F13B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: F13B_HUMAN
• UniProt AC: P05160
• Protein Name: Coagulation factor XIII B chain
• Gene Name: F13B
• Organism: Homo sapiens (Human).
• Sequence Length: 661
• Subcellular Localization: Secreted .
• Protein Description: The B chain of factor XIII is not catalytically active, but is thought to stabilize the A subunits and regulate the rate of transglutaminase formation by thrombin..
• Protein Sequence: MRLKNLTFIIILIISGELYAEEKPCGFPHVENGRIAQYYYTFKSFYFPMSIDKKLSFFCLAGYTTESGRQEEQTTCTTEGWSPEPRCFKKCTKPDLSNGYISDVKLLYKIQENMRYGCASGYKTTGGKDEEVVQCLSDGWSSQPTCRKEHETCLAPELYNGNYSTTQKTFKVKDKVQYECATGYYTAGGKKTEEVECLTYGWSLTPKCTKLKCSSLRLIENGYFHPVKQTYEEGDVVQFFCHENYYLSGSDLIQCYNFGWYPESPVCEGRRNRCPPPPLPINSKIQTHSTTYRHGEIVHIECELNFEIHGSAEIRCEDGKWTEPPKCIEGQEKVACEEPPFIENGAANLHSKIYYNGDKVTYACKSGYLLHGSNEITCNRGKWTLPPECVENNENCKHPPVVMNGAVADGILASYATGSSVEYRCNEYYLLRGSKISRCEQGKWSSPPVCLEPCTVNVDYMNRNNIEMKWKYEGKVLHGDLIDFVCKQGYDLSPLTPLSELSVQCNRGEVKYPLCTRKESKGMCTSPPLIKHGVIISSTVDTYENGSSVEYRCFDHHFLEGSREAYCLDGMWTTPPLCLEPCTLSFTEMEKNNLLLKWDFDNRPHILHGEYIEFICRGDTYPAELYITGSILRMQCDRGQLKYPRCIPRQSTLSYQEPLRT

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
162	N-linked_Glycosylation	APELYNGNYSTTQKT CCCCCCCCCCCCEEE	24.76	17623646
162	N-linked_Glycosylation	APELYNGNYSTTQKT CCCCCCCCCCCCEEE	24.76	17623646
182	Phosphorylation	KVQYECATGYYTAGG EEEEEEECCEEECCC	37.06	-
373	Phosphorylation	SGYLLHGSNEITCNR CCEEECCCCEEECCC	22.12	27130503
377	Phosphorylation	LHGSNEITCNRGKWT ECCCCEEECCCCCEE	9.50	28270605
512	Phosphorylation	CNRGEVKYPLCTRKE CCCCCCCCCEECCCC	13.45	-
516	O-linked_Glycosylation	EVKYPLCTRKESKGM CCCCCEECCCCCCCC	53.08	30620550
520	O-linked_Glycosylation	PLCTRKESKGMCTSP CEECCCCCCCCCCCC	37.23	30620550
545	N-linked_Glycosylation	STVDTYENGSSVEYR CEEEECCCCCCEEEE	45.28	17623646
545	N-linked_Glycosylation	STVDTYENGSSVEYR CEEEECCCCCCEEEE	45.28	16335952
562	Phosphorylation	DHHFLEGSREAYCLD CCHHCCCCCEEEEEC	19.99	24505115
643	Phosphorylation	CDRGQLKYPRCIPRQ ECCCCCCCCCCCCCC	12.42	-
652	O-linked_Glycosylation	RCIPRQSTLSYQEPL CCCCCCCCCCCCCCC	16.04	OGP
661	Phosphorylation	SYQEPLRT------- CCCCCCCC-------	51.12	-

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

Oops, there are no upstream regulatory protein records of F13B_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of F13B_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 F13B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FIBG_HUMAN	FGG	physical	8756701

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 613235: Factor XIII subunit B deficiency (FA13BD)
• 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-162, AND MASSSPECTROMETRY.
PubMed: 19159218

"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-545, AND MASSSPECTROMETRY.
PubMed: 16335952