FARP2_HUMAN - dbPTM
FARP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FARP2_HUMAN
UniProt AC O94887
Protein Name FERM, ARHGEF and pleckstrin domain-containing protein 2
Gene Name FARP2
Organism Homo sapiens (Human).
Sequence Length 1054
Subcellular Localization
Protein Description Functions as guanine nucleotide exchange factor that activates RAC1. May have relatively low activity. Plays a role in the response to class 3 semaphorins and remodeling of the actin cytoskeleton. Plays a role in TNFSF11-mediated osteoclast differentiation, especially in podosome rearrangement and reorganization of the actin cytoskeleton. Regulates the activation of ITGB3, integrin signaling and cell adhesion (By similarity)..
Protein Sequence MGEIEGTYRVLQTAGMRLGAQTPVGVSTLEPGQTLLPRMQEKHLHLRVKLLDNTMEIFDIEPKCDGQVLLTQVWKRLNLVECDYFGMEFQNTQSYWIWLEPMKPIIRQIRRPKNVVLRLAVKFFPPDPGQLQEEYTRYLFALQLKRDLLEERLTCADTTAALLTSHLLQSEIGDYDETLDREHLKVNEYLPGQQHCLEKILEFHQKHVGQTPAESDFQVLEIARKLEMYGIRFHMASDREGTKIQLAVSHMGVLVFQGTTKINTFNWSKVRKLSFKRKRFLIKLHPEVHGPYQDTLEFLLGSRDECKNFWKICVEYHTFFRLLDQPKPKAKAVFFSRGSSFRYSGRTQKQLVDYFKDSGMKRIPYERRHSKTHTSVRALTADLPKQSISFPEGLRTPASPSSANAFYSLSPSTLVPSGLPEFKDSSSSLTDPQVSYVKSPAAERRSGAVAGGPDTPSAQPLGPPALQPGPGLSTKSPQPSPSSRKSPLSLSPAFQVPLGPAEQGSSPLLSPVLSDAGGAGMDCEEPRHKRVPADEAYFIVKEILATERTYLKDLEVITVWFRSAVVKEDAMPATLMTLLFSNIDPIYEFHRGFLREVEQRLALWEGPSKAHTKGSHQRIGDILLRNMRQLKEFTSYFQRHDEVLTELEKATKRCKKLEAVYKEFELQKVCYLPLNTFLLKPIQRLLHYRLLLRRLCGHYSPGHHDYADCHDALKAITEVTTTLQHILIRLENLQKLTELQRDLVGIENLIAPGREFIREGCLHKLTKKGLQQRMFFLFSDMLLYTSKGVAGTSHFRIRGLLPLQGMLVEESDNEWSVPHCFTIYAAQKTIVVAASTRLEKEKWMLDLNSAIQAAKSGGDTAPALPGRTVCTRPPRSPNEVSLEQESEDDARGVRSSLEGHGQHRANTTMHVCWYRNTSVSRADHSAAVENQLSGYLLRKFKNSHGWQKLWVVFTNFCLFFYKTHQDDYPLASLPLLGYSVSIPREADGIHKDYVFKLQFKSHVYFFRAESKYTFERWMEVIQGASSSAGRAPSIVQDGPQPSSGLEGMVRGKEE
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
8PhosphorylationMGEIEGTYRVLQTAG
CCCCCHHHHHHHCCC
15.0225159151
22PhosphorylationGMRLGAQTPVGVSTL
CCCCCCCCCCCCCCC
21.2929255136
27PhosphorylationAQTPVGVSTLEPGQT
CCCCCCCCCCCCCCC
22.7329255136
28PhosphorylationQTPVGVSTLEPGQTL
CCCCCCCCCCCCCCC
32.5029255136
34PhosphorylationSTLEPGQTLLPRMQE
CCCCCCCCCHHHHHH
35.8627732954
49UbiquitinationKHLHLRVKLLDNTME
HCCHHEEECCCCCEE
36.58-
104UbiquitinationIWLEPMKPIIRQIRR
EEEEECHHHHHHHCC
22.4627667366
145UbiquitinationYLFALQLKRDLLEER
HHHHHHHHHHHHHHH
30.7929967540
145UbiquitinationYLFALQLKRDLLEER
HHHHHHHHHHHHHHH
30.79-
185UbiquitinationTLDREHLKVNEYLPG
HCCHHHCCHHHCCCC
44.9429967540
199UbiquitinationGQQHCLEKILEFHQK
CHHHHHHHHHHHHHH
39.3829967540
206UbiquitinationKILEFHQKHVGQTPA
HHHHHHHHHCCCCCC
31.5229967540
229PhosphorylationIARKLEMYGIRFHMA
HHHHHHHHCCEEEEC
10.4628555341
245UbiquitinationDREGTKIQLAVSHMG
CCCCCEEEEEECCCC
25.5627667366
274PhosphorylationWSKVRKLSFKRKRFL
HHHHEEEECCCCEEE
31.5824719451
282UbiquitinationFKRKRFLIKLHPEVH
CCCCEEEEECCCCCC
4.0327667366
331UbiquitinationDQPKPKAKAVFFSRG
CCCCCCCEEEEEECC
51.7327667366
331UbiquitinationDQPKPKAKAVFFSRG
CCCCCCCEEEEEECC
51.73-
336PhosphorylationKAKAVFFSRGSSFRY
CCEEEEEECCCCCCC
25.0221712546
337MethylationAKAVFFSRGSSFRYS
CEEEEEECCCCCCCC
43.80-
339PhosphorylationAVFFSRGSSFRYSGR
EEEEECCCCCCCCCC
25.7823403867
340PhosphorylationVFFSRGSSFRYSGRT
EEEECCCCCCCCCCC
19.3022617229
342MethylationFSRGSSFRYSGRTQK
EECCCCCCCCCCCHH
27.01-
343PhosphorylationSRGSSFRYSGRTQKQ
ECCCCCCCCCCCHHH
17.2923403867
344PhosphorylationRGSSFRYSGRTQKQL
CCCCCCCCCCCHHHH
19.9728355574
347PhosphorylationSFRYSGRTQKQLVDY
CCCCCCCCHHHHHHH
43.5828102081
349UbiquitinationRYSGRTQKQLVDYFK
CCCCCCHHHHHHHHH
45.01-
349UbiquitinationRYSGRTQKQLVDYFK
CCCCCCHHHHHHHHH
45.01-
354PhosphorylationTQKQLVDYFKDSGMK
CHHHHHHHHHHCCCC
12.6827642862
356UbiquitinationKQLVDYFKDSGMKRI
HHHHHHHHHCCCCCC
44.76-
356UbiquitinationKQLVDYFKDSGMKRI
HHHHHHHHHCCCCCC
44.76-
358PhosphorylationLVDYFKDSGMKRIPY
HHHHHHHCCCCCCCC
41.1825159151
365PhosphorylationSGMKRIPYERRHSKT
CCCCCCCCHHCCCCC
21.5022817900
370PhosphorylationIPYERRHSKTHTSVR
CCCHHCCCCCCCHHH
37.1233259812
375PhosphorylationRHSKTHTSVRALTAD
CCCCCCCHHHHHHCC
11.2925627689
380PhosphorylationHTSVRALTADLPKQS
CCHHHHHHCCCCCCC
19.6928348404
385UbiquitinationALTADLPKQSISFPE
HHHCCCCCCCCCCCC
65.072190698
385 (in isoform 2)Ubiquitination-65.0721906983
385 (in isoform 1)Ubiquitination-65.0721906983
385UbiquitinationALTADLPKQSISFPE
HHHCCCCCCCCCCCC
65.0721906983
387PhosphorylationTADLPKQSISFPEGL
HCCCCCCCCCCCCCC
26.7325106551
389PhosphorylationDLPKQSISFPEGLRT
CCCCCCCCCCCCCCC
39.7428348404
396PhosphorylationSFPEGLRTPASPSSA
CCCCCCCCCCCCCCC
28.4025850435
399PhosphorylationEGLRTPASPSSANAF
CCCCCCCCCCCCCCC
26.9021712546
401PhosphorylationLRTPASPSSANAFYS
CCCCCCCCCCCCCCC
39.3221712546
402PhosphorylationRTPASPSSANAFYSL
CCCCCCCCCCCCCCC
29.0021712546
407PhosphorylationPSSANAFYSLSPSTL
CCCCCCCCCCCHHHC
13.2921712546
408PhosphorylationSSANAFYSLSPSTLV
CCCCCCCCCCHHHCC
18.8725106551
410PhosphorylationANAFYSLSPSTLVPS
CCCCCCCCHHHCCCC
15.7426657352
412PhosphorylationAFYSLSPSTLVPSGL
CCCCCCHHHCCCCCC
30.8823186163
413PhosphorylationFYSLSPSTLVPSGLP
CCCCCHHHCCCCCCC
34.8521712546
425PhosphorylationGLPEFKDSSSSLTDP
CCCCCCCCCCCCCCC
32.4821945579
426PhosphorylationLPEFKDSSSSLTDPQ
CCCCCCCCCCCCCCC
33.8021945579
427PhosphorylationPEFKDSSSSLTDPQV
CCCCCCCCCCCCCCH
33.0621945579
428PhosphorylationEFKDSSSSLTDPQVS
CCCCCCCCCCCCCHH
36.9221945579
430PhosphorylationKDSSSSLTDPQVSYV
CCCCCCCCCCCHHEE
47.8121945579
435PhosphorylationSLTDPQVSYVKSPAA
CCCCCCHHEECCCHH
20.9721945579
436PhosphorylationLTDPQVSYVKSPAAE
CCCCCHHEECCCHHH
17.0321945579
438UbiquitinationDPQVSYVKSPAAERR
CCCHHEECCCHHHHC
42.3529967540
439PhosphorylationPQVSYVKSPAAERRS
CCHHEECCCHHHHCC
15.1029255136
446PhosphorylationSPAAERRSGAVAGGP
CCHHHHCCCCCCCCC
37.0127251789
455PhosphorylationAVAGGPDTPSAQPLG
CCCCCCCCCCCCCCC
23.4426657352
457PhosphorylationAGGPDTPSAQPLGPP
CCCCCCCCCCCCCCC
41.4523312004
473PhosphorylationLQPGPGLSTKSPQPS
CCCCCCCCCCCCCCC
39.4427251789
474PhosphorylationQPGPGLSTKSPQPSP
CCCCCCCCCCCCCCC
40.3523312004
476PhosphorylationGPGLSTKSPQPSPSS
CCCCCCCCCCCCCCC
28.9327422710
480PhosphorylationSTKSPQPSPSSRKSP
CCCCCCCCCCCCCCC
31.9727251789
482PhosphorylationKSPQPSPSSRKSPLS
CCCCCCCCCCCCCCC
47.3027251789
483PhosphorylationSPQPSPSSRKSPLSL
CCCCCCCCCCCCCCC
47.3025072903
537PhosphorylationRVPADEAYFIVKEIL
CCCHHHHHHHHHHHH
7.56-
574PhosphorylationKEDAMPATLMTLLFS
CCCCCCHHHHHHHHC
15.93-
577PhosphorylationAMPATLMTLLFSNID
CCCHHHHHHHHCCCH
24.34-
581PhosphorylationTLMTLLFSNIDPIYE
HHHHHHHCCCHHHHH
32.61-
645PhosphorylationQRHDEVLTELEKATK
HHHHHHHHHHHHHHH
43.64-
792PhosphorylationTSKGVAGTSHFRIRG
HCCCCCCCCCCEECC
14.8622468782
793PhosphorylationSKGVAGTSHFRIRGL
CCCCCCCCCCEECCE
21.5122468782
835PhosphorylationKTIVVAASTRLEKEK
EEEEEEECCCHHHHH
12.3429449344
836PhosphorylationTIVVAASTRLEKEKW
EEEEEECCCHHHHHH
34.2527251789
868PhosphorylationAPALPGRTVCTRPPR
CCCCCCCEEECCCCC
26.3328348404
871PhosphorylationLPGRTVCTRPPRSPN
CCCCEEECCCCCCCC
41.7026657352
876PhosphorylationVCTRPPRSPNEVSLE
EECCCCCCCCCCCCC
37.5423927012
881PhosphorylationPRSPNEVSLEQESED
CCCCCCCCCCCCCCC
21.7323927012
886PhosphorylationEVSLEQESEDDARGV
CCCCCCCCCCCHHHH
46.1223927012
895PhosphorylationDDARGVRSSLEGHGQ
CCHHHHHHHHCCCCC
36.5524719451
896PhosphorylationDARGVRSSLEGHGQH
CHHHHHHHHCCCCCC
21.6327251275
907PhosphorylationHGQHRANTTMHVCWY
CCCCCCCCEEEEEEE
25.22-
908PhosphorylationGQHRANTTMHVCWYR
CCCCCCCEEEEEEEC
12.70-
914PhosphorylationTTMHVCWYRNTSVSR
CEEEEEEECCCCCCC
6.72-
981PhosphorylationPLLGYSVSIPREADG
CCCCEEEECCCCCCC
22.4224719451
1033PhosphorylationSSAGRAPSIVQDGPQ
CCCCCCCCHHCCCCC
34.1128857561
1042PhosphorylationVQDGPQPSSGLEGMV
HCCCCCCCCCCCCCC
31.6130624053
1043PhosphorylationQDGPQPSSGLEGMVR
CCCCCCCCCCCCCCC
54.8230624053

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 FARP2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FARP2_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 FARP2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UB2G2_HUMANUBE2G2physical
21988832
RS27A_HUMANRPS27Aphysical
28514442
TRI41_HUMANTRIM41physical
28514442
ICLN_HUMANCLNS1Aphysical
28514442
ANM5_HUMANPRMT5physical
28514442
RIOK1_HUMANRIOK1physical
28514442
COPRS_HUMANCOPRSphysical
28514442
KPCI_HUMANPRKCIphysical
28514442
GRDN_HUMANCCDC88Aphysical
28514442
NCBP3_HUMANC17orf85physical
28514442
HERC2_HUMANHERC2physical
28514442

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 FARP2_HUMAN

loading...

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-428; THR-430 ANDSER-886, 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 SER-439, AND MASSSPECTROMETRY.

TOP