TFG_HUMAN - dbPTM
TFG_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TFG_HUMAN
UniProt AC Q92734
Protein Name Protein TFG
Gene Name TFG
Organism Homo sapiens (Human).
Sequence Length 400
Subcellular Localization Endoplasmic reticulum . Localizes to endoplasmic reticulum exit site (ERES) (PubMed:27813252).
Protein Description Plays a role in the normal dynamic function of the endoplasmic reticulum (ER) and its associated microtubules. [PubMed: 23479643]
Protein Sequence MNGQLDLSGKLIIKAQLGEDIRRIPIHNEDITYDELVLMMQRVFRGKLLSNDEVTIKYKDEDGDLITIFDSSDLSFAIQCSRILKLTLFVNGQPRPLESSQVKYLRRELIELRNKVNRLLDSLEPPGEPGPSTNIPENDTVDGREEKSASDSSGKQSTQVMAASMSAFDPLKNQDEINKNVMSAFGLTDDQVSGPPSAPAEDRSGTPDSIASSSSAAHPPGVQPQQPPYTGAQTQAGQIEGQMYQQYQQQAGYGAQQPQAPPQQPQQYGIQYSASYSQQTGPQQPQQFQGYGQQPTSQAPAPAFSGQPQQLPAQPPQQYQASNYPAQTYTAQTSQPTNYTVAPASQPGMAPSQPGAYQPRPGFTSLPGSTMTPPPSGPNPYARNRPPFGQGYTQPGPGYR
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
1Sulfoxidation-------MNGQLDLS
-------CCCCCCCC
13.1928465586
1Acetylation-------MNGQLDLS
-------CCCCCCCC
13.1922223895
8PhosphorylationMNGQLDLSGKLIIKA
CCCCCCCCCCEEEEE
33.2822199227
22MethylationAQLGEDIRRIPIHNE
EECCCCHHCCCCCCC
42.68115918401
33PhosphorylationIHNEDITYDELVLMM
CCCCCCCHHHHHHHH
14.0422817900
47AcetylationMQRVFRGKLLSNDEV
HHHHHCCCCCCCCCE
41.8323954790
47UbiquitinationMQRVFRGKLLSNDEV
HHHHHCCCCCCCCCE
41.8321890473
472-HydroxyisobutyrylationMQRVFRGKLLSNDEV
HHHHHCCCCCCCCCE
41.83-
50PhosphorylationVFRGKLLSNDEVTIK
HHCCCCCCCCCEEEE
53.3129255136
57UbiquitinationSNDEVTIKYKDEDGD
CCCCEEEEEECCCCC
36.56-
99PhosphorylationGQPRPLESSQVKYLR
CEECCCCHHHHHHHH
33.4827732954
100PhosphorylationQPRPLESSQVKYLRR
EECCCCHHHHHHHHH
29.6225850435
103AcetylationPLESSQVKYLRRELI
CCCHHHHHHHHHHHH
30.8123954790
103UbiquitinationPLESSQVKYLRRELI
CCCHHHHHHHHHHHH
30.8121890473
103MalonylationPLESSQVKYLRRELI
CCCHHHHHHHHHHHH
30.8126320211
140PhosphorylationTNIPENDTVDGREEK
CCCCCCCCCCCCCCC
31.8830576142
147UbiquitinationTVDGREEKSASDSSG
CCCCCCCCCCCCCCC
46.7121906983
147UbiquitinationTVDGREEKSASDSSG
CCCCCCCCCCCCCCC
46.7121906983
147UbiquitinationTVDGREEKSASDSSG
CCCCCCCCCCCCCCC
46.7121906983
148PhosphorylationVDGREEKSASDSSGK
CCCCCCCCCCCCCCC
35.9623927012
150PhosphorylationGREEKSASDSSGKQS
CCCCCCCCCCCCCHH
45.1523927012
152PhosphorylationEEKSASDSSGKQSTQ
CCCCCCCCCCCHHHH
38.2023927012
153PhosphorylationEKSASDSSGKQSTQV
CCCCCCCCCCHHHHH
55.8123927012
155AcetylationSASDSSGKQSTQVMA
CCCCCCCCHHHHHHH
42.9226051181
155UbiquitinationSASDSSGKQSTQVMA
CCCCCCCCHHHHHHH
42.9221906983
155UbiquitinationSASDSSGKQSTQVMA
CCCCCCCCHHHHHHH
42.9221890473
157PhosphorylationSDSSGKQSTQVMAAS
CCCCCCHHHHHHHHH
25.0525850435
158PhosphorylationDSSGKQSTQVMAASM
CCCCCHHHHHHHHHH
23.7625850435
161SulfoxidationGKQSTQVMAASMSAF
CCHHHHHHHHHHHHH
1.5330846556
164PhosphorylationSTQVMAASMSAFDPL
HHHHHHHHHHHHCCC
12.0630576142
165SulfoxidationTQVMAASMSAFDPLK
HHHHHHHHHHHCCCC
2.6230846556
166PhosphorylationQVMAASMSAFDPLKN
HHHHHHHHHHCCCCC
24.2425850435
172UbiquitinationMSAFDPLKNQDEINK
HHHHCCCCCHHHHHH
58.9321906983
172AcetylationMSAFDPLKNQDEINK
HHHHCCCCCHHHHHH
58.9326051181
172UbiquitinationMSAFDPLKNQDEINK
HHHHCCCCCHHHHHH
58.9321906983
179UbiquitinationKNQDEINKNVMSAFG
CCHHHHHHHHHHHHC
57.4921906983
179UbiquitinationKNQDEINKNVMSAFG
CCHHHHHHHHHHHHC
57.4921890473
182SulfoxidationDEINKNVMSAFGLTD
HHHHHHHHHHHCCCC
3.1528183972
183PhosphorylationEINKNVMSAFGLTDD
HHHHHHHHHHCCCCC
19.0322167270
188PhosphorylationVMSAFGLTDDQVSGP
HHHHHCCCCCCCCCC
37.6030266825
193PhosphorylationGLTDDQVSGPPSAPA
CCCCCCCCCCCCCCC
39.6930266825
197PhosphorylationDQVSGPPSAPAEDRS
CCCCCCCCCCCCCCC
50.4429255136
204PhosphorylationSAPAEDRSGTPDSIA
CCCCCCCCCCCCCHH
60.3825137130
206PhosphorylationPAEDRSGTPDSIASS
CCCCCCCCCCCHHCC
25.7624275569
209PhosphorylationDRSGTPDSIASSSSA
CCCCCCCCHHCCCCC
22.6625137130
212PhosphorylationGTPDSIASSSSAAHP
CCCCCHHCCCCCCCC
29.1424275569
213PhosphorylationTPDSIASSSSAAHPP
CCCCHHCCCCCCCCC
21.2024275569
214PhosphorylationPDSIASSSSAAHPPG
CCCHHCCCCCCCCCC
22.8525137130
215PhosphorylationDSIASSSSAAHPPGV
CCHHCCCCCCCCCCC
31.2725137130
229PhosphorylationVQPQQPPYTGAQTQA
CCCCCCCCCCCCCCC
25.2124275569
230PhosphorylationQPQQPPYTGAQTQAG
CCCCCCCCCCCCCCC
31.6424275569
234PhosphorylationPPYTGAQTQAGQIEG
CCCCCCCCCCCEECH
21.6124275569
247PhosphorylationEGQMYQQYQQQAGYG
CHHHHHHHHHHCCCC
7.8622817900
330O-linked_GlycosylationNYPAQTYTAQTSQPT
CCCCCEEEECCCCCC
18.7123301498
333O-linked_GlycosylationAQTYTAQTSQPTNYT
CCEEEECCCCCCCEE
27.1923301498
334O-linked_GlycosylationQTYTAQTSQPTNYTV
CEEEECCCCCCCEEE
23.2923301498
337O-linked_GlycosylationTAQTSQPTNYTVAPA
EECCCCCCCEEECCC
32.9723301498
369PhosphorylationGFTSLPGSTMTPPPS
CCCCCCCCCCCCCCC
17.0525627689
369O-linked_GlycosylationGFTSLPGSTMTPPPS
CCCCCCCCCCCCCCC
17.0523301498
370PhosphorylationFTSLPGSTMTPPPSG
CCCCCCCCCCCCCCC
30.8628348404
372PhosphorylationSLPGSTMTPPPSGPN
CCCCCCCCCCCCCCC
32.5025159151
376O-linked_GlycosylationSTMTPPPSGPNPYAR
CCCCCCCCCCCCCCC
73.0623301498
376PhosphorylationSTMTPPPSGPNPYAR
CCCCCCCCCCCCCCC
73.06-
381PhosphorylationPPSGPNPYARNRPPF
CCCCCCCCCCCCCCC
25.49-
383DimethylationSGPNPYARNRPPFGQ
CCCCCCCCCCCCCCC
33.57-
383MethylationSGPNPYARNRPPFGQ
CCCCCCCCCCCCCCC
33.5730989511
385MethylationPNPYARNRPPFGQGY
CCCCCCCCCCCCCCC
34.4124129315
385DimethylationPNPYARNRPPFGQGY
CCCCCCCCCCCCCCC
34.41-
392PhosphorylationRPPFGQGYTQPGPGY
CCCCCCCCCCCCCCC
8.3621945579
393PhosphorylationPPFGQGYTQPGPGYR
CCCCCCCCCCCCCCC
34.8021945579
399PhosphorylationYTQPGPGYR------
CCCCCCCCC------
19.1121945579
400MethylationTQPGPGYR-------
CCCCCCCC-------
46.0824129315
400DimethylationTQPGPGYR-------
CCCCCCCC-------
46.08-

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
33YPhosphorylationKinaseSRCP12931
PSP
247YPhosphorylationKinaseSRCP12931
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TFG_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 TFG_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ERG28_HUMANC14orf1physical
16169070
GASP1_HUMANGPRASP1physical
16169070
GBP2_HUMANGBP2physical
16169070
DPYL1_HUMANCRMP1physical
16169070
CE126_HUMANKIAA1377physical
16169070
TFG_HUMANTFGphysical
16169070
TFG_HUMANTFGphysical
7565764
TRI25_HUMANTRIM25physical
23810392
TRI68_HUMANTRIM68physical
24999993
TFG_HUMANTFGphysical
25416956
SC24A_HUMANSEC24Aphysical
25416956
RBPMS_HUMANRBPMSphysical
25416956
ARHGG_HUMANARHGEF16physical
25416956
SPG21_HUMANSPG21physical
25416956
VP37C_HUMANVPS37Cphysical
25416956
CEP55_HUMANCEP55physical
25416956
BOLL_HUMANBOLLphysical
25416956
MISSL_HUMANMAPK1IP1Lphysical
25416956
RIPP2_HUMANRIPPLY2physical
25416956
PEF1_HUMANPEF1physical
25416956
SC31A_HUMANSEC31Aphysical
26186194
ISK5_HUMANSPINK5physical
26186194
PKP1_HUMANPKP1physical
26186194
IF1AX_HUMANEIF1AXphysical
26186194
S10A3_HUMANS100A3physical
26186194
LRC15_HUMANLRRC15physical
26186194
S10A7_HUMANS100A7physical
26186194
FBX11_HUMANFBXO11physical
26186194
HNRC1_HUMANHNRNPCL1physical
26186194
DSG4_HUMANDSG4physical
26186194
SBP1_HUMANSELENBP1physical
26186194
DUS14_HUMANDUSP14physical
26186194
HPHL1_HUMANHEPHL1physical
26186194
MAGD1_HUMANMAGED1physical
21516116
ANXA1_HUMANANXA1physical
26496610
VATB2_HUMANATP6V1B2physical
26496610
VPP1_HUMANATP6V0A1physical
26496610
CLCA_HUMANCLTAphysical
26496610
FLOT2_HUMANFLOT2physical
26496610
RL10A_HUMANRPL10Aphysical
26496610
CHM1A_HUMANCHMP1Aphysical
26496610
SYRC_HUMANRARSphysical
26496610
RL4_HUMANRPL4physical
26496610
ITSN1_HUMANITSN1physical
26496610
TOP2A_HUMANTOP2Aphysical
26496610
TS101_HUMANTSG101physical
26496610
NCOA4_HUMANNCOA4physical
26496610
SNX3_HUMANSNX3physical
26496610
AURKB_HUMANAURKBphysical
26496610
EPN4_HUMANCLINT1physical
26496610
IST1_HUMANIST1physical
26496610
NPA1P_HUMANURB1physical
26496610
PDC6I_HUMANPDCD6IPphysical
26496610
RCL1_HUMANRCL1physical
26496610
ATP5H_HUMANATP5Hphysical
26496610
SC31A_HUMANSEC31Aphysical
26496610
MTUS2_HUMANMTUS2physical
26496610
NIPBL_HUMANNIPBLphysical
26496610
NEPRO_HUMANC3orf17physical
26496610
TARSH_HUMANABI3BPphysical
26496610
FBXL6_HUMANFBXL6physical
26496610
CHM2A_HUMANCHMP2Aphysical
26496610
CHM4A_HUMANCHMP4Aphysical
26496610
PHF20_HUMANPHF20physical
26496610
CHMP5_HUMANCHMP5physical
26496610
SCLY_HUMANSCLYphysical
26496610
CHMP3_HUMANCHMP3physical
26496610
DPM3_HUMANDPM3physical
26496610
DGCR8_HUMANDGCR8physical
26496610
NAT10_HUMANNAT10physical
26496610
CHM1B_HUMANCHMP1Bphysical
26496610
ERGI1_HUMANERGIC1physical
26496610
BICC1_HUMANBICC1physical
26496610
KLH13_HUMANKLHL13physical
26496610
TOP1M_HUMANTOP1MTphysical
26496610
CHM4B_HUMANCHMP4Bphysical
26496610
MITD1_HUMANMITD1physical
26496610
PLBL2_HUMANPLBD2physical
26496610
UMAD1_HUMANUMAD1physical
26496610
ISK5_HUMANSPINK5physical
28514442
DSG4_HUMANDSG4physical
28514442
S10A3_HUMANS100A3physical
28514442
HPHL1_HUMANHEPHL1physical
28514442
LRC15_HUMANLRRC15physical
28514442
HNRC1_HUMANHNRNPCL1physical
28514442
SEC13_HUMANSEC13physical
28514442
CRYAB_HUMANCRYABphysical
28514442
SBP1_HUMANSELENBP1physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
188550Thyroid papillary carcinoma (TPC)
604484Hereditary motor and sensory neuropathy, proximal type (HMSNP)
615658Spastic paraplegia 57, autosomal recessive (SPG57)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TFG_HUMAN

loading...

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, AND MASS SPECTROMETRY.
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-197, 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-197, AND MASSSPECTROMETRY.

TOP