FARP1_HUMAN - dbPTM
FARP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FARP1_HUMAN
UniProt AC Q9Y4F1
Protein Name FERM, ARHGEF and pleckstrin domain-containing protein 1
Gene Name FARP1
Organism Homo sapiens (Human).
Sequence Length 1045
Subcellular Localization Cell membrane
Peripheral membrane protein
Cytoplasmic side. Cell junction, synapse. Cell junction, synapse, synaptosome. Cytoplasm, cytosol. Cell projection, filopodium. Cell projection, dendrite. Cell projection, dendritic spine. Recruited to the
Protein Description Functions as guanine nucleotide exchange factor for RAC1. May play a role in semaphorin signaling. Plays a role in the assembly and disassembly of dendritic filopodia, the formation of dendritic spines, regulation of dendrite length and ultimately the formation of synapses (By similarity)..
Protein Sequence MGEIEQRPTPGSRLGAPENSGISTLERGQKPPPTPSGKLVSIKIQMLDDTQEAFEVPQRAPGKVLLDAVCNHLNLVEGDYFGLEFPDHKKITVWLDLLKPIVKQIRRPKHVVVKFVVKFFPPDHTQLQEELTRYLFALQVKQDLAQGRLTCNDTSAALLISHIVQSEIGDFDEALDREHLAKNKYIPQQDALEDKIVEFHHNHIGQTPAESDFQLLEIARRLEMYGIRLHPAKDREGTKINLAVANTGILVFQGFTKINAFNWAKVRKLSFKRKRFLIKLRPDANSAYQDTLEFLMASRDFCKSFWKICVEHHAFFRLFEEPKPKPKPVLFSRGSSFRFSGRTQKQVLDYVKEGGHKKVQFERKHSKIHSIRSLASQPTELNSEVLEQSQQSTSLTFGEGAESPGGQSCRRGKEPKVSAGEPGSHPSPAPRRSPAGNKQADGAASAPTEEEEEVVKDRTQQSKPQPPQPSTGSLTGSPHLSELSVNSQGGVAPANVTLSPNLSPDTKQASPLISPLLNDQACPRTDDEDEGRRKRFPTDKAYFIAKEVSTTERTYLKDLEVITSWFQSTVSKEDAMPEALKSLIFPNFEPLHKFHTNFLKEIEQRLALWEGRSNAQIRDYQRIGDVMLKNIQGMKHLAAHLWKHSEALEALENGIKSSRRLENFCRDFELQKVCYLPLNTFLLRPLHRLMHYKQVLERLCKHHPPSHADFRDCRAALAEITEMVAQLHGTMIKMENFQKLHELKKDLIGIDNLVVPGREFIRLGSLSKLSGKGLQQRMFFLFNDVLLYTSRGLTASNQFKVHGQLPLYGMTIEESEDEWGVPHCLTLRGQRQSIIVAASSRSEMEKWVEDIQMAIDLAEKSSSPAPEFLASSPPDNKSPDEATAADQESEDDLSASRTSLERQAPHRGNTMVHVCWHRNTSVSMVDFSIAVENQLSGNLLRKFKNSNGWQKLWVVFTNFCLFFYKSHQDNHPLASLPLLGYSLTIPSESENIQKDYVFKLHFKSHVYYFRAESEYTFERWMEVIRSATSSASRPHVLSHKESLVY
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
9PhosphorylationGEIEQRPTPGSRLGA
CCCCCCCCCCCCCCC		42.3329255136
12PhosphorylationEQRPTPGSRLGAPEN
CCCCCCCCCCCCCCC		26.0729255136
20PhosphorylationRLGAPENSGISTLER
CCCCCCCCCCCCCCC		35.5226329039
23PhosphorylationAPENSGISTLERGQK
CCCCCCCCCCCCCCC		30.3929255136
23 (in isoform 3)Phosphorylation-30.39-
24PhosphorylationPENSGISTLERGQKP
CCCCCCCCCCCCCCC		30.6229255136
24 (in isoform 2)Phosphorylation-30.6221406692
24 (in isoform 3)Phosphorylation-30.62-
30UbiquitinationSTLERGQKPPPTPSG
CCCCCCCCCCCCCCC		63.42-
34PhosphorylationRGQKPPPTPSGKLVS
CCCCCCCCCCCCEEE		35.5424732914
36PhosphorylationQKPPPTPSGKLVSIK
CCCCCCCCCCEEEEE		51.5423403867
38UbiquitinationPPPTPSGKLVSIKIQ
CCCCCCCCEEEEEEE		50.48-
63UbiquitinationVPQRAPGKVLLDAVC
CCCCCCCCHHHHHHH		28.75-
90UbiquitinationLEFPDHKKITVWLDL
CCCCCCCCEEHHHHH		39.94-
92PhosphorylationFPDHKKITVWLDLLK
CCCCCCEEHHHHHHH		17.9520068231
182UbiquitinationLDREHLAKNKYIPQQ
HCHHHHHHCCCCCHH		61.40-
184UbiquitinationREHLAKNKYIPQQDA
HHHHHHCCCCCHHHH		43.80-
211PhosphorylationIGQTPAESDFQLLEI
CCCCCCCCHHHHHHH		45.92-
270PhosphorylationWAKVRKLSFKRKRFL
HHHHEECEECCCEEE		31.5824719451
335PhosphorylationPVLFSRGSSFRFSGR
CEEEECCCCCCCCCC		25.7820068231
336PhosphorylationVLFSRGSSFRFSGRT
EEEECCCCCCCCCCC		24.2225463755
340PhosphorylationRGSSFRFSGRTQKQV
CCCCCCCCCCCHHHH		24.1025463755
350PhosphorylationTQKQVLDYVKEGGHK
CHHHHHHHHHHCCCC		14.8424173317
352UbiquitinationKQVLDYVKEGGHKKV
HHHHHHHHHCCCCEE		44.40-
366PhosphorylationVQFERKHSKIHSIRS
EEEECCHHHHHHHHH		36.0228152594
370PhosphorylationRKHSKIHSIRSLASQ
CCHHHHHHHHHHHCC		24.1428152594
373PhosphorylationSKIHSIRSLASQPTE
HHHHHHHHHHCCCCC		26.9827251275
383PhosphorylationSQPTELNSEVLEQSQ
CCCCCCCHHHHHHHH		41.5327251275
389PhosphorylationNSEVLEQSQQSTSLT
CHHHHHHHHCCCCEE		22.3227251275
392PhosphorylationVLEQSQQSTSLTFGE
HHHHHHCCCCEECCC		16.6027251275
393PhosphorylationLEQSQQSTSLTFGEG
HHHHHCCCCEECCCC		24.3427251275
394PhosphorylationEQSQQSTSLTFGEGA
HHHHCCCCEECCCCC		30.5627251275
396PhosphorylationSQQSTSLTFGEGAES
HHCCCCEECCCCCCC		29.3927251275
403PhosphorylationTFGEGAESPGGQSCR
ECCCCCCCCCCCCCC		28.4529507054
408PhosphorylationAESPGGQSCRRGKEP
CCCCCCCCCCCCCCC		16.9330278072
418PhosphorylationRGKEPKVSAGEPGSH
CCCCCCCCCCCCCCC		36.3626055452
424PhosphorylationVSAGEPGSHPSPAPR
CCCCCCCCCCCCCCC		42.8329255136
427PhosphorylationGEPGSHPSPAPRRSP
CCCCCCCCCCCCCCC		28.4229255136
427 (in isoform 2)Phosphorylation-28.4221406692
433PhosphorylationPSPAPRRSPAGNKQA
CCCCCCCCCCCCCCC		22.0025159151
433 (in isoform 2)Phosphorylation-22.0021406692
445PhosphorylationKQADGAASAPTEEEE
CCCCCCCCCCCHHHH		33.9626471730
448PhosphorylationDGAASAPTEEEEEVV
CCCCCCCCHHHHHHH		56.6027251275
456UbiquitinationEEEEEVVKDRTQQSK
HHHHHHHHHHHHCCC		46.822190698
456 (in isoform 1)Ubiquitination-46.8221906983
456 (in isoform 2)Ubiquitination-46.8221906983
470PhosphorylationKPQPPQPSTGSLTGS
CCCCCCCCCCCCCCC		39.9030175587
471PhosphorylationPQPPQPSTGSLTGSP
CCCCCCCCCCCCCCC		37.1624275569
473PhosphorylationPPQPSTGSLTGSPHL
CCCCCCCCCCCCCCH		23.8930177828
475PhosphorylationQPSTGSLTGSPHLSE
CCCCCCCCCCCCHHH		36.9930177828
477PhosphorylationSTGSLTGSPHLSELS
CCCCCCCCCCHHHEE		12.1524275569
481PhosphorylationLTGSPHLSELSVNSQ
CCCCCCHHHEEECCC		33.1924275569
484PhosphorylationSPHLSELSVNSQGGV
CCCHHHEEECCCCCC		18.3930576142
487PhosphorylationLSELSVNSQGGVAPA
HHHEEECCCCCCCCC		28.2230576142
497PhosphorylationGVAPANVTLSPNLSP
CCCCCEEEECCCCCC		22.7130177828
499PhosphorylationAPANVTLSPNLSPDT
CCCEEEECCCCCCCC		11.4629449344
503PhosphorylationVTLSPNLSPDTKQAS
EEECCCCCCCCCCCC		27.6324505115
506PhosphorylationSPNLSPDTKQASPLI
CCCCCCCCCCCCCCC		28.5629449344
510PhosphorylationSPDTKQASPLISPLL
CCCCCCCCCCCHHHC		20.1130266825
514PhosphorylationKQASPLISPLLNDQA
CCCCCCCHHHCCCCC		19.7130266825
525PhosphorylationNDQACPRTDDEDEGR
CCCCCCCCCCCCCHH		32.7026657352
572 (in isoform 2)Ubiquitination-56.10-
582PhosphorylationAMPEALKSLIFPNFE
HCHHHHHHCCCCCCH		27.7827251275
613PhosphorylationLALWEGRSNAQIRDY
HHHHCCCCCHHHCCH		47.5828857561
767PhosphorylationFIRLGSLSKLSGKGL
HHCCCCHHHHCCCCH		32.9927282143
768MalonylationIRLGSLSKLSGKGLQ
HCCCCHHHHCCCCHH		52.5526320211
768UbiquitinationIRLGSLSKLSGKGLQ
HCCCCHHHHCCCCHH		52.55-
770PhosphorylationLGSLSKLSGKGLQQR
CCCHHHHCCCCHHHH		42.0429391485
788PhosphorylationLFNDVLLYTSRGLTA
HHHHCHHHHCCCCCC		9.86-
790PhosphorylationNDVLLYTSRGLTASN
HHCHHHHCCCCCCCC		15.70-
833PhosphorylationTLRGQRQSIIVAASS
EECCCCEEEEEEECC		19.2330266825
839PhosphorylationQSIIVAASSRSEMEK
EEEEEEECCHHHHHH		19.2929759185
840PhosphorylationSIIVAASSRSEMEKW
EEEEEECCHHHHHHH		34.7922210691
861PhosphorylationAIDLAEKSSSPAPEF
HHHHHHHCCCCCCHH		27.7923911959
862PhosphorylationIDLAEKSSSPAPEFL
HHHHHHCCCCCCHHH		51.9525022875
863PhosphorylationDLAEKSSSPAPEFLA
HHHHHCCCCCCHHHH		31.9725022875
871PhosphorylationPAPEFLASSPPDNKS
CCCHHHHCCCCCCCC		45.5930266825
872PhosphorylationAPEFLASSPPDNKSP
CCHHHHCCCCCCCCH		34.5419664994
878PhosphorylationSSPPDNKSPDEATAA
CCCCCCCCHHHCCCC		43.7823403867
883PhosphorylationNKSPDEATAADQESE
CCCHHHCCCCCCCCH		21.9630278072
889PhosphorylationATAADQESEDDLSAS
CCCCCCCCHHHHHHC		40.4719664994
894PhosphorylationQESEDDLSASRTSLE
CCCHHHHHHCHHHHH		31.0622167270
896PhosphorylationSEDDLSASRTSLERQ
CHHHHHHCHHHHHHH		32.4930278072
898PhosphorylationDDLSASRTSLERQAP
HHHHHCHHHHHHHCC		34.8630278072
899PhosphorylationDLSASRTSLERQAPH
HHHHCHHHHHHHCCC		27.4230278072
903 (in isoform 2)Phosphorylation-50.2821406692
910PhosphorylationQAPHRGNTMVHVCWH
HCCCCCCEEEEEEEE		24.3228857561
920PhosphorylationHVCWHRNTSVSMVDF
EEEEECCCCCEEEEE		30.3819651622
920 (in isoform 2)Phosphorylation-30.3821406692
929 (in isoform 2)Phosphorylation-5.1321406692
930 (in isoform 2)Phosphorylation-11.0221406692
966PhosphorylationFCLFFYKSHQDNHPL
HHHHHHHHCCCCCCC		18.2720068231
975PhosphorylationQDNHPLASLPLLGYS
CCCCCCCCCCEEEEE		37.9020068231
981PhosphorylationASLPLLGYSLTIPSE
CCCCEEEEEEECCCC		10.6520068231
982PhosphorylationSLPLLGYSLTIPSES
CCCEEEEEEECCCCC		19.7620068231
984PhosphorylationPLLGYSLTIPSESEN
CEEEEEEECCCCCCC		25.5420068231
987PhosphorylationGYSLTIPSESENIQK
EEEEECCCCCCCCCC		50.3220068231
989PhosphorylationSLTIPSESENIQKDY
EEECCCCCCCCCCCE		40.0420068231
996PhosphorylationSENIQKDYVFKLHFK
CCCCCCCEEEEEEEC		18.1520068231
1004PhosphorylationVFKLHFKSHVYYFRA
EEEEEECCEEEEEEE		19.7623898821
1013PhosphorylationVYYFRAESEYTFERW
EEEEEECCCCHHHHH		34.6120068231
1026PhosphorylationRWMEVIRSATSSASR
HHHHHHHHHCCCCCC		25.4426699800
1028PhosphorylationMEVIRSATSSASRPH
HHHHHHHCCCCCCCC		25.1826699800
1029PhosphorylationEVIRSATSSASRPHV
HHHHHHCCCCCCCCC		24.5128152594
1030PhosphorylationVIRSATSSASRPHVL
HHHHHCCCCCCCCCC		26.3828152594
1032PhosphorylationRSATSSASRPHVLSH
HHHCCCCCCCCCCCC		48.5728152594
1038PhosphorylationASRPHVLSHKESLVY
CCCCCCCCCCCCCCC		31.2728152594
1042PhosphorylationHVLSHKESLVY----
CCCCCCCCCCC----		28.1228152594
1045PhosphorylationSHKESLVY-------
CCCCCCCC-------		20.3826699800
1071 (in isoform 2)Ubiquitination--
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 FARP1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FARP1_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 FARP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of FARP1_HUMAN !!
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 FARP1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND SER-872, AND MASSSPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-889; SER-896; THR-898AND SER-899, AND MASS SPECTROMETRY.
"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 THR-24; SER-336 AND SER-340,AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-24 AND SER-427, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-24, AND MASSSPECTROMETRY.

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