FER_HUMAN - dbPTM
FER_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FER_HUMAN
UniProt AC P16591
Protein Name Tyrosine-protein kinase Fer
Gene Name FER
Organism Homo sapiens (Human).
Sequence Length 822
Subcellular Localization Cytoplasm. Cytoplasm, cytoskeleton. Cell membrane
Peripheral membrane protein
Cytoplasmic side. Cell projection. Cell junction. Membrane
Peripheral membrane protein
Cytoplasmic side. Nucleus. Cytoplasm, cell cortex. Associated with the chromatin.
Protein Description Tyrosine-protein kinase that acts downstream of cell surface receptors for growth factors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, lamellipodia formation, cell adhesion, cell migration and chemotaxis. Acts downstream of EGFR, KIT, PDGFRA and PDGFRB. Acts downstream of EGFR to promote activation of NF-kappa-B and cell proliferation. May play a role in the regulation of the mitotic cell cycle. Plays a role in the insulin receptor signaling pathway and in activation of phosphatidylinositol 3-kinase. Acts downstream of the activated FCER1 receptor and plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Plays a role in the regulation of mast cell degranulation. Plays a role in leukocyte recruitment and diapedesis in response to bacterial lipopolysaccharide (LPS). Plays a role in synapse organization, trafficking of synaptic vesicles, the generation of excitatory postsynaptic currents and neuron-neuron synaptic transmission. Plays a role in neuronal cell death after brain damage. Phosphorylates CTTN, CTNND1, PTK2/FAK1, GAB1, PECAM1 and PTPN11. May phosphorylate JUP and PTPN1. Can phosphorylate STAT3, but the biological relevance of this depends on cell type and stimulus..
Protein Sequence MGFGSDLKNSHEAVLKLQDWELRLLETVKKFMALRIKSDKEYASTLQNLCNQVDKESTVQMNYVSNVSKSWLLMIQQTEQLSRIMKTHAEDLNSGPLHRLTMMIKDKQQVKKSYIGVHQQIEAEMIKVTKTELEKLKCSYRQLIKEMNSAKEKYKEALAKGKETEKAKERYDKATMKLHMLHNQYVLALKGAQLHQNQYYDITLPLLLDSLQKMQEEMIKALKGIFDEYSQITSLVTEEIVNVHKEIQMSVEQIDPSTEYNNFIDVHRTTAAKEQEIEFDTSLLEENENLQANEIMWNNLTAESLQVMLKTLAEELMQTQQMLLNKEEAVLELEKRIEESSETCEKKSDIVLLLSQKQALEELKQSVQQLRCTEAKFSAQKELLEQKVQENDGKEPPPVVNYEEDARSVTSMERKERLSKFESIRHSIAGIIRSPKSALGSSALSDMISISEKPLAEQDWYHGAIPRIEAQELLKKQGDFLVRESHGKPGEYVLSVYSDGQRRHFIIQYVDNMYRFEGTGFSNIPQLIDHHYTTKQVITKKSGVVLLNPIPKDKKWILSHEDVILGELLGKGNFGEVYKGTLKDKTSVAVKTCKEDLPQELKIKFLQEAKILKQYDHPNIVKLIGVCTQRQPVYIIMELVSGGDFLTFLRRKKDELKLKQLVKFSLDAAAGMLYLESKNCIHRDLAARNCLVGENNVLKISDFGMSRQEDGGVYSSSGLKQIPIKWTAPEALNYGRYSSESDVWSFGILLWETFSLGVCPYPGMTNQQAREQVERGYRMSAPQHCPEDISKIMMKCWDYKPENRPKFSELQKELTIIKRKLT
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
27PhosphorylationWELRLLETVKKFMAL
HHHHHHHHHHHHHHH		37.2823403867
29UbiquitinationLRLLETVKKFMALRI
HHHHHHHHHHHHHHC		47.95-
38PhosphorylationFMALRIKSDKEYAST
HHHHHCCCCHHHHHH		52.0920363803
40UbiquitinationALRIKSDKEYASTLQ
HHHCCCCHHHHHHHH		60.77-
42PhosphorylationRIKSDKEYASTLQNL
HCCCCHHHHHHHHHH		16.1620363803
44PhosphorylationKSDKEYASTLQNLCN
CCCHHHHHHHHHHHH		28.8430576142
63PhosphorylationESTVQMNYVSNVSKS
CCCCCHHHCCCCCHH		10.4230576142
65PhosphorylationTVQMNYVSNVSKSWL
CCCHHHCCCCCHHHH		22.5830576142
68PhosphorylationMNYVSNVSKSWLLMI
HHHCCCCCHHHHHHH		25.8130576142
70PhosphorylationYVSNVSKSWLLMIQQ
HCCCCCHHHHHHHHH		18.56-
101PhosphorylationSGPLHRLTMMIKDKQ
CCCHHHHEEECCCHH		12.4929083192
113PhosphorylationDKQQVKKSYIGVHQQ
CHHHHHHHHCCHHHH		19.1019835603
114PhosphorylationKQQVKKSYIGVHQQI
HHHHHHHHCCHHHHH		15.5819835603
145UbiquitinationCSYRQLIKEMNSAKE
CHHHHHHHHHHHHHH		60.55-
155UbiquitinationNSAKEKYKEALAKGK
HHHHHHHHHHHHHCC		47.80-
173AcetylationKAKERYDKATMKLHM
HHHHHHHHHHHHHHH		36.507665123
199PhosphorylationAQLHQNQYYDITLPL
CCCCCCCCCCCHHHH		15.62-
200PhosphorylationQLHQNQYYDITLPLL
CCCCCCCCCCHHHHH		7.3625159151
229PhosphorylationLKGIFDEYSQITSLV
HHHHHHHHHHHHHHH		14.0225159151
260PhosphorylationQIDPSTEYNNFIDVH
HCCCCCCCCCCEEEC		18.5927642862
311PhosphorylationSLQVMLKTLAEELMQ
HHHHHHHHHHHHHHH		27.5227251275
319PhosphorylationLAEELMQTQQMLLNK
HHHHHHHHHHHHHCH		13.5527251275
326AcetylationTQQMLLNKEEAVLEL
HHHHHHCHHHHHHHH		57.837824003
340PhosphorylationLEKRIEESSETCEKK
HHHHHHHCHHHHHHH		22.2329449344
341PhosphorylationEKRIEESSETCEKKS
HHHHHHCHHHHHHHH		39.9629449344
343PhosphorylationRIEESSETCEKKSDI
HHHHCHHHHHHHHHH		28.1029449344
347AcetylationSSETCEKKSDIVLLL
CHHHHHHHHHHHHHH		30.9430588743
364UbiquitinationKQALEELKQSVQQLR
HHHHHHHHHHHHHHH		43.75-
376UbiquitinationQLRCTEAKFSAQKEL
HHHHHHHHHHHHHHH		33.35-
381UbiquitinationEAKFSAQKELLEQKV
HHHHHHHHHHHHHHH		50.47-
394UbiquitinationKVQENDGKEPPPVVN
HHHHCCCCCCCCCCC		70.66-
401PhosphorylationKEPPPVVNYEEDARS
CCCCCCCCHHHCCCC		38.4417016520
402PhosphorylationEPPPVVNYEEDARSV
CCCCCCCHHHCCCCC		14.7521945579
408PhosphorylationNYEEDARSVTSMERK
CHHHCCCCCCCHHHH		31.3125884760
410PhosphorylationEEDARSVTSMERKER
HHCCCCCCCHHHHHH		24.4925159151
411PhosphorylationEDARSVTSMERKERL
HCCCCCCCHHHHHHH		19.2525159151
419PhosphorylationMERKERLSKFESIRH
HHHHHHHHHHHHHHH		41.3323898821
423PhosphorylationERLSKFESIRHSIAG
HHHHHHHHHHHHHHH		28.2320873877
427PhosphorylationKFESIRHSIAGIIRS
HHHHHHHHHHHHHCC		12.3220873877
434PhosphorylationSIAGIIRSPKSALGS
HHHHHHCCCCHHHCC		26.6925159151
453UbiquitinationDMISISEKPLAEQDW
HHCCCCCCCCCCCCC		38.24-
461PhosphorylationPLAEQDWYHGAIPRI
CCCCCCCCCCCCCHH		9.9225159151
475UbiquitinationIEAQELLKKQGDFLV
HHHHHHHHHHCCEEE		56.53-
476UbiquitinationEAQELLKKQGDFLVR
HHHHHHHHHCCEEEE		60.53-
492PhosphorylationSHGKPGEYVLSVYSD
CCCCCCEEEEEEEEC		16.7728152594
495PhosphorylationKPGEYVLSVYSDGQR
CCCEEEEEEEECCCE		14.6828152594
497PhosphorylationGEYVLSVYSDGQRRH
CEEEEEEEECCCEEE		9.5425884760
498PhosphorylationEYVLSVYSDGQRRHF
EEEEEEEECCCEEEE		32.8628152594
509PhosphorylationRRHFIIQYVDNMYRF
EEEEEEEECCCCCCC		10.2028450419
514PhosphorylationIQYVDNMYRFEGTGF
EEECCCCCCCCCCCC		20.5728450419
532PhosphorylationPQLIDHHYTTKQVIT
HHHHHCCCCCCEEEE		16.8228152594
533PhosphorylationQLIDHHYTTKQVITK
HHHHCCCCCCEEEEE		24.1428152594
534PhosphorylationLIDHHYTTKQVITKK
HHHCCCCCCEEEEEC		16.5928152594
552UbiquitinationVLLNPIPKDKKWILS
EEEECCCCCCCEEEC		80.87-
579UbiquitinationGNFGEVYKGTLKDKT
CCCCCEECCCCCCCC		51.07-
586PhosphorylationKGTLKDKTSVAVKTC
CCCCCCCCEEEEEEC		38.27-
587PhosphorylationGTLKDKTSVAVKTCK
CCCCCCCEEEEEECC		17.51-
591UbiquitinationDKTSVAVKTCKEDLP
CCCEEEEEECCCCCC		38.17-
592PhosphorylationKTSVAVKTCKEDLPQ
CCEEEEEECCCCCCH		23.39-
594UbiquitinationSVAVKTCKEDLPQEL
EEEEEECCCCCCHHH		60.54-
602UbiquitinationEDLPQELKIKFLQEA
CCCCHHHHHHHHHHH		43.00-
604UbiquitinationLPQELKIKFLQEAKI
CCHHHHHHHHHHHHH		38.13-
610UbiquitinationIKFLQEAKILKQYDH
HHHHHHHHHHHHCCC		48.0621890473
610UbiquitinationIKFLQEAKILKQYDH
HHHHHHHHHHHHCCC		48.0621890473
610AcetylationIKFLQEAKILKQYDH
HHHHHHHHHHHHCCC		48.0625953088
613UbiquitinationLQEAKILKQYDHPNI
HHHHHHHHHCCCCCH		50.73-
615PhosphorylationEAKILKQYDHPNIVK
HHHHHHHCCCCCHHH		18.0319159681
634PhosphorylationCTQRQPVYIIMELVS
CCCCCCEEEEEEECC		7.4524043423
641PhosphorylationYIIMELVSGGDFLTF
EEEEEECCCCCHHHH		50.0824043423
647PhosphorylationVSGGDFLTFLRRKKD
CCCCCHHHHHHHCCC		22.1824043423
699UbiquitinationVGENNVLKISDFGMS
ECCCCEEEEECCCCC		35.56-
701PhosphorylationENNVLKISDFGMSRQ
CCCEEEEECCCCCCC		25.8721945579
706PhosphorylationKISDFGMSRQEDGGV
EEECCCCCCCCCCCE		31.0621945579
714PhosphorylationRQEDGGVYSSSGLKQ
CCCCCCEECCCCCCC		13.2021945579
715PhosphorylationQEDGGVYSSSGLKQI
CCCCCEECCCCCCCC		18.6721945579
716PhosphorylationEDGGVYSSSGLKQIP
CCCCEECCCCCCCCC		15.6721945579
717PhosphorylationDGGVYSSSGLKQIPI
CCCEECCCCCCCCCC		42.0521945579
720UbiquitinationVYSSSGLKQIPIKWT
EECCCCCCCCCCEEE		50.102190698
725AcetylationGLKQIPIKWTAPEAL
CCCCCCCEEECCCHH		32.8925953088
734PhosphorylationTAPEALNYGRYSSES
ECCCHHCCCCCCCHH		12.1127273156
795UbiquitinationDISKIMMKCWDYKPE
HHHHHHHHHHCCCCC		18.13-
795AcetylationDISKIMMKCWDYKPE
HHHHHHHHHHCCCCC		18.1324179885
812UbiquitinationPKFSELQKELTIIKR
CCHHHHHHHHHHHHH		68.28-
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
615YPhosphorylationKinaseFERP16591
PSP
714YPhosphorylationKinaseFERP16591
PSP
714YPhosphorylationKinaseSRCP12931
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FER_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 FER_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TMF1_HUMANTMF1physical
9742951
CTNB1_HUMANCTNNB1physical
12640114
SRC8_HUMANCTTNphysical
9722593
DYN1_HUMANDNM1physical
9722593
DYN2_HUMANDNM2physical
9722593
DYN3_HUMANDNM3physical
9722593
FER_HUMANFERphysical
9722593
EGFR_HUMANEGFRphysical
7623846
ERBB3_HUMANERBB3physical
16273093
KCTD4_HUMANKCTD4physical
25814554
P85A_HUMANPIK3R1physical
25814554
P55G_HUMANPIK3R3physical
25814554
PP1R7_HUMANPPP1R7physical
25814554
CRK_HUMANCRKphysical
25814554
FER_HUMANFERphysical
26702831
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 FER_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-402; THR-410; SER-411;SER-434 AND TYR-714, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-402; SER-411; SER-434AND TYR-714, AND MASS SPECTROMETRY.
"Proteomics analysis of protein kinases by target class-selectiveprefractionation and tandem mass spectrometry.";
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,Keri G., Wehland J., Daub H.;
Mol. Cell. Proteomics 6:537-547(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-402; SER-434 ANDTYR-714, AND MASS SPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-402, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-402 AND TYR-714, ANDMASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory