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Q8R5H1

- UBP15_MOUSE

UniProt

Q8R5H1 - UBP15_MOUSE

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Protein
Ubiquitin carboxyl-terminal hydrolase 15
Gene
Usp15, Kiaa0529
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Hydrolase that removes conjugated ubiquitin from target proteins and regulates various pathways such as the TGF-beta receptor signaling and NF-kappa-B pathways. Acts as a key regulator of TGF-beta receptor signaling pathway, but the precise mechanism is still unclear: according to a report, acts by promoting deubiquitination of monoubiquitinated R-SMADs (SMAD1, SMAD2 and/or SMAD3), thereby alleviating inhibition of R-SMADs and promoting activation of TGF-beta target genes. According to another reports, regulates the TGF-beta receptor signaling pathway by mediating deubiquitination and stabilization of TGFBR1, leading to an enhanced TGF-beta signal. Able to mediate deubiquitination of monoubiquitinated substrates as well as 'Lys-48'-linked polyubiquitin chains, protecting them against proteasomal degradation. Acts as an associated component of COP9 signalosome complex (CSN) and regulates different pathways via this association: regulates NF-kappa-B by mediating deubiquitination of NFKBIA and deubiquitinates substrates bound to VCP 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 sitei298 – 2981Nucleophile By similarityBy similarity
Active sitei891 – 8911Proton acceptor By similarityBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. BMP signaling pathway Source: UniProtKB
  2. monoubiquitinated protein deubiquitination Source: UniProtKB
  3. pathway-restricted SMAD protein phosphorylation Source: UniProtKB
  4. protein deubiquitination Source: UniProtKB
  5. transforming growth factor beta receptor signaling pathway Source: UniProtKB
  6. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_215733. Downregulation of TGF-beta receptor signaling.

Protein family/group databases

MEROPSiC19.022.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin carboxyl-terminal hydrolase 15 (EC:3.4.19.12)
Alternative name(s):
Deubiquitinating enzyme 15
Ubiquitin thioesterase 15
Ubiquitin-specific-processing protease 15
Gene namesi
Name:Usp15
Synonyms:Kiaa0529
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:101857. Usp15.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 981980Ubiquitin carboxyl-terminal hydrolase 15
PRO_0000080642Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei229 – 2291Phosphoserine1 Publication
Modified residuei242 – 2421Phosphoserine By similarity
Modified residuei961 – 9611Phosphoserine By similarity
Modified residuei965 – 9651Phosphoserine By similarity

Post-translational modificationi

Phosphorylated. Phosphorylation protects against ubiquitination and subsequent degradation by the proteasome By similarity.
Ubiquitinated, leading to degradation by the proteasome By similarity.

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ8R5H1.
PaxDbiQ8R5H1.
PRIDEiQ8R5H1.

PTM databases

PhosphoSiteiQ8R5H1.

Expressioni

Tissue specificityi

Widely expressed with highest levels in testis, heart and liver.1 Publication

Gene expression databases

ArrayExpressiQ8R5H1.
BgeeiQ8R5H1.
CleanExiMM_USP15.
GenevestigatoriQ8R5H1.

Interactioni

Subunit structurei

Identified in a complex with the COP9 signalosome complex (CSN). Interacts with SMAD1, SMAD2 and SMAD3; the interaction is direct. Forms a complex with SMURF2 and SMAD7. Interacts with TGFBR1 By similarity.

Protein-protein interaction databases

IntActiQ8R5H1. 1 interaction.
MINTiMINT-4139191.

Structurei

3D structure databases

ProteinModelPortaliQ8R5H1.
SMRiQ8R5H1. Positions 2-222, 285-470, 786-934.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 118112DUSP
Add
BLAST
Domaini289 – 933645USP
Add
BLAST

Sequence similaritiesi

Belongs to the peptidase C19 family.
Contains 1 DUSP domain.
Contains 1 USP domain.

Phylogenomic databases

eggNOGiCOG5560.
GeneTreeiENSGT00670000097750.
HOGENOMiHOG000264375.
HOVERGENiHBG000864.
InParanoidiQ8R5H1.
KOiK11835.
OMAiRYVKTCT.
OrthoDBiEOG77Q4VW.
PhylomeDBiQ8R5H1.
TreeFamiTF106276.

Family and domain databases

Gene3Di3.30.2230.10. 1 hit.
InterProiIPR006615. Pept_C19_DUSP.
IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b.
IPR028135. Ub_USP-typ.
IPR029071. Ubiquitin-rel_dom.
IPR028889. UCH/PAN2.
[Graphical view]
PfamiPF06337. DUSP. 1 hit.
PF14836. Ubiquitin_3. 1 hit.
PF00443. UCH. 1 hit.
[Graphical view]
SMARTiSM00695. DUSP. 1 hit.
[Graphical view]
SUPFAMiSSF143791. SSF143791. 1 hit.
SSF54236. SSF54236. 1 hit.
SSF55205. SSF55205. 1 hit.
PROSITEiPS51283. DUSP. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. Align

Note: Experimental confirmation may be lacking for some isoforms.

Isoform 1 (identifier: Q8R5H1-1) [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

MAEGGAADLD TQRSDIATLL KTSLRKGDTW YLVDSRWFKQ WKKYVGFDSW    50
DKYQMGDQNV YPGPIDNSGL LKDGDAQSLK EHLIDELDYI LLPTEGWNKL 100
VSWYTLMEGQ EPIARKVVEQ GMFVKHCKVE VYLTELKLCE NGNMNNVVTR 150
RFSKADTIDT IEKEIRKIFN IPDEKEARLW NKYMSNTFEP LNKPDSTIQD 200
AGLYQGQVLV IEQKNEDGTW PRGPSTPKSP GASNFSTLPK ISPSSLSNNY 250
NNINNRNVKN SNYCLPSYTA YKNYDYSEPG RNNEQPGLCG LSNLGNTCFM 300
NSAIQCLSNT PPLTEYFLND KYQEELNFDN PLGMRGEIAK SYAELIKQMW 350
SGKFSYVTPR AFKTQVGRFA PQFSGYQQQD CQELLAFLLD GLHEDLNRIR 400
KKPYIQLKDA DGRPDKVVAE EAWENHLKRN DSIIVDIFHG LFKSTLVCPE 450
CAKISVTFDP FCYLTLPLPM KKERSLEVYL VRMDPLAKPM QYKVIVPKIG 500
NILDLCTALS ALSGVPADKM IVTDIYNHRF HRIFAVDENL SSIMERDDIY 550
VFEININRAE DTEHVVIPVC LREKFRHSSY THHTGSSLFG QPFLMAIPRN 600
NTEDKLYNLL LLRMCRYVKM STETEETDGH LRCCEDQNIN GNGPNGLHEE 650
GSPSEMETDE PDDESSQDQE LPSENENSQS EDSVGGDNDS ENGLCTEETC 700
KGQLTGHKKR LFTFQFNNLG NNDINYIKDD TSHIRFDDRQ LRLDERSFLA 750
LDWDPDLKKR YFDENAAEDF EKHESVEYKP PKRPFVKLKD CIELFTTKEK 800
LGAEDPWYCP NCKEHQQATK KLDLWSLPPV LVVHLKRFSY SRYMRDKLDT 850
LVDFPISDLD MSEFLINPNA GPCRYNLIAV SNHYGGMGGG HYTAFAKNKD 900
DGKWYYFDDS SVSTASEDQI VSKAAYVLFY QRQDTFSGTG FFPLDRETKG 950
ASAATGIPLE SDEDSNDNDN DLENENCMHT N 981
Length:981
Mass (Da):112,325
Last modified:June 1, 2002 - v1
Checksum:i6D5377C3FEA6E40A
GO
Isoform 2 (identifier: Q8R5H1-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     18-25: TLLKTSLR → DAWLKPRSG
     228-256: Missing.

Show »
Length:953
Mass (Da):109,318
Checksum:iD56685B92C029188
GO
Isoform 3 (identifier: Q8R5H1-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     229-981: Missing.

Show »
Length:228
Mass (Da):26,305
Checksum:i43F1F4F48122703B
GO
Isoform 4 (identifier: Q8R5H1-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     209-227: LVIEQKNEDGTWPRGPSTP → PRCIQFFNFTKDLSFISIK
     228-981: Missing.

Show »
Length:227
Mass (Da):26,357
Checksum:iA92B80D4BEE7E26E
GO
Isoform 5 (identifier: Q8R5H1-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     228-256: Missing.

Show »
Length:952
Mass (Da):109,220
Checksum:iD779A1FB3667963A
GO

Sequence cautioni

The sequence BAC65583.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence EDL24441.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei18 – 258TLLKTSLR → DAWLKPRSG in isoform 2. 1 Publication
VSP_005262
Alternative sequencei209 – 22719LVIEQ…GPSTP → PRCIQFFNFTKDLSFISIK in isoform 4.
VSP_005265Add
BLAST
Alternative sequencei228 – 981754Missing in isoform 4.
VSP_005266Add
BLAST
Alternative sequencei228 – 25629Missing in isoform 2 and isoform 5. 1 Publication
VSP_005263Add
BLAST
Alternative sequencei229 – 981753Missing in isoform 3.
VSP_005264Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti130 – 1301E → G in BAE40593. 1 Publication
Sequence conflicti158 – 1581I → M in BAE36413. 1 Publication
Sequence conflicti184 – 1841M → V in AAH50042. 1 Publication
Sequence conflicti662 – 6621D → G in AAH50042. 1 Publication
Sequence conflicti800 – 8001K → E in AAH50042. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF468037 mRNA. Translation: AAL77418.1.
AK046332 mRNA. Translation: BAC32683.1.
AK083303 mRNA. Translation: BAC38854.1.
AK133852 mRNA. Translation: BAE21887.1.
AK145749 mRNA. Translation: BAE26626.1.
AK161469 mRNA. Translation: BAE36413.1.
AK168755 mRNA. Translation: BAE40593.1.
AK122301 mRNA. Translation: BAC65583.1. Different initiation.
CH466578 Genomic DNA. Translation: EDL24441.1. Different initiation.
BC050042 mRNA. Translation: AAH50042.1.
CCDSiCCDS24217.1. [Q8R5H1-1]
RefSeqiNP_081880.2. NM_027604.3. [Q8R5H1-1]
XP_006513287.1. XM_006513224.1. [Q8R5H1-5]
UniGeneiMm.244209.
Mm.470032.

Genome annotation databases

EnsembliENSMUST00000020334; ENSMUSP00000020334; ENSMUSG00000020124. [Q8R5H1-1]
GeneIDi14479.
KEGGimmu:14479.
UCSCiuc007hgn.1. mouse. [Q8R5H1-1]
uc007hgt.1. mouse. [Q8R5H1-3]
uc011xpf.1. mouse. [Q8R5H1-4]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF468037 mRNA. Translation: AAL77418.1 .
AK046332 mRNA. Translation: BAC32683.1 .
AK083303 mRNA. Translation: BAC38854.1 .
AK133852 mRNA. Translation: BAE21887.1 .
AK145749 mRNA. Translation: BAE26626.1 .
AK161469 mRNA. Translation: BAE36413.1 .
AK168755 mRNA. Translation: BAE40593.1 .
AK122301 mRNA. Translation: BAC65583.1 . Different initiation.
CH466578 Genomic DNA. Translation: EDL24441.1 . Different initiation.
BC050042 mRNA. Translation: AAH50042.1 .
CCDSi CCDS24217.1. [Q8R5H1-1 ]
RefSeqi NP_081880.2. NM_027604.3. [Q8R5H1-1 ]
XP_006513287.1. XM_006513224.1. [Q8R5H1-5 ]
UniGenei Mm.244209.
Mm.470032.

3D structure databases

ProteinModelPortali Q8R5H1.
SMRi Q8R5H1. Positions 2-222, 285-470, 786-934.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q8R5H1. 1 interaction.
MINTi MINT-4139191.

Protein family/group databases

MEROPSi C19.022.

PTM databases

PhosphoSitei Q8R5H1.

Proteomic databases

MaxQBi Q8R5H1.
PaxDbi Q8R5H1.
PRIDEi Q8R5H1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000020334 ; ENSMUSP00000020334 ; ENSMUSG00000020124 . [Q8R5H1-1 ]
GeneIDi 14479.
KEGGi mmu:14479.
UCSCi uc007hgn.1. mouse. [Q8R5H1-1 ]
uc007hgt.1. mouse. [Q8R5H1-3 ]
uc011xpf.1. mouse. [Q8R5H1-4 ]

Organism-specific databases

CTDi 9958.
MGIi MGI:101857. Usp15.
Rougei Search...

Phylogenomic databases

eggNOGi COG5560.
GeneTreei ENSGT00670000097750.
HOGENOMi HOG000264375.
HOVERGENi HBG000864.
InParanoidi Q8R5H1.
KOi K11835.
OMAi RYVKTCT.
OrthoDBi EOG77Q4VW.
PhylomeDBi Q8R5H1.
TreeFami TF106276.

Enzyme and pathway databases

Reactomei REACT_215733. Downregulation of TGF-beta receptor signaling.

Miscellaneous databases

ChiTaRSi USP15. mouse.
NextBioi 286150.
PROi Q8R5H1.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8R5H1.
Bgeei Q8R5H1.
CleanExi MM_USP15.
Genevestigatori Q8R5H1.

Family and domain databases

Gene3Di 3.30.2230.10. 1 hit.
InterProi IPR006615. Pept_C19_DUSP.
IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b.
IPR028135. Ub_USP-typ.
IPR029071. Ubiquitin-rel_dom.
IPR028889. UCH/PAN2.
[Graphical view ]
Pfami PF06337. DUSP. 1 hit.
PF14836. Ubiquitin_3. 1 hit.
PF00443. UCH. 1 hit.
[Graphical view ]
SMARTi SM00695. DUSP. 1 hit.
[Graphical view ]
SUPFAMi SSF143791. SSF143791. 1 hit.
SSF54236. SSF54236. 1 hit.
SSF55205. SSF55205. 1 hit.
PROSITEi PS51283. DUSP. 1 hit.
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. "Isolation and characterization of the mouse ubiquitin-specific protease Usp15."
    Angelats C., Wang X.-W., Jermiin L.S., Copeland N.G., Jenkins N.A., Baker R.T.
    Mamm. Genome 14:31-46(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
    Strain: C57BL/6.
  2. "Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
    DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
    Tissue: Brain.
  3. "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] (ISOFORMS 1; 3; 4 AND 5).
    Strain: C57BL/6J.
    Tissue: Amnion, Corpora quadrigemina, Testis and Thymus.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 1).
    Tissue: Trophoblast stem cell.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiUBP15_MOUSE
AccessioniPrimary (citable) accession number: Q8R5H1
Secondary accession number(s): Q3TGF5
, Q3TTB2, Q3UL25, Q3UZH0, Q80TY6, Q80UK9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2003
Last sequence update: June 1, 2002
Last modified: September 3, 2014
This is version 111 of the entry and version 1 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

Similar proteinsi