CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020078
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Matrix-remodeling-associated protein 8 
Protein Synonyms/Alias
 Limitrin 
Gene Name
 MXRA8 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
383KSGKSKGKDVNLAEFubiquitination[1]
410EDIQLDYKNNILKERubiquitination[1]
428AHSPLPAKYIDLDKGubiquitination[1]
434AKYIDLDKGFRKENCubiquitination[1]
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
Functional Description
 May play a role in the maturation and maintenance of blood-brain barrier (By similarity). 
Sequence Annotation
 DOMAIN 29 157 Ig-like V-type 1.
 DOMAIN 160 288 Ig-like V-type 2.
 CARBOHYD 119 119 N-linked (GlcNAc...) (Potential).
 CARBOHYD 306 306 N-linked (GlcNAc...) (Potential).
 DISULFID 54 137 By similarity.
 DISULFID 186 272 By similarity.  
Keyword
 Alternative splicing; Complete proteome; Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane; Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 442 AA 
Protein Sequence
MALPSRILLW KLVLLQSSAV LLHSGSSVPA AAGSSVVSES AVSWEAGARA VLRCQSPRMV 60
WTQDRLHDRQ RVLHWDLRGP GGGPARRLLD LYSAGEQRVY EARDRGRLEL SASAFDDGNF 120
SLLIRAVEET DAGLYTCNLH HHYCHLYESL AVRLEVTDGP PATPAYWDGE KEVLAVARGA 180
PALLTCVNRG HVWTDRHVEE AQQVVHWDRQ PPGVPHDRAD RLLDLYASGE RRAYGPLFLR 240
DRVAVGADAF ERGDFSLRIE PLEVADEGTY SCHLHHHYCG LHERRVFHLT VAEPHAEPPP 300
RGSPGNGSSH SGAPGPDPTL ARGHNVINVI VPESRAHFFQ QLGYVLATLL LFILLLVTVL 360
LAARRRRGGY EYSDQKSGKS KGKDVNLAEF AVAAGDQMLY RSEDIQLDYK NNILKERAEL 420
AHSPLPAKYI DLDKGFRKEN CK 442 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. 
Interpro
 IPR007110; Ig-like_dom.
 IPR013783; Ig-like_fold.
 IPR003599; Ig_sub.
 IPR013106; Ig_V-set. 
Pfam
 PF07686; V-set 
SMART
 SM00409; IG 
PROSITE
 PS50835; IG_LIKE 
PRINTS