CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006811
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Fibulin-2 
Protein Synonyms/Alias
 FIBL-2 
Gene Name
 Fbln2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
144GCVHSGRKYAAGHTVacetylation[1]
475QCCISYLKEKSCVAGacetylation[1]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441
Functional Description
 Its binding to fibronectin and some other ligands is calcium dependent. 
Sequence Annotation
 DOMAIN 435 477 Anaphylatoxin-like 1.
 DOMAIN 478 510 Anaphylatoxin-like 2.
 DOMAIN 511 543 Anaphylatoxin-like 3.
 DOMAIN 594 635 EGF-like 1; calcium-binding (Potential).
 DOMAIN 669 708 EGF-like 2.
 DOMAIN 709 755 EGF-like 3; calcium-binding (Potential).
 DOMAIN 756 800 EGF-like 4; calcium-binding (Potential).
 DOMAIN 801 846 EGF-like 5; calcium-binding (Potential).
 DOMAIN 847 894 EGF-like 6; calcium-binding (Potential).
 DOMAIN 895 937 EGF-like 7; calcium-binding (Potential).
 DOMAIN 938 979 EGF-like 8; calcium-binding (Potential).
 DOMAIN 980 1018 EGF-like 9; calcium-binding (Potential).
 DOMAIN 1019 1061 EGF-like 10; calcium-binding (Potential).
 DOMAIN 1062 1106 EGF-like 11; calcium-binding (Potential).
 REGION 27 434 N.
 REGION 27 176 Subdomain NA (Cys-rich).
 REGION 177 434 Subdomain NB (Cys-free).
 REGION 1111 1221 Domain III.
 MOTIF 421 423 Cell attachment site (Potential).
 CARBOHYD 179 179 N-linked (GlcNAc...) (Potential).
 CARBOHYD 497 497 N-linked (GlcNAc...) (Potential).
 CARBOHYD 737 737 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1072 1072 N-linked (GlcNAc...) (Potential).
 DISULFID 435 462 By similarity.
 DISULFID 436 469 By similarity.
 DISULFID 449 470 By similarity.
 DISULFID 479 508 By similarity.
 DISULFID 492 509 By similarity.
 DISULFID 511 535 By similarity.
 DISULFID 512 542 By similarity.
 DISULFID 525 543 By similarity.
 DISULFID 598 610 By similarity.
 DISULFID 606 619 By similarity.
 DISULFID 621 634 By similarity.
 DISULFID 673 683 By similarity.
 DISULFID 679 692 By similarity.
 DISULFID 694 707 By similarity.
 DISULFID 713 726 By similarity.
 DISULFID 720 735 By similarity.
 DISULFID 742 754 By similarity.
 DISULFID 805 818 By similarity.
 DISULFID 812 827 By similarity.
 DISULFID 833 845 By similarity.
 DISULFID 899 912 By similarity.
 DISULFID 906 921 By similarity.
 DISULFID 923 936 By similarity.
 DISULFID 942 954 By similarity.
 DISULFID 950 963 By similarity.
 DISULFID 965 978 By similarity.
 DISULFID 984 993 By similarity.
 DISULFID 989 1002 By similarity.
 DISULFID 1004 1017 By similarity.
 DISULFID 1023 1035 By similarity.
 DISULFID 1031 1044 By similarity.
 DISULFID 1046 1060 By similarity.
 DISULFID 1066 1079 By similarity.
 DISULFID 1073 1088 By similarity.
 DISULFID 1093 1105 By similarity.  
Keyword
 Alternative splicing; Calcium; Complete proteome; Direct protein sequencing; Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein; Reference proteome; Repeat; Secreted; Signal. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1221 AA 
Protein Sequence
MLLQESAGVW LALALVTALT PSPSMAVPWQ DCTGAECPLL ENCIEEALEP GACCATCVQQ 60
GCACEGYQYY DCVQGGFVDG RVPAGQSYFV DFGSTECSCP PGGGKISCQF MLCPELPPNC 120
IEAVVVADSC PQCGQVGCVH SGRKYAAGHT VHLSSCRACH CPDAGGELIC YQLPGCHGNF 180
SDAEEGDSER QYEDPYSYDQ EVAEAEATTA IVNEVQAGAE GPPAALGGGN LPPSSIRVTP 240
WPVALPRPTA AAALGPPAPV QAKARRVTLD TEEDEEEEEE ETLVTEPPTA GSPGRLDSLP 300
TRSPARPGFP VQEKEAEAKA GPEENLIPDA QVTPRSVMQE GAAPLPRSGL AALSPSLATD 360
SSSEDPVKPS DHPTLSTLPP DRAQVSPSPE TPEEIPQHPQ LLPRFRAEED IDPNSVHSVP 420
RGDLDGSTKD LIETCCAAGQ QWAIDNDECQ EIPENGAQSD ICRIAQRQCC ISYLKEKSCV 480
AGVMGAKEGE TCGAEDNDTC GVSLYKQCCD CCGLGLRVRA EGQSCESNPN LGYPCNHVML 540
SCCEGEEPLI VPEVRRPPEP EAAPRRVSEM EMASREALSL GTEAELPNSL PGDDQDECLM 600
LPGELCQHLC INTVGSYRCA CFPGFELQGD GRTCRPDRGA PQLDTARESA PRSESAQVSP 660
NTIPLPVPQP NTCKDNGPCR QVCRVVGDTA MCSCFPGYAI MADGVSCEDQ DECLMGTHDC 720
SWKQFCVNTL GSFYCVNHTV LCAEGYILNA HRKCVDINEC VTDLHTCTRA EHCVNTPGSF 780
QCYKALTCEP GYVLTDGECT DVDECVTGTH NCQAGFSCQN TKGSFYCQAR QRCMDGFLQD 840
PEGNCVDINE CTSLLEPCRS GFSCINTVGS YTCQRNPLVC GRGYHANEEG SECVDVNECE 900
TGVHRCGEGQ LCYNLPGSYR CDCKPGFQRD AFGRTCIDVN ECWVSPGRLC QHTCENTPGS 960
YRCSCAAGFL LAADGKHCED VNECETRRCS QECANIYGSY QCYCRQGYQL AEDGHTCTDI 1020
DECAQGAGIL CTFRCVNVPG SYQCACPEQG YTMMANGRSC KDLDECALGT HNCSEAETCH 1080
NIQGSFRCLR FDCPPNYVRV SETKCERTTC QDITECQTSP ARITHYQLNF QTGLLVPAHI 1140
FRIGPAPAFA GDTISLTITK GNEEGYFVTR RLNAYTGVVS LQRSVLEPRD FALDVEMKLW 1200
RQGSVTTFLA KMYIFFTTFA P 1221 
Gene Ontology
 GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0050840; F:extracellular matrix binding; IDA:MGI.
 GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:MGI. 
Interpro
 IPR000020; Anaphylatoxin/fibulin.
 IPR026823; cEGF.
 IPR000742; EG-like_dom.
 IPR001881; EGF-like_Ca-bd.
 IPR013032; EGF-like_CS.
 IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
 IPR018097; EGF_Ca-bd_CS. 
Pfam
 PF01821; ANATO
 PF12662; cEGF
 PF07645; EGF_CA 
SMART
 SM00104; ANATO
 SM00181; EGF
 SM00179; EGF_CA 
PROSITE
 PS01177; ANAPHYLATOXIN_1
 PS01178; ANAPHYLATOXIN_2
 PS00010; ASX_HYDROXYL
 PS00022; EGF_1
 PS01186; EGF_2
 PS50026; EGF_3
 PS01187; EGF_CA 
PRINTS