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Q3UN04 (UBP30_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 53. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin carboxyl-terminal hydrolase 30
EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 30
Ubiquitin thioesterase 30
Ubiquitin-specific-processing protease 30
Short name=Ub-specific protease 30
Gene names
Name:Usp30
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length517 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

May participate in the maintenance of mitochondrial morphology 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).

Subcellular location

Mitochondrion outer membrane By similarity.

Sequence similarities

Belongs to the peptidase C19 family.

Sequence caution

The sequence AAH38606.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 517517Ubiquitin carboxyl-terminal hydrolase 30
PRO_0000377537

Regions

Topological domain1 – 3535Mitochondrial intermembrane Potential
Transmembrane36 – 5621Helical; Potential
Topological domain57 – 517461Cytoplasmic Potential

Sites

Active site771Nucleophile By similarity
Active site4521Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3UN04 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: 561866EF23103048

FASTA51758,221
        10         20         30         40         50         60 
MLSSRAQAAR TAADKALQRF LRTGAAVRYK VMKNWGVIGG IAAALAAGIY VIWGPITERK 

        70         80         90        100        110        120 
KRRKGLVPGL VNLGNTCFMN SLLQGLSACP AFVKWLEEFT TQYSRDQQGP HTHQCLSLTL 

       130        140        150        160        170        180 
LNLLKALSCQ EVTEDEVLDA SCLLDVLRMY RWQISSFEEQ DAHELFHVIT SSLEDERDRQ 

       190        200        210        220        230        240 
PRVTHLFDVH SLEQQSEMAP RQVTCHTRGS PHPTTNHWKS QHPFHGRLTS NMVCKHCEHQ 

       250        260        270        280        290        300 
SPVRFDTFDS LSLSIPAATW GHPLTLDHCL HHFISSESVR DVVCDNCTKI EARGTLTGEK 

       310        320        330        340        350        360 
VEHQRSTFVK QLKLGKLPQC LCIHLQRLSW SSHGTPLKRH EHVQFNEFLM MDFYKYRLLG 

       370        380        390        400        410        420 
HKPSQHGPKA TENPGSAPEV QDAQAAPKPG LSQPGAPKTQ IFLNGACSPS LLPALPSPVA 

       430        440        450        460        470        480 
FPLPVVPDYS SSTYLFRLMA VVVHHGDMHS GHFVTYRRSP PSAKNPLSTS NQWLWISDDT 

       490        500        510 
VRKASLQEVL SSSAYLLFYE RVLSRVQQQG REYRSEE

« Hide

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].
Strain: C57BL/6J.
Tissue: Embryo, Lung and Medulla oblongata.
[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].
Strain: FVB/N.
Tissue: Salivary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK078164 mRNA. Translation: BAC37154.1.
AK144578 mRNA. Translation: BAE25944.1.
AK162153 mRNA. Translation: BAE36756.1.
AK162269 mRNA. Translation: BAE36827.1.
BC038606 mRNA. Translation: AAH38606.1. Different initiation.
IPIIPI00229762.
RefSeqNP_001028374.1. NM_001033202.3.
UniGeneMm.240421.

3D structure databases

ProteinModelPortalQ3UN04.
SMRQ3UN04. Positions 69-331, 415-501.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000031588.

Protein family/group databases

MEROPSC19.060.

Proteomic databases

PaxDbQ3UN04.
PRIDEQ3UN04.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031588; ENSMUSP00000031588; ENSMUSG00000029592.
GeneID100756.
KEGGmmu:100756.
UCSCuc008yzc.1. mouse.

Organism-specific databases

CTD84749.
MGIMGI:2140991. Usp30.

Phylogenomic databases

eggNOGNOG259866.
GeneTreeENSGT00550000075075.
HOGENOMHOG000065744.
InParanoidQ8BVI3.
KOK11851.
OMAMDIYKYR.
OrthoDBEOG451DQH.

Gene expression databases

BgeeQ3UN04.
GenevestigatorQ3UN04.

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

NextBio354628.
SOURCESearch...

Entry information

Entry nameUBP30_MOUSE
AccessionPrimary (citable) accession number: Q3UN04
Secondary accession number(s): Q3TS48 expand/collapse secondary AC list , Q3TSB9, Q8BVI3, Q8CHW7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2009
Last sequence update: October 11, 2005
Last modified: May 1, 2013
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents