F13A_HUMAN - dbPTM
F13A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID F13A_HUMAN
UniProt AC P00488
Protein Name Coagulation factor XIII A chain
Gene Name F13A1
Organism Homo sapiens (Human).
Sequence Length 732
Subcellular Localization Cytoplasm. Secreted . Secreted into the blood plasma. Cytoplasmic in most tissues, but also secreted in the blood plasma.
Protein Description Factor XIII is activated by thrombin and calcium ion to a transglutaminase that catalyzes the formation of gamma-glutamyl-epsilon-lysine cross-links between fibrin chains, thus stabilizing the fibrin clot. Also cross-link alpha-2-plasmin inhibitor, or fibronectin, to the alpha chains of fibrin..
Protein Sequence MSETSRTAFGGRRAVPPNNSNAAEDDLPTVELQGVVPRGVNLQEFLNVTSVHLFKERWDTNKVDHHTDKYENNKLIVRRGQSFYVQIDFSRPYDPRRDLFRVEYVIGRYPQENKGTYIPVPIVSELQSGKWGAKIVMREDRSVRLSIQSSPKCIVGKFRMYVAVWTPYGVLRTSRNPETDTYILFNPWCEDDAVYLDNEKEREEYVLNDIGVIFYGEVNDIKTRSWSYGQFEDGILDTCLYVMDRAQMDLSGRGNPIKVSRVGSAMVNAKDDEGVLVGSWDNIYAYGVPPSAWTGSVDILLEYRSSENPVRYGQCWVFAGVFNTFLRCLGIPARIVTNYFSAHDNDANLQMDIFLEEDGNVNSKLTKDSVWNYHCWNEAWMTRPDLPVGFGGWQAVDSTPQENSDGMYRCGPASVQAIKHGHVCFQFDAPFVFAEVNSDLIYITAKKDGTHVVENVDATHIGKLIVTKQIGGDGMMDITDTYKFQEGQEEERLALETALMYGAKKPLNTEGVMKSRSNVDMDFEVENAVLGKDFKLSITFRNNSHNRYTITAYLSANITFYTGVPKAEFKKETFDVTLEPLSFKKEAVLIQAGEYMGQLLEQASLHFFVTARINETRDVLAKQKSTVLTIPEIIIKVRGTQVVGSDMTVTVQFTNPLKETLRNVWVHLDGPGVTRPMKKMFREIRPNSTVQWEEVCRPWVSGHRKLIASMSSDSLRHVYGELDVQIQRRPSM
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
2Acetylation------MSETSRTAF
------CCCCCCCCC		49.972877456
55AcetylationVTSVHLFKERWDTNK
CEEEEEEEHHCCCCC		53.3715274630
69AcetylationKVDHHTDKYENNKLI
CCCCCCCCCCCCEEE		56.4717691819
74AcetylationTDKYENNKLIVRRGQ
CCCCCCCEEEEECCC		51.6915274630
84PhosphorylationVRRGQSFYVQIDFSR
EECCCEEEEEEECCC		9.19-
104PhosphorylationRDLFRVEYVIGRYPQ
CCEEEEEEEEECCCC		8.4320393185
109PhosphorylationVEYVIGRYPQENKGT
EEEEEECCCCCCCCE		12.2124260401
114AcetylationGRYPQENKGTYIPVP
ECCCCCCCCEEEECC		52.4517691819
116PhosphorylationYPQENKGTYIPVPIV
CCCCCCCEEEECCCE		21.6424260401
124PhosphorylationYIPVPIVSELQSGKW
EEECCCEEEHHCCCC		33.0528857561
128PhosphorylationPIVSELQSGKWGAKI
CCEEEHHCCCCEEEE		55.7727251275
130AcetylationVSELQSGKWGAKIVM
EEEHHCCCCEEEEEE		47.9317691819
134AcetylationQSGKWGAKIVMREDR
HCCCCEEEEEECCCC		31.7115274630
150PhosphorylationVRLSIQSSPKCIVGK
EEEEEECCCCEEEEE		16.4128060719
157AcetylationSPKCIVGKFRMYVAV
CCCEEEEEEEEEEEE		20.9215274630
161PhosphorylationIVGKFRMYVAVWTPY
EEEEEEEEEEEEECC		4.88-
200AcetylationAVYLDNEKEREEYVL
CEEECCHHHHHHEEE		69.2217691819
222AcetylationYGEVNDIKTRSWSYG
EEEECCCCCCCCCCC		40.5215274630
223PhosphorylationGEVNDIKTRSWSYGQ
EEECCCCCCCCCCCC		30.2128348404
225PhosphorylationVNDIKTRSWSYGQFE
ECCCCCCCCCCCCCC		26.1328348404
227PhosphorylationDIKTRSWSYGQFEDG
CCCCCCCCCCCCCCC		22.1928348404
228PhosphorylationIKTRSWSYGQFEDGI
CCCCCCCCCCCCCCH		14.5323532336
238PhosphorylationFEDGILDTCLYVMDR
CCCCHHHHHHHEEEH		10.8528348404
241PhosphorylationGILDTCLYVMDRAQM
CHHHHHHHEEEHHHH		8.8923532336
258AcetylationSGRGNPIKVSRVGSA
CCCCCCEEEEEEECE		35.1015274630
450PhosphorylationITAKKDGTHVVENVD
EEECCCCCEEEECCC		22.9425954137
459PhosphorylationVVENVDATHIGKLIV
EEECCCCCEEEEEEE		15.0125954137
463AcetylationVDATHIGKLIVTKQI
CCCCEEEEEEEEEEE		34.1415274630
467PhosphorylationHIGKLIVTKQIGGDG
EEEEEEEEEEECCCC		15.3925954137
468AcetylationIGKLIVTKQIGGDGM
EEEEEEEEEECCCCE		29.0815274630
483AcetylationMDITDTYKFQEGQEE
ECCCEEEECCCCCHH		42.5415274630
504AcetylationTALMYGAKKPLNTEG
HHHHHCCCCCCCCCC		51.0317691819
505AcetylationALMYGAKKPLNTEGV
HHHHCCCCCCCCCCC		54.9617691819
514AcetylationLNTEGVMKSRSNVDM
CCCCCCCCCCCCCCC		40.0717691819
532AcetylationVENAVLGKDFKLSIT
EEEEEECCCEEEEEE		56.6917691819
535AcetylationAVLGKDFKLSITFRN
EEECCCEEEEEEEEC		52.0015274630
582PhosphorylationDVTLEPLSFKKEAVL
EEEECCCCCCCEEEE		45.8224719451
584AcetylationTLEPLSFKKEAVLIQ
EECCCCCCCEEEEEE		46.4515274630
585AcetylationLEPLSFKKEAVLIQA
ECCCCCCCEEEEEEC		49.2315274630
614N-linked_GlycosylationFFVTARINETRDVLA
EEEEEECCCCHHHHH		38.7516335952
622AcetylationETRDVLAKQKSTVLT
CCHHHHHHHCCEEEE		54.8415274630
624AcetylationRDVLAKQKSTVLTIP
HHHHHHHCCEEEECC		47.6015274630
636AcetylationTIPEIIIKVRGTQVV
ECCEEEEEEECEEEE		18.5715274630
640PhosphorylationIIIKVRGTQVVGSDM
EEEEEECEEEECCCE		13.97-
645PhosphorylationRGTQVVGSDMTVTVQ
ECEEEECCCEEEEEE		16.76-
648PhosphorylationQVVGSDMTVTVQFTN
EEECCCEEEEEEECC		20.30-
650PhosphorylationVGSDMTVTVQFTNPL
ECCCEEEEEEECCCH		10.22-
678AcetylationPGVTRPMKKMFREIR
CCCCCCHHHHHHHHC		43.7115274630
679AcetylationGVTRPMKKMFREIRP
CCCCCHHHHHHHHCC		36.7015274630
688PhosphorylationFREIRPNSTVQWEEV
HHHHCCCCCCCHHHH		32.4128857561
689PhosphorylationREIRPNSTVQWEEVC
HHHCCCCCCCHHHHC		24.2928857561
705AcetylationPWVSGHRKLIASMSS
HHHCCCHHHHEECCH		38.2715274630
711PhosphorylationRKLIASMSSDSLRHV
HHHHEECCHHHHHHH		28.6229970186
731PhosphorylationVQIQRRPSM------
HEEEECCCC------		35.0024670416
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 F13A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of F13A_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 F13A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
F13A_HUMANF13A1physical
2491853
F13B_HUMANF13Bphysical
2491853
F13B_HUMANF13Bphysical
8905624
FINC_HUMANFN1physical
8905624
FIBA_HUMANFGAphysical
10956659
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613225Factor XIII subunit A deficiency (FA13AD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00130L-Glutamine
Regulatory Network of F13A_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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-614, AND MASSSPECTROMETRY.

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