F13B_MOUSE - dbPTM
F13B_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID F13B_MOUSE
UniProt AC Q07968
Protein Name Coagulation factor XIII B chain
Gene Name F13b
Organism Mus musculus (Mouse).
Sequence Length 669
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 MMTLRHLPFILLLILSGELYAEEKQCDFPTVENGRIAQYYYTFKSFYFPMSVDKKLSFFCLAGYATESGKQEEQIRCTAEGWSPNPRCYKKCLKPDLRNGYVSNDKVLYKLQERMSYGCSSGYKTTGGKDEEVVHCLSAGWSSQPSCRKEQETCLAPELEHGNYSTTQRTFKVKDIVAYTCTAGYYTTTGKQTGEAECQANGWSLTPQCNKLMCSSLRLIENGYFHPVKQTYEEGDVVQFFCHENYYLSGSDLIQCYNFGWYPESPICEGRRNRCPPPPVPLNSKIQPHSTTYRHGERVHIECELNFVIQGSEELLCENGKWTEPPKCIEEKEKVACEQPPSVENGVAHPHSEIYYSGDKVTYRCGGGYSLRGSSTITCNRGRWTLPPECVENIENCKPPPDIANGVVVDGLLASYTTGSSVEYRCNEYYLLKGSETSRCEQGAWSSPPVCLEPCTIDVDHMNRNNIQLKWKYEGKILHGDLIDFVCKQGYNLSPSIPLSEISAQCNRGDVRYPMCIRKESKGMCASPPVIRNGDIVSSAARTYENGSSVEYRCFDNHFLQGSQNVYCVDGVWTTPPSCLEPCTLSFVEMDKNYLQLKWNFDNRPLILHGEYIEFMCKRDAYISETSIAGSVLRVQCDRGRLKYPKCTPRDRRLSFQEALRTRRQMEKR
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 Orthologous
Protein Cluster
125PhosphorylationGCSSGYKTTGGKDEE
CCCCCCCCCCCCCHH
39.5228576409
163N-linked_GlycosylationAPELEHGNYSTTQRT
CCCCCCCCCCCCCCE
16.40-
164PhosphorylationPELEHGNYSTTQRTF
CCCCCCCCCCCCCEE
29.0429899451
166PhosphorylationLEHGNYSTTQRTFKV
CCCCCCCCCCCEEEH
15.3129899451
342PhosphorylationVACEQPPSVENGVAH
CCCCCCCCCCCCCCC
9.0323140645
352PhosphorylationNGVAHPHSEIYYSGD
CCCCCCCCEEEECCC
31.7923140645
355PhosphorylationAHPHSEIYYSGDKVT
CCCCCEEEECCCEEE
16.3123140645
357PhosphorylationPHSEIYYSGDKVTYR
CCCEEEECCCEEEEE
23.7223140645
362PhosphorylationYYSGDKVTYRCGGGY
EECCCEEEEEECCCE
13.5923140645
363PhosphorylationYSGDKVTYRCGGGYS
ECCCEEEEEECCCEE
11.8423140645
546N-linked_GlycosylationSAARTYENGSSVEYR
CCCEEEECCCCEEEE
14.9016944957
655PhosphorylationTPRDRRLSFQEALRT
CHHHHHHHHHHHHHH
10.0923140645

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 F13B_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of F13B_MOUSE !!

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 F13B_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of F13B_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of F13B_MOUSE

loading...

Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides.";
Bernhard O.K., Kapp E.A., Simpson R.J.;
J. Proteome Res. 6:987-995(2007).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-545, AND MASSSPECTROMETRY.
"Proteome-wide characterization of N-glycosylation events by diagonalchromatography.";
Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,Gevaert K.;
J. Proteome Res. 5:2438-2447(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-545, AND MASSSPECTROMETRY.

TOP