CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-040156
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Lysine-specific histone demethylase 1A 
Protein Synonyms/Alias
  
Gene Name
 KDM1A 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
288LINFGIYKRIKPLPTubiquitination[1, 2, 3, 4]
296RIKPLPTKKTGKVIIubiquitination[3]
297IKPLPTKKTGKVIIIubiquitination[3]
300LPTKKTGKVIIIGSGubiquitination[3]
342GRVATFRKGNYVADLubiquitination[3, 5]
375QVNMELAKIKQKCPLubiquitination[3, 6]
398RIIVPKEKDEMVEQEubiquitination[3, 5, 6]
448QLQEKHVKDEQIEHWubiquitination[3, 4, 5, 6]
456DEQIEHWKKIVKTQEubiquitination[3, 6]
457EQIEHWKKIVKTQEEubiquitination[3]
460EHWKKIVKTQEELKEubiquitination[3]
466VKTQEELKELLNKMVubiquitination[3, 6]
471ELKELLNKMVNLKEKubiquitination[2, 3, 7]
476LNKMVNLKEKIKELHubiquitination[3]
478KMVNLKEKIKELHQQubiquitination[3]
480VNLKEKIKELHQQYKubiquitination[3, 5]
493YKEASEVKPPRDITAubiquitination[3]
505ITAEFLVKSKHRDLTubiquitination[3, 5, 6]
516RDLTALCKEYDELAEubiquitination[3]
527ELAETQGKLEEKLQEubiquitination[3, 6]
531TQGKLEEKLQELEANubiquitination[3]
609LAEGLDIKLNTAVRQubiquitination[1, 3]
641TSQTFIYKCDAVLCTubiquitination[3]
655TLPLGVLKQQPPAVQubiquitination[3]
671VPPLPEWKTSAVQRMubiquitination[1, 3, 4, 6, 8]
685MGFGNLNKVVLCFDRubiquitination[3]
756GRCLAILKGIFGSSAubiquitination[3]
768SSAVPQPKETVVSRWubiquitination[2, 3, 5, 6, 8]
Reference
 [1] 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]
 [2] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [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] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 876 AA 
Protein Sequence
MLSGKKAAAA AAAAAAAATG TEAGPGTAGG SENGSEVAAQ PAGLSGPAEV GPGAVGERTP 60
RKKEPPRASP PGGLAEPPGS AGPQAGPTVV PGSATPMETG IAETPEGRRT SRRKRAKVEY 120
REMDESLANL SEDEYYSEEE RNAKAEKEKK LPPPPPQAPP EEENESEPEE PSGQAGGLQD 180
DSSGGYGDGQ ASGVEGAAFQ SRLPHDRMTS QEAACFPDII SGPQQTQKVF LFIRNRTLQL 240
WLDNPKIQLT FEATLQQLEA PYNSDTVLVH RVHSYLERHG LINFGIYKRI KPLPTKKTGK 300
VIIIGSGVSG LAAARQLQSF GMDVTLLEAR DRVGGRVATF RKGNYVADLG AMVVTGLGGN 360
PMAVVSKQVN MELAKIKQKC PLYEANGQAE RIIVPKEKDE MVEQEFNRLL EATSYLSHQL 420
DFNVLNNKPV SLGQALEVVI QLQEKHVKDE QIEHWKKIVK TQEELKELLN KMVNLKEKIK 480
ELHQQYKEAS EVKPPRDITA EFLVKSKHRD LTALCKEYDE LAETQGKLEE KLQELEANPP 540
SDVYLSSRDR QILDWHFANL EFANATPLST LSLKHWDQDD DFEFTGSHLT VRNGYSCVPV 600
ALAEGLDIKL NTAVRQVRYT ASGCEVIAVN TRSTSQTFIY KCDAVLCTLP LGVLKQQPPA 660
VQFVPPLPEW KTSAVQRMGF GNLNKVVLCF DRVFWDPSVN LFGHVGSTTA SRGELFLFWN 720
LYKAPILLAL VAGEAAGIME NISDDVIVGR CLAILKGIFG SSAVPQPKET VVSRWRADPW 780
ARGSYSYVAA GSSGNDYDLM AQPITPGPSI PGAPQPIPRL FFAGEHTIRN YPATVHGALL 840
SGLREAGRIA DQFLGAMYTL PRQATPGVPA QQSPSM 876 
Gene Ontology
 GO:0005634; C:nucleus; IEA:InterPro.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
 GO:0016491; F:oxidoreductase activity; IEA:InterPro.
 GO:0034720; P:histone H3-K4 demethylation; IEA:InterPro.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro. 
Interpro
 IPR002937; Amino_oxidase.
 IPR017366; Hist_Lys-spec_deMease.
 IPR009057; Homeodomain-like.
 IPR007526; SWIRM.
 IPR011991; WHTH_DNA-bd_dom. 
Pfam
 PF01593; Amino_oxidase
 PF04433; SWIRM 
SMART
  
PROSITE
 PS50934; SWIRM 
PRINTS