F10C1_HUMAN - dbPTM
F10C1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID F10C1_HUMAN
UniProt AC Q70Z53
Protein Name Protein FRA10AC1
Gene Name FRA10AC1
Organism Homo sapiens (Human).
Sequence Length 315
Subcellular Localization Nucleus .
Protein Description
Protein Sequence MHGHGGYDSDFSDDERCGESSKRKKRTVEDDLLLQKPFQKEKHGKVAHKQVAAELLDREEARNRRFHLIAMDAYQRHTKFVNDYILYYGGKKEDFKRLGENDKTDLDVIRENHRFLWNEEDEMDMTWEKRLAKKYYDKLFKEYCIADLSKYKENKFGFRWRVEKEVISGKGQFFCGNKYCDKKEGLKSWEVNFGYIEHGEKRNALVKLRLCQECSIKLNFHHRRKEIKSKKRKDKTKKDCEESSHKKSRLSSAEEASKKKDKGHSSSKKSEDSLLRNSDEEESASESELWKGPLPETDEKSQEEEFDEYFQDLFL
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
1Acetylation-------MHGHGGYD
-------CCCCCCCC		8.4619413330
7Phosphorylation-MHGHGGYDSDFSDD
-CCCCCCCCCCCCCC		19.5033259812
9PhosphorylationHGHGGYDSDFSDDER
CCCCCCCCCCCCCCC		31.8822617229
12PhosphorylationGGYDSDFSDDERCGE
CCCCCCCCCCCCCCC		49.4922617229
20PhosphorylationDDERCGESSKRKKRT
CCCCCCCCCCCCCCC		26.8326074081
21PhosphorylationDERCGESSKRKKRTV
CCCCCCCCCCCCCCH		31.9826074081
36AcetylationEDDLLLQKPFQKEKH
HHHHHHCCCCCCCCC		48.0123954790
36SumoylationEDDLLLQKPFQKEKH
HHHHHHCCCCCCCCC		48.01-
36UbiquitinationEDDLLLQKPFQKEKH
HHHHHHCCCCCCCCC		48.0129967540
40AcetylationLLQKPFQKEKHGKVA
HHCCCCCCCCCCCCC		69.9419820223
42AcetylationQKPFQKEKHGKVAHK
CCCCCCCCCCCCCHH		65.7719820231
42UbiquitinationQKPFQKEKHGKVAHK
CCCCCCCCCCCCCHH		65.77-
45AcetylationFQKEKHGKVAHKQVA
CCCCCCCCCCHHHHH		35.6519820239
49AcetylationKHGKVAHKQVAAELL
CCCCCCHHHHHHHHH		36.4125953088
58MethylationVAAELLDREEARNRR
HHHHHHCHHHHHHCC		43.56-
84PhosphorylationHTKFVNDYILYYGGK
HHHHHHCEEEEECCC		6.39-
88PhosphorylationVNDYILYYGGKKEDF
HHCEEEEECCCHHHH		18.89-
92AcetylationILYYGGKKEDFKRLG
EEEECCCHHHHHHHC		66.8318584541
103UbiquitinationKRLGENDKTDLDVIR
HHHCCCCCCCHHHHH		56.3624816145
110UbiquitinationKTDLDVIRENHRFLW
CCCHHHHHHCCCCCC		38.2124816145
150UbiquitinationYCIADLSKYKENKFG
HHHHHHHHHCCCCCC		68.5829967540
178AcetylationGQFFCGNKYCDKKEG
CEEECCCCCCCCCCC		32.3225953088
178UbiquitinationGQFFCGNKYCDKKEG
CEEECCCCCCCCCCC		32.3229967540
201AcetylationGYIEHGEKRNALVKL
EEECCHHHHCHHHHH		56.3925953088
248PhosphorylationEESSHKKSRLSSAEE
HHHHHHHHHHHHHHH		43.1725106551
251 (in isoform 5)Phosphorylation-26.79-
251 (in isoform 2)Phosphorylation-26.79-
251 (in isoform 4)Phosphorylation-26.79-
251 (in isoform 3)Phosphorylation-26.79-
251PhosphorylationSHKKSRLSSAEEASK
HHHHHHHHHHHHHHH		26.7925159151
252 (in isoform 4)Phosphorylation-44.27-
252 (in isoform 5)Phosphorylation-44.27-
252 (in isoform 2)Phosphorylation-44.27-
252 (in isoform 3)Phosphorylation-44.27-
252PhosphorylationHKKSRLSSAEEASKK
HHHHHHHHHHHHHHH		44.2725159151
257PhosphorylationLSSAEEASKKKDKGH
HHHHHHHHHHHCCCC		48.5729396449
259AcetylationSAEEASKKKDKGHSS
HHHHHHHHHCCCCCC		64.8026051181
260AcetylationAEEASKKKDKGHSSS
HHHHHHHHCCCCCCC		69.2926051181
266PhosphorylationKKDKGHSSSKKSEDS
HHCCCCCCCCCHHHH		40.2727282143
267PhosphorylationKDKGHSSSKKSEDSL
HCCCCCCCCCHHHHH		47.3027282143
269AcetylationKGHSSSKKSEDSLLR
CCCCCCCCHHHHHHH		62.1119806579
270 (in isoform 3)Phosphorylation-50.8226437602
270PhosphorylationGHSSSKKSEDSLLRN
CCCCCCCHHHHHHHC		50.8222617229
273PhosphorylationSSKKSEDSLLRNSDE
CCCCHHHHHHHCCCC		25.8330266825
273 (in isoform 3)Phosphorylation-25.8326437602
278PhosphorylationEDSLLRNSDEEESAS
HHHHHHCCCCHHHCC		39.7123927012
283PhosphorylationRNSDEEESASESELW
HCCCCHHHCCHHHHH		40.1323927012
285PhosphorylationSDEEESASESELWKG
CCCHHHCCHHHHHCC		51.4323927012
287PhosphorylationEEESASESELWKGPL
CHHHCCHHHHHCCCC		35.1823927012
291 (in isoform 5)Phosphorylation-64.3726552605
294 (in isoform 5)Phosphorylation-9.0226552605
297PhosphorylationWKGPLPETDEKSQEE
HCCCCCCCCCHHHHH		47.7427732954
299 (in isoform 5)Phosphorylation-63.1326552605
301PhosphorylationLPETDEKSQEEEFDE
CCCCCCHHHHHHHHH		40.5527732954
303 (in isoform 5)Phosphorylation-67.5926552605
307 (in isoform 5)Phosphorylation-53.6326552605
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 F10C1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of F10C1_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 F10C1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARHL2_HUMANADPRHL2physical
16169070
CG025_HUMANC7orf25physical
16169070
GDPD2_HUMANGDPD2physical
16169070
PLPR4_HUMANLPPR4physical
16169070
GLRX3_HUMANGLRX3physical
16169070
VPS29_HUMANVPS29physical
16169070
EF1D_HUMANEEF1Dphysical
16169070
PR40A_HUMANPRPF40Aphysical
22365833
SF3B2_HUMANSF3B2physical
22365833
U2AF1_HUMANU2AF1physical
22365833
CHERP_HUMANCHERPphysical
22365833
PRPF3_HUMANPRPF3physical
22365833
MFAP1_HUMANMFAP1physical
22365833
RED_HUMANIKphysical
22365833
THOC1_HUMANTHOC1physical
22365833
CWC27_HUMANCWC27physical
22365833
DGC14_HUMANDGCR14physical
22365833
ZN830_HUMANZNF830physical
22365833
S30BP_HUMANSAP30BPphysical
22365833
NKAP_HUMANNKAPphysical
22365833
TTC14_HUMANTTC14physical
22365833
ZCH10_HUMANZCCHC10physical
22365833
M3K12_HUMANMAP3K12physical
16169070
KASH5_HUMANCCDC155physical
25416956
CLIC1_HUMANCLIC1physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of F10C1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-9; SER-12; SER-278 AND SER-283, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-9; SER-12; SER-278 AND SER-283, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251 AND SER-252, ANDMASS SPECTROMETRY.

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