CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002115
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 von Willebrand factor 
Protein Synonyms/Alias
 vWF; von Willebrand antigen 2; von Willebrand antigen II 
Gene Name
 VWF 
Gene Synonyms/Alias
 F8VWF 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
1720FAKAFISKANIGPRLubiquitination[1, 2]
Reference
 [1] Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry.
 Denis NJ, Vasilescu J, Lambert JP, Smith JC, Figeys D.
 Proteomics. 2007 Mar;7(6):868-74. [PMID: 17370265]
 [2] 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] 
Functional Description
 Important in the maintenance of hemostasis, it promotes adhesion of platelets to the sites of vascular injury by forming a molecular bridge between sub-endothelial collagen matrix and platelet-surface receptor complex GPIb-IX-V. Also acts as a chaperone for coagulation factor VIII, delivering it to the site of injury, stabilizing its heterodimeric structure and protecting it from premature clearance from plasma. 
Sequence Annotation
 DOMAIN 34 240 VWFD 1.
 DOMAIN 295 348 TIL 1.
 DOMAIN 387 598 VWFD 2.
 DOMAIN 652 707 TIL 2.
 DOMAIN 776 827 TIL 3.
 DOMAIN 866 1074 VWFD 3.
 DOMAIN 1146 1196 TIL 4.
 DOMAIN 1277 1453 VWFA 1; binding site for platelet
 DOMAIN 1498 1665 VWFA 2.
 DOMAIN 1691 1871 VWFA 3; main binding site for collagens
 DOMAIN 1949 2153 VWFD 4.
 DOMAIN 2255 2328 VWFC 1.
 DOMAIN 2429 2495 VWFC 2.
 DOMAIN 2580 2645 VWFC 3.
 DOMAIN 2724 2812 CTCK.
 REGION 764 787 Amino-terminal.
 REGION 788 833 E1.
 REGION 826 853 CX.
 REGION 2216 2261 E2.
 MOTIF 2507 2509 Cell attachment site.
 CARBOHYD 99 99 N-linked (GlcNAc...) (Potential).
 CARBOHYD 156 156 N-linked (GlcNAc...) (Potential).
 CARBOHYD 211 211 N-linked (GlcNAc...) (Potential).
 CARBOHYD 666 666 N-linked (GlcNAc...) (Potential).
 CARBOHYD 857 857 N-linked (GlcNAc...).
 CARBOHYD 1147 1147 N-linked (GlcNAc...); atypical.
 CARBOHYD 1231 1231 N-linked (GlcNAc...).
 CARBOHYD 1248 1248 O-linked (GalNAc...) (Probable).
 CARBOHYD 1255 1255 O-linked (GalNAc...) (Probable).
 CARBOHYD 1256 1256 O-linked (GalNAc...) (Probable).
 CARBOHYD 1263 1263 O-linked (GalNAc...) (Probable).
 CARBOHYD 1468 1468 O-linked (GalNAc...) (Probable).
 CARBOHYD 1477 1477 O-linked (GalNAc...) (Probable).
 CARBOHYD 1486 1486 O-linked (GalNAc...) (Probable).
 CARBOHYD 1487 1487 O-linked (GalNAc...) (Probable).
 CARBOHYD 1515 1515 N-linked (GlcNAc...).
 CARBOHYD 1574 1574 N-linked (GlcNAc...).
 CARBOHYD 1679 1679 O-linked (GalNAc...) (Probable).
 CARBOHYD 2223 2223 N-linked (GlcNAc...).
 CARBOHYD 2290 2290 N-linked (GlcNAc...).
 CARBOHYD 2298 2298 O-linked (GalNAc...) (Probable).
 CARBOHYD 2357 2357 N-linked (GlcNAc...).
 CARBOHYD 2400 2400 N-linked (GlcNAc...).
 CARBOHYD 2546 2546 N-linked (GlcNAc...).
 CARBOHYD 2585 2585 N-linked (GlcNAc...).
 CARBOHYD 2790 2790 N-linked (GlcNAc...).
 DISULFID 767 808
 DISULFID 776 804
 DISULFID 810 821
 DISULFID 867 996
 DISULFID 889 1031
 DISULFID 898 993
 DISULFID 914 921
 DISULFID 1060 1084
 DISULFID 1071 1111
 DISULFID 1089 1091
 DISULFID 1126 1130
 DISULFID 1149 1169
 DISULFID 1153 1165
 DISULFID 1196 1199
 DISULFID 1234 1237
 DISULFID 1272 1458
 DISULFID 1669 1670
 DISULFID 1686 1872
 DISULFID 1879 1904
 DISULFID 1899 1940 Or C-1899 with C-1942.
 DISULFID 1927 2088
 DISULFID 1950 2085
 DISULFID 1972 2123
 DISULFID 1993 2001
 DISULFID 2724 2774 By similarity.
 DISULFID 2739 2788 By similarity.
 DISULFID 2750 2804 By similarity.
 DISULFID 2754 2806 By similarity.
 DISULFID ? 2811 By similarity.
 CROSSLNK 1720 1720 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Blood coagulation; Cell adhesion; Cleavage on pair of basic residues; Complete proteome; Direct protein sequencing; Disease mutation; Disulfide bond; Extracellular matrix; Glycoprotein; Hemostasis; Isopeptide bond; Polymorphism; Reference proteome; Repeat; Secreted; Signal; Ubl conjugation; von Willebrand disease. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2813 AA 
Protein Sequence
MIPARFAGVL LALALILPGT LCAEGTRGRS STARCSLFGS DFVNTFDGSM YSFAGYCSYL 60
LAGGCQKRSF SIIGDFQNGK RVSLSVYLGE FFDIHLFVNG TVTQGDQRVS MPYASKGLYL 120
ETEAGYYKLS GEAYGFVARI DGSGNFQVLL SDRYFNKTCG LCGNFNIFAE DDFMTQEGTL 180
TSDPYDFANS WALSSGEQWC ERASPPSSSC NISSGEMQKG LWEQCQLLKS TSVFARCHPL 240
VDPEPFVALC EKTLCECAGG LECACPALLE YARTCAQEGM VLYGWTDHSA CSPVCPAGME 300
YRQCVSPCAR TCQSLHINEM CQERCVDGCS CPEGQLLDEG LCVESTECPC VHSGKRYPPG 360
TSLSRDCNTC ICRNSQWICS NEECPGECLV TGQSHFKSFD NRYFTFSGIC QYLLARDCQD 420
HSFSIVIETV QCADDRDAVC TRSVTVRLPG LHNSLVKLKH GAGVAMDGQD VQLPLLKGDL 480
RIQHTVTASV RLSYGEDLQM DWDGRGRLLV KLSPVYAGKT CGLCGNYNGN QGDDFLTPSG 540
LAEPRVEDFG NAWKLHGDCQ DLQKQHSDPC ALNPRMTRFS EEACAVLTSP TFEACHRAVS 600
PLPYLRNCRY DVCSCSDGRE CLCGALASYA AACAGRGVRV AWREPGRCEL NCPKGQVYLQ 660
CGTPCNLTCR SLSYPDEECN EACLEGCFCP PGLYMDERGD CVPKAQCPCY YDGEIFQPED 720
IFSDHHTMCY CEDGFMHCTM SGVPGSLLPD AVLSSPLSHR SKRSLSCRPP MVKLVCPADN 780
LRAEGLECTK TCQNYDLECM SMGCVSGCLC PPGMVRHENR CVALERCPCF HQGKEYAPGE 840
TVKIGCNTCV CQDRKWNCTD HVCDATCSTI GMAHYLTFDG LKYLFPGECQ YVLVQDYCGS 900
NPGTFRILVG NKGCSHPSVK CKKRVTILVE GGEIELFDGE VNVKRPMKDE THFEVVESGR 960
YIILLLGKAL SVVWDRHLSI SVVLKQTYQE KVCGLCGNFD GIQNNDLTSS NLQVEEDPVD 1020
FGNSWKVSSQ CADTRKVPLD SSPATCHNNI MKQTMVDSSC RILTSDVFQD CNKLVDPEPY 1080
LDVCIYDTCS CESIGDCACF CDTIAAYAHV CAQHGKVVTW RTATLCPQSC EERNLRENGY 1140
ECEWRYNSCA PACQVTCQHP EPLACPVQCV EGCHAHCPPG KILDELLQTC VDPEDCPVCE 1200
VAGRRFASGK KVTLNPSDPE HCQICHCDVV NLTCEACQEP GGLVVPPTDA PVSPTTLYVE 1260
DISEPPLHDF YCSRLLDLVF LLDGSSRLSE AEFEVLKAFV VDMMERLRIS QKWVRVAVVE 1320
YHDGSHAYIG LKDRKRPSEL RRIASQVKYA GSQVASTSEV LKYTLFQIFS KIDRPEASRI 1380
TLLLMASQEP QRMSRNFVRY VQGLKKKKVI VIPVGIGPHA NLKQIRLIEK QAPENKAFVL 1440
SSVDELEQQR DEIVSYLCDL APEAPPPTLP PDMAQVTVGP GLLGVSTLGP KRNSMVLDVA 1500
FVLEGSDKIG EADFNRSKEF MEEVIQRMDV GQDSIHVTVL QYSYMVTVEY PFSEAQSKGD 1560
ILQRVREIRY QGGNRTNTGL ALRYLSDHSF LVSQGDREQA PNLVYMVTGN PASDEIKRLP 1620
GDIQVVPIGV GPNANVQELE RIGWPNAPIL IQDFETLPRE APDLVLQRCC SGEGLQIPTL 1680
SPAPDCSQPL DVILLLDGSS SFPASYFDEM KSFAKAFISK ANIGPRLTQV SVLQYGSITT 1740
IDVPWNVVPE KAHLLSLVDV MQREGGPSQI GDALGFAVRY LTSEMHGARP GASKAVVILV 1800
TDVSVDSVDA AADAARSNRV TVFPIGIGDR YDAAQLRILA GPAGDSNVVK LQRIEDLPTM 1860
VTLGNSFLHK LCSGFVRICM DEDGNEKRPG DVWTLPDQCH TVTCQPDGQT LLKSHRVNCD 1920
RGLRPSCPNS QSPVKVEETC GCRWTCPCVC TGSSTRHIVT FDGQNFKLTG SCSYVLFQNK 1980
EQDLEVILHN GACSPGARQG CMKSIEVKHS ALSVELHSDM EVTVNGRLVS VPYVGGNMEV 2040
NVYGAIMHEV RFNHLGHIFT FTPQNNEFQL QLSPKTFASK TYGLCGICDE NGANDFMLRD 2100
GTVTTDWKTL VQEWTVQRPG QTCQPILEEQ CLVPDSSHCQ VLLLPLFAEC HKVLAPATFY 2160
AICQQDSCHQ EQVCEVIASY AHLCRTNGVC VDWRTPDFCA MSCPPSLVYN HCEHGCPRHC 2220
DGNVSSCGDH PSEGCFCPPD KVMLEGSCVP EEACTQCIGE DGVQHQFLEA WVPDHQPCQI 2280
CTCLSGRKVN CTTQPCPTAK APTCGLCEVA RLRQNADQCC PEYECVCDPV SCDLPPVPHC 2340
ERGLQPTLTN PGECRPNFTC ACRKEECKRV SPPSCPPHRL PTLRKTQCCD EYECACNCVN 2400
STVSCPLGYL ASTATNDCGC TTTTCLPDKV CVHRSTIYPV GQFWEEGCDV CTCTDMEDAV 2460
MGLRVAQCSQ KPCEDSCRSG FTYVLHEGEC CGRCLPSACE VVTGSPRGDS QSSWKSVGSQ 2520
WASPENPCLI NECVRVKEEV FIQQRNVSCP QLEVPVCPSG FQLSCKTSAC CPSCRCERME 2580
ACMLNGTVIG PGKTVMIDVC TTCRCMVQVG VISGFKLECR KTTCNPCPLG YKEENNTGEC 2640
CGRCLPTACT IQLRGGQIMT LKRDETLQDG CDTHFCKVNE RGEYFWEKRV TGCPPFDEHK 2700
CLAEGGKIMK IPGTCCDTCE EPECNDITAR LQYVKVGSCK SEVEVDIHYC QGKCASKAMY 2760
SIDINDVQDQ CSCCSPTRTE PMQVALHCTN GSVVYHEVLN AMECKCSPRK CSK 2813 
Gene Ontology
 GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
 GO:0009897; C:external side of plasma membrane; IEA:Compara.
 GO:0031012; C:extracellular matrix; IDA:UniProtKB.
 GO:0005576; C:extracellular region; IDA:UniProtKB.
 GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
 GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
 GO:0033093; C:Weibel-Palade body; IDA:UniProtKB.
 GO:0051087; F:chaperone binding; IDA:UniProtKB.
 GO:0005518; F:collagen binding; IDA:UniProtKB.
 GO:0001948; F:glycoprotein binding; IDA:UniProtKB.
 GO:0019865; F:immunoglobulin binding; IDA:UniProtKB.
 GO:0002020; F:protease binding; IDA:MGI.
 GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
 GO:0007597; P:blood coagulation, intrinsic pathway; TAS:Reactome.
 GO:0031589; P:cell-substrate adhesion; IDA:UniProtKB.
 GO:0001889; P:liver development; IEA:Compara.
 GO:0001890; P:placenta development; IEA:Compara.
 GO:0030168; P:platelet activation; IDA:UniProtKB.
 GO:0002576; P:platelet degranulation; TAS:Reactome.
 GO:0051260; P:protein homooligomerization; IDA:UniProtKB. 
Interpro
 IPR006207; Cys_knot_C.
 IPR002919; TIL_dom.
 IPR014853; Unchr_dom_Cys-rich.
 IPR012011; VWF.
 IPR002035; VWF_A.
 IPR001007; VWF_C.
 IPR001846; VWF_type-D. 
Pfam
 PF08742; C8
 PF01826; TIL
 PF00092; VWA
 PF00093; VWC
 PF00094; VWD 
SMART
 SM00832; C8
 SM00041; CT
 SM00327; VWA
 SM00214; VWC
 SM00216; VWD 
PROSITE
 PS01185; CTCK_1
 PS01225; CTCK_2
 PS50234; VWFA
 PS01208; VWFC_1
 PS50184; VWFC_2
 PS51233; VWFD 
PRINTS