dbPTM

FIBB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FIBB_HUMAN
UniProt AC	P02675
Protein Name	Fibrinogen beta chain
Gene Name	FGB
Organism	Homo sapiens (Human).
Sequence Length	491
Subcellular Localization	Secreted .
Protein Description	Cleaved by the protease thrombin to yield monomers which, together with fibrinogen alpha (FGA) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the antibacterial immune response via both innate and T-cell mediated pathways..
Protein Sequence	MKRMVSWSFHKLKTMKHLLLLLLCVFLVKSQGVNDNEEGFFSARGHRPLDKKREEAPSLRPAPPPISGGGYRARPAKAAATQKKVERKAPDAGGCLHADPDLGVLCPTGCQLQEALLQQERPIRNSVDELNNNVEAVSQTSSSSFQYMYLLKDLWQKRQKQVKDNENVVNEYSSELEKHQLYIDETVNSNIPTNLRVLRSILENLRSKIQKLESDVSAQMEYCRTPCTVSCNIPVVSGKECEEIIRKGGETSEMYLIQPDSSVKPYRVYCDMNTENGGWTVIQNRQDGSVDFGRKWDPYKQGFGNVATNTDGKNYCGLPGEYWLGNDKISQLTRMGPTELLIEMEDWKGDKVKAHYGGFTVQNEANKYQISVNKYRGTAGNALMDGASQLMGENRTMTIHNGMFFSTYDRDNDGWLTSDPRKQCSKEDGGGWWYNRCHAANPNGRYYWGGQYTWDMAKHGTDDGVVWMNWKGSWYSMRKMSMKIRPFFPQQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
30	Phosphorylation	LCVFLVKSQGVNDNE HHHHHHHHCCCCCCC	25.37	24505115
31	Pyrrolidone_carboxylic_acid	CVFLVKSQGVNDNEE HHHHHHHCCCCCCCC	54.88	420779
31	Pyrrolidone_carboxylic_acid	CVFLVKSQGVNDNEE HHHHHHHCCCCCCCC	54.88	420779
31	Pyrrolidone_carboxylic_acid	CVFLVKSQGVNDNEE HHHHHHHCCCCCCCC	54.88	-
58	Phosphorylation	KKREEAPSLRPAPPP CCCCCCCCCCCCCCC	44.02	28060719
58	O-linked_Glycosylation	KKREEAPSLRPAPPP CCCCCCCCCCCCCCC	44.02	OGP
67	Phosphorylation	RPAPPPISGGGYRAR CCCCCCCCCCCCCCC	36.84	28857561
71	Phosphorylation	PPISGGGYRARPAKA CCCCCCCCCCCCCHH	12.36	28857561
71	Nitration	PPISGGGYRARPAKA CCCCCCCCCCCCCHH	12.36	-
108	O-linked_Glycosylation	DLGVLCPTGCQLQEA CCCCCCCCCHHHHHH	49.98	OGP
138	Phosphorylation	NNNVEAVSQTSSSSF HHCHHHHHCCCCHHH	34.49	-
147	Nitration	TSSSSFQYMYLLKDL CCCHHHHHHHHHHHH	5.92	-
149	Nitration	SSSFQYMYLLKDLWQ CHHHHHHHHHHHHHH	12.16	-
172	Nitration	NENVVNEYSSELEKH CHHHHHHHHHHHHHC	16.58	-
172	Phosphorylation	NENVVNEYSSELEKH CHHHHHHHHHHHHHC	16.58	28060719
173	Phosphorylation	ENVVNEYSSELEKHQ HHHHHHHHHHHHHCC	15.91	26657352
174	Phosphorylation	NVVNEYSSELEKHQL HHHHHHHHHHHHCCE	45.35	24505115
182	Nitration	ELEKHQLYIDETVNS HHHHCCEECCHHHHC	10.35	-
182	Phosphorylation	ELEKHQLYIDETVNS HHHHCCEECCHHHHC	10.35	22817900
200	Phosphorylation	TNLRVLRSILENLRS HHHHHHHHHHHHHHH	27.62	30087585
208	Acetylation	ILENLRSKIQKLESD HHHHHHHHHHHHHHC	42.60	24471073
227	S-nitrosylation	MEYCRTPCTVSCNIP HHHCCCCCEEEECCC	6.08	25040305
228	Phosphorylation	EYCRTPCTVSCNIPV HHCCCCCEEEECCCE	19.36	23911959
230	Phosphorylation	CRTPCTVSCNIPVVS CCCCCEEEECCCEEC	5.36	28857561
231	S-nitrosylation	RTPCTVSCNIPVVSG CCCCEEEECCCEECC	4.68	25040305
237	Phosphorylation	SCNIPVVSGKECEEI EECCCEECCHHHHHH	44.36	23911959
255	Phosphorylation	GGETSEMYLIQPDSS CCCCCEEEEECCCCC	9.15	-
261	Phosphorylation	MYLIQPDSSVKPYRV EEEECCCCCCCCEEE	43.65	-
262	Phosphorylation	YLIQPDSSVKPYRVY EEECCCCCCCCEEEE	41.35	-
264	Acetylation	IQPDSSVKPYRVYCD ECCCCCCCCEEEEEE	37.98	22507986
266	Phosphorylation	PDSSVKPYRVYCDMN CCCCCCCEEEEEECC	13.64	-
269	Phosphorylation	SVKPYRVYCDMNTEN CCCCEEEEEECCCCC	3.61	-
280	Phosphorylation	NTENGGWTVIQNRQD CCCCCCEEEEECCCC	15.82	-
289	Phosphorylation	IQNRQDGSVDFGRKW EECCCCCCCCCCCCC	27.14	28857561
295	Acetylation	GSVDFGRKWDPYKQG CCCCCCCCCCCCCCC	57.22	27178108
295	Glycation	GSVDFGRKWDPYKQG CCCCCCCCCCCCCCC	57.22	-
299	Phosphorylation	FGRKWDPYKQGFGNV CCCCCCCCCCCCCCE	17.30	25690035
300	Acetylation	GRKWDPYKQGFGNVA CCCCCCCCCCCCCEE	49.70	30585635
313	Acetylation	VATNTDGKNYCGLPG EEECCCCCCCCCCCC	47.77	7619179
315	Phosphorylation	TNTDGKNYCGLPGEY ECCCCCCCCCCCCCE	7.44	-
316	S-nitrosylation	NTDGKNYCGLPGEYW CCCCCCCCCCCCCEE	6.71	25040305
322	Nitration	YCGLPGEYWLGNDKI CCCCCCCEECCCCHH	16.32	-
333	Phosphorylation	NDKISQLTRMGPTEL CCHHHHHHHCCCCEE	15.80	-
338	Phosphorylation	QLTRMGPTELLIEME HHHHCCCCEEEEEEE	33.27	-
348	Acetylation	LIEMEDWKGDKVKAH EEEEECCCCCEEEEE	70.34	30585629
353	Glycation	DWKGDKVKAHYGGFT CCCCCEEEEEECCEE	34.88	-
356	Nitration	GDKVKAHYGGFTVQN CCEEEEEECCEEEEC	24.65	-
356	Phosphorylation	GDKVKAHYGGFTVQN CCEEEEEECCEEEEC	24.65	-
368	Nitration	VQNEANKYQISVNKY EECCCCCEEEEEEEC	15.75	-
368	Phosphorylation	VQNEANKYQISVNKY EECCCCCEEEEEEEC	15.75	28270605
371	Phosphorylation	EANKYQISVNKYRGT CCCCEEEEEEECCCC	12.24	23911959
374	Acetylation	KYQISVNKYRGTAGN CEEEEEEECCCCHHH	33.88	27178108
375	Phosphorylation	YQISVNKYRGTAGNA EEEEEEECCCCHHHH	14.74	28270605
394	N-linked_Glycosylation	ASQLMGENRTMTIHN HHHHHCCCCEEEEEC	38.71	16263699
394	N-linked_Glycosylation	ASQLMGENRTMTIHN HHHHHCCCCEEEEEC	38.71	16263699
396	Phosphorylation	QLMGENRTMTIHNGM HHHCCCCEEEEECCE	30.19	-
408	Phosphorylation	NGMFFSTYDRDNDGW CCEEEECEECCCCCC	14.05	21253578
417	Phosphorylation	RDNDGWLTSDPRKQC CCCCCCCCCCCCCCC	25.28	22210691
418	Phosphorylation	DNDGWLTSDPRKQCS CCCCCCCCCCCCCCC	43.37	22210691
425	Phosphorylation	SDPRKQCSKEDGGGW CCCCCCCCCCCCCCC	36.26	28857561
434	Nitration	EDGGGWWYNRCHAAN CCCCCCCCCCEEEEC	6.04	-
452	Nitration	RYYWGGQYTWDMAKH CEECCCEECCCHHHH	17.05	-
452	Phosphorylation	RYYWGGQYTWDMAKH CEECCCEECCCHHHH	17.05	-
471	Acetylation	GVVWMNWKGSWYSMR CEEEEECCCCHHHHC	37.75	7822959
475	Nitration	MNWKGSWYSMRKMSM EECCCCHHHHCCCCC	8.35	-
475	Phosphorylation	MNWKGSWYSMRKMSM EECCCCHHHHCCCCC	8.35	-
481	Phosphorylation	WYSMRKMSMKIRPFF HHHHCCCCCCEECCC	21.69	24719451

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 FIBB_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of FIBB_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
208	Acetylation	206 (2)	P ⇒ L	rs6054	Fibrinogen levels	26561523
255	Phosphorylation	265 (10)	P ⇒ L	rs6054	Fibrinogen levels	26561523
261	Phosphorylation	265 (4)	P ⇒ L	rs6054	Fibrinogen levels	26561523
262	Phosphorylation	265 (3)	P ⇒ L	rs6054	Fibrinogen levels	26561523
264	Acetylation	265 (1)	P ⇒ L	rs6054	Fibrinogen levels	26561523
266	Phosphorylation	265 (1)	P ⇒ L	rs6054	Fibrinogen levels	26561523
269	Phosphorylation	265 (4)	P ⇒ L	rs6054	Fibrinogen levels	26561523

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CALR_HUMAN	CALR	physical	7592883
SBDS_HUMAN	SBDS	physical	28514442
SPRE_HUMAN	SPR	physical	28514442
ADK_HUMAN	ADK	physical	28514442
SYNC_HUMAN	NARS	physical	28514442
OXSR1_HUMAN	OXSR1	physical	28514442
NAA15_HUMAN	NAA15	physical	28514442
NDKB_HUMAN	NME2	physical	28514442
PO2F1_HUMAN	POU2F1	physical	28514442
SLK_HUMAN	SLK	physical	28514442
TCEA1_HUMAN	TCEA1	physical	28514442
EIF2A_HUMAN	EIF2A	physical	28514442
BLVRB_HUMAN	BLVRB	physical	28514442
CTBL1_HUMAN	CTNNBL1	physical	28514442
TBC24_HUMAN	TBC1D24	physical	28514442
MP2K1_HUMAN	MAP2K1	physical	28514442
UBCP1_HUMAN	UBLCP1	physical	28514442
SNX3_HUMAN	SNX3	physical	28514442
RHG01_HUMAN	ARHGAP1	physical	28514442
ATG3_HUMAN	ATG3	physical	28514442
VRK1_HUMAN	VRK1	physical	28514442
PMVK_HUMAN	PMVK	physical	28514442
PPID_HUMAN	PPID	physical	28514442
MCTS1_HUMAN	MCTS1	physical	28514442
PUS7_HUMAN	PUS7	physical	28514442
ARMT1_HUMAN	C6orf211	physical	28514442
EF1A2_HUMAN	EEF1A2	physical	28514442
PIR_HUMAN	PIR	physical	28514442
PAK2_HUMAN	PAK2	physical	28514442
ITPA_HUMAN	ITPA	physical	28514442
LZIC_HUMAN	LZIC	physical	28514442
DUS3_HUMAN	DUSP3	physical	28514442
VIGLN_HUMAN	HDLBP	physical	28514442
PUR8_HUMAN	ADSL	physical	28514442
DENR_HUMAN	DENR	physical	28514442
HMCS1_HUMAN	HMGCS1	physical	28514442
KIF2A_HUMAN	KIF2A	physical	28514442
ERF1_HUMAN	ETF1	physical	28514442
FEN1_HUMAN	FEN1	physical	28514442
UBE2T_HUMAN	UBE2T	physical	28514442
GRAN_HUMAN	GCA	physical	28514442
LETM1_HUMAN	LETM1	physical	28514442
PYM1_HUMAN	WIBG	physical	28514442
PSME2_HUMAN	PSME2	physical	28514442
CGL_HUMAN	CTH	physical	28514442
OTUB1_HUMAN	OTUB1	physical	28514442
FTO_HUMAN	FTO	physical	28514442
HDGR2_HUMAN	HDGFRP2	physical	28514442
GPKOW_HUMAN	GPKOW	physical	28514442
PNPO_HUMAN	PNPO	physical	28514442
VP26A_HUMAN	VPS26A	physical	28514442
NAA50_HUMAN	NAA50	physical	28514442
RBM12_HUMAN	RBM12	physical	28514442
K1143_HUMAN	KIAA1143	physical	28514442
EIF3J_HUMAN	EIF3J	physical	28514442
KPCI_HUMAN	PRKCI	physical	28514442
SF3A1_HUMAN	SF3A1	physical	28514442
RPR1A_HUMAN	RPRD1A	physical	28514442
PAPS1_HUMAN	PAPSS1	physical	28514442
TLN1_HUMAN	TLN1	physical	28514442
UBA1_HUMAN	UBA1	physical	28514442
RPR1B_HUMAN	RPRD1B	physical	28514442
SYFB_HUMAN	FARSB	physical	28514442
USO1_HUMAN	USO1	physical	28514442
DDAH1_HUMAN	DDAH1	physical	28514442
TOPK_HUMAN	PBK	physical	28514442
CAB39_HUMAN	CAB39	physical	28514442
RHOA_HUMAN	RHOA	physical	28514442
PTN11_HUMAN	PTPN11	physical	28514442
TES_HUMAN	TES	physical	28514442
PYGB_HUMAN	PYGB	physical	28514442
RRP44_HUMAN	DIS3	physical	28514442
SCRN1_HUMAN	SCRN1	physical	28514442
PAK1_HUMAN	PAK1	physical	28514442
GNAQ_HUMAN	GNAQ	physical	28514442
SYAP1_HUMAN	SYAP1	physical	28514442
SNX6_HUMAN	SNX6	physical	28514442
PAPOA_HUMAN	PAPOLA	physical	28514442
LSM1_HUMAN	LSM1	physical	28514442
GLSK_HUMAN	GLS	physical	28514442
T2FA_HUMAN	GTF2F1	physical	28514442
GNL1_HUMAN	GNL1	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
202400	Congenital afibrinogenemia (CAFBN)
616004	Dysfibrinogenemia, congenital (DYSFIBRIN)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of FIBB_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-394, AND MASSSPECTROMETRY.	19159218 [Abstract]
"Elucidation of N-glycosylation sites on human platelet proteins: aglycoproteomic approach."; Lewandrowski U., Moebius J., Walter U., Sickmann A.; Mol. Cell. Proteomics 5:226-233(2006). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-394, AND MASSSPECTROMETRY.	16263699 [Abstract]
"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-394, AND MASSSPECTROMETRY.	16335952 [Abstract]