Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-01356
Entry Name
UniProt Accession
Theoretical PI
9.33
Molecular Weight
63836.99
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
21-DEC-2004
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
75
Canonical
GYGWAAACAGARKKR
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Predicted from GPS-Lipid
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
Topological domain: 1 48 Lumenal.
Transmembrane: 49 69 Helical.
Topological domain: 70 582 Cytoplasmic.
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.
Modified residue: 143 143 Phosphothreonine.
Modified residue: 264 264 N6-acetyllysine.
Modified residue: 298 298 Phosphoserine.
Modified residue: 306 306 Phosphoserine.
Modified residue: 308 308 Phosphoserine.
Modified residue: 311 311 Phosphoserine.
Modified residue: 344 344 Phosphoserine.
Modified residue: 369 369 Phosphoserine.
Modified residue: 415 415 Phosphoserine.
Modified residue: 426 426 Phosphoserine.
Modified residue: 458 458 Phosphothreonine.
Modified residue: 568 568 Phosphoserine.
Protein Length
582 AA.
Protein Sequence
(Canonical)
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
FASTA
(Canonical)
>LipidDB-9606-01356|Q86UE4
MAARSWQDELAQQAEEGSARLREMLSVGLGFLRTELGLDLGLEPKRYPGWVILVGTGALG
LLLLFLLGYGWAAACAGARKKRRSPPRKREEAAAVPAAAPDDLALLKNLRSEEQKKKNRK
KLSEKPKPNGRTVEVAEGEAVRTPQSVTAKQPPEIDKKNEKSKKNKKKSKSDAKAVQNSS
RHDGKEVDEGAWETKISHREKRQQRKRDKVLTDSGSLDSTIPGIENTITVTTEQLTTASF
PVGSKKNKGDSHLNVQVSNFKSGKGDSTLQVSSGLNENLTVNGGGWNEKSVKLSSQISAG
EEKWNSVSPASAGKRKTEPSAWSQDTGDANTNGKDWGRSWSDRSIFSGIGSTAEPVSQST
TSDYQWDVSRNQPYIDDEWSGLNGLSSADPNSDWNAPAEEWGNWVDEERASLLKSQEPIP
DDQKVSDDDKEKGEGALPTGKSKKKKKKKKKQGEDNSTAQDTEELEKEIREDLPVNTSKT
RPKQEKAFSLKTISTSDPAEVLVKNSQPIKTLPPATSTEPSVILSKSDSDKSSSQVPPIL
QETDKSKSNTKQNSVPPSQTKSETSWESPKQIKKKKKARRET
Gene Ontology
GO:0016324; C:apical plasma membrane; ISS:UniProtKB
GO:0005737; C:cytoplasm; IDA:UniProtKB
GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB
GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0046581; C:intercellular canaliculus; ISS:UniProtKB
GO:0016604; C:nuclear body; IDA:UniProtKB
GO:0005730; C:nucleolus; IDA:HPA
GO:0005634; C:nucleus; IDA:UniProtKB
GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB
GO:0005923; C:tight junction; ISS:UniProtKB
GO:0003725; F:double-stranded RNA binding; IDA:MGI
GO:0051059; F:NF-kappaB binding; IPI:UniProtKB
GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB
GO:0001085; F:RNA polymerase II transcription factor binding; IPI: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 signaling; 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; IDA:UniProtKB
GO:0070830; P:tight junction assembly; IEA:Ensembl
Interpro
Pfam
SMART
PROSITE
PRINTS