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UniProtKB/Swiss-Prot entry Q9Y4P1


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

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Entry information
Entry name ATG4B_HUMAN
Primary accession number Q9Y4P1
Secondary accession numbers Q6ZUV8 Q8WYM9 Q96K07 Q96K96 Q96SZ1 Q9Y2F2
Integrated into Swiss-Prot on March 15, 2005
Sequence was last modified on November 1, 1999 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 66)
Name and origin of the protein
Protein name Cysteine protease ATG4B
Synonyms EC 3.4.22.-
Autophagy-related protein 4 homolog B
hAPG4B
Autophagin-1
Autophagy-related cysteine endopeptidase 1
AUT-like 1 cysteine endopeptidase
Gene name
Name: ATG4B
Synonyms: APG4B, AUTL1, KIAA0943
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Liver;
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 [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION IN GABARAPL2; GABARAP AND MAP1LC3A CLEAVAGE, AND MUTAGENESIS OF CYS-74.
DOI=10.1242/jcs.01131; PubMed=15169837 [NCBI, ExPASy, EBI, Israel, Japan]
Kabeya Y., Mizushima N., Yamamoto A., Oshitani-Okamoto S., Ohsumi Y., Yoshimori T.;
"LC3, GABARAP and GATE16 localize to autophagosomal membrane depending on form-II formation.";
J. Cell Sci. 117:2805-2812(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
DOI=10.1093/dnares/6.1.63; PubMed=10231032 [NCBI, ExPASy, EBI, Israel, Japan]
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro.";
DNA Res. 6:63-70(1999).
[4]
SEQUENCE REVISION.
Ohara O., Nagase T., Kikuno R.;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4 AND 6), AND VARIANT LEU-354.
TISSUE=Embryo, and Placenta;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
The German cDNA consortium;
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
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).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383 AND SER-392, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, AND MASS SPECTROMETRY.
DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan]
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Anal. Sci. 24:161-166(2008).
[10]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND MUTAGENESIS OF CYS-74; TRP-142; ARG-229; ASP-278 AND HIS-280.
DOI=10.1074/jbc.M509158200; PubMed=16183633 [NCBI, ExPASy, EBI, Israel, Japan]
Sugawara K., Suzuki N.N., Fujioka Y., Mizushima N., Ohsumi Y., Inagaki F.;
"Structural basis for the specificity and catalysis of human Atg4B responsible for mammalian autophagy.";
J. Biol. Chem. 280:40058-40065(2005).
[11]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND MUTAGENESIS OF CYS-74; ASP-278 AND HIS-280.
DOI=10.1016/j.jmb.2005.11.018; PubMed=16325851 [NCBI, ExPASy, EBI, Israel, Japan]
Kumanomidou T., Mizushima T., Komatsu M., Suzuki A., Tanida I., Sou Y.-S., Ueno T., Kominami E., Tanaka K., Yamane T.;
"The crystal structure of human Atg4b, a processing and de-conjugating enzyme for autophagosome-forming modifiers.";
J. Mol. Biol. 355:612-618(2006).
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
AJ504652; CAD43219.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB066215; BAB83890.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB023160; BAA76787.2; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK027332; BAB55042.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK027462; BAB55127.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK027763; BAB55353.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK125277; BAC86110.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL080168; CAB45756.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000719; AAH00719.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T12492; T12492.
RefSeq NP_037457.3; -.
NP_847896.1; -.
UniGene Hs.283610
3D structure databases
PDB
2CY7; X-ray; 1.90 A; A=1-393.[ExPASy / RCSB / EBI]
2D1I; X-ray; 2.00 A; A/B=1-393.[ExPASy / RCSB / EBI]
2Z0D; X-ray; 1.90 A; A=1-354.[ExPASy / RCSB / EBI]
2Z0E; X-ray; 1.90 A; A=1-354.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2CY7; -.
2D1I; -.
2Z0D; -.
2Z0E; -.
ModBase Q9Y4P1.
Protein-protein interaction databases
IntAct Q9Y4P1; -.
Protein family/group databases
MEROPS C54.003; -.
PTM databases
PhosphoSite Q9Y4P1; -.
Organism-specific databases
H-InvDB HIX0030185; -.
HIX0057233; -.
HGNC HGNC:20790; ATG4B.
GenAtlas ATG4B.
MIM 611338; gene. [NCBI / EBI]
PharmGKB PA134898340; -.
GeneCards Q9Y4P1.
HUGE KIAA0943.
Gene expression databases
CleanEx HS_ATG4B; -.
GermOnline ENSG00000168397; Homo sapiens.
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:0008234; Molecular function: cysteine-type peptidase activity (inferred from direct assay from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction 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:0006508; Biological process: proteolysis (inferred from direct assay 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 Q9Y4P1.
Genome annotation databases
Ensembl ENSG00000168397; Homo sapiens. [Contig view]
ENSG00000215697; Homo sapiens. [Contig view]
GeneID 23192; -.
KEGG hsa:23192; -.
Phylogenomic databases
HOVERGEN Q9Y4P1; -.
Other
SOURCE ATG4B; Homo sapiens.
ProtoNet Q9Y4P1.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Autophagy; Cytoplasm; Hydrolase; Phosphoprotein; Polymorphism; 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_0000215844
ACT_SITE   74    74        Nucleophile. 
ACT_SITE   278   278        Potential. 
ACT_SITE   280   280         
MOD_RES   34    34        Phosphoserine (By similarity). 
MOD_RES   316   316        Phosphoserine. 
MOD_RES   383   383        Phosphoserine. 
MOD_RES   392   392        Phosphoserine. 
VAR_SEQ   1    74        Missing (in isoform 3 and isoform 4). VSP_013028
VAR_SEQ   1     1        M -> MAHSVPSDSRTSRRPTTRPHAARGAPRGSRRPGRTPKWRL PRISARAPYRLRRLRRHTYWPPRRPVAASRCWPVGATPLG SVGGRTGKM (in isoform 2). VSP_013029
VAR_SEQ   321   354        FFCKTEDDFNDWCQQVKKLSLLGGALPMFELVEQ -> KQGRLVRSLIPWAPRPSSWCAAVLGAAVVMCGTP (in isoform 3). VSP_013031
VAR_SEQ   355   393        Missing (in isoform 3). VSP_013032
VAR_SEQ   369   369        L -> LGESCQVQVGSLG (in isoform 4). VSP_013033
VAR_SEQ   370   393        DSSDVERLERFFDSEDEDFEILSL -> GESCQVQILLM (in isoform 2 and isoform 6). VSP_013034
VARIANT   354   354  1     Q -> L (in dbSNP:rs7601000 [NCBI]). VAR_021486 [3D]
MUTAGEN   74    74        C->S: Complete loss of protease activity. 
MUTAGEN   142   142        W->A: Strongly reduced protease activity. 
MUTAGEN   229   229        R->A: Strongly reduced protease activity. 
MUTAGEN   278   278        D->A: Complete loss of protease activity. 
MUTAGEN   280   280        H->A: Complete loss of protease activity. 
CONFLICT   136   136        Missing (in Ref. 2; BAB83890). 
CONFLICT   188   188        P -> L (in Ref. 5; BAB55127). 
CONFLICT   247   247        F -> Y (in Ref. 5; BAB55353). 
CONFLICT   273   273        E -> G (in Ref. 5; BAB55042). 
CONFLICT   312   312        E -> N (in Ref. 2; BAB83890). 
HELIX   10    13  4      
STRAND   26    28  3      
STRAND   31    33  3      
TURN   35    37  3      
HELIX   39    48  10      
STRAND   54    57  4      
TURN   61    64  4      
TURN   70    72  3      
HELIX   74    91  18      
HELIX   106   113  8      
STRAND   116   118  3      
HELIX   125   133  9      
TURN   134   136  3      
HELIX   145   156  12      
TURN   160   162  3      
STRAND   165   168  4      
STRAND   173   175  3      
HELIX   176   183  8      
STRAND   184   186  3      
STRAND   222   229  8      
STRAND   232   234  3      
HELIX   237   239  3      
HELIX   240   246  7      
STRAND   252   257  6      
STRAND   264   270  7      
STRAND   273   277  5      
STRAND   281   284  4      
HELIX   297   299  3      
STRAND   306   309  4      
HELIX   310   312  3      
STRAND   315   325  11      
HELIX   326   341  16      
STRAND   349   353  5      
STRAND   364   370  7      
HELIX   371   376  6      
Sequence information
Length: 393 AA [This is the length of the unprocessed precursor] Molecular weight: 44309 Da [This is the MW of the unprocessed precursor] CRC64: 7E850A192176E0F5 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MDAATLTYDT LRFAEFEDFP ETSEPVWILG RKYSIFTEKD EILSDVASRL WFTYRKNFPA 

        70         80         90        100        110        120 
IGGTGPTSDT GWGCMLRCGQ MIFAQALVCR HLGRDWRWTQ RKRQPDSYFS VLNAFIDRKD 

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

       190        200        210        220        230        240 
RLCRTSVPCA GATAFPADSD RHCNGFPAGA EVTNRPSPWR PLVLLIPLRL GLTDINEAYV 

       250        260        270        280        290        300 
ETLKHCFMMP QSLGVIGGKP NSAHYFIGYV GEELIYLDPH TTQPAVEPTD GCFIPDESFH 

       310        320        330        340        350        360 
CQHPPCRMSI AELDPSIAVG FFCKTEDDFN DWCQQVKKLS LLGGALPMFE LVEQQPSHLA 

       370        380        390 
CPDVLNLSLD SSDVERLERF FDSEDEDFEI LSL 

Q9Y4P1 in FASTA format

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