Details for: AMBRA1
Associated with
Other Information
Genular Protein ID: 3826256658
Symbol: AMRA1_HUMAN
Name: N/A
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 17589504
Title: Ambra1 regulates autophagy and development of the nervous system.
PubMed ID: 17589504
DOI: 10.1038/nature05925
PubMed ID: 11214970
Title: Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro.
PubMed ID: 11214970
PubMed ID: 14702039
Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.
PubMed ID: 14702039
DOI: 10.1038/ng1285
PubMed ID: 17974005
Title: The full-ORF clone resource of the German cDNA consortium.
PubMed ID: 17974005
PubMed ID: 16554811
Title: Human chromosome 11 DNA sequence and analysis including novel gene identification.
PubMed ID: 16554811
DOI: 10.1038/nature04632
PubMed ID: 15489334
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
PubMed ID: 15489334
DOI: 10.1101/gr.2596504
PubMed ID: 16949367
Title: A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is required for S phase destruction of the replication factor Cdt1.
PubMed ID: 16949367
PubMed ID: 18691976
Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.
PubMed ID: 18691976
PubMed ID: 18669648
Title: A quantitative atlas of mitotic phosphorylation.
PubMed ID: 18669648
PubMed ID: 19690332
Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
PubMed ID: 19690332
PubMed ID: 20921139
Title: The dynamic interaction of AMBRA1 with the dynein motor complex regulates mammalian autophagy.
PubMed ID: 20921139
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 21358617
Title: Mitochondrial BCL-2 inhibits AMBRA1-induced autophagy.
PubMed ID: 21358617
PubMed ID: 21753002
Title: Parkin interacts with Ambra1 to induce mitophagy.
PubMed ID: 21753002
PubMed ID: 22441670
Title: Proteolysis of Ambra1 during apoptosis has a role in the inhibition of the autophagic pro-survival response.
PubMed ID: 22441670
DOI: 10.1038/cdd.2012.27
PubMed ID: 22814378
Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.
PubMed ID: 22814378
PubMed ID: 23954414
Title: Beclin 2 functions in autophagy, degradation of G protein-coupled receptors, and metabolism.
PubMed ID: 23954414
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
DOI: 10.1021/pr300630k
PubMed ID: 23524951
Title: mTOR inhibits autophagy by controlling ULK1 ubiquitylation, self-association and function through AMBRA1 and TRAF6.
PubMed ID: 23524951
DOI: 10.1038/ncb2708
PubMed ID: 25499913
Title: AMBRA1 interplay with cullin E3 ubiquitin ligases regulates autophagy dynamics.
PubMed ID: 25499913
PubMed ID: 24275569
Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
PubMed ID: 24275569
PubMed ID: 24587252
Title: Ambra1 is an essential regulator of autophagy and apoptosis in SW620 cells: pro-survival role of Ambra1.
PubMed ID: 24587252
PubMed ID: 25803737
Title: AMBRA1 and BECLIN 1 interplay in the crosstalk between autophagy and cell proliferation.
PubMed ID: 25803737
PubMed ID: 25215947
Title: AMBRA1 is able to induce mitophagy via LC3 binding, regardless of PARKIN and p62/SQSTM1.
PubMed ID: 25215947
DOI: 10.1038/cdd.2014.139
PubMed ID: 25438055
Title: AMBRA1 links autophagy to cell proliferation and tumorigenesis by promoting c-Myc dephosphorylation and degradation.
PubMed ID: 25438055
DOI: 10.1038/ncb3072
PubMed ID: 28059583
Title: MIR7-3HG, a MYC-dependent modulator of cell proliferation, inhibits autophagy by a regulatory loop involving AMBRA1.
PubMed ID: 28059583
PubMed ID: 30513302
Title: AMBRA1 controls regulatory T-cell differentiation and homeostasis upstream of the FOXO3-FOXP3 axis.
PubMed ID: 30513302
PubMed ID: 30166453
Title: CRL4AMBRA1 targets Elongin C for ubiquitination and degradation to modulate CRL5 signaling.
PubMed ID: 30166453
PubMed ID: 30217973
Title: HUWE1 E3 ligase promotes PINK1/PARKIN-independent mitophagy by regulating AMBRA1 activation via IKKalpha.
PubMed ID: 30217973
PubMed ID: 31123703
Title: Autophagy induction in atrophic muscle cells requires ULK1 activation by TRIM32 through unanchored K63-linked polyubiquitin chains.
PubMed ID: 31123703
PubMed ID: 32616651
Title: The autophagy protein Ambra1 regulates gene expression by supporting novel transcriptional complexes.
PubMed ID: 32616651
PubMed ID: 33854232
Title: AMBRA1 regulates cyclin D to guard S-phase entry and genomic integrity.
PubMed ID: 33854232
PubMed ID: 33854235
Title: CRL4AMBRA1 is a master regulator of D-type cyclins.
PubMed ID: 33854235
PubMed ID: 33854239
Title: The AMBRA1 E3 ligase adaptor regulates the stability of cyclin D.
PubMed ID: 33854239
PubMed ID: 32333458
Title: Rare mutations in the autophagy-regulating gene AMBRA1 contribute to human neural tube defects.
PubMed ID: 32333458
DOI: 10.1002/humu.24028
Sequence Information:
- Length: 1298
- Mass: 142507
- Checksum: 44FE9CDFFFE6811E
- Sequence:
MKVVPEKNAV RILWGRERGA RAMGAQRLLQ ELVEDKTRWM KWEGKRVELP DSPRSTFLLA FSPDRTLLAS THVNHNIYIT EVKTGKCVHS LIGHRRTPWC VTFHPTISGL IASGCLDGEV RIWDLHGGSE SWFTDSNNAI ASLAFHPTAQ LLLIATANEI HFWDWSRREP FAVVKTASEM ERVRLVRFDP LGHYLLTAIV NPSNQQGDDE PEIPIDGTEL SHYRQRALLQ SQPVRRTPLL HNFLHMLSSR SSGIQVGEQS TVQDSATPSP PPPPPQPSTE RPRTSAYIRL RQRVSYPTAE CCQHLGILCL CSRCSGTRVP SLLPHQDSVP PASARATTPS FSFVQTEPFH PPEQASSTQQ DQGLLNRPSA FSTVQSSTAG NTLRNLSLGP TRRSLGGPLS SHPSRYHREI APGLTGSEWT RTVLSLNSRS EAESMPPPRT SASSVSLLSV LRQQEGGSQA SVYTSATEGR GFPASGLATE SDGGNGSSQN NSGSIRHELQ CDLRRFFLEY DRLQELDQSL SGEAPQTQQA QEMLNNNIES ERPGPSHQPT PHSSENNSNL SRGHLNRCRA CHNLLTFNND TLRWERTTPN YSSGEASSSW QVPSSFESVP SSGSQLPPLE RTEGQTPSSS RLELSSSASP QEERTVGVAF NQETGHWERI YTQSSRSGTV SQEALHQDMP EESSEEDSLR RRLLESSLIS LSRYDGAGSR EHPIYPDPAR LSPAAYYAQR MIQYLSRRDS IRQRSMRYQQ NRLRSSTSSS SSDNQGPSVE GTDLEFEDFE DNGDRSRHRA PRNARMSAPS LGRFVPRRFL LPEYLPYAGI FHERGQPGLA THSSVNRVLA GAVIGDGQSA VASNIANTTY RLQWWDFTKF DLPEISNASV NVLVQNCKIY NDASCDISAD GQLLAAFIPS SQRGFPDEGI LAVYSLAPHN LGEMLYTKRF GPNAISVSLS PMGRYVMVGL ASRRILLHPS TEHMVAQVFR LQQAHGGETS MRRVFNVLYP MPADQRRHVS INSARWLPEP GLGLAYGTNK GDLVICRPEA LNSGVEYYWD QLNETVFTVH SNSRSSERPG TSRATWRTDR DMGLMNAIGL QPRNPATSVT SQGTQTLALQ LQNAETQTER EVPEPGTAAS GPGEGEGSEY GASGEDALSR IQRLMAEGGM TAVVQREQST TMASMGGFGN NIIVSHRIHR SSQTGTEPGA AHTSSPQPST SRGLLPEAGQ LAERGLSPRT ASWDQPGTPG REPTQPTLPS SSPVPIPVSL PSAEGPTLHC ELTNNNHLLD GGSSRGDAAG PRGEPRNR
Genular Protein ID: 4116070470
Symbol: A0A075B6T1_HUMAN
Name: N/A
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 16554811
Title: Human chromosome 11 DNA sequence and analysis including novel gene identification.
PubMed ID: 16554811
DOI: 10.1038/nature04632
PubMed ID: 18691976
Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.
PubMed ID: 18691976
PubMed ID: 18669648
Title: A quantitative atlas of mitotic phosphorylation.
PubMed ID: 18669648
PubMed ID: 19690332
Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
PubMed ID: 19690332
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 22814378
Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.
PubMed ID: 22814378
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
PubMed ID: 24275569
Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
PubMed ID: 24275569
Sequence Information:
- Length: 1179
- Mass: 129599
- Checksum: 9A569E9A45962D99
- Sequence:
MKVVPEKNAV RILWGRERGA RAMGAQRLLQ ELVEDKTRWM KWEGKRVELP DSPRSTFLLA FSPDRTLLAS THVNHNIYIT EVKTGKCVHS LIGHRRTPWC VTFHPTISGL IASGCLDGEV RIWDLHGGSE SWFTDSNNAI ASLAFHPTAQ LLLIATANEI HFWDWSRREP FAVVKTASEM ERVRLVRFDP LGHYLLTAIV NPSNQQGDDE PEIPIDGTEL SHYRQRALLQ SQPVRRTPLL HNFLHMLSSR SSGIQTEPFH PPEQASSTQQ DQGLLNRPSA FSTVQSSTAG NTLRNLSLGP TRRSLGGPLS SHPSRYHREI APGLTGSEWT RTVLSLNSRS EAESMPPPRT SASSVSLLSV LRQQEGGSQA SVYTSATEGR GFPASGLATE SDGGNGSSQN NSGSIRHELQ CDLRRFFLEY DRLQELDQSL SGEAPQTQQA QEMLNNNIES ERPGPSHQPT PHSSENNSNL SRGHLNRCRA CHNLLTFNND TLRWERTTPN YSSGEASSSW QVPSSFESVP SSGSQLPPLE RTEGQTPSSS RLELSSSASP QEERTVGVAF NQETGHWERI YTQSSRSGTV SQEALHQDMP EESSEEDSLR RLSPAAYYAQ RMIQYLSRRD SIRQRSMRYQ QNRLRSSTSS SSSDNQGPSV EGTDLEFEDF EDNGDRSRHR APRNARMSAP SLGRFVPRRF LLPEYLPYAG IFHERGQPGL ATHSSVNRVL AGAVIGDGQS AVASNIANTT YRLQWWDFTK FDLPEISNAS VNVLVQNCKI YNDASCDISA DGQLLAAFIP SSQRGFPDEG ILAVYSLAPH NLGEMLYTKR FGPNAISVSL SPMGRYVMVG LASRRILLHP STEHMVAQVF RLQQAHGGET SMRRVFNVLY PMPADQRRHV SINSARWLPE PGLGLAYGTN KGDLVICRPE ALNSGVEYYW DQLNETVFTV HSNSRSSERP GTSRATWRTD RDMGLMNAIG LQPRNPATSV TSQGTQTLAL QLQNAETQTE REVPEPGTAA SGPGEGEGSE YGASGEDALS RIQRLMAEGG MTAVVQREQS TTMASMGGFG NNIIVSHRIH RSSQTGTEPG AAHTSSPQPS TSRGLLPEAG QLAERGLSPR TASWDQPGTP GREPTQPTLP SSSPVPIPVS LPSAEGPTLH CELTNNNHLL DGGSSRGDAA GPRGEPRNR
Database document:
This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.