CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011407
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Amyloid-like protein 2 
Protein Synonyms/Alias
 APLP-2; APPH; Amyloid protein homolog; CDEI box-binding protein; CDEBP 
Gene Name
 APLP2 
Gene Synonyms/Alias
 APPL2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
744PEERHLNKMQNHGYEubiquitination[1, 2, 3, 4, 5]
756GYENPTYKYLEQMQIubiquitination[1, 2, 3, 4, 5]
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] 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]
 [4] 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]
 [5] 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] 
Functional Description
 May play a role in the regulation of hemostasis. The soluble form may have inhibitory properties towards coagulation factors. May interact with cellular G-protein signaling pathways. May bind to the DNA 5'-GTCACATG-3'(CDEI box). Inhibits trypsin, chymotrypsin, plasmin, factor XIA and plasma and glandular kallikrein. Modulates the Cu/Zn nitric oxide-catalyzed autodegradation of GPC1 heparan sulfate side chains in fibroblasts (By similarity). 
Sequence Annotation
 DOMAIN 306 364 BPTI/Kunitz inhibitor.
 REGION 749 763 Interaction with DAB2 (By similarity).
 MOTIF 750 755 NPXY motif.
 DISULFID 310 360 By similarity.
 DISULFID 319 343 By similarity.
 DISULFID 335 356 By similarity.  
Keyword
 Alternative splicing; Cell membrane; Complete proteome; Disulfide bond; DNA-binding; Glycoprotein; Membrane; Nucleus; Polymorphism; Protease inhibitor; Reference proteome; Serine protease inhibitor; Signal; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 763 AA 
Protein Sequence
MAATGTAAAA ATGRLLLLLL VGLTAPALAL AGYIEALAAN AGTGFAVAEP QIAMFCGKLN 60
MHVNIQTGKW EPDPTGTKSC FETKEEVLQY CQEMYPELQI TNVMEANQRV SIDNWCRRDK 120
KQCKSRFVTP FKCLVGEFVS DVLLVPEKCQ FFHKERMEVC ENHQHWHTVV KEACLTQGMT 180
LYSYGMLLPC GVDQFHGTEY VCCPQTKIIG SVSKEEEEED EEEEEEEDEE EDYDVYKSEF 240
PTEADLEDFT EAAVDEDDED EEEGEEVVED RDYYYDTFKG DDYNEENPTE PGSDGTMSDK 300
EITHDVKAVC SQEAMTGPCR AVMPRWYFDL SKGKCVRFIY GGCGGNRNNF ESEDYCMAVC 360
KAMIPPTPLP TNDVDVYFET SADDNEHARF QKAKEQLEIR HRNRMDRVKK EWEEAELQAK 420
NLPKAERQTL IQHFQAMVKA LEKEAASEKQ QLVETHLARV EAMLNDRRRM ALENYLAALQ 480
SDPPRPHRIL QALRRYVRAE NKDRLHTIRH YQHVLAVDPE KAAQMKSQVM THLHVIEERR 540
NQSLSLLYKV PYVAQEIQEE IDELLQEQRA DMDQFTASIS ETPVDVRVSS EESEEIPPFH 600
PFHPFPALPE NEDTQPELYH PMKKGSGVGE QDGGLIGAEE KVINSKNKVD ENMVIDETLD 660
VKEMIFNAER VGGLEEERES VGPLREDFSL SSSALIGLLV IAVAIATVIV ISLVMLRKRQ 720
YGTISHGIVE VDPMLTPEER HLNKMQNHGY ENPTYKYLEQ MQI 763 
Gene Ontology
 GO:0016021; C:integral to membrane; NAS:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0003677; F:DNA binding; NAS:UniProtKB.
 GO:0008201; F:heparin binding; IEA:InterPro.
 GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
 GO:0046914; F:transition metal ion binding; IEA:InterPro.
 GO:0006878; P:cellular copper ion homeostasis; IEA:Compara.
 GO:0008203; P:cholesterol metabolic process; IEA:Compara.
 GO:0009790; P:embryo development; IEA:Compara.
 GO:0030198; P:extracellular matrix organization; IEA:Compara.
 GO:0030900; P:forebrain development; IEA:Compara.
 GO:0007186; P:G-protein coupled receptor signaling pathway; NAS:UniProtKB.
 GO:0007626; P:locomotory behavior; IEA:Compara.
 GO:0007617; P:mating behavior; IEA:Compara.
 GO:0030901; P:midbrain development; IEA:Compara.
 GO:0050885; P:neuromuscular process controlling balance; IEA:Compara.
 GO:0007176; P:regulation of epidermal growth factor-activated receptor activity; IEA:Compara.
 GO:0043393; P:regulation of protein binding; IEA:Compara.
 GO:0001967; P:suckling behavior; IEA:Compara. 
Interpro
 IPR008155; Amyloid_glyco.
 IPR011178; Amyloid_glyco_Cu-bd.
 IPR024329; Amyloid_glyco_E2_domain.
 IPR008154; Amyloid_glyco_extra.
 IPR019744; Amyloid_glyco_extracell_CS.
 IPR015849; Amyloid_glyco_heparin-bd.
 IPR019745; Amyloid_glyco_intracell_CS.
 IPR019543; APP_amyloid_C.
 IPR002223; Prot_inh_Kunz-m.
 IPR020901; Prtase_inh_Kunz-CS. 
Pfam
 PF10515; APP_amyloid
 PF12924; APP_Cu_bd
 PF12925; APP_E2
 PF02177; APP_N
 PF00014; Kunitz_BPTI 
SMART
 SM00006; A4_EXTRA
 SM00131; KU 
PROSITE
 PS00319; A4_EXTRA
 PS00320; A4_INTRA
 PS00280; BPTI_KUNITZ_1
 PS50279; BPTI_KUNITZ_2 
PRINTS
 PR00203; AMYLOIDA4.
 PR00759; BASICPTASE.