Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9Y4P1 (ATG4B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cysteine protease ATG4B

EC=3.4.22.-
Alternative name(s):
AUT-like 1 cysteine endopeptidase
Autophagin-1
Autophagy-related cysteine endopeptidase 1
Autophagy-related protein 4 homolog B
Short name=hAPG4B
Gene names
Name:ATG4B
Synonyms:APG4B, AUTL1, KIAA0943
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length393 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cysteine protease required for the cytoplasm to vacuole transport (Cvt) and autophagy. Cleaves the C-terminal amino acid of ATG8 family proteins MAP1LC3, GABARAPL1, GABARAPL2 and GABARAP, to reveal a C-terminal glycine. Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy. Has also an activity of delipidating enzyme for the PE-conjugated forms. Ref.2 Ref.10 Ref.12 Ref.18 Ref.20 Ref.25

Enzyme regulation

Inhibited by N-ethylmaleimide. Redox-regulated during autophagy since reducing conditions activate ATG4A whereas an oxidizing environment such as the presence of H2O2 inhibits its activity. Ref.12

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Mainly expressed in the skeletal muscle, followed by brain, heart, liver and pancreas. Ref.1 Ref.2

Sequence similarities

Belongs to the peptidase C54 family.

Biophysicochemical properties

Kinetic parameters:

KM=5.1 µM for MAP1LC3B Ref.18 Ref.20

KM=5.8 µM for GABARAP

KM=4.4 µM for GABARAPL1

KM=6.1 µM for GABARAPL2

Sequence caution

The sequence BAA76787.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAC86110.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Binary interactions

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y4P1-1)

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.
Isoform 2 (identifier: Q9Y4P1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MAHSVPSDSR...GSVGGRTGKM
     370-393: DSSDVERLERFFDSEDEDFEILSL → GESCQVQILLM
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9Y4P1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-74: Missing.
     321-354: FFCKTEDDFNDWCQQVKKLSLLGGALPMFELVEL → KQGRLVRSLIPWAPRPSSWCAAVLGAAVVMCGTP
     355-393: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q9Y4P1-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-74: Missing.
     369-369: L → LGESCQVQVGSLG
Isoform 6 (identifier: Q9Y4P1-6)

The sequence of this isoform differs from the canonical sequence as follows:
     370-393: DSSDVERLERFFDSEDEDFEILSL → GESCQVQILLM
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 393393Cysteine protease ATG4B
PRO_0000215844

Sites

Active site741Nucleophile
Active site2781 Potential
Active site2801

Amino acid modifications

Modified residue11N-acetylmethionine Ref.9 Ref.13 Ref.21 Ref.22
Modified residue3831Phosphoserine Ref.11 Ref.14 Ref.15 Ref.16 Ref.19

Natural variations

Alternative sequence1 – 7474Missing in isoform 3 and isoform 4.
VSP_013028
Alternative sequence11M → MAHSVPSDSRTSRRPTTRPH AARGAPRGSRRPGRTPKWRL PRISARAPYRLRRLRRHTYW PPRRPVAASRCWPVGATPLG SVGGRTGKM in isoform 2.
VSP_013029
Alternative sequence321 – 35434FFCKT…ELVEL → KQGRLVRSLIPWAPRPSSWC AAVLGAAVVMCGTP in isoform 3.
VSP_013031
Alternative sequence355 – 39339Missing in isoform 3.
VSP_013032
Alternative sequence3691L → LGESCQVQVGSLG in isoform 4.
VSP_013033
Alternative sequence370 – 39324DSSDV…EILSL → GESCQVQILLM in isoform 2 and isoform 6.
VSP_013034
Natural variant3541L → Q. Ref.1 Ref.2 Ref.3 Ref.6 Ref.8
Corresponds to variant rs7601000 [ dbSNP | Ensembl ].
VAR_021486

Experimental info

Mutagenesis741C → S: Complete loss of protease activity. Ref.2 Ref.10 Ref.23 Ref.24
Mutagenesis781C → A: Reduces the redox sensitivity and retains activity in presence of H(2)O(2). Ref.12
Mutagenesis1421W → A: Strongly reduced protease activity. Ref.23
Mutagenesis2291R → A: Strongly reduced protease activity. Ref.23
Mutagenesis2781D → A: Complete loss of protease activity. Ref.23 Ref.24
Mutagenesis2801H → A: Complete loss of protease activity. Ref.23 Ref.24
Sequence conflict1361Missing in BAB83890. Ref.2
Sequence conflict1881P → L in BAB55127. Ref.5
Sequence conflict2471F → Y in BAB55353. Ref.5
Sequence conflict2731E → G in BAB55042. Ref.5
Sequence conflict3121E → N in BAB83890. Ref.2

Secondary structure

........................................................................ 393
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 18, 2010. Version 2.
Checksum: F4ADB3192176E0E5

FASTA39344,294
        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 LVELQPSHLA 

       370        380        390 
CPDVLNLSLD SSDVERLERF FDSEDEDFEI LSL 

« Hide

Isoform 2 [UniParc].

Checksum: F9731E7C406960D6
Show »

FASTA46852,529
Isoform 3 [UniParc].

Checksum: 0904A795A1B596B3
Show »

FASTA28031,042
Isoform 4 [UniParc].

Checksum: 97592E25838601B2
Show »

FASTA33137,037
Isoform 6 [UniParc].

Checksum: 48140873BCE7533D
Show »

FASTA38042,622

References

« Hide 'large scale' references
[1]"Human autophagins, a family of cysteine proteinases potentially implicated in cell degradation by autophagy."
Marino G., Uria J.A., Puente X.S., Quesada V., Bordallo J., Lopez-Otin C.
J. Biol. Chem. 278:3671-3678(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT GLN-354.
Tissue: Liver.
[2]"LC3, GABARAP and GATE16 localize to autophagosomal membrane depending on form-II formation."
Kabeya Y., Mizushima N., Yamamoto A., Oshitani-Okamoto S., Ohsumi Y., Yoshimori T.
J. Cell Sci. 117:2805-2812(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION IN GABARAPL2; GABARAP AND MAP1LC3A CLEAVAGE, MUTAGENESIS OF CYS-74, VARIANT GLN-354.
[3]"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."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLN-354.
Tissue: Brain.
[4]Ohara O., Nagase T., Kikuno R.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4 AND 6).
Tissue: Embryo and Placenta.
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLN-354.
Tissue: Testis.
[7]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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), VARIANT GLN-354.
Tissue: Placenta.
[9]Bienvenut W.V.
Submitted (JAN-2010) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-12; 33-49; 120-137; 185-201 AND 230-244, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Ovarian carcinoma.
[10]"HsAtg4B/HsApg4B/autophagin-1 cleaves the carboxyl termini of three human Atg8 homologues and delipidates microtubule-associated protein light chain 3- and GABAA receptor-associated protein-phospholipid conjugates."
Tanida I., Sou Y.-S., Ezaki J., Minematsu-Ikeguchi N., Ueno T., Kominami E.
J. Biol. Chem. 279:36268-36276(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF CYS-74.
[11]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4."
Scherz-Shouval R., Shvets E., Fass E., Shorer H., Gil L., Elazar Z.
EMBO J. 26:1749-1760(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, MUTAGENESIS OF CYS-78.
[13]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Kinetics comparisons of mammalian Atg4 homologues indicate selective preferences toward diverse Atg8 substrates."
Li M., Hou Y., Wang J., Chen X., Shao Z.M., Yin X.M.
J. Biol. Chem. 286:7327-7338(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[19]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"A high-throughput FRET-based assay for determination of Atg4 activity."
Li M., Chen X., Ye Q.Z., Vogt A., Yin X.M.
Autophagy 8:401-412(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[21]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Structural basis for the specificity and catalysis of human Atg4B responsible for mammalian autophagy."
Sugawara K., Suzuki N.N., Fujioka Y., Mizushima N., Ohsumi Y., Inagaki F.
J. Biol. Chem. 280:40058-40065(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), MUTAGENESIS OF CYS-74; TRP-142; ARG-229; ASP-278 AND HIS-280.
[24]"The crystal structure of human Atg4b, a processing and de-conjugating enzyme for autophagosome-forming modifiers."
Kumanomidou T., Mizushima T., Komatsu M., Suzuki A., Tanida I., Sou Y.-S., Ueno T., Kominami E., Tanaka K., Yamane T.
J. Mol. Biol. 355:612-618(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), MUTAGENESIS OF CYS-74; ASP-278 AND HIS-280.
[25]"The structure of Atg4B-LC3 complex reveals the mechanism of LC3 processing and delipidation during autophagy."
Satoo K., Noda N.N., Kumeta H., Fujioka Y., Mizushima N., Ohsumi Y., Inagaki F.
EMBO J. 28:1341-1350(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-353 IN COMPLEX WITH RAT MAP1LC3B/LC3, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ504652 mRNA. Translation: CAD43219.1.
AB066215 mRNA. Translation: BAB83890.1.
AB023160 mRNA. Translation: BAA76787.2. Different initiation.
AK027332 mRNA. Translation: BAB55042.1.
AK027462 mRNA. Translation: BAB55127.1.
AK027763 mRNA. Translation: BAB55353.1.
AK125277 mRNA. Translation: BAC86110.1. Different initiation.
AL080168 mRNA. Translation: CAB45756.1.
AC133528 Genomic DNA. Translation: AAY14919.1.
BC000719 mRNA. Translation: AAH00719.1.
PIRT12492.
RefSeqNP_037457.3. NM_013325.4.
NP_847896.1. NM_178326.2.
UniGeneHs.283610.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CY7X-ray1.90A1-393[»]
2D1IX-ray2.00A/B1-393[»]
2Z0DX-ray1.90A1-353[»]
2Z0EX-ray1.90A1-353[»]
2ZZPX-ray2.05A1-353[»]
ProteinModelPortalQ9Y4P1.
SMRQ9Y4P1. Positions 10-373.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116801. 21 interactions.
IntActQ9Y4P1. 18 interactions.
MINTMINT-1414043.
STRING9606.ENSP00000384259.

Chemistry

BindingDBQ9Y4P1.
ChEMBLCHEMBL1741221.

Protein family/group databases

MEROPSC54.003.

PTM databases

PhosphoSiteQ9Y4P1.

Polymorphism databases

DMDM296434400.

Proteomic databases

PaxDbQ9Y4P1.
PRIDEQ9Y4P1.

Protocols and materials databases

DNASU23192.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000402096; ENSP00000384661; ENSG00000168397. [Q9Y4P1-4]
ENST00000404914; ENSP00000384259; ENSG00000168397. [Q9Y4P1-1]
ENST00000405546; ENSP00000383964; ENSG00000168397. [Q9Y4P1-6]
GeneID23192.
KEGGhsa:23192.
UCSCuc002wbu.3. human. [Q9Y4P1-4]
uc002wbv.3. human. [Q9Y4P1-1]
uc002wbw.3. human. [Q9Y4P1-6]

Organism-specific databases

CTD23192.
GeneCardsGC02P242578.
H-InvDBHIX0180188.
HGNCHGNC:20790. ATG4B.
HPACAB037195.
MIM611338. gene.
neXtProtNX_Q9Y4P1.
PharmGKBPA134898340.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG239662.
HOVERGENHBG050536.
KOK08342.
OMARNFPAIG.
OrthoDBEOG73V6KD.
PhylomeDBQ9Y4P1.
TreeFamTF314847.

Gene expression databases

ArrayExpressQ9Y4P1.
BgeeQ9Y4P1.
CleanExHS_ATG4B.
GenevestigatorQ9Y4P1.

Family and domain databases

InterProIPR005078. Peptidase_C54.
[Graphical view]
PANTHERPTHR22624. PTHR22624. 1 hit.
PfamPF03416. Peptidase_C54. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSATG4B. human.
EvolutionaryTraceQ9Y4P1.
GeneWikiATG4B.
GenomeRNAi23192.
NextBio44679.
PROQ9Y4P1.
SOURCESearch...

Entry information

Entry nameATG4B_HUMAN
AccessionPrimary (citable) accession number: Q9Y4P1
Secondary accession number(s): B7WNK2 expand/collapse secondary AC list , Q53NU4, Q6ZUV8, Q8WYM9, Q96K07, Q96K96, Q96SZ1, Q9Y2F2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM