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Q99LX0 (PARK7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. 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

Names and origin

Protein namesRecommended name:
Protein DJ-1

EC=3.4.-.-
Alternative name(s):
Parkinson disease protein 7 homolog
Gene names
Name:Park7
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length189 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protects cells against oxidative stress and cell death. Plays a role in regulating expression or stability of the mitochondrial uncoupling proteins SLC25A14 and SLC25A27 in dopaminergic neurons of the substantia nigra pars compacta and attenuates the oxidative stress induced by calcium entry into the neurons via L-type channels during pacemaking. Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death. May act as an atypical peroxiredoxin-like peroxidase that scavenges hydrogen peroxide. Following removal of a C-terminal peptide, displays protease activity and enhanced cytoprotective action against oxidative stress-induced apoptosis. Stabilizes NFE2L2 by preventing its association with KEAP1 and its subsequent ubiquitination. Binds to OTUD7B and inhibits its deubiquitinating activity. Enhances RELA nuclear translocation. Binds to a number of mRNAs containing multiple copies of GG or CC motifs and partially inhibits their translation but dissociates following oxidative stress. Required for correct mitochondrial morphology and function and for autophagy of dysfunctional mitochondria. Regulates astrocyte inflammatory responses. Acts as a positive regulator of androgen receptor-dependent transcription. Prevents aggregation of SNCA. Plays a role in fertilization. Has no proteolytic activity. Has cell-growth promoting activity and transforming activity. May function as a redox-sensitive chaperone. May regulate lipid rafts-dependent endocytosis in astrocytes and neuronal cells. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15

Subunit structure

Homodimer. Binds EFCAB6/DJBP and PIAS2. Part of a ternary complex containing PARK7, EFCAB6/DJBP and AR By similarity. Interacts (via N-terminus) with OTUD7B. Interacts with BBS1, CLCF1 and MTERF. Binds to HIPK1 By similarity. Ref.12

Subcellular location

Cell membrane; Lipid-anchor. Cytoplasm By similarity. Membrane raft. Nucleus By similarity. Mitochondrion By similarity. Note: Under normal conditions, located predominantly in the cytoplasm and, to a lesser extent, in the nucleus and mitochondrion. Translocates to the mitochondrion and subsequently to the nucleus in response to oxidative stress and exerts an increased cytoprotective effect against oxidative damage. Membrane raft localization in astrocytes and neuronal cells requires palmitoylation By similarity. Ref.15

Tissue specificity

Expressed in erythroblasts and in mature red blood cells from peripheral blood (at protein level). Ref.11

Developmental stage

Expression increases during erythroid development (at protein level). Ref.11

Induction

By hydrogen peroxide. Ref.6

Post-translational modification

Sumoylated on Lys-130 by PIAS2 or PIAS4; which is essential for cell-growth promoting activity and transforming activity By similarity.

Undergoes cleavage of a C-terminal peptide and subsequent activation of protease activity in response to oxidative stress By similarity.

Disruption phenotype

Increased sensitivity of embryonic cortical neurons to oxidative stress. Age-dependent increase in mitochondrial hydrogen peroxide production and reduced mitochondrial aconitase activity. Down-regulation of Slc25a14 and Slc25a27, compromised calcium-induced uncoupling and increased oxidation of mitochondrial matrix proteins specifically in the dopaminergic neurons of the substantia nigra pars compacta. Reduced N2el2 protein expression. Impaired mitochondrial function and morphology with reduced autophagy leading to accumulation of defective mitochondria. Targeted knockouts in astrocytes exhibit augmented LPS-induced CRK/p38 phosphorylation and signaling, they don't stimulate TLR4 endocytosis upon LPS stimulation. Ref.7 Ref.8 Ref.9 Ref.13 Ref.14 Ref.15

Sequence similarities

Belongs to the peptidase C56 family.

Ontologies

Keywords
   Biological processAutophagy
Fertilization
Inflammatory response
Stress response
   Cellular componentCell membrane
Cytoplasm
Membrane
Mitochondrion
Nucleus
   DiseaseTumor suppressor
   LigandRNA-binding
   Molecular functionChaperone
Hydrolase
Protease
   PTMAcetylation
Isopeptide bond
Lipoprotein
Oxidation
Palmitate
Phosphoprotein
Ubl conjugation
Zymogen
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processadult locomotory behavior

Inferred from mutant phenotype PubMed 15721235PubMed 15799973. Source: MGI

autophagy

Inferred from electronic annotation. Source: UniProtKB-KW

cell proliferation

Traceable author statement Ref.1. Source: MGI

cellular response to hydrogen peroxide

Inferred from mutant phenotype Ref.7. Source: UniProtKB

cellular response to oxidative stress

Inferred from mutant phenotype Ref.13. Source: UniProtKB

cellular response to reactive oxygen species

Inferred from mutant phenotype PubMed 16624565. Source: MGI

dopamine uptake involved in synaptic transmission

Inferred from mutant phenotype PubMed 15721235. Source: MGI

hydrogen peroxide metabolic process

Inferred from mutant phenotype Ref.9. Source: MGI

inflammatory response

Inferred from electronic annotation. Source: UniProtKB-KW

membrane depolarization

Inferred from mutant phenotype PubMed 16624565. Source: MGI

membrane hyperpolarization

Inferred from mutant phenotype PubMed 16624565. Source: MGI

mitochondrion organization

Inferred from mutant phenotype Ref.14. Source: UniProtKB

negative regulation of cell death

Inferred from mutant phenotype Ref.7. Source: UniProtKB

negative regulation of extrinsic apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein binding

Inferred from sequence or structural similarity. Source: UniProtKB

oxidation-reduction process

Inferred from mutant phenotype Ref.9. Source: GOC

positive regulation of oxidative phosphorylation uncoupler activity

Inferred from mutant phenotype Ref.13. Source: UniProtKB

protein stabilization

Inferred from mutant phenotype Ref.8. Source: UniProtKB

regulation of androgen receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

regulation of inflammatory response

Inferred from mutant phenotype Ref.10. Source: UniProtKB

regulation of neuron apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

response to hydrogen peroxide

Inferred from direct assay Ref.7. Source: MGI

single fertilization

Inferred from electronic annotation. Source: UniProtKB-KW

synaptic transmission, dopaminergic

Inferred from mutant phenotype PubMed 15799973. Source: MGI

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from electronic annotation. Source: Ensembl

membrane raft

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay Ref.9PubMed 18614015. Source: MGI

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRNA binding

Traceable author statement Ref.1. Source: MGI

mRNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

peptidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

peroxidase activity

Inferred from mutant phenotype Ref.9. Source: UniProtKB

peroxiredoxin activity

Inferred from mutant phenotype Ref.9. Source: MGI

protein homodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ?Protein DJ-1PRO_0000157850
Propeptide? – 189Removed in mature form By similarityPRO_0000405560

Sites

Active site1061 By similarity
Active site1261 By similarity

Amino acid modifications

Modified residue671Phosphotyrosine By similarity
Modified residue1061Cysteine sulfinic acid (-SO2H); alternate By similarity
Modified residue1481N6-acetyllysine Ref.16
Modified residue1821N6-succinyllysine Ref.16
Lipidation461S-palmitoyl cysteine By similarity
Lipidation531S-palmitoyl cysteine By similarity
Lipidation1061S-palmitoyl cysteine; alternate By similarity
Cross-link130Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Experimental info

Mutagenesis461C → A: Sulfinic acid detected following treatment with hydrogen peroxide. Ref.9
Mutagenesis531C → A: Sulfinic acid detected following treatment with hydrogen peroxide. Ref.9
Mutagenesis1061C → A: No sulfinic acid detected following treatment with hydrogen peroxide. Ref.9
Sequence conflict1271P → T in BAE40278. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q99LX0 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 877C825CCA07468F

FASTA18920,021
        10         20         30         40         50         60 
MASKRALVIL AKGAEEMETV IPVDVMRRAG IKVTVAGLAG KDPVQCSRDV MICPDTSLED 

        70         80         90        100        110        120 
AKTQGPYDVV VLPGGNLGAQ NLSESPMVKE ILKEQESRKG LIAAICAGPT ALLAHEVGFG 

       130        140        150        160        170        180 
CKVTTHPLAK DKMMNGSHYS YSESRVEKDG LILTSRGPGT SFEFALAIVE ALVGKDMANQ 


VKAPLVLKD 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of human and mouse DJ-1 genes and identification of Sp1-dependent activation of the human DJ-1 promoter."
Taira T., Takahashi K., Kitagawa R., Iguchi-Ariga S.M.M., Ariga H.
Gene 263:285-292(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
[2]"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: BALB/c and NOD.
Tissue: Thymus.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"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: Mammary tumor.
[5]Lubec G., Klug S.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 13-27; 63-89 AND 99-122, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Hippocampus.
[6]"DJ-1 has a role in antioxidative stress to prevent cell death."
Taira T., Saito Y., Niki T., Iguchi-Ariga S.M., Takahashi K., Ariga H.
EMBO Rep. 5:213-218(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[7]"Hypersensitivity of DJ-1-deficient mice to 1-methyl-4-phenyl-1,2,3,6-tetrahydropyrindine (MPTP) and oxidative stress."
Kim R.H., Smith P.D., Aleyasin H., Hayley S., Mount M.P., Pownall S., Wakeham A., You-Ten A.J., Kalia S.K., Horne P., Westaway D., Lozano A.M., Anisman H., Park D.S., Mak T.W.
Proc. Natl. Acad. Sci. U.S.A. 102:5215-5220(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[8]"DJ-1, a cancer- and Parkinson's disease-associated protein, stabilizes the antioxidant transcriptional master regulator Nrf2."
Clements C.M., McNally R.S., Conti B.J., Mak T.W., Ting J.P.
Proc. Natl. Acad. Sci. U.S.A. 103:15091-15096(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[9]"DJ-1 gene deletion reveals that DJ-1 is an atypical peroxiredoxin-like peroxidase."
Andres-Mateos E., Perier C., Zhang L., Blanchard-Fillion B., Greco T.M., Thomas B., Ko H.S., Sasaki M., Ischiropoulos H., Przedborski S., Dawson T.M., Dawson V.L.
Proc. Natl. Acad. Sci. U.S.A. 104:14807-14812(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF CYS-46; CYS-53 AND CYS-106.
[10]"Regulation of astrocyte inflammatory responses by the Parkinson's disease-associated gene DJ-1."
Waak J., Weber S.S., Waldenmaier A., Gorner K., Alunni-Fabbroni M., Schell H., Vogt-Weisenhorn D., Pham T.T., Reumers V., Baekelandt V., Wurst W., Kahle P.J.
FASEB J. 23:2478-2489(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"The familial Parkinson's disease gene DJ-1 (PARK7) is expressed in red cells and plays a role in protection against oxidative damage."
Xu X., Martin F., Friedman J.S.
Blood Cells Mol. Dis. 45:227-232(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[12]"DJ-1 enhances cell survival through the binding of cezanne, a negative regulator of NF-{kappa}B."
McNally R.S., Davis B.K., Clements C.M., Accavitti-Loper M.A., Mak T.W., Ting J.P.
J. Biol. Chem. 286:4098-4106(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BBS1; CLCF1; MTERF AND OTUD7B.
[13]"Oxidant stress evoked by pacemaking in dopaminergic neurons is attenuated by DJ-1."
Guzman J.N., Sanchez-Padilla J., Wokosin D., Kondapalli J., Ilijic E., Schumacker P.T., Surmeier D.J.
Nature 468:696-700(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[14]"Reduced basal autophagy and impaired mitochondrial dynamics due to loss of Parkinson's disease-associated protein DJ-1."
Krebiehl G., Ruckerbauer S., Burbulla L.F., Kieper N., Maurer B., Waak J., Wolburg H., Gizatullina Z., Gellerich F.N., Woitalla D., Riess O., Kahle P.J., Proikas-Cezanne T., Kruger R.
PLoS ONE 5:E9367-E9367(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[15]"DJ-1 associates with lipid rafts by palmitoylation and regulates lipid rafts-dependent endocytosis in astrocytes."
Kim K.S., Kim J.S., Park J.Y., Suh Y.H., Jou I., Joe E.H., Park S.M.
Hum. Mol. Genet. 22:4805-4817(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
[16]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-148, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB015652 mRNA. Translation: BAA29063.2.
AK146368 mRNA. Translation: BAE27118.1.
AK153948 mRNA. Translation: BAE32271.1.
AK168341 mRNA. Translation: BAE40278.1.
AL607084 Genomic DNA. Translation: CAM19230.1.
BC002187 mRNA. Translation: AAH02187.1.
CCDSCCDS18975.1.
RefSeqNP_065594.2. NM_020569.3.
UniGeneMm.277349.

3D structure databases

ProteinModelPortalQ99LX0.
SMRQ99LX0. Positions 1-189.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid208257. 12 interactions.
IntActQ99LX0. 7 interactions.
MINTMINT-1869265.
STRING10090.ENSMUSP00000101300.

Protein family/group databases

MEROPSC56.002.

PTM databases

PhosphoSiteQ99LX0.

2D gel databases

REPRODUCTION-2DPAGEQ99LX0.
UCD-2DPAGEQ99LX0.

Proteomic databases

MaxQBQ99LX0.
PaxDbQ99LX0.
PRIDEQ99LX0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030805; ENSMUSP00000030805; ENSMUSG00000028964.
ENSMUST00000105673; ENSMUSP00000101298; ENSMUSG00000028964.
ENSMUST00000105674; ENSMUSP00000101299; ENSMUSG00000028964.
ENSMUST00000105675; ENSMUSP00000101300; ENSMUSG00000028964.
GeneID57320.
KEGGmmu:57320.
UCSCuc008vxz.2. mouse.

Organism-specific databases

CTD11315.
MGIMGI:2135637. Park7.

Phylogenomic databases

eggNOGCOG0693.
GeneTreeENSGT00390000001231.
HOGENOMHOG000063194.
HOVERGENHBG053511.
InParanoidQ99LX0.
KOK05687.
OMAVGREKAY.
OrthoDBEOG7CVPZX.
PhylomeDBQ99LX0.
TreeFamTF300119.

Gene expression databases

ArrayExpressQ99LX0.
BgeeQ99LX0.
GenevestigatorQ99LX0.

Family and domain databases

Gene3D3.40.50.880. 1 hit.
InterProIPR029062. Class_I_gatase-like.
IPR006287. DJ1.
IPR002818. ThiJ/PfpI.
[Graphical view]
PfamPF01965. DJ-1_PfpI. 1 hit.
[Graphical view]
SUPFAMSSF52317. SSF52317. 1 hit.
TIGRFAMsTIGR01383. not_thiJ. 1 hit.
ProtoNetSearch...

Other

NextBio313682.
PROQ99LX0.
SOURCESearch...

Entry information

Entry namePARK7_MOUSE
AccessionPrimary (citable) accession number: Q99LX0
Secondary accession number(s): O88306, Q3THB9, Q3U509
Entry history
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 104 of the entry and version 1 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