ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q8BGE6


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name ATG4B_MOUSE
Primary accession number Q8BGE6
Secondary accession numbers Q6ZQ22 Q8R098
Integrated into Swiss-Prot on March 15, 2005
Sequence was last modified on March 15, 2005 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 44)
Name and origin of the protein
Protein name Cysteine protease ATG4B
Synonyms EC 3.4.22.-
Autophagy-related protein 4 homolog B
Autophagin-1
Autophagy-related cysteine endopeptidase 1
AUT-like 1 cysteine endopeptidase
Gene name
Name: Atg4b
Synonyms: Apg4b, Autl1, Kiaa0943
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/c;
DOI=10.1074/jbc.M208247200; PubMed=12446702 [NCBI, ExPASy, EBI, Israel, Japan]
Marino G., Uria J.A., Puente X.S., Quesada V., Bordallo J., Lopez-Otin C.;
"Human autophagins, a family of cysteine proteinases potentially implicated in cell degradation by autophagy.";
J. Biol. Chem. 278:3671-3678(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Pancreas, Skin, and Testis;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N;
TISSUE=Kidney;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 128-393.
TISSUE=Brain;
DOI=10.1093/dnares/10.4.167; PubMed=14621295 [NCBI, ExPASy, EBI, Israel, Japan]
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries.";
DNA Res. 10:167-180(2003).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1021/pr0604155; PubMed=17203969 [NCBI, ExPASy, EBI, Israel, Japan]
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry.";
J. Proteome Res. 6:250-262(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1073/pnas.0609836104; PubMed=17242355 [NCBI, ExPASy, EBI, Israel, Japan]
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AJ504653; CAD43220.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK028712; BAC26079.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK031570; BAC27455.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK075796; BAC35965.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK088811; BAC40587.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC027184; AAH27184.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK129242; BAC98052.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
UniGene Mm.29087
3D structure databases
SMR Q8BGE6; 10-373.
ModBase Q8BGE6.
Protein family/group databases
MEROPS C54.003; -.
PTM databases
PhosphoSite Q8BGE6; -.
Organism-specific databases
MGI MGI:1913865; Atg4b.
Gene expression databases
ArrayExpress Q8BGE6; -.
CleanEx MM_ATG4B; -.
GermOnline ENSMUSG00000026280; Mus musculus.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from sequence or structural similarity from UniProtKB).
GO:0005875; Cellular component: microtubule associated complex (inferred from sequence or structural similarity from UniProtKB).
GO:0004197; Molecular function: cysteine-type endopeptidase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0008017; Molecular function: microtubule binding (inferred from sequence or structural similarity from UniProtKB).
GO:0000045; Biological process: autophagosome formation (inferred from sequence or structural similarity from UniProtKB).
GO:0006612; Biological process: protein targeting to membrane (inferred from sequence or structural similarity from UniProtKB).
GO:0006623; Biological process: protein targeting to vacuole (inferred from sequence or structural similarity from UniProtKB).
GO:0006508; Biological process: proteolysis (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR005078; Peptidase_C54.
Graphical view of domain structure.
PANTHER PTHR22624; Peptidase_C54; 1.
Pfam PF03416; Peptidase_C54; 1.
Pfam graphical view of domain structure.
BLOCKS Q8BGE6.
Genome annotation databases
Ensembl ENSMUSG00000026280; Mus musculus. [Contig view]
Phylogenomic databases
HOGENOM Q8BGE6; -.
HOVERGEN Q8BGE6; -.
Other
SOURCE Atg4b; Mus musculus.
ROUGE KIAA0943.
ProtoNet Q8BGE6.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Autophagy; Cytoplasm; Hydrolase; Phosphoprotein; Protease; Protein transport; Thiol protease; Transport; Ubl conjugation pathway.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   393  393     Cysteine protease ATG4B. PRO_0000215845
ACT_SITE   74    74        Nucleophile (By similarity). 
ACT_SITE   278   278        Potential. 
ACT_SITE   280   280        By similarity. 
MOD_RES   34    34        Phosphoserine. 
MOD_RES   316   316        Phosphoserine (By similarity). 
MOD_RES   383   383        Phosphoserine. 
MOD_RES   392   392        Phosphoserine (By similarity). 
CONFLICT   128   153        IAQMGVGEGKSIGQWYGPNTVAQVLK -> NCLNCHCCGVMLMLYKAHGSVLAFCR (in Ref. 3). 
CONFLICT   190   190        A -> V (in Ref. 1; CAD43220 and 2; BAC26079/BAC27455/BAC35965). 
CONFLICT   325   325        T -> K (in Ref. 2; BAC40587, 3 and 4). 
Sequence information
Length: 393 AA [This is the length of the unprocessed precursor] Molecular weight: 44375 Da [This is the MW of the unprocessed precursor] CRC64: EB9BF54B06F79135 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MDAATLTYDT LRFAEFEDFP ETSEPVWILG RKYSIFTEKD EILSDVASRL WFTYRRNFPA 

        70         80         90        100        110        120 
IGGTGPTSDT GWGCMLRCGQ MIFAQALVCR HLGRDWRWTQ RKRQPDSYFN VLNAFLDRKD 

       130        140        150        160        170        180 
SYYSIHQIAQ MGVGEGKSIG QWYGPNTVAQ VLKKLAVFDT WSSLAVHIAM DNTVVMEEIR 

       190        200        210        220        230        240 
RLCRANLPCA GAAALPTDSE RHCNGFPAGA EVTNRPSAWR PLVLLIPLRL GLTDINEAYV 

       250        260        270        280        290        300 
ETLKHCFMMP QSLGVIGGKP NSAHYFIGYV GEELIYLDPH TTQPAVELTD SCFIPDESFH 

       310        320        330        340        350        360 
CQHPPSRMGI GELDPSIAVG FFCKTEEDFN DWCQQVKKLS QLGGALPMFE LVEQQPSHLA 

       370        380        390 
CQDVLNLSLD SSDVERLERF FDSEDEDFEI LSL 

Q8BGE6 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!