FBN1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FBN1_HUMAN
• UniProt AC: P35555
• Protein Name: Fibrillin-1
• Gene Name: FBN1
• Organism: Homo sapiens (Human).
• Sequence Length: 2871
• Subcellular Localization: Secreted . Fibrillin-1 and Asprosin chains are still linked together during the secretion from cells, but are subsequently separated by furin (PubMed:24982166).; Asprosin: Secreted . Secreted into the plasma.; Fibrillin-1: Secreted, extracellula
• Protein Description: Fibrillin-1: Structural component of the 10-12 nm diameter microfibrils of the extracellular matrix, which conveys both structural and regulatory properties to load-bearing connective tissues. [PubMed: 1860873]
• Protein Sequence: MRRGRLLEIALGFTVLLASYTSHGADANLEAGNVKETRASRAKRRGGGGHDALKGPNVCGSRYNAYCCPGWKTLPGGNQCIVPICRHSCGDGFCSRPNMCTCPSGQIAPSCGSRSIQHCNIRCMNGGSCSDDHCLCQKGYIGTHCGQPVCESGCLNGGRCVAPNRCACTYGFTGPQCERDYRTGPCFTVISNQMCQGQLSGIVCTKTLCCATVGRAWGHPCEMCPAQPHPCRRGFIPNIRTGACQDVDECQAIPGLCQGGNCINTVGSFECKCPAGHKLNEVSQKCEDIDECSTIPGICEGGECTNTVSSYFCKCPPGFYTSPDGTRCIDVRPGYCYTALTNGRCSNQLPQSITKMQCCCDAGRCWSPGVTVAPEMCPIRATEDFNKLCSVPMVIPGRPEYPPPPLGPIPPVLPVPPGFPPGPQIPVPRPPVEYLYPSREPPRVLPVNVTDYCQLVRYLCQNGRCIPTPGSCRCECNKGFQLDLRGECIDVDECEKNPCAGGECINNQGSYTCQCRAGYQSTLTRTECRDIDECLQNGRICNNGRCINTDGSFHCVCNAGFHVTRDGKNCEDMDECSIRNMCLNGMCINEDGSFKCICKPGFQLASDGRYCKDINECETPGICMNGRCVNTDGSYRCECFPGLAVGLDGRVCVDTHMRSTCYGGYKRGQCIKPLFGAVTKSECCCASTEYAFGEPCQPCPAQNSAEYQALCSSGPGMTSAGSDINECALDPDICPNGICENLRGTYKCICNSGYEVDSTGKNCVDINECVLNSLLCDNGQCRNTPGSFVCTCPKGFIYKPDLKTCEDIDECESSPCINGVCKNSPGSFICECSSESTLDPTKTICIETIKGTCWQTVIDGRCEININGATLKSQCCSSLGAAWGSPCTLCQVDPICGKGYSRIKGTQCEDIDECEVFPGVCKNGLCVNTRGSFKCQCPSGMTLDATGRICLDIRLETCFLRYEDEECTLPIAGRHRMDACCCSVGAAWGTEECEECPMRNTPEYEELCPRGPGFATKEITNGKPFFKDINECKMIPSLCTHGKCRNTIGSFKCRCDSGFALDSEERNCTDIDECRISPDLCGRGQCVNTPGDFECKCDEGYESGFMMMKNCMDIDECQRDPLLCRGGVCHNTEGSYRCECPPGHQLSPNISACIDINECELSAHLCPNGRCVNLIGKYQCACNPGYHSTPDRLFCVDIDECSIMNGGCETFCTNSEGSYECSCQPGFALMPDQRSCTDIDECEDNPNICDGGQCTNIPGEYRCLCYDGFMASEDMKTCVDVNECDLNPNICLSGTCENTKGSFICHCDMGYSGKKGKTGCTDINECEIGAHNCGKHAVCTNTAGSFKCSCSPGWIGDGIKCTDLDECSNGTHMCSQHADCKNTMGSYRCLCKEGYTGDGFTCTDLDECSENLNLCGNGQCLNAPGGYRCECDMGFVPSADGKACEDIDECSLPNICVFGTCHNLPGLFRCECEIGYELDRSGGNCTDVNECLDPTTCISGNCVNTPGSYICDCPPDFELNPTRVGCVDTRSGNCYLDIRPRGDNGDTACSNEIGVGVSKASCCCSLGKAWGTPCEMCPAVNTSEYKILCPGGEGFRPNPITVILEDIDECQELPGLCQGGKCINTFGSFQCRCPTGYYLNEDTRVCDDVNECETPGICGPGTCYNTVGNYTCICPPDYMQVNGGNNCMDMRRSLCYRNYYADNQTCDGELLFNMTKKMCCCSYNIGRAWNKPCEQCPIPSTDEFATLCGSQRPGFVIDIYTGLPVDIDECREIPGVCENGVCINMVGSFRCECPVGFFYNDKLLVCEDIDECQNGPVCQRNAECINTAGSYRCDCKPGYRFTSTGQCNDRNECQEIPNICSHGQCIDTVGSFYCLCHTGFKTNDDQTMCLDINECERDACGNGTCRNTIGSFNCRCNHGFILSHNNDCIDVDECASGNGNLCRNGQCINTVGSFQCQCNEGYEVAPDGRTCVDINECLLEPRKCAPGTCQNLDGSYRCICPPGYSLQNEKCEDIDECVEEPEICALGTCSNTEGSFKCLCPEGFSLSSSGRRCQDLRMSYCYAKFEGGKCSSPKSRNHSKQECCCALKGEGWGDPCELCPTEPDEAFRQICPYGSGIIVGPDDSAVDMDECKEPDVCKHGQCINTDGSYRCECPFGYILAGNECVDTDECSVGNPCGNGTCKNVIGGFECTCEEGFEPGPMMTCEDINECAQNPLLCAFRCVNTYGSYECKCPVGYVLREDRRMCKDEDECEEGKHDCTEKQMECKNLIGTYMCICGPGYQRRPDGEGCVDENECQTKPGICENGRCLNTRGSYTCECNDGFTASPNQDECLDNREGYCFTEVLQNMCQIGSSNRNPVTKSECCCDGGRGWGPHCEICPFQGTVAFKKLCPHGRGFMTNGADIDECKVIHDVCRNGECVNDRGSYHCICKTGYTPDITGTSCVDLNECNQAPKPCNFICKNTEGSYQCSCPKGYILQEDGRSCKDLDECATKQHNCQFLCVNTIGGFTCKCPPGFTQHHTSCIDNNECTSDINLCGSKGICQNTPGSFTCECQRGFSLDQTGSSCEDVDECEGNHRCQHGCQNIIGGYRCSCPQGYLQHYQWNQCVDENECLSAHICGGASCHNTLGSYKCMCPAGFQYEQFSGGCQDINECGSAQAPCSYGCSNTEGGYLCGCPPGYFRIGQGHCVSGMGMGRGNPEPPVSGEMDDNSLSPEACYECKINGYPKRGRKRRSTNETDASNIEDQSETEANVSLASWDVEKTAIFAFNISHVSNKVRILELLPALTTLTNHNRYLIESGNEDGFFKINQKEGISYLHFTKKKPVAGTYSLQISSTPLYKKKELNQLEDKYDKDYLSGELGDNLKMKIQVLLH

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
54	Sumoylation	GGGHDALKGPNVCGS CCCCCCCCCCCCCCC	74.23	-
54	Sumoylation	GGGHDALKGPNVCGS CCCCCCCCCCCCCCC	74.23	-
115	Phosphorylation	APSCGSRSIQHCNIR CCCCCCCCCEECCEE	28.44	24719451
232	Methylation	PAQPHPCRRGFIPNI CCCCCCCCCCCCCCC	46.32	-
278	Sumoylation	CKCPAGHKLNEVSQK EECCCCCCHHHHHHH	52.68	-
278	Sumoylation	CKCPAGHKLNEVSQK EECCCCCCHHHHHHH	52.68	-
322	Phosphorylation	CPPGFYTSPDGTRCI CCCCEEECCCCCEEE	15.04	29083192
326	Phosphorylation	FYTSPDGTRCIDVRP EEECCCCCEEEECCC	29.73	29083192
346	Phosphorylation	ALTNGRCSNQLPQSI ECCCCCCCCCCCCCC	26.67	-
352	Phosphorylation	CSNQLPQSITKMQCC CCCCCCCCCCHHCCE	30.22	-
448	N-linked_Glycosylation	PPRVLPVNVTDYCQL CCCEECCCHHHHHHH	29.09	19159218
568	Sumoylation	FHVTRDGKNCEDMDE EEEECCCCCCCCCCC	63.81	-
568	Sumoylation	FHVTRDGKNCEDMDE EEEECCCCCCCCCCC	63.81	-
595	Ubiquitination	INEDGSFKCICKPGF ECCCCCEEEEECCCE	25.12	23503661
599	Sumoylation	GSFKCICKPGFQLAS CCEEEEECCCEEECC	28.41	-
599	Sumoylation	GSFKCICKPGFQLAS CCEEEEECCCEEECC	28.41	-
599	Ubiquitination	GSFKCICKPGFQLAS CCEEEEECCCEEECC	28.41	23503661
612	Sumoylation	ASDGRYCKDINECET CCCCCCCCCCCCCCC	53.35	-
612	Sumoylation	ASDGRYCKDINECET CCCCCCCCCCCCCCC	53.35	-
666	Sumoylation	STCYGGYKRGQCIKP CCCCCCCCCCCCCHH	54.01	-
666	Acetylation	STCYGGYKRGQCIKP CCCCCCCCCCCCCHH	54.01	30585833
666	Sumoylation	STCYGGYKRGQCIKP CCCCCCCCCCCCCHH	54.01	-
666	Ubiquitination	STCYGGYKRGQCIKP CCCCCCCCCCCCCHH	54.01	-
672	Acetylation	YKRGQCIKPLFGAVT CCCCCCCHHCCCCCC	43.21	19814835
672	Ubiquitination	YKRGQCIKPLFGAVT CCCCCCCHHCCCCCC	43.21	-
747	Ubiquitination	ENLRGTYKCICNSGY HHCCCCEEECCCCCC	19.57	29967540
799	Sumoylation	CPKGFIYKPDLKTCE CCCCEEECCCCCCCC	27.52	-
799	Acetylation	CPKGFIYKPDLKTCE CCCCEEECCCCCCCC	27.52	27178108
799	Sumoylation	CPKGFIYKPDLKTCE CCCCEEECCCCCCCC	27.52	-
799	Ubiquitination	CPKGFIYKPDLKTCE CCCCEEECCCCCCCC	27.52	-
904	Sumoylation	GKGYSRIKGTQCEDI CCCCCCCCCCCCCCC	55.59	-
904	Sumoylation	GKGYSRIKGTQCEDI CCCCCCCCCCCCCCC	55.59	-
904	Ubiquitination	GKGYSRIKGTQCEDI CCCCCCCCCCCCCCC	55.59	29967540
962	Phosphorylation	LETCFLRYEDEECTL EEEEEEEECCCCCCC	29.85	-
1017	Sumoylation	RGPGFATKEITNGKP CCCCCCCEECCCCCC	43.63	-
1017	Sumoylation	RGPGFATKEITNGKP CCCCCCCEECCCCCC	43.63	-
1023	Sumoylation	TKEITNGKPFFKDIN CEECCCCCCCCCCHH	40.50	-
1023	Sumoylation	TKEITNGKPFFKDIN CEECCCCCCCCCCHH	40.50	-
1027	Sumoylation	TNGKPFFKDINECKM CCCCCCCCCHHHCCC	59.06	-
1027	Sumoylation	TNGKPFFKDINECKM CCCCCCCCCHHHCCC	59.06	-
1033	Sumoylation	FKDINECKMIPSLCT CCCHHHCCCCHHHCC	33.41	-
1033	Sumoylation	FKDINECKMIPSLCT CCCHHHCCCCHHHCC	33.41	-
1037	Phosphorylation	NECKMIPSLCTHGKC HHCCCCHHHCCCCCH	25.75	-
1043	Sumoylation	PSLCTHGKCRNTIGS HHHCCCCCHHCCCCC	23.55	-
1043	Sumoylation	PSLCTHGKCRNTIGS HHHCCCCCHHCCCCC	23.55	-
1043	Ubiquitination	PSLCTHGKCRNTIGS HHHCCCCCHHCCCCC	23.55	29967540
1067	N-linked_Glycosylation	ALDSEERNCTDIDEC CCCCCCCCCCCHHHC	36.00	19159218
1089	O-linked_Glycosylation	GRGQCVNTPGDFECK CCCCCCCCCCCCCCC	14.30	OGP
1096	Ubiquitination	TPGDFECKCDEGYES CCCCCCCCCCCCCCC	37.21	23503661
1103	Phosphorylation	KCDEGYESGFMMMKN CCCCCCCCCCEEEEC	28.93	21082442
1149	N-linked_Glycosylation	PGHQLSPNISACIDI CCCCCCCCCEEEEEC	37.15	UniProtKB CARBOHYD
1317	Sumoylation	GYSGKKGKTGCTDIN CCCCCCCCCCCCCCH	51.10	-
1317	Sumoylation	GYSGKKGKTGCTDIN CCCCCCCCCCCCCCH	51.10	-
1369	N-linked_Glycosylation	TDLDECSNGTHMCSQ CCHHHHCCCCCCCCC	71.66	UniProtKB CARBOHYD
1484	N-linked_Glycosylation	ELDRSGGNCTDVNEC EECCCCCCCCCHHHH	29.10	19159218
1535	Phosphorylation	DTRSGNCYLDIRPRG ECCCCCEEEEEECCC	16.06	-
1581	N-linked_Glycosylation	CEMCPAVNTSEYKIL CCCCCCCCCCCCEEE	39.74	19159218
1669	N-linked_Glycosylation	TCYNTVGNYTCICPP CCCCCCCCEEEECCC	25.30	UniProtKB CARBOHYD
1703	N-linked_Glycosylation	YRNYYADNQTCDGEL CCCCCCCCCCCCCCE	30.78	UniProtKB CARBOHYD
1713	N-linked_Glycosylation	CDGELLFNMTKKMCC CCCCEEECCCCCEEC	36.86	UniProtKB CARBOHYD
1836	Sumoylation	GSYRCDCKPGYRFTS CCCCCCCCCCCEECC	28.38	-
1836	Sumoylation	GSYRCDCKPGYRFTS CCCCCCCCCCCEECC	28.38	-
1902	N-linked_Glycosylation	CERDACGNGTCRNTI HCCCCCCCCCCCCCC	42.35	UniProtKB CARBOHYD
2047	Phosphorylation	CPEGFSLSSSGRRCQ CCCCCCCCCCCCCCH	22.66	-
2048	Phosphorylation	PEGFSLSSSGRRCQD CCCCCCCCCCCCCHH	41.95	-
2049	Phosphorylation	EGFSLSSSGRRCQDL CCCCCCCCCCCCHHH	32.70	-
2064	Sumoylation	RMSYCYAKFEGGKCS CHHHEEEEECCCCCC	19.92	-
2064	Sumoylation	RMSYCYAKFEGGKCS CHHHEEEEECCCCCC	19.92	-
2069	Sumoylation	YAKFEGGKCSSPKSR EEEECCCCCCCCCCC	41.63	-
2069	Sumoylation	YAKFEGGKCSSPKSR EEEECCCCCCCCCCC	41.63	-
2077	N-linked_Glycosylation	CSSPKSRNHSKQECC CCCCCCCCCCCCCEE	51.37	UniProtKB CARBOHYD
2178	N-linked_Glycosylation	SVGNPCGNGTCKNVI CCCCCCCCCCCCCCC	49.68	UniProtKB CARBOHYD
2246	Sumoylation	REDRRMCKDEDECEE ECCHHHCCCHHHHHC	55.60	-
2246	Sumoylation	REDRRMCKDEDECEE ECCHHHCCCHHHHHC	55.60	-
2246	Ubiquitination	REDRRMCKDEDECEE ECCHHHCCCHHHHHC	55.60	23503661
2255	Ubiquitination	EDECEEGKHDCTEKQ HHHHHCCCCCCCHHH	39.28	23503661
2261	Ubiquitination	GKHDCTEKQMECKNL CCCCCCHHHHHHHHH	36.47	23503661
2266	Ubiquitination	TEKQMECKNLIGTYM CHHHHHHHHHHEEEE	41.29	23503661
2297	Phosphorylation	VDENECQTKPGICEN CCCCCCCCCCCCCCC	51.36	-
2298	Sumoylation	DENECQTKPGICENG CCCCCCCCCCCCCCC	18.50	-
2298	Sumoylation	DENECQTKPGICENG CCCCCCCCCCCCCCC	18.50	-
2313	Phosphorylation	RCLNTRGSYTCECND EECCCCCCEEEECCC	17.61	24505115
2323	Phosphorylation	CECNDGFTASPNQDE EECCCCEEECCCHHH	31.58	24505115
2387	Acetylation	FQGTVAFKKLCPHGR CCCEEEHHHHCCCCC	34.79	7825087
2388	Sumoylation	QGTVAFKKLCPHGRG CCEEEHHHHCCCCCC	49.20	-
2388	Acetylation	QGTVAFKKLCPHGRG CCEEEHHHHCCCCCC	49.20	15210189
2388	Sumoylation	QGTVAFKKLCPHGRG CCEEEHHHHCCCCCC	49.20	-
2388	Ubiquitination	QGTVAFKKLCPHGRG CCEEEHHHHCCCCCC	49.20	29967540
2407	Sumoylation	GADIDECKVIHDVCR CCCHHHCCCHHHHHC	42.02	-
2407	Sumoylation	GADIDECKVIHDVCR CCCHHHCCCHHHHHC	42.02	-
2557	Phosphorylation	CECQRGFSLDQTGSS EEECCCCCCCCCCCC	33.58	23312004
2561	Phosphorylation	RGFSLDQTGSSCEDV CCCCCCCCCCCCCCH	38.40	23312004
2563	Phosphorylation	FSLDQTGSSCEDVDE CCCCCCCCCCCCHHH	34.89	24719451
2564	Phosphorylation	SLDQTGSSCEDVDEC CCCCCCCCCCCHHHC	23.91	26657352
2702	Phosphorylation	GNPEPPVSGEMDDNS CCCCCCCCCCCCCCC	34.51	26657352
2709	Phosphorylation	SGEMDDNSLSPEACY CCCCCCCCCCHHHHH	36.90	26657352
2711	O-linked_Glycosylation	EMDDNSLSPEACYEC CCCCCCCCHHHHHCC	22.10	OGP
2711	Phosphorylation	EMDDNSLSPEACYEC CCCCCCCCHHHHHCC	22.10	26657352
2734	N-linked_Glycosylation	GRKRRSTNETDASNI CCCCCCCCCCCHHCC	51.95	UniProtKB CARBOHYD
2739	Phosphorylation	STNETDASNIEDQSE CCCCCCHHCCCCCHH	40.94	29759185
2750	N-linked_Glycosylation	DQSETEANVSLASWD CCHHHHHCEEEEECC	20.06	UniProtKB CARBOHYD
2767	N-linked_Glycosylation	KTAIFAFNISHVSNK CEEEEEEEHHHHCCH	31.27	UniProtKB CARBOHYD
2788	Phosphorylation	LPALTTLTNHNRYLI HHHHHHHHCCCCEEE	32.13	-
2805	Sumoylation	GNEDGFFKINQKEGI CCCCCEEEECCCCCE	38.19	-
2805	Sumoylation	GNEDGFFKINQKEGI CCCCCEEEECCCCCE	38.19	-
2809	Sumoylation	GFFKINQKEGISYLH CEEEECCCCCEEEEE	54.11	-
2809	Sumoylation	GFFKINQKEGISYLH CEEEECCCCCEEEEE	54.11	-
2813	Phosphorylation	INQKEGISYLHFTKK ECCCCCEEEEEEECC	32.28	-
2821	Sumoylation	YLHFTKKKPVAGTYS EEEEECCCCCCEEEE	46.40	-
2821	Sumoylation	YLHFTKKKPVAGTYS EEEEECCCCCCEEEE	46.40	-
2826	Phosphorylation	KKKPVAGTYSLQISS CCCCCCEEEEEEEEC	10.53	22817900
2827	Phosphorylation	KKPVAGTYSLQISST CCCCCEEEEEEEECC	13.38	-
2832	Phosphorylation	GTYSLQISSTPLYKK EEEEEEEECCCCCCH	18.39	22817900
2834	Phosphorylation	YSLQISSTPLYKKKE EEEEEECCCCCCHHH	15.55	22817900
2837	Phosphorylation	QISSTPLYKKKELNQ EEECCCCCCHHHHHH	23.20	-
2848	Sumoylation	ELNQLEDKYDKDYLS HHHHHHHHCCHHHHC	46.07	-
2848	Sumoylation	ELNQLEDKYDKDYLS HHHHHHHHCCHHHHC	46.07	-
2849	Phosphorylation	LNQLEDKYDKDYLSG HHHHHHHCCHHHHCC	40.31	22817900
2851	Sumoylation	QLEDKYDKDYLSGEL HHHHHCCHHHHCCCC	45.22	-
2851	Sumoylation	QLEDKYDKDYLSGEL HHHHHCCHHHHCCCC	45.22	-
2851	Ubiquitination	QLEDKYDKDYLSGEL HHHHHCCHHHHCCCC	45.22	29967540
2863	Sumoylation	GELGDNLKMKIQVLL CCCCHHHEEEEEEEC	44.39	-
2863	Sumoylation	GELGDNLKMKIQVLL CCCCHHHEEEEEEEC	44.39	-
2865	Sumoylation	LGDNLKMKIQVLLH- CCHHHEEEEEEECC-	28.53	-
2865	Sumoylation	LGDNLKMKIQVLLH- CCHHHEEEEEEECC-	28.53	-

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
2702	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of FBN1_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of FBN1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MFAP2_HUMAN	MFAP2	physical	11481325

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 154700: Marfan syndrome (MFS)
• 129600: Ectopia lentis 1, isolated, autosomal dominant (ECTOL1)
• 608328: Weill-Marchesani syndrome 2 (WMS2)
• 604308: Overlap connective tissue disease (OCTD)
• 184900: Stiff skin syndrome (SSKS)
• 614185: Geleophysic dysplasia 2 (GPHYSD2)
• 102370: Acromicric dysplasia (ACMICD)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"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-448; ASN-1067; ASN-1484AND ASN-1581, AND MASS SPECTROMETRY.
PubMed: 19159218