CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020440
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Activating molecule in BECN1-regulated autophagy protein 1 
Protein Synonyms/Alias
  
Gene Name
 AMBRA1 
Gene Synonyms/Alias
 KIAA1736 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
36LQELVEDKTRWMKWEubiquitination[1]
41EDKTRWMKWEGKRVEubiquitination[1]
83NIYITEVKTGKCVHSubiquitination[2]
175REPFAVVKTASEMERubiquitination[1, 2, 3, 4, 5, 6, 7, 8, 9, 10]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [3] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [6] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [7] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [8] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [9] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [10] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
Functional Description
 Regulates autophagy and development of the nervous system. Involved in autophagy in controlling protein turnover during neuronal development, and in regulating normal cell survival and proliferation (By similarity). 
Sequence Annotation
 REPEAT 51 90 WD 1.
 REPEAT 93 133 WD 2.
 REPEAT 135 175 WD 3.
 MOD_RES 639 639 Phosphoserine.  
Keyword
 Alternative splicing; Autophagy; Complete proteome; Cytoplasmic vesicle; Developmental protein; Differentiation; Neurogenesis; Phosphoprotein; Reference proteome; Repeat; WD repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1298 AA 
Protein Sequence
MKVVPEKNAV RILWGRERGA RAMGAQRLLQ ELVEDKTRWM KWEGKRVELP DSPRSTFLLA 60
FSPDRTLLAS THVNHNIYIT EVKTGKCVHS LIGHRRTPWC VTFHPTISGL IASGCLDGEV 120
RIWDLHGGSE SWFTDSNNAI ASLAFHPTAQ LLLIATANEI HFWDWSRREP FAVVKTASEM 180
ERVRLVRFDP LGHYLLTAIV NPSNQQGDDE PEIPIDGTEL SHYRQRALLQ SQPVRRTPLL 240
HNFLHMLSSR SSGIQVGEQS TVQDSATPSP PPPPPQPSTE RPRTSAYIRL RQRVSYPTAE 300
CCQHLGILCL CSRCSGTRVP SLLPHQDSVP PASARATTPS FSFVQTEPFH PPEQASSTQQ 360
DQGLLNRPSA FSTVQSSTAG NTLRNLSLGP TRRSLGGPLS SHPSRYHREI APGLTGSEWT 420
RTVLSLNSRS EAESMPPPRT SASSVSLLSV LRQQEGGSQA SVYTSATEGR GFPASGLATE 480
SDGGNGSSQN NSGSIRHELQ CDLRRFFLEY DRLQELDQSL SGEAPQTQQA QEMLNNNIES 540
ERPGPSHQPT PHSSENNSNL SRGHLNRCRA CHNLLTFNND TLRWERTTPN YSSGEASSSW 600
QVPSSFESVP SSGSQLPPLE RTEGQTPSSS RLELSSSASP QEERTVGVAF NQETGHWERI 660
YTQSSRSGTV SQEALHQDMP EESSEEDSLR RRLLESSLIS LSRYDGAGSR EHPIYPDPAR 720
LSPAAYYAQR MIQYLSRRDS IRQRSMRYQQ NRLRSSTSSS SSDNQGPSVE GTDLEFEDFE 780
DNGDRSRHRA PRNARMSAPS LGRFVPRRFL LPEYLPYAGI FHERGQPGLA THSSVNRVLA 840
GAVIGDGQSA VASNIANTTY RLQWWDFTKF DLPEISNASV NVLVQNCKIY NDASCDISAD 900
GQLLAAFIPS SQRGFPDEGI LAVYSLAPHN LGEMLYTKRF GPNAISVSLS PMGRYVMVGL 960
ASRRILLHPS TEHMVAQVFR LQQAHGGETS MRRVFNVLYP MPADQRRHVS INSARWLPEP 1020
GLGLAYGTNK GDLVICRPEA LNSGVEYYWD QLNETVFTVH SNSRSSERPG TSRATWRTDR 1080
DMGLMNAIGL QPRNPATSVT SQGTQTLALQ LQNAETQTER EVPEPGTAAS GPGEGEGSEY 1140
GASGEDALSR IQRLMAEGGM TAVVQREQST TMASMGGFGN NIIVSHRIHR SSQTGTEPGA 1200
AHTSSPQPST SRGLLPEAGQ LAERGLSPRT ASWDQPGTPG REPTQPTLPS SSPVPIPVSL 1260
PSAEGPTLHC ELTNNNHLLD GGSSRGDAAG PRGEPRNR 1298 
Gene Ontology
 GO:0005776; C:autophagic vacuole; IEA:UniProtKB-SubCell.
 GO:0005737; C:cytoplasm; IDA:MGI.
 GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
 GO:0006914; P:autophagy; IEA:UniProtKB-KW.
 GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
 GO:0008285; P:negative regulation of cell proliferation; IEA:Compara.
 GO:0021915; P:neural tube development; IEA:Compara.
 GO:0043065; P:positive regulation of apoptotic process; IEA:Compara. 
Interpro
 IPR015943; WD40/YVTN_repeat-like_dom.
 IPR001680; WD40_repeat.
 IPR019775; WD40_repeat_CS.
 IPR017986; WD40_repeat_dom. 
Pfam
 PF00400; WD40 
SMART
 SM00320; WD40 
PROSITE
 PS00678; WD_REPEATS_1
 PS50082; WD_REPEATS_2
 PS50294; WD_REPEATS_REGION 
PRINTS