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Q9Y4P1

- ATG4B_HUMAN

UniProt

Q9Y4P1 - ATG4B_HUMAN

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Protein

Cysteine protease ATG4B

Gene
ATG4B, APG4B, AUTL1, KIAA0943
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.6 Publications

Enzyme regulationi

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.1 Publication

Kineticsi

  1. KM=5.1 µM for MAP1LC3B2 Publications
  2. KM=5.8 µM for GABARAP
  3. KM=4.4 µM for GABARAPL1
  4. KM=6.1 µM for GABARAPL2

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei74 – 741Nucleophile
Active sitei278 – 2781 Reviewed prediction
Active sitei280 – 2801

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: RefGenome
  2. cysteine-type peptidase activity Source: UniProtKB
  3. endopeptidase activity Source: BHF-UCL
  4. protein binding Source: UniProtKB

GO - Biological processi

  1. autophagic vacuole assembly Source: UniProtKB
  2. autophagy Source: UniProtKB
  3. cellular response to nitrogen starvation Source: RefGenome
  4. C-terminal protein lipidation Source: RefGenome
  5. late nucleophagy Source: RefGenome
  6. mitochondrion degradation Source: RefGenome
  7. piecemeal microautophagy of nucleus Source: RefGenome
  8. positive regulation of autophagy Source: BHF-UCL
  9. positive regulation of protein catabolic process Source: Ensembl
  10. protein delipidation Source: RefGenome
  11. protein processing Source: RefGenome
  12. protein targeting to membrane Source: RefGenome
  13. proteolysis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Autophagy, Protein transport, Transport, Ubl conjugation pathway

Protein family/group databases

MEROPSiC54.003.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:ATG4B
Synonyms:APG4B, AUTL1, KIAA0943
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:20790. ATG4B.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi74 – 741C → S: Complete loss of protease activity. 4 Publications
Mutagenesisi78 – 781C → A: Reduces the redox sensitivity and retains activity in presence of H(2)O(2). 1 Publication
Mutagenesisi142 – 1421W → A: Strongly reduced protease activity. 1 Publication
Mutagenesisi229 – 2291R → A: Strongly reduced protease activity. 1 Publication
Mutagenesisi278 – 2781D → A: Complete loss of protease activity. 2 Publications
Mutagenesisi280 – 2801H → A: Complete loss of protease activity. 2 Publications

Organism-specific databases

PharmGKBiPA134898340.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 393393Cysteine protease ATG4BPRO_0000215844Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine4 Publications
Modified residuei383 – 3831Phosphoserine5 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9Y4P1.
PaxDbiQ9Y4P1.
PRIDEiQ9Y4P1.

PTM databases

PhosphoSiteiQ9Y4P1.

Expressioni

Tissue specificityi

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

Gene expression databases

ArrayExpressiQ9Y4P1.
BgeeiQ9Y4P1.
CleanExiHS_ATG4B.
GenevestigatoriQ9Y4P1.

Organism-specific databases

HPAiCAB037195.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
GABARAPO951668EBI-712014,EBI-712001
GABARAPL1Q9H0R87EBI-712014,EBI-746969
GABARAPL2P605207EBI-712014,EBI-720116
MAP1LC3BQ9GZQ811EBI-712014,EBI-373144

Protein-protein interaction databases

BioGridi116801. 21 interactions.
IntActiQ9Y4P1. 18 interactions.
MINTiMINT-1414043.
STRINGi9606.ENSP00000384259.

Structurei

Secondary structure

1
393
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 73
Helixi10 – 134
Helixi14 – 185
Beta strandi22 – 243
Beta strandi26 – 283
Beta strandi31 – 333
Turni35 – 373
Helixi39 – 4810
Beta strandi54 – 574
Turni61 – 644
Turni70 – 723
Helixi74 – 9118
Beta strandi100 – 1023
Helixi106 – 1138
Beta strandi116 – 1183
Helixi125 – 1339
Turni134 – 1363
Helixi145 – 15612
Turni160 – 1623
Beta strandi165 – 1684
Beta strandi173 – 1753
Helixi176 – 1838
Beta strandi184 – 1863
Beta strandi222 – 2298
Beta strandi232 – 2343
Helixi237 – 2393
Helixi240 – 2467
Beta strandi252 – 2576
Beta strandi264 – 2707
Beta strandi273 – 2775
Beta strandi281 – 2844
Beta strandi290 – 2923
Helixi297 – 2993
Beta strandi306 – 3094
Helixi310 – 3123
Beta strandi315 – 32511
Helixi326 – 34116
Beta strandi349 – 3535
Helixi371 – 3766

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CY7X-ray1.90A1-393[»]
2D1IX-ray2.00A/B1-393[»]
2Z0DX-ray1.90A1-353[»]
2Z0EX-ray1.90A1-353[»]
2ZZPX-ray2.05A1-353[»]
ProteinModelPortaliQ9Y4P1.
SMRiQ9Y4P1. Positions 10-373.

Miscellaneous databases

EvolutionaryTraceiQ9Y4P1.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C54 family.

Phylogenomic databases

eggNOGiNOG239662.
HOVERGENiHBG050536.
KOiK08342.
OMAiDDFDDWC.
OrthoDBiEOG73V6KD.
PhylomeDBiQ9Y4P1.
TreeFamiTF314847.

Family and domain databases

InterProiIPR005078. Peptidase_C54.
[Graphical view]
PANTHERiPTHR22624. PTHR22624. 1 hit.
PfamiPF03416. Peptidase_C54. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y4P1-1) [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

MDAATLTYDT LRFAEFEDFP ETSEPVWILG RKYSIFTEKD EILSDVASRL    50
WFTYRKNFPA IGGTGPTSDT GWGCMLRCGQ MIFAQALVCR HLGRDWRWTQ 100
RKRQPDSYFS VLNAFIDRKD SYYSIHQIAQ MGVGEGKSIG QWYGPNTVAQ 150
VLKKLAVFDT WSSLAVHIAM DNTVVMEEIR RLCRTSVPCA GATAFPADSD 200
RHCNGFPAGA EVTNRPSPWR PLVLLIPLRL GLTDINEAYV ETLKHCFMMP 250
QSLGVIGGKP NSAHYFIGYV GEELIYLDPH TTQPAVEPTD GCFIPDESFH 300
CQHPPCRMSI AELDPSIAVG FFCKTEDDFN DWCQQVKKLS LLGGALPMFE 350
LVELQPSHLA CPDVLNLSLD SSDVERLERF FDSEDEDFEI LSL 393
Length:393
Mass (Da):44,294
Last modified:May 18, 2010 - v2
Checksum:iF4ADB3192176E0E5
GO
Isoform 2 (identifier: Q9Y4P1-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:468
Mass (Da):52,529
Checksum:iF9731E7C406960D6
GO
Isoform 3 (identifier: Q9Y4P1-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:280
Mass (Da):31,042
Checksum:i0904A795A1B596B3
GO
Isoform 4 (identifier: Q9Y4P1-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-74: Missing.
     369-369: L → LGESCQVQVGSLG

Show »
Length:331
Mass (Da):37,037
Checksum:i97592E25838601B2
GO
Isoform 6 (identifier: Q9Y4P1-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     370-393: DSSDVERLERFFDSEDEDFEILSL → GESCQVQILLM

Note: No experimental confirmation available.

Show »
Length:380
Mass (Da):42,622
Checksum:i48140873BCE7533D
GO

Sequence cautioni

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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti354 – 3541L → Q.5 Publications
Corresponds to variant rs7601000 [ dbSNP | Ensembl ].
VAR_021486

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7474Missing in isoform 3 and isoform 4. VSP_013028Add
BLAST
Alternative sequencei1 – 11M → MAHSVPSDSRTSRRPTTRPH AARGAPRGSRRPGRTPKWRL PRISARAPYRLRRLRRHTYW PPRRPVAASRCWPVGATPLG SVGGRTGKM in isoform 2. VSP_013029
Alternative sequencei321 – 35434FFCKT…ELVEL → KQGRLVRSLIPWAPRPSSWC AAVLGAAVVMCGTP in isoform 3. VSP_013031Add
BLAST
Alternative sequencei355 – 39339Missing in isoform 3. VSP_013032Add
BLAST
Alternative sequencei369 – 3691L → LGESCQVQVGSLG in isoform 4. VSP_013033
Alternative sequencei370 – 39324DSSDV…EILSL → GESCQVQILLM in isoform 2 and isoform 6. VSP_013034Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti136 – 1361Missing in BAB83890. 1 Publication
Sequence conflicti188 – 1881P → L in BAB55127. 1 Publication
Sequence conflicti247 – 2471F → Y in BAB55353. 1 Publication
Sequence conflicti273 – 2731E → G in BAB55042. 1 Publication
Sequence conflicti312 – 3121E → N in BAB83890. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS46564.1. [Q9Y4P1-1]
CCDS46565.1. [Q9Y4P1-6]
PIRiT12492.
RefSeqiNP_037457.3. NM_013325.4. [Q9Y4P1-1]
NP_847896.1. NM_178326.2. [Q9Y4P1-6]
UniGeneiHs.283610.

Genome annotation databases

EnsembliENST00000402096; ENSP00000384661; ENSG00000168397. [Q9Y4P1-4]
ENST00000404914; ENSP00000384259; ENSG00000168397. [Q9Y4P1-1]
ENST00000405546; ENSP00000383964; ENSG00000168397. [Q9Y4P1-6]
GeneIDi23192.
KEGGihsa:23192.
UCSCiuc002wbu.3. human. [Q9Y4P1-4]
uc002wbv.3. human. [Q9Y4P1-1]
uc002wbw.3. human. [Q9Y4P1-6]

Polymorphism databases

DMDMi296434400.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS46564.1. [Q9Y4P1-1 ]
CCDS46565.1. [Q9Y4P1-6 ]
PIRi T12492.
RefSeqi NP_037457.3. NM_013325.4. [Q9Y4P1-1 ]
NP_847896.1. NM_178326.2. [Q9Y4P1-6 ]
UniGenei Hs.283610.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CY7 X-ray 1.90 A 1-393 [» ]
2D1I X-ray 2.00 A/B 1-393 [» ]
2Z0D X-ray 1.90 A 1-353 [» ]
2Z0E X-ray 1.90 A 1-353 [» ]
2ZZP X-ray 2.05 A 1-353 [» ]
ProteinModelPortali Q9Y4P1.
SMRi Q9Y4P1. Positions 10-373.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116801. 21 interactions.
IntActi Q9Y4P1. 18 interactions.
MINTi MINT-1414043.
STRINGi 9606.ENSP00000384259.

Chemistry

BindingDBi Q9Y4P1.
ChEMBLi CHEMBL1741221.

Protein family/group databases

MEROPSi C54.003.

PTM databases

PhosphoSitei Q9Y4P1.

Polymorphism databases

DMDMi 296434400.

Proteomic databases

MaxQBi Q9Y4P1.
PaxDbi Q9Y4P1.
PRIDEi Q9Y4P1.

Protocols and materials databases

DNASUi 23192.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000402096 ; ENSP00000384661 ; ENSG00000168397 . [Q9Y4P1-4 ]
ENST00000404914 ; ENSP00000384259 ; ENSG00000168397 . [Q9Y4P1-1 ]
ENST00000405546 ; ENSP00000383964 ; ENSG00000168397 . [Q9Y4P1-6 ]
GeneIDi 23192.
KEGGi hsa:23192.
UCSCi uc002wbu.3. human. [Q9Y4P1-4 ]
uc002wbv.3. human. [Q9Y4P1-1 ]
uc002wbw.3. human. [Q9Y4P1-6 ]

Organism-specific databases

CTDi 23192.
GeneCardsi GC02P242578.
H-InvDB HIX0180188.
HGNCi HGNC:20790. ATG4B.
HPAi CAB037195.
MIMi 611338. gene.
neXtProti NX_Q9Y4P1.
PharmGKBi PA134898340.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG239662.
HOVERGENi HBG050536.
KOi K08342.
OMAi DDFDDWC.
OrthoDBi EOG73V6KD.
PhylomeDBi Q9Y4P1.
TreeFami TF314847.

Miscellaneous databases

ChiTaRSi ATG4B. human.
EvolutionaryTracei Q9Y4P1.
GeneWikii ATG4B.
GenomeRNAii 23192.
NextBioi 44679.
PROi Q9Y4P1.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Y4P1.
Bgeei Q9Y4P1.
CleanExi HS_ATG4B.
Genevestigatori Q9Y4P1.

Family and domain databases

InterProi IPR005078. Peptidase_C54.
[Graphical view ]
PANTHERi PTHR22624. PTHR22624. 1 hit.
Pfami PF03416. Peptidase_C54. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.
    , 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. 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. 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. 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.

Entry informationi

Entry nameiATG4B_HUMAN
AccessioniPrimary (citable) accession number: Q9Y4P1
Secondary accession number(s): B7WNK2
, Q53NU4, Q6ZUV8, Q8WYM9, Q96K07, Q96K96, Q96SZ1, Q9Y2F2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: May 18, 2010
Last modified: September 3, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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