dbPTM

FA8_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FA8_HUMAN
UniProt AC	P00451
Protein Name	Coagulation factor VIII
Gene Name	F8
Organism	Homo sapiens (Human).
Sequence Length	2351
Subcellular Localization	Secreted, extracellular space.
Protein Description	Factor VIII, along with calcium and phospholipid, acts as a cofactor for F9/factor IXa when it converts F10/factor X to the activated form, factor Xa..
Protein Sequence	MQIELSTCFFLCLLRFCFSATRRYYLGAVELSWDYMQSDLGELPVDARFPPRVPKSFPFNTSVVYKKTLFVEFTDHLFNIAKPRPPWMGLLGPTIQAEVYDTVVITLKNMASHPVSLHAVGVSYWKASEGAEYDDQTSQREKEDDKVFPGGSHTYVWQVLKENGPMASDPLCLTYSYLSHVDLVKDLNSGLIGALLVCREGSLAKEKTQTLHKFILLFAVFDEGKSWHSETKNSLMQDRDAASARAWPKMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEVHSIFLEGHTFLVRNHRQASLEISPITFLTAQTLLMDLGQFLLFCHISSHQHDGMEAYVKVDSCPEEPQLRMKNNEEAEDYDDDLTDSEMDVVRFDDDNSPSFIQIRSVAKKHPKTWVHYIAAEEEDWDYAPLVLAPDDRSYKSQYLNNGPQRIGRKYKKVRFMAYTDETFKTREAIQHESGILGPLLYGEVGDTLLIIFKNQASRPYNIYPHGITDVRPLYSRRLPKGVKHLKDFPILPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFVNMERDLASGLIGPLLICYKESVDQRGNQIMSDKRNVILFSVFDENRSWYLTENIQRFLPNPAGVQLEDPEFQASNIMHSINGYVFDSLQLSVCLHEVAYWYILSIGAQTDFLSVFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWILGCHNSDFRNRGMTALLKVSSCDKNTGDYYEDSYEDISAYLLSKNNAIEPRSFSQNSRHPSTRQKQFNATTIPENDIEKTDPWFAHRTPMPKIQNVSSSDLLMLLRQSPTPHGLSLSDLQEAKYETFSDDPSPGAIDSNNSLSEMTHFRPQLHHSGDMVFTPESGLQLRLNEKLGTTAATELKKLDFKVSSTSNNLISTIPSDNLAAGTDNTSSLGPPSMPVHYDSQLDTTLFGKKSSPLTESGGPLSLSEENNDSKLLESGLMNSQESSWGKNVSSTESGRLFKGKRAHGPALLTKDNALFKVSISLLKTNKTSNNSATNRKTHIDGPSLLIENSPSVWQNILESDTEFKKVTPLIHDRMLMDKNATALRLNHMSNKTTSSKNMEMVQQKKEGPIPPDAQNPDMSFFKMLFLPESARWIQRTHGKNSLNSGQGPSPKQLVSLGPEKSVEGQNFLSEKNKVVVGKGEFTKDVGLKEMVFPSSRNLFLTNLDNLHENNTHNQEKKIQEEIEKKETLIQENVVLPQIHTVTGTKNFMKNLFLLSTRQNVEGSYDGAYAPVLQDFRSLNDSTNRTKKHTAHFSKKGEEENLEGLGNQTKQIVEKYACTTRISPNTSQQNFVTQRSKRALKQFRLPLEETELEKRIIVDDTSTQWSKNMKHLTPSTLTQIDYNEKEKGAITQSPLSDCLTRSHSIPQANRSPLPIAKVSSFPSIRPIYLTRVLFQDNSSHLPAASYRKKDSGVQESSHFLQGAKKNNLSLAILTLEMTGDQREVGSLGTSATNSVTYKKVENTVLPKPDLPKTSGKVELLPKVHIYQKDLFPTETSNGSPGHLDLVEGSLLQGTEGAIKWNEANRPGKVPFLRVATESSAKTPSKLLDPLAWDNHYGTQIPKEEWKSQEKSPEKTAFKKKDTILSLNACESNHAIAAINEGQNKPEIEVTWAKQGRTERLCSQNPPVLKRHQREITRTTLQSDQEEIDYDDTISVEMKKEDFDIYDEDENQSPRSFQKKTRHYFIAAVERLWDYGMSSSPHVLRNRAQSGSVPQFKKVVFQEFTDGSFTQPLYRGELNEHLGLLGPYIRAEVEDNIMVTFRNQASRPYSFYSSLISYEEDQRQGAEPRKNFVKPNETKTYFWKVQHHMAPTKDEFDCKAWAYFSDVDLEKDVHSGLIGPLLVCHTNTLNPAHGRQVTVQEFALFFTIFDETKSWYFTENMERNCRAPCNIQMEDPTFKENYRFHAINGYIMDTLPGLVMAQDQRIRWYLLSMGSNENIHSIHFSGHVFTVRKKEEYKMALYNLYPGVFETVEMLPSKAGIWRVECLIGEHLHAGMSTLFLVYSNKCQTPLGMASGHIRDFQITASGQYGQWAPKLARLHYSGSINAWSTKEPFSWIKVDLLAPMIIHGIKTQGARQKFSSLYISQFIIMYSLDGKKWQTYRGNSTGTLMVFFGNVDSSGIKHNIFNPPIIARYIRLHPTHYSIRSTLRMELMGCDLNSCSMPLGMESKAISDAQITASSYFTNMFATWSPSKARLHLQGRSNAWRPQVNNPKEWLQVDFQKTMKVTGVTTQGVKSLLTSMYVKEFLISSSQDGHQWTLFFQNGKVKVFQGNQDSFTPVVNSLDPPLLTRYLRIHPQSWVHQIALRMEVLGCEAQDLY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
56	Phosphorylation	FPPRVPKSFPFNTSV CCCCCCCCCCCCCEE	31.89	29083192
60	N-linked_Glycosylation	VPKSFPFNTSVVYKK CCCCCCCCCEEEEEE	31.51	UniProtKB CARBOHYD
61	Phosphorylation	PKSFPFNTSVVYKKT CCCCCCCCEEEEEEE	24.23	29083192
62	Phosphorylation	KSFPFNTSVVYKKTL CCCCCCCEEEEEEEE	15.64	29083192
65	Phosphorylation	PFNTSVVYKKTLFVE CCCCEEEEEEEEEEE	12.47	29083192
94	Phosphorylation	WMGLLGPTIQAEVYD CCCCCCCCEEEEEEE	24.75	28348404
100	Phosphorylation	PTIQAEVYDTVVITL CCEEEEEEEEEEEEE	9.45	28348404
102	Phosphorylation	IQAEVYDTVVITLKN EEEEEEEEEEEEECH	10.05	28348404
106	Phosphorylation	VYDTVVITLKNMASH EEEEEEEEECHHHCC	21.77	28348404
189	Phosphorylation	DLVKDLNSGLIGALL HHHHHCCCCHHHHHH	42.12	26699800
258	N-linked_Glycosylation	HTVNGYVNRSLPGLI HCCCCCCCCCCCCCC	21.24	UniProtKB CARBOHYD
260	Phosphorylation	VNGYVNRSLPGLIGC CCCCCCCCCCCCCCC	33.44	23879269
365	Sulfation	NNEEAEDYDDDLTDS CCCCCCCCCCCCCCC	16.87	-
365	Sulfation	NNEEAEDYDDDLTDS CCCCCCCCCCCCCCC	16.87	10368977
425	Phosphorylation	VLAPDDRSYKSQYLN EECCCCCCHHHHHHH	43.86	25278378
426	Phosphorylation	LAPDDRSYKSQYLNN ECCCCCCHHHHHHHC	18.62	25278378
428	Phosphorylation	PDDRSYKSQYLNNGP CCCCCHHHHHHHCCH	18.80	22210691
430	Phosphorylation	DRSYKSQYLNNGPQR CCCHHHHHHHCCHHH	20.63	22210691
442	Phosphorylation	PQRIGRKYKKVRFMA HHHCCCCCCEEEEEE	18.06	24719451
450	Phosphorylation	KKVRFMAYTDETFKT CEEEEEEECCCCHHH	11.70	24719451
451	Phosphorylation	KVRFMAYTDETFKTR EEEEEEECCCCHHHH	20.16	24719451
507	Phosphorylation	TDVRPLYSRRLPKGV CCCHHCCCCCCCCCC	20.71	24719451
601	N-linked_Glycosylation	LFSVFDENRSWYLTE EEEEECCCCCEEEEH	45.17	16335952
737	Sulfation	CDKNTGDYYEDSYED CCCCCCCCCCCCHHH	15.31	-
737	Sulfation	CDKNTGDYYEDSYED CCCCCCCCCCCCHHH	15.31	10368977
738	Sulfation	DKNTGDYYEDSYEDI CCCCCCCCCCCHHHH	20.28	-
738	Sulfation	DKNTGDYYEDSYEDI CCCCCCCCCCCHHHH	20.28	10368977
742	Sulfation	GDYYEDSYEDISAYL CCCCCCCHHHHHHHH	29.91	-
742	Sulfation	GDYYEDSYEDISAYL CCCCCCCHHHHHHHH	29.91	10368977
776	N-linked_Glycosylation	STRQKQFNATTIPEN CHHHHCCCCCCCCHH	33.61	UniProtKB CARBOHYD
803	N-linked_Glycosylation	TPMPKIQNVSSSDLL CCCCCCCCCCHHHHH	38.83	UniProtKB CARBOHYD
818	O-linked_Glycosylation	MLLRQSPTPHGLSLS HHHHCCCCCCCCCHH	32.91	OGP
846	Phosphorylation	PSPGAIDSNNSLSEM CCCCCCCCCCCHHHH	31.62	22210691
847	N-linked_Glycosylation	SPGAIDSNNSLSEMT CCCCCCCCCCHHHHH	38.06	UniProtKB CARBOHYD
869	O-linked_Glycosylation	HSGDMVFTPESGLQL CCCCEEECCCCCCEE	18.09	OGP
869	Phosphorylation	HSGDMVFTPESGLQL CCCCEEECCCCCCEE	18.09	22210691
872	Phosphorylation	DMVFTPESGLQLRLN CEEECCCCCCEEEHH	46.11	22210691
919	N-linked_Glycosylation	NLAAGTDNTSSLGPP CCCCCCCCCCCCCCC	41.52	UniProtKB CARBOHYD
951	Phosphorylation	KSSPLTESGGPLSLS CCCCCCCCCCCCCCC	43.76	28270605
956	Phosphorylation	TESGGPLSLSEENND CCCCCCCCCCCCCCC	32.74	28270605
958	Phosphorylation	SGGPLSLSEENNDSK CCCCCCCCCCCCCHH	39.22	24505115
962	N-linked_Glycosylation	LSLSEENNDSKLLES CCCCCCCCCHHHHHH	59.20	UniProtKB CARBOHYD
964	Phosphorylation	LSEENNDSKLLESGL CCCCCCCHHHHHHHC	27.59	28270605
969	Phosphorylation	NDSKLLESGLMNSQE CCHHHHHHHCCCCCC	36.88	28270605
974	Phosphorylation	LESGLMNSQESSWGK HHHHCCCCCCCCCCC	22.74	28270605
977	Phosphorylation	GLMNSQESSWGKNVS HCCCCCCCCCCCCCC	24.61	28270605
978	Phosphorylation	LMNSQESSWGKNVSS CCCCCCCCCCCCCCC	38.81	28270605
982	N-linked_Glycosylation	QESSWGKNVSSTESG CCCCCCCCCCCCCCC	34.66	UniProtKB CARBOHYD
1013	Phosphorylation	DNALFKVSISLLKTN CCHHEEEEEEHHHCC	13.67	27251275
1015	Phosphorylation	ALFKVSISLLKTNKT HHEEEEEEHHHCCCC	21.83	24719451
1020	N-linked_Glycosylation	SISLLKTNKTSNNSA EEEHHHCCCCCCCCC	43.98	UniProtKB CARBOHYD
1022	Phosphorylation	SLLKTNKTSNNSATN EHHHCCCCCCCCCCC	38.46	-
1023	Phosphorylation	LLKTNKTSNNSATNR HHHCCCCCCCCCCCC	35.31	-
1024	N-linked_Glycosylation	LKTNKTSNNSATNRK HHCCCCCCCCCCCCC	52.27	UniProtKB CARBOHYD
1026	Phosphorylation	TNKTSNNSATNRKTH CCCCCCCCCCCCCCC	40.49	-
1028	Phosphorylation	KTSNNSATNRKTHID CCCCCCCCCCCCCCC	35.06	-
1074	N-linked_Glycosylation	DRMLMDKNATALRLN HHHCCCCCCHHHHHH	37.95	UniProtKB CARBOHYD
1084	Phosphorylation	ALRLNHMSNKTTSSK HHHHHHHCCCCCCCC	27.85	-
1085	N-linked_Glycosylation	LRLNHMSNKTTSSKN HHHHHHCCCCCCCCH	37.81	UniProtKB CARBOHYD
1204	N-linked_Glycosylation	NLDNLHENNTHNQEK CHHHCCCCCCCCHHH	48.21	UniProtKB CARBOHYD
1274	N-linked_Glycosylation	LQDFRSLNDSTNRTK HHHHHCCCCCCCCHH	42.29	UniProtKB CARBOHYD
1278	N-linked_Glycosylation	RSLNDSTNRTKKHTA HCCCCCCCCHHHCCC	54.28	UniProtKB CARBOHYD
1281	Acetylation	NDSTNRTKKHTAHFS CCCCCCHHHCCCCCC	39.04	22424773
1284	Phosphorylation	TNRTKKHTAHFSKKG CCCHHHCCCCCCCCC	30.61	-
1301	N-linked_Glycosylation	ENLEGLGNQTKQIVE HHCCCCCHHHHHHHH	51.93	UniProtKB CARBOHYD
1319	N-linked_Glycosylation	CTTRISPNTSQQNFV CCCEECCCHHHCCCC	45.64	UniProtKB CARBOHYD
1385	Phosphorylation	EKEKGAITQSPLSDC HHHCCCCCCCCHHHH	23.59	23403867
1387	Phosphorylation	EKGAITQSPLSDCLT HCCCCCCCCHHHHHH	21.11	23403867
1390	Phosphorylation	AITQSPLSDCLTRSH CCCCCCHHHHHHHCC	29.66	23403867
1394	Phosphorylation	SPLSDCLTRSHSIPQ CCHHHHHHHCCCCCC	36.14	23403867
1396	O-linked_Glycosylation	LSDCLTRSHSIPQAN HHHHHHHCCCCCCCC	19.15	OGP
1396	Phosphorylation	LSDCLTRSHSIPQAN HHHHHHHCCCCCCCC	19.15	22210691
1398	Phosphorylation	DCLTRSHSIPQANRS HHHHHCCCCCCCCCC	36.89	22210691
1405	Phosphorylation	SIPQANRSPLPIAKV CCCCCCCCCCCCEEC	30.51	-
1413	Phosphorylation	PLPIAKVSSFPSIRP CCCCEECCCCCCCCC	26.09	-
1424	Phosphorylation	SIRPIYLTRVLFQDN CCCCEEEEEEEECCC	11.19	-
1431	N-linked_Glycosylation	TRVLFQDNSSHLPAA EEEEECCCCCCCCCH	34.33	UniProtKB CARBOHYD
1461	N-linked_Glycosylation	LQGAKKNNLSLAILT HCHHHHCCCEEEEEE	39.63	UniProtKB CARBOHYD
1576	Phosphorylation	ATESSAKTPSKLLDP ECCCCCCCCHHHCCC	32.29	-
1578	Phosphorylation	ESSAKTPSKLLDPLA CCCCCCCHHHCCCCC	40.96	-
1601	Phosphorylation	IPKEEWKSQEKSPEK CCHHHHHCCCCCCCC	44.65	28509920
1605	Phosphorylation	EWKSQEKSPEKTAFK HHHCCCCCCCCCCCC	37.22	28509920
1614	Acetylation	EKTAFKKKDTILSLN CCCCCCCHHCEEEEE	61.77	20167786
1683	Sulfation	SDQEEIDYDDTISVE CCCCCCCCCCCEEEE	22.75	-
1683	Sulfation	SDQEEIDYDDTISVE CCCCCCCCCCCEEEE	22.75	10368977
1699	Sulfation	KKEDFDIYDEDENQS EHHHCCCCCCCCCCC	18.35	-
1699	Sulfation	KKEDFDIYDEDENQS EHHHCCCCCCCCCCC	18.35	10368977
1728	Phosphorylation	AVERLWDYGMSSSPH HHHHHHHCCCCCCHH	11.80	22210691
1731	Phosphorylation	RLWDYGMSSSPHVLR HHHHCCCCCCHHHHH	24.25	22210691
1732	Phosphorylation	LWDYGMSSSPHVLRN HHHCCCCCCHHHHHH	38.71	22210691
1743	Phosphorylation	VLRNRAQSGSVPQFK HHHHCHHCCCCCCCE	31.86	22210691
1745	Phosphorylation	RNRAQSGSVPQFKKV HHCHHCCCCCCCEEE	35.55	23898821
1758	Phosphorylation	KVVFQEFTDGSFTQP EEEEEECCCCCCCCC	38.40	18767875
1761	Phosphorylation	FQEFTDGSFTQPLYR EEECCCCCCCCCCCC	28.12	18767875
1763	Phosphorylation	EFTDGSFTQPLYRGE ECCCCCCCCCCCCCH	30.86	18767875
1793	Phosphorylation	VEDNIMVTFRNQASR EECCEEEEECCCCCC	10.25	24719451
1829	N-linked_Glycosylation	RKNFVKPNETKTYFW CCCCCCCCCCCEEEE	64.94	UniProtKB CARBOHYD
1930	Phosphorylation	NIQMEDPTFKENYRF CCCCCCCCHHHCCEE	60.71	-
1947	Phosphorylation	INGYIMDTLPGLVMA ECCEEECCCCCCHHC	19.92	-
1990	Phosphorylation	TVRKKEEYKMALYNL EEECHHHHHHHHHHH	13.73	-
1995	Phosphorylation	EEYKMALYNLYPGVF HHHHHHHHHHCCCHH	8.12	26657352
1998	Phosphorylation	KMALYNLYPGVFETV HHHHHHHCCCHHHCH	8.36	26657352
2004	Phosphorylation	LYPGVFETVEMLPSK HCCCHHHCHHCCCCC	15.42	26657352
2010	Phosphorylation	ETVEMLPSKAGIWRV HCHHCCCCCCCCEEE	31.04	24719451
2062	Phosphorylation	QITASGQYGQWAPKL EEEEECCCCCCCCCE	18.14	22210691
2082	Phosphorylation	SGSINAWSTKEPFSW CCCCCCCCCCCCCCC	27.47	22210691
2083	Phosphorylation	GSINAWSTKEPFSWI CCCCCCCCCCCCCCE	28.82	22210691
2113	Phosphorylation	QGARQKFSSLYISQF CCHHHHHHHHHEEEE	26.86	24719451
2116	Phosphorylation	RQKFSSLYISQFIIM HHHHHHHHEEEEEEE	10.65	24719451
2125	Phosphorylation	SQFIIMYSLDGKKWQ EEEEEEEECCCCCEE	11.56	27135362
2137	N-linked_Glycosylation	KWQTYRGNSTGTLMV CEEEECCCCCCEEEE	27.65	UniProtKB CARBOHYD
2176	Phosphorylation	RLHPTHYSIRSTLRM HHCCCHHHHHHHHHH	12.15	24719451
2179	Phosphorylation	PTHYSIRSTLRMELM CCHHHHHHHHHHHHC	30.08	30631047
2192	Phosphorylation	LMGCDLNSCSMPLGM HCCCCCCCCCCCCCC	18.18	30631047
2256	Phosphorylation	LQVDFQKTMKVTGVT EEEEHHHEECEECCC	16.08	29396449
2260	Phosphorylation	FQKTMKVTGVTTQGV HHHEECEECCCHHHH	22.03	29396449
2263	Phosphorylation	TMKVTGVTTQGVKSL EECEECCCHHHHHHH	18.10	29396449
2264	Phosphorylation	MKVTGVTTQGVKSLL ECEECCCHHHHHHHH	22.40	29396449

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
Oops, there are no upstream regulatory protein records of FA8_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of FA8_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 FA8_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PAHX_HUMAN	PHYH	physical	11574539
CALX_HUMAN	CANX	physical	9525969
PROS_HUMAN	PROS1	physical	7620160
GGA1_HUMAN	GGA1	physical	21988832
UBQL1_HUMAN	UBQLN1	physical	21988832

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
306700	Hemophilia A (HEMA)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of FA8_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-601, AND MASSSPECTROMETRY.	16335952 [Abstract]
Sulfation
Reference	PubMed
"Identification and functional importance of tyrosine sulfate residueswithin recombinant factor VIII."; Pittman D.D., Wang J.H., Kaufman R.J.; Biochemistry 31:3315-3325(1992). Cited for: SULFATION AT TYR-365; TYR-1683 AND TYR-1699, AND INTERACTION WITH VWF.	1554716 [Abstract]
"Sulfation of Tyr1680 of human blood coagulation factor VIII isessential for the interaction of factor VIII with von Willebrandfactor."; Leyte A., van Schijndel H.B., Niehrs C., Huttner W.B., Verbeet M.P.,Mertens K., van Mourik J.A.; J. Biol. Chem. 266:740-746(1991). Cited for: SULFATION AT TYR-1699.	1898735 [Abstract]
"Characterization of tyrosine sulfate residues in antihemophilicrecombinant factor VIII by liquid chromatography electrosprayionization tandem mass spectrometry and amino acid analysis."; Severs J.C., Carnine M., Eguizabal H., Mock K.K.; Rapid Commun. Mass Spectrom. 13:1016-1023(1999). Cited for: PROTEIN SEQUENCE OF 356-378; 727-752 AND 1672-1708, MASS SPECTROMETRY,AND SULFATION AT TYR-365; TYR-737; TYR-738; TYR-742; TYR-1683 ANDTYR-1699.	10368977 [Abstract]