CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021455
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Anthrax toxin receptor 1 
Protein Synonyms/Alias
 Tumor endothelial marker 8 
Gene Name
 ANTXR1 
Gene Synonyms/Alias
 ATR; TEM8 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
374DDGLPKKKWPTVDASubiquitination[1, 2]
401MEVRWGEKGSTEEGAubiquitination[2, 3]
419KAKNARVKMPEQEYEubiquitination[2, 3, 4]
445RRPSSPRKWYSPIKGubiquitination[5, 6]
451RKWYSPIKGKLDALWubiquitination[2, 3]
453WYSPIKGKLDALWVLubiquitination[1, 2, 3, 5, 6, 7, 8]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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] 
Functional Description
 Plays a role in cell attachment and migration. Interacts with extracellular matrix proteins and with the actin cytoskeleton. Mediates adhesion of cells to type 1 collagen and gelatin, reorganization of the actin cytoskeleton and promotes cell spreading. Plays a role in the angiogenic response of cultured umbilical vein endothelial cells. 
Sequence Annotation
 DOMAIN 44 215 VWFA.
 REGION 154 160 Interaction with PA.
 METAL 52 52 Divalent metal cation (By similarity).
 METAL 54 54 Divalent metal cation (By similarity).
 METAL 118 118 Divalent metal cation (By similarity).
 MOD_RES 362 362 Phosphoserine.
 CARBOHYD 166 166 N-linked (GlcNAc...) (Potential).
 CARBOHYD 184 184 N-linked (GlcNAc...).
 CARBOHYD 262 262 N-linked (GlcNAc...) (Potential).
 DISULFID 39 220  
Keyword
 3D-structure; Alternative splicing; Cell membrane; Cell projection; Complete proteome; Disulfide bond; Glycoprotein; Membrane; Metal-binding; Phosphoprotein; Polymorphism; Receptor; Reference proteome; Signal; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 564 AA 
Protein Sequence
MATAERRALG IGFQWLSLAT LVLICAGQGG RREDGGPACY GGFDLYFILD KSGSVLHHWN 60
EIYYFVEQLA HKFISPQLRM SFIVFSTRGT TLMKLTEDRE QIRQGLEELQ KVLPGGDTYM 120
HEGFERASEQ IYYENRQGYR TASVIIALTD GELHEDLFFY SEREANRSRD LGAIVYCVGV 180
KDFNETQLAR IADSKDHVFP VNDGFQALQG IIHSILKKSC IEILAAEPST ICAGESFQVV 240
VRGNGFRHAR NVDRVLCSFK INDSVTLNEK PFSVEDTYLL CPAPILKEVG MKAALQVSMN 300
DGLSFISSSV IITTTHCSDG SILAIALLIL FLLLALALLW WFWPLCCTVI IKEVPPPPAE 360
ESEEEDDDGL PKKKWPTVDA SYYGGRGVGG IKRMEVRWGE KGSTEEGAKL EKAKNARVKM 420
PEQEYEFPEP RNLNNNMRRP SSPRKWYSPI KGKLDALWVL LRKGYDRVSV MRPQPGDTGR 480
CINFTRVKNN QPAKYPLNNA YHTSSPPPAP IYTPPPPAPH CPPPPPSAPT PPIPSPPSTL 540
PPPPQAPPPN RAPPPSRPPP RPSV 564 
Gene Ontology
 GO:0031527; C:filopodium membrane; IDA:UniProtKB.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0031258; C:lamellipodium membrane; IDA:UniProtKB.
 GO:0051015; F:actin filament binding; IDA:UniProtKB.
 GO:0005518; F:collagen binding; IDA:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004888; F:transmembrane signaling receptor activity; IDA:UniProtKB.
 GO:0031532; P:actin cytoskeleton reorganization; IDA:UniProtKB.
 GO:0022414; P:reproductive process; IEA:Compara.
 GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:UniProtKB. 
Interpro
 IPR017360; Anthrax_toxin_rcpt.
 IPR008399; Anthrax_toxin_rcpt_C.
 IPR008400; Anthrax_toxin_rcpt_extracel.
 IPR002035; VWF_A. 
Pfam
 PF05586; Ant_C
 PF05587; Anth_Ig
 PF00092; VWA 
SMART
 SM00327; VWA 
PROSITE
 PS50234; VWFA 
PRINTS