AFAP1_HUMAN - dbPTM
AFAP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AFAP1_HUMAN
UniProt AC Q8N556
Protein Name Actin filament-associated protein 1
Gene Name AFAP1
Organism Homo sapiens (Human).
Sequence Length 730
Subcellular Localization Cytoplasm, cytoskeleton . Localizes with stress fibers in quiescent cells, concentrated in cell motility structures such as lamellipodia, filopodia and membrane ruffles upon their induction.
Protein Description Can cross-link actin filaments into both network and bundle structures (By similarity). May modulate changes in actin filament integrity and induce lamellipodia formation. May function as an adapter molecule that links other proteins, such as SRC and PKC to the actin cytoskeleton. Seems to play a role in the development and progression of prostate adenocarcinoma by regulating cell-matrix adhesions and migration in the cancer cells..
Protein Sequence MEELIVELRLFLELLDHEYLTSTVREKKAVITNILLRIQSSKGFDVKDHAQKQETANSLPAPPQMPLPEIPQPWLPPDSGPPPLPTSSLPEGYYEEAVPLSPGKAPEYITSNYDSDAMSSSYESYDEEEEDGKGKKTRHQWPSEEASMDLVKDAKICAFLLRKKRFGQWTKLLCVIKDTKLLCYKSSKDQQPQMELPLQGCNITYIPKDSKKKKHELKITQQGTDPLVLAVQSKEQAEQWLKVIKEAYSGCSGPVDSECPPPPSSPVHKAELEKKLSSERPSSDGEGVVENGITTCNGKEQVKRKKSSKSEAKGTVSKVTGKKITKIISLGKKKPSTDEQTSSAEEDVPTCGYLNVLSNSRWRERWCRVKDNKLIFHKDRTDLKTHIVSIPLRGCEVIPGLDSKHPLTFRLLRNGQEVAVLEASSSEDMGRWIGILLAETGSSTDPEALHYDYIDVEMSASVIQTAKQTFCFMNRRVISANPYLGGTSNGYAHPSGTALHYDDVPCINGSLKGKKPPVASNGVTGKGKTLSSQPKKADPAAVVKRTGSNAAQYKYGKNRVEADAKRLQTKEEELLKRKEALRNRLAQLRKERKDLRAAIEVNAGRKPQAILEEKLKQLEEECRQKEAERVSLELELTEVKESLKKALAGGVTLGLAIEPKSGTSSPQSPVFRHRTLENSPISSCDTSDTEGPVPVNSAAVLKKSQAAPGSSPCRGHVLRKAKEWELKNGT
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-------MEELIVEL
-------CHHHHHHH
9.0122814378
19PhosphorylationLELLDHEYLTSTVRE
HHHHCHHHHHCHHHH
16.3268854629
42UbiquitinationLLRIQSSKGFDVKDH
HHHHHHCCCCCCCHH
69.69-
47UbiquitinationSSKGFDVKDHAQKQE
HCCCCCCCHHHHHHH
45.71-
93PhosphorylationTSSLPEGYYEEAVPL
CCCCCCCCCCCCCCC
13.179655255
94PhosphorylationSSLPEGYYEEAVPLS
CCCCCCCCCCCCCCC
20.399655255
101PhosphorylationYEEAVPLSPGKAPEY
CCCCCCCCCCCCCCH
26.0780868205
119PhosphorylationNYDSDAMSSSYESYD
CCCCCCCCCCCCCCC
20.1827251275
120PhosphorylationYDSDAMSSSYESYDE
CCCCCCCCCCCCCCC
24.6927251275
121PhosphorylationDSDAMSSSYESYDEE
CCCCCCCCCCCCCCC
26.1327251275
122PhosphorylationSDAMSSSYESYDEEE
CCCCCCCCCCCCCCC
15.7327251275
124PhosphorylationAMSSSYESYDEEEED
CCCCCCCCCCCCCCC
29.6527251275
125PhosphorylationMSSSYESYDEEEEDG
CCCCCCCCCCCCCCC
18.559655255
147PhosphorylationQWPSEEASMDLVKDA
CCCCHHHCCHHHHHH
18.9928387310
155AcetylationMDLVKDAKICAFLLR
CHHHHHHHHHHHHHH
48.7526051181
171AcetylationKRFGQWTKLLCVIKD
HHHCCCEEEEEEEEC
36.1826051181
177AcetylationTKLLCVIKDTKLLCY
EEEEEEEECCEEEEE
38.6626051181
180AcetylationLCVIKDTKLLCYKSS
EEEEECCEEEEEECC
49.9826051181
208AcetylationCNITYIPKDSKKKKH
CCEEEECCCCCCCCC
66.1434677437
212AcetylationYIPKDSKKKKHELKI
EECCCCCCCCCEEEE
71.6334677445
220PhosphorylationKKHELKITQQGTDPL
CCCEEEEEECCCCCE
17.1620068231
224PhosphorylationLKITQQGTDPLVLAV
EEEEECCCCCEEEEE
30.0620068231
233PhosphorylationPLVLAVQSKEQAEQW
CEEEEECCHHHHHHH
31.4020068231
234UbiquitinationLVLAVQSKEQAEQWL
EEEEECCHHHHHHHH
36.43-
242AcetylationEQAEQWLKVIKEAYS
HHHHHHHHHHHHHHC
38.6726051181
242UbiquitinationEQAEQWLKVIKEAYS
HHHHHHHHHHHHHHC
38.67-
248PhosphorylationLKVIKEAYSGCSGPV
HHHHHHHHCCCCCCC
13.4924732914
249PhosphorylationKVIKEAYSGCSGPVD
HHHHHHHCCCCCCCC
40.1324732914
252PhosphorylationKEAYSGCSGPVDSEC
HHHHCCCCCCCCCCC
50.0524732914
257PhosphorylationGCSGPVDSECPPPPS
CCCCCCCCCCCCCCC
41.1323927012
264PhosphorylationSECPPPPSSPVHKAE
CCCCCCCCCCCCHHH
53.7122167270
265PhosphorylationECPPPPSSPVHKAEL
CCCCCCCCCCCHHHH
36.3922167270
277PhosphorylationAELEKKLSSERPSSD
HHHHHHHCCCCCCCC
38.7529255136
278PhosphorylationELEKKLSSERPSSDG
HHHHHHCCCCCCCCC
48.3230266825
282PhosphorylationKLSSERPSSDGEGVV
HHCCCCCCCCCCCCC
47.4829255136
283PhosphorylationLSSERPSSDGEGVVE
HCCCCCCCCCCCCCC
52.9329255136
294PhosphorylationGVVENGITTCNGKEQ
CCCCCCCEECCCHHH
27.0523403867
295PhosphorylationVVENGITTCNGKEQV
CCCCCCEECCCHHHH
11.3123403867
307PhosphorylationEQVKRKKSSKSEAKG
HHHHCCCCCCCCCCC
46.1426074081
308PhosphorylationQVKRKKSSKSEAKGT
HHHCCCCCCCCCCCC
49.4326074081
310PhosphorylationKRKKSSKSEAKGTVS
HCCCCCCCCCCCCEE
44.7426074081
315PhosphorylationSKSEAKGTVSKVTGK
CCCCCCCCEEEHHCC
22.3930576142
317PhosphorylationSEAKGTVSKVTGKKI
CCCCCCEEEHHCCCH
22.6526074081
320PhosphorylationKGTVSKVTGKKITKI
CCCEEEHHCCCHHEE
47.2026074081
329PhosphorylationKKITKIISLGKKKPS
CCHHEEEECCCCCCC
34.2420860994
336PhosphorylationSLGKKKPSTDEQTSS
ECCCCCCCCCCCCCC
58.3225463755
337PhosphorylationLGKKKPSTDEQTSSA
CCCCCCCCCCCCCCC
52.6725463755
341PhosphorylationKPSTDEQTSSAEEDV
CCCCCCCCCCCHHCC
23.7023927012
342PhosphorylationPSTDEQTSSAEEDVP
CCCCCCCCCCHHCCC
27.5225463755
343PhosphorylationSTDEQTSSAEEDVPT
CCCCCCCCCHHCCCC
42.9925463755
350PhosphorylationSAEEDVPTCGYLNVL
CCHHCCCCCCHHHHH
20.5741242819
353PhosphorylationEDVPTCGYLNVLSNS
HCCCCCCHHHHHCCC
9.3923927012
358PhosphorylationCGYLNVLSNSRWRER
CCHHHHHCCCCHHHH
28.6024732914
360PhosphorylationYLNVLSNSRWRERWC
HHHHHCCCCHHHHEE
29.8224732914
373UbiquitinationWCRVKDNKLIFHKDR
EEEEECCEEEEECCC
53.76-
378MalonylationDNKLIFHKDRTDLKT
CCEEEEECCCCCCCC
37.8526320211
378UbiquitinationDNKLIFHKDRTDLKT
CCEEEEECCCCCCCC
37.85-
384UbiquitinationHKDRTDLKTHIVSIP
ECCCCCCCCCEEEEE
40.65-
389PhosphorylationDLKTHIVSIPLRGCE
CCCCCEEEEECCCCE
20.2024719451
424PhosphorylationEVAVLEASSSEDMGR
EEEEEEECCCCHHHH
25.6427732954
425PhosphorylationVAVLEASSSEDMGRW
EEEEEECCCCHHHHH
44.8127732954
426PhosphorylationAVLEASSSEDMGRWI
EEEEECCCCHHHHHH
34.8127732954
451PhosphorylationTDPEALHYDYIDVEM
CCHHHHCCCEEEHHH
15.99131049
453PhosphorylationPEALHYDYIDVEMSA
HHHHCCCEEEHHHCH
7.589655255
483PhosphorylationRVISANPYLGGTSNG
EEEECCCCCCCCCCC
20.1326356563
487PhosphorylationANPYLGGTSNGYAHP
CCCCCCCCCCCCCCC
19.7426356563
488PhosphorylationNPYLGGTSNGYAHPS
CCCCCCCCCCCCCCC
31.3726356563
491PhosphorylationLGGTSNGYAHPSGTA
CCCCCCCCCCCCCCC
13.14119545
495PhosphorylationSNGYAHPSGTALHYD
CCCCCCCCCCCCCCC
38.6226356563
497PhosphorylationGYAHPSGTALHYDDV
CCCCCCCCCCCCCCC
30.3126356563
501PhosphorylationPSGTALHYDDVPCIN
CCCCCCCCCCCCCCC
18.0626356563
510PhosphorylationDVPCINGSLKGKKPP
CCCCCCCCCCCCCCC
23.5526356563
512AcetylationPCINGSLKGKKPPVA
CCCCCCCCCCCCCCC
71.0826051181
520PhosphorylationGKKPPVASNGVTGKG
CCCCCCCCCCCCCCC
34.0646160037
524PhosphorylationPVASNGVTGKGKTLS
CCCCCCCCCCCCCCC
34.2872840035
528UbiquitinationNGVTGKGKTLSSQPK
CCCCCCCCCCCCCCC
50.18-
529PhosphorylationGVTGKGKTLSSQPKK
CCCCCCCCCCCCCCC
40.3123403867
531PhosphorylationTGKGKTLSSQPKKAD
CCCCCCCCCCCCCCC
31.9623403867
532PhosphorylationGKGKTLSSQPKKADP
CCCCCCCCCCCCCCH
54.3223403867
537PhosphorylationLSSQPKKADPAAVVK
CCCCCCCCCHHHHEE
33.86-
537 (in isoform 2)Phosphorylation-33.8625884760
546PhosphorylationPAAVVKRTGSNAAQY
HHHHEECCCCCHHHH
38.9625159151
548PhosphorylationAVVKRTGSNAAQYKY
HHEECCCCCHHHHHH
23.7628355574
553PhosphorylationTGSNAAQYKYGKNRV
CCCCHHHHHHCCCHH
11.0530835073
554UbiquitinationGSNAAQYKYGKNRVE
CCCHHHHHHCCCHHH
35.13-
555PhosphorylationSNAAQYKYGKNRVEA
CCHHHHHHCCCHHHH
28.5323312004
570UbiquitinationDAKRLQTKEEELLKR
HHHHHHHHHHHHHHH
50.60-
606UbiquitinationIEVNAGRKPQAILEE
HHHCCCCCHHHHHHH
40.33-
614UbiquitinationPQAILEEKLKQLEEE
HHHHHHHHHHHHHHH
52.16-
631PhosphorylationQKEAERVSLELELTE
HHHHHHHHHHEEHHH
23.5046160043
632PhosphorylationKEAERVSLELELTEV
HHHHHHHHHEEHHHH
8.7824719451
637PhosphorylationVSLELELTEVKESLK
HHHHEEHHHHHHHHH
29.3846160055
652PhosphorylationKALAGGVTLGLAIEP
HHHHCCCEEEEEECC
20.5522964224
661PhosphorylationGLAIEPKSGTSSPQS
EEEECCCCCCCCCCC
59.0022167270
663PhosphorylationAIEPKSGTSSPQSPV
EECCCCCCCCCCCCE
32.8722167270
664PhosphorylationIEPKSGTSSPQSPVF
ECCCCCCCCCCCCEE
43.4722167270
665PhosphorylationEPKSGTSSPQSPVFR
CCCCCCCCCCCCEEC
27.1422167270
668PhosphorylationSGTSSPQSPVFRHRT
CCCCCCCCCEECCCC
26.8119664994
675PhosphorylationSPVFRHRTLENSPIS
CCEECCCCCCCCCCC
32.099497717
679PhosphorylationRHRTLENSPISSCDT
CCCCCCCCCCCCCCC
17.7823927012
682PhosphorylationTLENSPISSCDTSDT
CCCCCCCCCCCCCCC
28.4425159151
683PhosphorylationLENSPISSCDTSDTE
CCCCCCCCCCCCCCC
19.4123927012
686PhosphorylationSPISSCDTSDTEGPV
CCCCCCCCCCCCCCC
32.5930278072
687PhosphorylationPISSCDTSDTEGPVP
CCCCCCCCCCCCCCC
29.3230278072
689PhosphorylationSSCDTSDTEGPVPVN
CCCCCCCCCCCCCCC
42.4830278072
697PhosphorylationEGPVPVNSAAVLKKS
CCCCCCCHHHHHHHH
20.1723403867
704PhosphorylationSAAVLKKSQAAPGSS
HHHHHHHHHCCCCCC
24.3824732914
710PhosphorylationKSQAAPGSSPCRGHV
HHHCCCCCCCCCHHH
30.0125159151
711PhosphorylationSQAAPGSSPCRGHVL
HHCCCCCCCCCHHHH
33.6525159151
730PhosphorylationEWELKNGT-------
HHHCCCCC-------
44.8421712546
748Phosphorylation-------------------------
-------------------------
24719451
749Phosphorylation--------------------------
--------------------------
24719451
752Phosphorylation-----------------------------
-----------------------------
24719451
763Phosphorylation----------------------------------------
----------------------------------------
24719451
766Phosphorylation-------------------------------------------
-------------------------------------------
27251275
770Phosphorylation-----------------------------------------------
-----------------------------------------------
24719451
771Phosphorylation------------------------------------------------
------------------------------------------------
27251275
794Phosphorylation-----------------------------------------------------------------------
-----------------------------------------------------------------------
24719451
795Phosphorylation------------------------------------------------------------------------
------------------------------------------------------------------------
27251275

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
93YPhosphorylationKinaseSRCP12931
PSP
94YPhosphorylationKinaseSRCP12931
PSP
125YPhosphorylationKinaseSRCP12931
PSP
277SPhosphorylationKinasePRKCAP17252
GPS
451YPhosphorylationKinaseSRCP12931
PSP
453YPhosphorylationKinaseSRCP12931
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AFAP1_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 AFAP1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AFAP1_HUMANAFAP1physical
9619827
ACTC_HUMANACTC1physical
12134071
KPCB_HUMANPRKCBphysical
12134071
KPCE_HUMANPRKCEphysical
12134071
KPCG_HUMANPRKCGphysical
12134071
KPCD_HUMANPRKCDphysical
12134071
KPCA_HUMANPRKCAphysical
12134071

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 AFAP1_HUMAN

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Related Literatures of Post-Translational Modification
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-668, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664; SER-668 ANDSER-687, 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-277; SER-278; SER-282;SER-283; THR-663; SER-664; SER-665; SER-668; SER-679; THR-686 ANDSER-687, 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 SER-668, AND MASSSPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-665 AND SER-668, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282; SER-336; THR-337;THR-341; SER-342 AND SER-343, AND MASS SPECTROMETRY.

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