

Ubiquitin carboxyl-terminal hydrolase 12

Gene

Usp12

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

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).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei48 – 481NucleophilePROSITE-ProRule annotation
Active sitei317 – 3171Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: UniProtKB
  2. ubiquitin-specific protease activity Source: UniProtKB
  3. ubiquitin thiolesterase activity Source: UniProtKB

GO - Biological processi

  1. protein deubiquitination Source: UniProtKB
  2. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Protein family/group databases

MEROPSiC19.020.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Usp12
Synonyms:Ubh1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:1270128. Usp12.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 370370Ubiquitin carboxyl-terminal hydrolase 12PRO_0000260312Add
BLAST

Proteomic databases

MaxQBiQ9D9M2.
PaxDbiQ9D9M2.
PRIDEiQ9D9M2.

PTM databases

PhosphoSiteiQ9D9M2.

Expressioni

Gene expression databases

BgeeiQ9D9M2.
CleanExiMM_USP12.
GenevestigatoriQ9D9M2.

Interactioni

Subunit structurei

Interacts with WDR48.By similarity

Protein-protein interaction databases

IntActiQ9D9M2. 1 interaction.
MINTiMINT-4127824.

Structurei

3D structure databases

ProteinModelPortaliQ9D9M2.
SMRiQ9D9M2. Positions 40-369.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 369331USPAdd
BLAST

Sequence similaritiesi

Contains 1 USP domain.Curated

Phylogenomic databases

eggNOGiCOG5077.
GeneTreeiENSGT00650000093027.
HOGENOMiHOG000231498.
HOVERGENiHBG054038.
InParanoidiQ9D9M2.
KOiK11842.
OMAiSKFASFC.
OrthoDBiEOG7RBZ8G.
PhylomeDBiQ9D9M2.
TreeFamiTF314144.

Family and domain databases

InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
[Graphical view]
PfamiPF00443. UCH. 1 hit.
[Graphical view]
PROSITEiPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9D9M2-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MEILMTVSKF ASICTMGANA SALEKEIGPE QFPVNEHYFG LVNFGNTCYC
60 70 80 90 100
NSVLQALYFC RPFREKVLAY KSQPRKKENL LTCLADLFHS IATQKKKVGV
110 120 130 140 150
IPPKKFITRL RKENELFDNY MQQDAHEFLN YLLNTIADIL QEERKQEKQN
160 170 180 190 200
GRLRNGDVDN EDNNSTPDPT WVHEIFQGTL TNETRCLTCE TISSKDEDFL
210 220 230 240 250
DLSVDVEQNT SITHCLRGFS NTETLCSEYK YYCEECRSKQ EAHKRMKVKK
260 270 280 290 300
LPLILALHLK RFKYMDQLHR YTKLSYRVVF PLELRLFNTS GDATNPDRMY
310 320 330 340 350
DLVAVVVHCG SGPNRGHYIA IVKSHDFWLL FDDDIVEKID AQAIEEFYGL
360 370
TSDISKNSES GYILFYQSRD
Length:370
Mass (Da):42,914
Last modified:July 5, 2004 - v2
Checksum:iB11AC16D9B12EBB8
GO
Isoform 2 (identifier: Q9D9M2-2) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:250
Mass (Da):29,157
Checksum:i4FBC07CA0DABD050
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 120120Missing in isoform 2. 1 PublicationVSP_037617Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS39395.1. [Q9D9M2-1]
RefSeqiNP_035799.1. NM_011669.3. [Q9D9M2-1]
XP_006504880.1. XM_006504817.1.
XP_006504881.1. XM_006504818.1. [Q9D9M2-2]
UniGeneiMm.167971.

Genome annotation databases

EnsembliENSMUST00000085614; ENSMUSP00000082754; ENSMUSG00000029640. [Q9D9M2-1]
GeneIDi22217.
KEGGimmu:22217.
UCSCiuc009anj.1. mouse. [Q9D9M2-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS39395.1. [Q9D9M2-1 ]
RefSeqi NP_035799.1. NM_011669.3. [Q9D9M2-1 ]
XP_006504880.1. XM_006504817.1.
XP_006504881.1. XM_006504818.1. [Q9D9M2-2 ]
UniGenei Mm.167971.

3D structure databases

ProteinModelPortali Q9D9M2.
SMRi Q9D9M2. Positions 40-369.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9D9M2. 1 interaction.
MINTi MINT-4127824.

Protein family/group databases

MEROPSi C19.020.

PTM databases

PhosphoSitei Q9D9M2.

Proteomic databases

MaxQBi Q9D9M2.
PaxDbi Q9D9M2.
PRIDEi Q9D9M2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000085614 ; ENSMUSP00000082754 ; ENSMUSG00000029640 . [Q9D9M2-1 ]
GeneIDi 22217.
KEGGi mmu:22217.
UCSCi uc009anj.1. mouse. [Q9D9M2-1 ]

Organism-specific databases

CTDi 219333.
MGIi MGI:1270128. Usp12.

Phylogenomic databases

eggNOGi COG5077.
GeneTreei ENSGT00650000093027.
HOGENOMi HOG000231498.
HOVERGENi HBG054038.
InParanoidi Q9D9M2.
KOi K11842.
OMAi SKFASFC.
OrthoDBi EOG7RBZ8G.
PhylomeDBi Q9D9M2.
TreeFami TF314144.

Miscellaneous databases

NextBioi 302225.
PROi Q9D9M2.
SOURCEi Search...

Gene expression databases

Bgeei Q9D9M2.
CleanExi MM_USP12.
Genevestigatori Q9D9M2.

Family and domain databases

InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
[Graphical view ]
Pfami PF00443. UCH. 1 hit.
[Graphical view ]
PROSITEi PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiUBP12_MOUSE
AccessioniPrimary (citable) accession number: Q9D9M2
Secondary accession number(s): Q790B0
, Q7TNV4, Q80Y43, Q8CBN8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: July 5, 2004
Last modified: October 29, 2014
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3