CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016200
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein LYRIC 
Protein Synonyms/Alias
 3D3/LYRIC; Astrocyte elevated gene-1 protein; AEG-1; Lysine-rich CEACAM1 co-isolated protein; Metadherin; Metastasis adhesion protein 
Gene Name
 MTDH 
Gene Synonyms/Alias
 AEG1; LYRIC 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
107PDDLALLKNLRSEEQubiquitination[1, 2, 3, 4, 5]
150TPQSVTAKQPPEIDKubiquitination[2]
174KKSKSDAKAVQNSSRubiquitination[2]
185NSSRHDGKEVDEGAWubiquitination[2, 4]
195DEGAWETKISHREKRubiquitination[4]
303QISAGEEKWNSVSPAubiquitination[2]
451KKKKKKKKQGEDNSTubiquitination[2]
491QEKAFSLKTISTSDPubiquitination[2]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 
Functional Description
 Downregulates SLC1A2/EAAT2 promoter activity when expressed ectopically. Activates the nuclear factor kappa-B (NF- kappa-B) transcription factor. Promotes anchorage-independent growth of immortalized melanocytes and astrocytes which is a key component in tumor cell expansion. Promotes lung metastasis and also has an effect on bone and brain metastasis, possibly by enhancing the seeding of tumor cells to the target organ endothelium. Induces chemoresistance. 
Sequence Annotation
 REGION 1 71 Activation of NF-kappa-B.
 REGION 72 169 Interaction with BCCIP.
 REGION 101 205 Interaction with RELA.
 REGION 381 443 Lung-homing for mammary tumors (By
 MOD_RES 143 143 Phosphothreonine.
 MOD_RES 295 295 Phosphoserine (By similarity).
 MOD_RES 298 298 Phosphoserine.
 MOD_RES 306 306 Phosphoserine.
 MOD_RES 308 308 Phosphoserine.
 MOD_RES 311 311 Phosphoserine.
 MOD_RES 344 344 Phosphoserine.
 MOD_RES 369 369 Phosphoserine.
 MOD_RES 415 415 Phosphoserine.
 MOD_RES 426 426 Phosphoserine.
 MOD_RES 458 458 Phosphothreonine.
 MOD_RES 568 568 Phosphoserine.  
Keyword
 Cell junction; Complete proteome; Cytoplasm; Endoplasmic reticulum; Membrane; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Tight junction; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 582 AA 
Protein Sequence
MAARSWQDEL AQQAEEGSAR LREMLSVGLG FLRTELGLDL GLEPKRYPGW VILVGTGALG 60
LLLLFLLGYG WAAACAGARK KRRSPPRKRE EAAAVPAAAP DDLALLKNLR SEEQKKKNRK 120
KLSEKPKPNG RTVEVAEGEA VRTPQSVTAK QPPEIDKKNE KSKKNKKKSK SDAKAVQNSS 180
RHDGKEVDEG AWETKISHRE KRQQRKRDKV LTDSGSLDST IPGIENTITV TTEQLTTASF 240
PVGSKKNKGD SHLNVQVSNF KSGKGDSTLQ VSSGLNENLT VNGGGWNEKS VKLSSQISAG 300
EEKWNSVSPA SAGKRKTEPS AWSQDTGDAN TNGKDWGRSW SDRSIFSGIG STAEPVSQST 360
TSDYQWDVSR NQPYIDDEWS GLNGLSSADP NSDWNAPAEE WGNWVDEERA SLLKSQEPIP 420
DDQKVSDDDK EKGEGALPTG KSKKKKKKKK KQGEDNSTAQ DTEELEKEIR EDLPVNTSKT 480
RPKQEKAFSL KTISTSDPAE VLVKNSQPIK TLPPATSTEP SVILSKSDSD KSSSQVPPIL 540
QETDKSKSNT KQNSVPPSQT KSETSWESPK QIKKKKKARR ET 582 
Gene Ontology
 GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
 GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0046581; C:intercellular canaliculus; ISS:UniProtKB.
 GO:0016604; C:nuclear body; IDA:UniProtKB.
 GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
 GO:0005923; C:tight junction; ISS:UniProtKB.
 GO:0003713; F:transcription coactivator activity; IMP:UniProtKB.
 GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IMP:UniProtKB.
 GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
 GO:0045766; P:positive regulation of angiogenesis; IDA:UniProtKB.
 GO:0010508; P:positive regulation of autophagy; IDA:UniProtKB.
 GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IDA:UniProtKB.
 GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
 GO:0051897; P:positive regulation of protein kinase B signaling cascade; IDA:UniProtKB.
 GO:0070830; P:tight junction assembly; IEA:Compara. 
Interpro
  
Pfam
  
SMART
  
PROSITE
  
PRINTS