CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003902
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Fibronectin 
Protein Synonyms/Alias
 FN; Anastellin 
Gene Name
 Fn1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
91RGFNCESKPEPEETCacetylation[1]
181GKGEWTCKPIAEKCFacetylation[1]
444EGRRDNMKWCGTTQNacetylation[1]
486RIGDQWDKQHDLGHMacetylation[1]
554GQGRGRWKCDPIDQCacetylation[1]
655KTSTGRWKEATIPGHacetylation[1]
1049NVGPLASKYPLRNLQacetylation[1]
1076KGNQQSPKATGVFTTubiquitination[2]
1622GDSPASSKPVSINYKacetylation[1]
1634NYKTEIDKPSQMQVTacetylation[3]
2026RITGYIIKYEKPGSPacetylation[1]
2029GYIIKYEKPGSPPREacetylation[3]
2071IALKNNQKSEPLIGRacetylation[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]
 [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337] 
Functional Description
 Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape healing, and maintenance of cell shape. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. Participates in the regulation of type I collagen deposition by osteoblasts. 
Sequence Annotation
 DOMAIN 51 91 Fibronectin type-I 1.
 DOMAIN 96 139 Fibronectin type-I 2.
 DOMAIN 140 183 Fibronectin type-I 3.
 DOMAIN 185 229 Fibronectin type-I 4.
 DOMAIN 230 274 Fibronectin type-I 5.
 DOMAIN 306 343 Fibronectin type-I 6.
 DOMAIN 355 403 Fibronectin type-II 1.
 DOMAIN 415 463 Fibronectin type-II 2.
 DOMAIN 468 516 Fibronectin type-I 7.
 DOMAIN 516 558 Fibronectin type-I 8.
 DOMAIN 559 602 Fibronectin type-I 9.
 DOMAIN 607 699 Fibronectin type-III 1.
 DOMAIN 719 808 Fibronectin type-III 2.
 DOMAIN 810 897 Fibronectin type-III 3.
 DOMAIN 905 994 Fibronectin type-III 4.
 DOMAIN 995 1083 Fibronectin type-III 5.
 DOMAIN 1091 1171 Fibronectin type-III 6.
 DOMAIN 1172 1264 Fibronectin type-III 7.
 DOMAIN 1265 1355 Fibronectin type-III 8; extra domain 1.
 DOMAIN 1356 1446 Fibronectin type-III 9.
 DOMAIN 1447 1536 Fibronectin type-III 10.
 DOMAIN 1537 1626 Fibronectin type-III 11.
 DOMAIN 1631 1720 Fibronectin type-III 12.
 DOMAIN 1721 1810 Fibronectin type-III 13; extra domain 2.
 DOMAIN 1813 1900 Fibronectin type-III 14.
 DOMAIN 1903 1991 Fibronectin type-III 15.
 DOMAIN 1992 2081 Fibronectin type-III 16.
 DOMAIN 2190 2280 Fibronectin type-III 17.
 DOMAIN 2294 2338 Fibronectin type-I 10.
 DOMAIN 2339 2381 Fibronectin type-I 11.
 DOMAIN 2383 2426 Fibronectin type-I 12.
 DNA_BIND 906 1171
 REGION 53 273 Fibrin- and heparin-binding 1.
 REGION 308 608 Collagen-binding.
 REGION 1357 1630 Cell-attachment.
 REGION 1811 2081 Heparin-binding 2.
 REGION 2082 2201 Connecting strand 3 (CS-3) (V region).
 REGION 2296 2427 Fibrin-binding 2.
 MOTIF 1614 1616 Cell attachment site.
 MOTIF 2181 2183 Cell attachment site.
 MOD_RES 33 33 Pyrrolidone carboxylic acid (By
 MOD_RES 875 875 Sulfotyrosine (Potential).
 MOD_RES 880 880 Sulfotyrosine (Potential).
 MOD_RES 2392 2392 Sulfotyrosine (Potential).
 MOD_RES 2475 2475 Phosphoserine.
 CARBOHYD 430 430 N-linked (GlcNAc...) (Potential).
 CARBOHYD 528 528 N-linked (GlcNAc...).
 CARBOHYD 542 542 N-linked (GlcNAc...) (Potential).
 CARBOHYD 876 876 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1001 1001 N-linked (GlcNAc...); atypical.
 CARBOHYD 1006 1006 N-linked (GlcNAc...).
 CARBOHYD 1243 1243 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1290 1290 N-linked (GlcNAc...).
 CARBOHYD 2198 2198 N-linked (GlcNAc...).
 DISULFID 53 79 By similarity.
 DISULFID 77 88 By similarity.
 DISULFID 98 126 By similarity.
 DISULFID 124 136 By similarity.
 DISULFID 142 170 By similarity.
 DISULFID 168 180 By similarity.
 DISULFID 187 216 By similarity.
 DISULFID 214 226 By similarity.
 DISULFID 232 261 By similarity.
 DISULFID 259 271 By similarity.
 DISULFID 308 335 By similarity.
 DISULFID 333 342 By similarity.
 DISULFID 360 386 By similarity.
 DISULFID 374 401 By similarity.
 DISULFID 420 446 By similarity.
 DISULFID 434 461 By similarity.
 DISULFID 470 498 By similarity.
 DISULFID 496 508 By similarity.
 DISULFID 518 545 By similarity.
 DISULFID 543 555 By similarity.
 DISULFID 561 589 By similarity.
 DISULFID 587 599 By similarity.
 DISULFID 2296 2325 By similarity.
 DISULFID 2323 2335 By similarity.
 DISULFID 2341 2368 By similarity.
 DISULFID 2366 2378 By similarity.
 DISULFID 2385 2411 By similarity.
 DISULFID 2409 2420 By similarity.
 DISULFID 2458 2458 Interchain (with C-2462).
 DISULFID 2462 2462 Interchain (with C-2458).
 CROSSLNK 35 35 Isoglutamyl lysine isopeptide (Gln-Lys)
 CROSSLNK 36 36 Isoglutamyl lysine isopeptide (Gln-Lys)
 CROSSLNK 48 48 Isoglutamyl lysine isopeptide (Gln-Lys)  
Keyword
 3D-structure; Acute phase; Alternative splicing; Angiogenesis; Cell adhesion; Cell shape; Complete proteome; Disulfide bond; Extracellular matrix; Glycoprotein; Heparin-binding; Isopeptide bond; Phosphoprotein; Pyrrolidone carboxylic acid; Reference proteome; Repeat; Secreted; Signal; Sulfation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2477 AA 
Protein Sequence
MLRGPGPGRL LLLAVLCLGT SVRCTEAGKS KRQAQQIVQP QSPVAVSQSK PGCFDNGKHY 60
QINQQWERTY LGNALVCTCY GGSRGFNCES KPEPEETCFD KYTGNTYKVG DTYERPKDSM 120
IWDCTCIGAG RGRISCTIAN RCHEGGQSYK IGDKWRRPHE TGGYMLECLC LGNGKGEWTC 180
KPIAEKCFDH AAGTSYVVGE TWEKPYQGWM MVDCTCLGEG NGRITCTSRN RCNDQDTRTS 240
YRIGDTWSKK DNRGNLLQCV CTGNGRGEWK CERHALQSAS AGSGSFTDVR TAIYQPQTHP 300
QPAPYGHCVT DSGVVYSVGM QWLKSQGNKQ MLCTCLGNGV SCQETAVTQT YGGNSNGEPC 360
VLPFTYNGRT FYSCTTEGRQ DGHLWCSTTS NYEQDQKYSF CTDHAVLVQT RGGNSNGALC 420
HFPFLYNNRN YTDCTSEGRR DNMKWCGTTQ NYDADQKFGF CPMAAHEEIC TTNEGVMYRI 480
GDQWDKQHDL GHMMRCTCVG NGRGEWACIP YSQLRDQCIV DDITYNVNDT FHKRHEEGHM 540
LNCTCFGQGR GRWKCDPIDQ CQDSETRTFY QIGDSWEKFV HGVRYQCYCY GRGIGEWHCQ 600
PLQTYPGTTG PVQVIITETP SQPNSHPIQW NAPEPSHITK YILRWRPKTS TGRWKEATIP 660
GHLNSYTIKG LTPGVIYEGQ LISIQQYGHR EVTRFDFTTS ASTPVTSNTV TGETAPYSPV 720
VATSESVTEI TASSFVVSWV SASDTVSGFR VEYELSEEGD EPQYLDLPST ATSVNIPDLL 780
PGRKYIVNVY QISEEGKQSL ILSTSQTTAP DAPPDPTVDQ VDDTSIVVRW SRPQAPITGY 840
RIVYSPSVEG SSTELNLPET ANSVTLSDLQ PGVQYNITIY AVEENQESTP VFIQQETTGT 900
PRSDNVPPPT DLQFVELTDV KVTIMWTPPD SVVSGYRVEV LPVSLPGEHG QRLPVNRNTF 960
AEITGLSPGV TYLFKVFAVH QGRESNPLTA QQTTKLDAPT NLQFVNETDR TVLVTWTPPR 1020
ARIAGYRLTA GLTRGGQPKQ YNVGPLASKY PLRNLQPGSE YTVTLVAVKG NQQSPKATGV 1080
FTTLQPLRSI PPYNTEVTET TIVITWTPAP RIGFKLGVRP SQGGEAPREV TSDSGSIVVS 1140
GLTPGVEYTY TIQVLRDGQE RDAPIVNRVV TPLSPPTNLH LEANPDTGVL TVSWERSTTP 1200
DITGYRITTT PTNGQQGTSL EEVVHADQSS CTFENLNPGL EYNVSVYTVK DDKESAPISD 1260
TVVPEVPQLT DLSFVDITDS SIGLRWTPLN SSTIIGYRIT VVAAGEGIPI FEDFVDSSVG 1320
YYTVTGLEPG IDYDISVITL INGGESAPTT LTQQTAVPPP TDLRFTNIGP DTMRVTWAPP 1380
PSIELTNLLV RYSPVKNEED VAELSISPSD NAVVLTNLLP GTEYLVSVSS VYEQHESIPL 1440
RGRQKTGLDS PTGFDSSDIT ANSFTVHWVA PRAPITGYII RHHAEHSVGR PRQDRVPPSR 1500
NSITLTNLNP GTEYVVSIIA VNGREESPPL IGQQATVSDI PRDLEVIAST PTSLLISWEP 1560
PAVSVRYYRI TYGETGGNSP VQEFTVPGSK STATINNIKP GADYTITLYA VTGRGDSPAS 1620
SKPVSINYKT EIDKPSQMQV TDVQDNSISV RWLPSTSPVT GYRVTTTPKN GLGPSKTKTA 1680
SPDQTEMTIE GLQPTVEYVV SVYAQNRNGE SQPLVQTAVT NIDRPKGLAF TDVDVDSIKI 1740
AWESPQGQVS RYRVTYSSPE DGIRELFPAP DGEDDTAELQ GLRPGSEYTV SVVALHDDME 1800
SQPLIGIQST AIPAPTNLKF SQVTPTSFTA QWIAPSVQLT GYRVRVNPKE KTGPMKEINL 1860
SPDSSSVIVS GLMVATKYEV SVYALKDTLT SRPAQGVITT LENVSPPRRA RVTDATETTI 1920
TISWRTKTET ITGFQVDAIP ANGQTPVQRS ISPDVRSYTI TGLQPGTDYK IHLYTLNDNA 1980
RSSPVIIDAS TAIDAPSNLR FLTTTPNSLL VSWQAPRARI TGYIIKYEKP GSPPREVVPR 2040
PRPGVTEATI TGLEPGTEYT IYVIALKNNQ KSEPLIGRKK TDELPQLVTL PHPNLHGPEI 2100
LDVPSTVQKT PFITNPGYDT ENGIQLPGTT HQQPSVGQQM IFEEHGFRRT TPPTAATPVR 2160
LRPRPYLPNV DEEVQIGHVP RGDVDYHLYP HVPGLNPNAS TGQEALSQTT ISWTPFQESS 2220
EYIISCQPVG TDEEPLQFQV PGTSTSATLT GLTRGVTYNI IVEALQNQRR HKVREEVVTV 2280
GNAVSEGLNQ PTDDSCFDPY TVSHYAIGEE WERLSDAGFK LTCQCLGFGS GHFRCDSSKW 2340
CHDNGVNYKI GEKWDRQGEN GQRMSCTCLG NGKGEFKCDP HEATCYDDGK TYHVGEQWQK 2400
EYLGAICSCT CFGGQRGWRC DNCRRPGAAE PSPDGTTGHT YNQYTQRYNQ RTNTNVNCPI 2460
ECFMPLDVQA DRDDSRE 2477 
Gene Ontology
 GO:0016324; C:apical plasma membrane; IDA:MGI.
 GO:0005604; C:basement membrane; IDA:MGI.
 GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:Compara.
 GO:0005577; C:fibrinogen complex; IEA:Compara.
 GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
 GO:0016504; F:peptidase activator activity; IDA:MGI.
 GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
 GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
 GO:0007161; P:calcium-independent cell-matrix adhesion; IDA:MGI.
 GO:0007044; P:cell-substrate junction assembly; IDA:MGI.
 GO:0018149; P:peptide cross-linking; IEA:Compara.
 GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
 GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Compara.
 GO:0042060; P:wound healing; IMP:MGI. 
Interpro
 IPR000083; Fibronectin_type1.
 IPR003961; Fibronectin_type3.
 IPR000562; FN_type2_col-bd.
 IPR013783; Ig-like_fold.
 IPR013806; Kringle-like. 
Pfam
 PF00039; fn1
 PF00040; fn2
 PF00041; fn3 
SMART
 SM00058; FN1
 SM00059; FN2
 SM00060; FN3 
PROSITE
 PS00022; EGF_1
 PS01253; FN1_1
 PS51091; FN1_2
 PS00023; FN2_1
 PS51092; FN2_2
 PS50853; FN3 
PRINTS