dbPTM

VWF_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	VWF_HUMAN
UniProt AC	P04275
Protein Name	von Willebrand factor
Gene Name	VWF
Organism	Homo sapiens (Human).
Sequence Length	2813
Subcellular Localization	Secreted . Secreted, extracellular space, extracellular matrix . Localized to storage granules.
Protein 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..
Protein Sequence	MIPARFAGVLLALALILPGTLCAEGTRGRSSTARCSLFGSDFVNTFDGSMYSFAGYCSYLLAGGCQKRSFSIIGDFQNGKRVSLSVYLGEFFDIHLFVNGTVTQGDQRVSMPYASKGLYLETEAGYYKLSGEAYGFVARIDGSGNFQVLLSDRYFNKTCGLCGNFNIFAEDDFMTQEGTLTSDPYDFANSWALSSGEQWCERASPPSSSCNISSGEMQKGLWEQCQLLKSTSVFARCHPLVDPEPFVALCEKTLCECAGGLECACPALLEYARTCAQEGMVLYGWTDHSACSPVCPAGMEYRQCVSPCARTCQSLHINEMCQERCVDGCSCPEGQLLDEGLCVESTECPCVHSGKRYPPGTSLSRDCNTCICRNSQWICSNEECPGECLVTGQSHFKSFDNRYFTFSGICQYLLARDCQDHSFSIVIETVQCADDRDAVCTRSVTVRLPGLHNSLVKLKHGAGVAMDGQDVQLPLLKGDLRIQHTVTASVRLSYGEDLQMDWDGRGRLLVKLSPVYAGKTCGLCGNYNGNQGDDFLTPSGLAEPRVEDFGNAWKLHGDCQDLQKQHSDPCALNPRMTRFSEEACAVLTSPTFEACHRAVSPLPYLRNCRYDVCSCSDGRECLCGALASYAAACAGRGVRVAWREPGRCELNCPKGQVYLQCGTPCNLTCRSLSYPDEECNEACLEGCFCPPGLYMDERGDCVPKAQCPCYYDGEIFQPEDIFSDHHTMCYCEDGFMHCTMSGVPGSLLPDAVLSSPLSHRSKRSLSCRPPMVKLVCPADNLRAEGLECTKTCQNYDLECMSMGCVSGCLCPPGMVRHENRCVALERCPCFHQGKEYAPGETVKIGCNTCVCQDRKWNCTDHVCDATCSTIGMAHYLTFDGLKYLFPGECQYVLVQDYCGSNPGTFRILVGNKGCSHPSVKCKKRVTILVEGGEIELFDGEVNVKRPMKDETHFEVVESGRYIILLLGKALSVVWDRHLSISVVLKQTYQEKVCGLCGNFDGIQNNDLTSSNLQVEEDPVDFGNSWKVSSQCADTRKVPLDSSPATCHNNIMKQTMVDSSCRILTSDVFQDCNKLVDPEPYLDVCIYDTCSCESIGDCACFCDTIAAYAHVCAQHGKVVTWRTATLCPQSCEERNLRENGYECEWRYNSCAPACQVTCQHPEPLACPVQCVEGCHAHCPPGKILDELLQTCVDPEDCPVCEVAGRRFASGKKVTLNPSDPEHCQICHCDVVNLTCEACQEPGGLVVPPTDAPVSPTTLYVEDISEPPLHDFYCSRLLDLVFLLDGSSRLSEAEFEVLKAFVVDMMERLRISQKWVRVAVVEYHDGSHAYIGLKDRKRPSELRRIASQVKYAGSQVASTSEVLKYTLFQIFSKIDRPEASRITLLLMASQEPQRMSRNFVRYVQGLKKKKVIVIPVGIGPHANLKQIRLIEKQAPENKAFVLSSVDELEQQRDEIVSYLCDLAPEAPPPTLPPDMAQVTVGPGLLGVSTLGPKRNSMVLDVAFVLEGSDKIGEADFNRSKEFMEEVIQRMDVGQDSIHVTVLQYSYMVTVEYPFSEAQSKGDILQRVREIRYQGGNRTNTGLALRYLSDHSFLVSQGDREQAPNLVYMVTGNPASDEIKRLPGDIQVVPIGVGPNANVQELERIGWPNAPILIQDFETLPREAPDLVLQRCCSGEGLQIPTLSPAPDCSQPLDVILLLDGSSSFPASYFDEMKSFAKAFISKANIGPRLTQVSVLQYGSITTIDVPWNVVPEKAHLLSLVDVMQREGGPSQIGDALGFAVRYLTSEMHGARPGASKAVVILVTDVSVDSVDAAADAARSNRVTVFPIGIGDRYDAAQLRILAGPAGDSNVVKLQRIEDLPTMVTLGNSFLHKLCSGFVRICMDEDGNEKRPGDVWTLPDQCHTVTCQPDGQTLLKSHRVNCDRGLRPSCPNSQSPVKVEETCGCRWTCPCVCTGSSTRHIVTFDGQNFKLTGSCSYVLFQNKEQDLEVILHNGACSPGARQGCMKSIEVKHSALSVELHSDMEVTVNGRLVSVPYVGGNMEVNVYGAIMHEVRFNHLGHIFTFTPQNNEFQLQLSPKTFASKTYGLCGICDENGANDFMLRDGTVTTDWKTLVQEWTVQRPGQTCQPILEEQCLVPDSSHCQVLLLPLFAECHKVLAPATFYAICQQDSCHQEQVCEVIASYAHLCRTNGVCVDWRTPDFCAMSCPPSLVYNHCEHGCPRHCDGNVSSCGDHPSEGCFCPPDKVMLEGSCVPEEACTQCIGEDGVQHQFLEAWVPDHQPCQICTCLSGRKVNCTTQPCPTAKAPTCGLCEVARLRQNADQCCPEYECVCDPVSCDLPPVPHCERGLQPTLTNPGECRPNFTCACRKEECKRVSPPSCPPHRLPTLRKTQCCDEYECACNCVNSTVSCPLGYLASTATNDCGCTTTTCLPDKVCVHRSTIYPVGQFWEEGCDVCTCTDMEDAVMGLRVAQCSQKPCEDSCRSGFTYVLHEGECCGRCLPSACEVVTGSPRGDSQSSWKSVGSQWASPENPCLINECVRVKEEVFIQQRNVSCPQLEVPVCPSGFQLSCKTSACCPSCRCERMEACMLNGTVIGPGKTVMIDVCTTCRCMVQVGVISGFKLECRKTTCNPCPLGYKEENNTGECCGRCLPTACTIQLRGGQIMTLKRDETLQDGCDTHFCKVNERGEYFWEKRVTGCPPFDEHKCLAEGGKIMKIPGTCCDTCEEPECNDITARLQYVKVGSCKSEVEVDIHYCQGKCASKAMYSIDINDVQDQCSCCSPTRTEPMQVALHCTNGSVVYHEVLNAMECKCSPRKCSK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
20	Phosphorylation	LALILPGTLCAEGTR HHHHHCCCCCCCCCC	19.41	24043423
26	Phosphorylation	GTLCAEGTRGRSSTA CCCCCCCCCCCCCCC	22.81	24043423
69	Phosphorylation	AGGCQKRSFSIIGDF CCCCCCCEEEEEEEC	30.31	30576142
71	Phosphorylation	GCQKRSFSIIGDFQN CCCCCEEEEEEECCC	17.97	30576142
99	N-linked_Glycosylation	FDIHLFVNGTVTQGD CEEEEEEECEECCCC	32.84	UniProtKB CARBOHYD
119	Phosphorylation	PYASKGLYLETEAGY CCCCCCEEEEECCEE	15.91	29759185
126	Phosphorylation	YLETEAGYYKLSGEA EEEECCEEEEECCEE	12.41	-
134	Phosphorylation	YKLSGEAYGFVARID EEECCEEEEEEEEEC	13.54	-
156	N-linked_Glycosylation	LLSDRYFNKTCGLCG EEECCCCCCCCCCCC	29.77	UniProtKB CARBOHYD
211	N-linked_Glycosylation	SPPSSSCNISSGEMQ CCCCCCCCCCCHHHH	38.84	UniProtKB CARBOHYD
214	Phosphorylation	SSSCNISSGEMQKGL CCCCCCCCHHHHCCH	34.67	30576142
286	Phosphorylation	GMVLYGWTDHSACSP CCEEEEECCCCCCCC	21.33	22210691
292	Phosphorylation	WTDHSACSPVCPAGM ECCCCCCCCCCCCCC	21.78	22210691
301	Phosphorylation	VCPAGMEYRQCVSPC CCCCCCCHHHCHHHH	9.33	22210691
306	Phosphorylation	MEYRQCVSPCARTCQ CCHHHCHHHHHHHHH	23.14	22210691
357	Phosphorylation	CVHSGKRYPPGTSLS CCCCCCCCCCCCCCC	19.77	22461510
362	Phosphorylation	KRYPPGTSLSRDCNT CCCCCCCCCCCCCCC	30.20	22461510
364	Phosphorylation	YPPGTSLSRDCNTCI CCCCCCCCCCCCCEE	26.32	24719451
441	Phosphorylation	DDRDAVCTRSVTVRL CCCCCEEEEEEEEEC	21.27	29978859
443	Phosphorylation	RDAVCTRSVTVRLPG CCCEEEEEEEEECCC	12.18	29978859
445	Phosphorylation	AVCTRSVTVRLPGLH CEEEEEEEEECCCHH	10.93	24719451
485	Phosphorylation	GDLRIQHTVTASVRL CCEEEEEEEEEEEEE	11.81	21712546
487	Phosphorylation	LRIQHTVTASVRLSY EEEEEEEEEEEEEEC	17.86	21712546
600	Phosphorylation	EACHRAVSPLPYLRN HHHHHHCCCCHHHCC	21.53	28270605
610	Phosphorylation	PYLRNCRYDVCSCSD HHHCCCCCEECCCCC	18.22	-
666	N-linked_Glycosylation	LQCGTPCNLTCRSLS EECCCCCCCEEECCC	39.32	UniProtKB CARBOHYD
746	O-linked_Glycosylation	TMSGVPGSLLPDAVL ECCCCCCCCCCHHHH	22.21	OGP
764	Phosphorylation	LSHRSKRSLSCRPPM CCCCCCCCCCCCCCE	28.50	22210691
766	Phosphorylation	HRSKRSLSCRPPMVK CCCCCCCCCCCCEEE	14.88	22210691
791	Phosphorylation	EGLECTKTCQNYDLE CCCCCCCCCCCCCCC	10.94	24043423
795	Phosphorylation	CTKTCQNYDLECMSM CCCCCCCCCCCHHHC	8.95	24043423
801	Phosphorylation	NYDLECMSMGCVSGC CCCCCHHHCCCCCCC	24.55	24043423
806	Phosphorylation	CMSMGCVSGCLCPPG HHHCCCCCCCCCCCC	28.06	24043423
836	Phosphorylation	CFHQGKEYAPGETVK CCCCCCCCCCCCEEE	22.91	24719451
841	Phosphorylation	KEYAPGETVKIGCNT CCCCCCCEEEECCCE	32.77	24719451
857	N-linked_Glycosylation	VCQDRKWNCTDHVCD EECCCCCCCCCHHCC	23.11	2535488
1147	N-linked_Glycosylation	YECEWRYNSCAPACQ EECEEECCCCCCCEE	23.26	3524673
1231	N-linked_Glycosylation	ICHCDVVNLTCEACQ CCCCEEEEEEECCCC	29.49	3524673
1248	O-linked_Glycosylation	GGLVVPPTDAPVSPT CCEECCCCCCCCCCC	38.43	3524673
1255	O-linked_Glycosylation	TDAPVSPTTLYVEDI CCCCCCCCEEEEECC	23.17	3524673
1256	O-linked_Glycosylation	DAPVSPTTLYVEDIS CCCCCCCEEEEECCC	21.34	3524673
1263	O-linked_Glycosylation	TLYVEDISEPPLHDF EEEEECCCCCCCHHH	57.27	3524673
1338	Phosphorylation	LKDRKRPSELRRIAS ECCCCCHHHHHHHHH	53.98	-
1345	Phosphorylation	SELRRIASQVKYAGS HHHHHHHHHHHHCCC	32.89	-
1349	Phosphorylation	RIASQVKYAGSQVAS HHHHHHHHCCCCCCC	19.82	-
1370	Phosphorylation	YTLFQIFSKIDRPEA HHHHHHHHCCCCHHH	30.26	24719451
1394	Phosphorylation	SQEPQRMSRNFVRYV CCCHHHHHHHHHHHH	26.68	-
1400	Phosphorylation	MSRNFVRYVQGLKKK HHHHHHHHHHCCCCC	7.57	-
1468	O-linked_Glycosylation	APEAPPPTLPPDMAQ CCCCCCCCCCCCHHH	58.64	3524673
1477	O-linked_Glycosylation	PPDMAQVTVGPGLLG CCCHHHCEECCCCEE	13.99	3524673
1486	O-linked_Glycosylation	GPGLLGVSTLGPKRN CCCCEECCCCCCCCC	19.00	3524673
1487	O-linked_Glycosylation	PGLLGVSTLGPKRNS CCCEECCCCCCCCCC	33.07	3524673
1495	Sulfoxidation	LGPKRNSMVLDVAFV CCCCCCCCEEEEEEE	3.86	21917758
1515	N-linked_Glycosylation	KIGEADFNRSKEFME CCCCCCCCCCHHHHH	48.11	UniProtKB CARBOHYD
1515	N-linked_Glycosylation	KIGEADFNRSKEFME CCCCCCCCCCHHHHH	48.11	19139490
1517	Phosphorylation	GEADFNRSKEFMEEV CCCCCCCCHHHHHHH	37.33	-
1534	Phosphorylation	RMDVGQDSIHVTVLQ HCCCCCCCEEEEEEE	13.50	23917254
1538	Phosphorylation	GQDSIHVTVLQYSYM CCCCEEEEEEEEEEE	11.01	23917254
1542	Phosphorylation	IHVTVLQYSYMVTVE EEEEEEEEEEEEEEE	9.52	23917254
1543	Phosphorylation	HVTVLQYSYMVTVEY EEEEEEEEEEEEEEC	8.19	23917254
1544	Phosphorylation	VTVLQYSYMVTVEYP EEEEEEEEEEEEECC	7.23	23917254
1547	Phosphorylation	LQYSYMVTVEYPFSE EEEEEEEEEECCCHH	7.35	23917254
1570	Phosphorylation	QRVREIRYQGGNRTN HHHHHHHCCCCCCCC	19.71	-
1574	N-linked_Glycosylation	EIRYQGGNRTNTGLA HHHCCCCCCCCCCHH	55.20	3524673
1576	Phosphorylation	RYQGGNRTNTGLALR HCCCCCCCCCCHHHH	40.92	23403867
1578	Phosphorylation	QGGNRTNTGLALRYL CCCCCCCCCHHHHHH	32.72	-
1584	Phosphorylation	NTGLALRYLSDHSFL CCCHHHHHHCCCCEE	16.06	-
1586	Phosphorylation	GLALRYLSDHSFLVS CHHHHHHCCCCEEEE	25.09	25690035
1593	Phosphorylation	SDHSFLVSQGDREQA CCCCEEEECCCHHHC	30.50	25690035
1606	Sulfoxidation	QAPNLVYMVTGNPAS HCCCEEEEEECCCCC	1.37	21917758
1613	Phosphorylation	MVTGNPASDEIKRLP EEECCCCCHHHHCCC	36.71	-
1679	O-linked_Glycosylation	GEGLQIPTLSPAPDC CCCCCCCCCCCCCCC	41.31	3524673
1715	Ubiquitination	DEMKSFAKAFISKAN HHHHHHHHHHHHHCC	41.65	22817900
1720	Ubiquitination	FAKAFISKANIGPRL HHHHHHHHCCCCCCC	40.41	22817900
1859	Phosphorylation	QRIEDLPTMVTLGNS EEHHCCCCEEEECHH	31.41	28060719
1860	Sulfoxidation	RIEDLPTMVTLGNSF EHHCCCCEEEECHHH	1.73	21917758
1862	Phosphorylation	EDLPTMVTLGNSFLH HCCCCEEEECHHHHH	20.37	28060719
1866	Phosphorylation	TMVTLGNSFLHKLCS CEEEECHHHHHHHHC	27.64	28060719
1914	Phosphorylation	DGQTLLKSHRVNCDR CCCCEEHHCCCCCCC	19.25	25690035
1932	Phosphorylation	PSCPNSQSPVKVEET CCCCCCCCCCEEECC	31.33	26546556
2010	Phosphorylation	KSIEVKHSALSVELH CHHEEEECEEEEEEC	25.78	-
2030	Phosphorylation	TVNGRLVSVPYVGGN EECCEEEEECCCCCC	23.20	-
2079	Phosphorylation	LSPKTFASKTYGLCG ECHHHCCCCCCEEEC	22.72	22210691
2082	Phosphorylation	KTFASKTYGLCGICD HHCCCCCCEEECCCC	16.31	22210691
2223	N-linked_Glycosylation	CPRHCDGNVSSCGDH CCCCCCCCCHHCCCC	19.76	3524673
2290	N-linked_Glycosylation	CLSGRKVNCTTQPCP ECCCCEEECCCCCCC	22.06	3524673
2298	O-linked_Glycosylation	CTTQPCPTAKAPTCG CCCCCCCCCCCCCCC	47.72	3524673
2357	N-linked_Glycosylation	NPGECRPNFTCACRK CCCCCCCCCEEEECH	26.05	3524673
2400	N-linked_Glycosylation	ECACNCVNSTVSCPL CHHHCCCCCCCCCCH	33.88	3524673
2546	N-linked_Glycosylation	EVFIQQRNVSCPQLE HHEEEECCCCCCCCC	26.22	3524673
2567	Phosphorylation	GFQLSCKTSACCPSC CEEEEECCCCCCCCC	26.36	22210691
2568	Phosphorylation	FQLSCKTSACCPSCR EEEEECCCCCCCCCC	12.57	22210691
2585	N-linked_Glycosylation	RMEACMLNGTVIGPG CCEEEEECCEEECCC	19.73	3524673
2738	Phosphorylation	LQYVKVGSCKSEVEV EEEEEECCCCCEEEE	22.74	30377224
2741	Phosphorylation	VKVGSCKSEVEVDIH EEECCCCCEEEEEEE	51.72	30377224
2749	Phosphorylation	EVEVDIHYCQGKCAS EEEEEEEEECCCCCC	6.18	30377224
2790	N-linked_Glycosylation	QVALHCTNGSVVYHE EEEEECCCCCHHHHH	46.25	3524673
2804	S-palmitoylation	EVLNAMECKCSPRKC HHHHHHCCCCCCCCC	3.28	29575903
2806	S-palmitoylation	LNAMECKCSPRKCSK HHHHCCCCCCCCCCC	11.64	29575903
2807	Phosphorylation	NAMECKCSPRKCSK- HHHCCCCCCCCCCC-	17.15	-
2811	S-palmitoylation	CKCSPRKCSK----- CCCCCCCCCC-----	7.09	29575903
2812	Phosphorylation	KCSPRKCSK------ CCCCCCCCC------	44.42	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
1517	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	PSP
1613	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of VWF_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of VWF_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CO1A1_HUMAN	COL1A1	physical	3490481
FA8_HUMAN	F8	physical	9218428
ENPL_HUMAN	HSP90B1	physical	10887119
GRP78_HUMAN	HSPA5	physical	10887119
PDIA4_HUMAN	PDIA4	physical	10887119
PDIA1_HUMAN	P4HB	physical	26670633

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
193400	von Willebrand disease 1 (VWD1)
613554	von Willebrand disease 2 (VWD2)
277480	von Willebrand disease 3 (VWD3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of VWF_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2546, AND MASSSPECTROMETRY.	19159218 [Abstract]
"Screening for N-glycosylated proteins by liquid chromatography massspectrometry."; Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.; Proteomics 4:454-465(2004). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1515, AND MASSSPECTROMETRY.	14760718 [Abstract]
O-linked Glycosylation
Reference	PubMed
"Amino acid sequence of human von Willebrand factor."; Titani K., Kumar S., Takio K., Ericsson L.H., Wade R.D., Ashida K.,Walsh K.A., Chopek M.W., Sadler J.E., Fujikawa K.; Biochemistry 25:3171-3184(1986). Cited for: PROTEIN SEQUENCE OF 764-2813, AND VARIANTS ARG-852 AND ALA-1381.	3524673 [Abstract]
Ubiquitylation
Reference	PubMed
"Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry."; Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.; Proteomics 7:868-874(2007). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-1720, AND MASSSPECTROMETRY.	17370265 [Abstract]