ARAP1_HUMAN - dbPTM
ARAP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARAP1_HUMAN
UniProt AC Q96P48
Protein Name Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 1
Gene Name ARAP1
Organism Homo sapiens (Human).
Sequence Length 1450
Subcellular Localization Cytoplasm. Golgi apparatus, Golgi stack membrane
Peripheral membrane protein. Cell membrane. Associated with Golgi stacks in resting cells. Throughout the cytoplasm and in surface protrusion in cells that are in the process of attaching to a surface
Protein Description Phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-activating protein that modulates actin cytoskeleton remodeling by regulating ARF and RHO family members. Is activated by phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) binding. Can be activated by phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4,5)P2) binding, albeit with lower efficiency. Has a preference for ARF1 and ARF5 (By similarity)..
Protein Sequence MAEAGDAALSVAEWLRALHLEQYTGLFEQHGLVWATECQGLSDTRLMDMGMLLPGHRRRILAGLLRAHTSPAPAPRPTPRPVPMKRHIFRSPPVPATPPEPLPTTTEDEGLPAAPPIPPRRSCLPPTCFTTPSTAAPDPVLPPLPAKRHLAELSVPPVPPRTGPPRLLVSLPTKEEESLLPSLSSPPQPQSEEPLSTLPQGPPQPPSPPPCPPEIPPKPVRLFPEFDDSDYDEVPEEGPGAPARVMTKKEEPPPSRVPRAVRVASLLSEGEELSGDDQGDEEEDDHAYEGVPNGGWHTSSLSLSLPSTIAAPHPMDGPPGGSTPVTPVIKAGWLDKNPPQGSYIYQKRWVRLDTDHLRYFDSNKDAYSKRFISVACISHVAAIGDQKFEVITNNRTFAFRAESDVERKEWMQALQQAMAEQRARARLSSAYLLGVPGSEQPDRAGSLELRGFKNKLYVAVVGDKVQLYKNLEEYHLGIGITFIDMSVGNVKEVDRRSFDLTTPYRIFSFSADSELEKEQWLEAMQGAIAEALSTSEVAERIWAAAPNRFCADCGAPQPDWASINLCVVICKRCAGEHRGLGAGVSKVRSLKMDRKVWTETLIELFLQLGNGAGNRFWAANVPPSEALQPSSSPSTRRCHLEAKYREGKYRRYHPLFGNQEELDKALCAAVTTTDLAETQALLGCGAGINCFSGDPEAPTPLALAEQAGQTLQMEFLRNNRTTEVPRLDSMKPLEKHYSVVLPTVSHSGFLYKTASAGKLLQDRRAREEFSRRWCVLGDGVLSYFENERAVTPNGEIRASEIVCLAVPPPDTHGFEHTFEVYTEGERLYLFGLESAEQAHEWVKCIAKAFVPPLAEDLLARDFERLGRLPYKAGLSLQRAQEGWFSLSGSELRAVFPEGPCEEPLQLRKLQELSIQGDSENQVLVLVERRRTLYIQGERRLDFMGWLGAIQKAAASMGDTLSEQQLGDSDIPVIVYRCVDYITQCGLTSEGIYRKCGQTSKTQRLLESLRQDARSVHLKEGEQHVDDVSSALKRFLRDLPDGLFTRAQRLTWLEASEIEDEEEKVSRYRELLVRLPPVNRATVKALISHLYCVQCFSDTNQMNVHNLAIVFGPTLFQTDGQDYKAGRVVEDLINHYVVVFSVDEEELRKQREEITAIVKMRVAGTASGTQHAGDFICTVYLEEKKAETEQHIKVPASMTAEELTLEILDRRNVGIREKDYWTCFEVNEREEAERPLHFAEKVLPILHGLGTDSHLVVKKHQAMEAMLLYLASRVGDTKHGMMKFREDRSLLGLGLPSGGFHDRYFILNSSCLRLYKEVRSQRPWSGAPETSHRPEKEWPIKSLKVYLGVKKKLRPPTCWGFTVVHETEKHEKQQWYLCCDTQMELREWFATFLFVQHDGLVWPSEPSRVSRAVPEVRLGSVSLIPLRGSENEMRRSVAAFTADPLSLLRNV
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
2 (in isoform 1)Phosphorylation-27.0122617229
2 (in isoform 2)Phosphorylation-27.0122617229
4 (in isoform 1)Phosphorylation-28.3822617229
4 (in isoform 2)Phosphorylation-28.3822617229
6 (in isoform 1)Phosphorylation-35.4022617229
6 (in isoform 2)Phosphorylation-35.4022617229
15 (in isoform 1)Phosphorylation-1.4020068231
15 (in isoform 2)Phosphorylation-1.4020068231
42PhosphorylationATECQGLSDTRLMDM
EEECCCCCCCCCCHH
43.70-
44PhosphorylationECQGLSDTRLMDMGM
ECCCCCCCCCCHHHC
23.48-
69PhosphorylationAGLLRAHTSPAPAPR
HHHHHHCCCCCCCCC
35.1129496963
70PhosphorylationGLLRAHTSPAPAPRP
HHHHHCCCCCCCCCC
14.8126055452
78PhosphorylationPAPAPRPTPRPVPMK
CCCCCCCCCCCCCCC
32.9630576142
91PhosphorylationMKRHIFRSPPVPATP
CCCCCCCCCCCCCCC
23.8629255136
91UbiquitinationMKRHIFRSPPVPATP
CCCCCCCCCCCCCCC
23.8629967540
97PhosphorylationRSPPVPATPPEPLPT
CCCCCCCCCCCCCCC
33.0529255136
104PhosphorylationTPPEPLPTTTEDEGL
CCCCCCCCCCCCCCC
54.7729255136
105PhosphorylationPPEPLPTTTEDEGLP
CCCCCCCCCCCCCCC
26.6729255136
106PhosphorylationPEPLPTTTEDEGLPA
CCCCCCCCCCCCCCC
43.8729255136
119UbiquitinationPAAPPIPPRRSCLPP
CCCCCCCCCCCCCCC
45.0729967540
170PhosphorylationGPPRLLVSLPTKEEE
CCCCEEEECCCCCHH
28.7126074081
173PhosphorylationRLLVSLPTKEEESLL
CEEEECCCCCHHHCC
57.2820068231
178PhosphorylationLPTKEEESLLPSLSS
CCCCCHHHCCCCCCC
38.1926074081
182PhosphorylationEEESLLPSLSSPPQP
CHHHCCCCCCCCCCC
40.6326074081
207PhosphorylationQGPPQPPSPPPCPPE
CCCCCCCCCCCCCCC
57.6426091039
229PhosphorylationLFPEFDDSDYDEVPE
ECCCCCCCCCCCCCC
39.6623927012
229 (in isoform 6)Phosphorylation-39.6618669648
231PhosphorylationPEFDDSDYDEVPEEG
CCCCCCCCCCCCCCC
20.2523927012
231 (in isoform 6)Phosphorylation-20.2518669648
255PhosphorylationKKEEPPPSRVPRAVR
CCCCCCCCCCCHHHH
52.2423828894
265PhosphorylationPRAVRVASLLSEGEE
CHHHHHHHHHHCCCC
27.3020736484
268PhosphorylationVRVASLLSEGEELSG
HHHHHHHHCCCCCCC
49.1820736484
274PhosphorylationLSEGEELSGDDQGDE
HHCCCCCCCCCCCCC
43.38-
323PhosphorylationDGPPGGSTPVTPVIK
CCCCCCCCCCCCEEE
25.6726074081
326PhosphorylationPGGSTPVTPVIKAGW
CCCCCCCCCEEECCC
17.0326074081
336UbiquitinationIKAGWLDKNPPQGSY
EECCCCCCCCCCCCE
70.0029967540
341UbiquitinationLDKNPPQGSYIYQKR
CCCCCCCCCEEEEEE
28.3429967540
342PhosphorylationDKNPPQGSYIYQKRW
CCCCCCCCEEEEEEE
11.7819690332
343PhosphorylationKNPPQGSYIYQKRWV
CCCCCCCEEEEEEEE
15.5219690332
345PhosphorylationPPQGSYIYQKRWVRL
CCCCCEEEEEEEEEE
10.3523917254
354PhosphorylationKRWVRLDTDHLRYFD
EEEEEECCCCHHCCC
29.8822817900
359PhosphorylationLDTDHLRYFDSNKDA
ECCCCHHCCCCCCCH
20.3528270605
362PhosphorylationDHLRYFDSNKDAYSK
CCHHCCCCCCCHHCH
35.5628270605
364UbiquitinationLRYFDSNKDAYSKRF
HHCCCCCCCHHCHHH
47.9229967540
367PhosphorylationFDSNKDAYSKRFISV
CCCCCCHHCHHHHHH
25.5128270605
368PhosphorylationDSNKDAYSKRFISVA
CCCCCHHCHHHHHHH
21.0528270605
428PhosphorylationQRARARLSSAYLLGV
HHHHHHHHHHHHCCC
13.8423401153
428 (in isoform 6)Phosphorylation-13.8418669648
429PhosphorylationRARARLSSAYLLGVP
HHHHHHHHHHHCCCC
26.0621712546
429 (in isoform 6)Phosphorylation-26.0618220336
431PhosphorylationRARLSSAYLLGVPGS
HHHHHHHHHCCCCCC
12.3821712546
431 (in isoform 6)Phosphorylation-12.3818669648
438PhosphorylationYLLGVPGSEQPDRAG
HHCCCCCCCCCCCCC
27.3029978859
446PhosphorylationEQPDRAGSLELRGFK
CCCCCCCCEEECCCC
20.0624719451
446UbiquitinationEQPDRAGSLELRGFK
CCCCCCCCEEECCCC
20.0629967540
497PhosphorylationVKEVDRRSFDLTTPY
CEEECCCCCCCCCCE
24.8130108239
502PhosphorylationRRSFDLTTPYRIFSF
CCCCCCCCCEEEEEC
26.14-
504PhosphorylationSFDLTTPYRIFSFSA
CCCCCCCEEEEECCC
17.7823917254
507UbiquitinationLTTPYRIFSFSADSE
CCCCEEEEECCCCCH
4.4529967540
513PhosphorylationIFSFSADSELEKEQW
EEECCCCCHHHHHHH
43.74-
565UbiquitinationPDWASINLCVVICKR
CCHHHCEEHHHHHHH
1.9221890473
565UbiquitinationPDWASINLCVVICKR
CCHHHCEEHHHHHHH
1.9221890473
565 (in isoform 5)Ubiquitination-1.9221890473
586UbiquitinationGLGAGVSKVRSLKMD
CCCCCHHHHHHCCCC
38.9829967540
624PhosphorylationWAANVPPSEALQPSS
EECCCCHHHHCCCCC
29.4530108239
626UbiquitinationANVPPSEALQPSSSP
CCCCHHHHCCCCCCC
18.8121890473
626 (in isoform 4)Ubiquitination-18.8121890473
630PhosphorylationPSEALQPSSSPSTRR
HHHHCCCCCCCCCCC
30.4130108239
631PhosphorylationSEALQPSSSPSTRRC
HHHCCCCCCCCCCCE
53.6130108239
631 (in isoform 1)Ubiquitination-53.6121890473
631 (in isoform 2)Ubiquitination-53.6121890473
632PhosphorylationEALQPSSSPSTRRCH
HHCCCCCCCCCCCEE
27.4930108239
634PhosphorylationLQPSSSPSTRRCHLE
CCCCCCCCCCCEEEE
36.1730108239
635PhosphorylationQPSSSPSTRRCHLEA
CCCCCCCCCCEEEEH
26.0530108239
694UbiquitinationGINCFSGDPEAPTPL
CCCCCCCCCCCCCHH
36.3529967540
712UbiquitinationEQAGQTLQMEFLRNN
HHHCCCHHHHHHHCC
32.5229967540
722O-linked_GlycosylationFLRNNRTTEVPRLDS
HHHCCCCCCCCCCCC
31.5729351928
726UbiquitinationNRTTEVPRLDSMKPL
CCCCCCCCCCCCCCH
57.1929967540
729PhosphorylationTEVPRLDSMKPLEKH
CCCCCCCCCCCHHHC
33.0428857561
735PhosphorylationDSMKPLEKHYSVVLP
CCCCCHHHCCEEEEE
56.3716497976
737PhosphorylationMKPLEKHYSVVLPTV
CCCHHHCCEEEEECC
17.7721945579
738PhosphorylationKPLEKHYSVVLPTVS
CCHHHCCEEEEECCC
12.8821945579
743PhosphorylationHYSVVLPTVSHSGFL
CCEEEEECCCCCCCE
30.4021945579
745PhosphorylationSVVLPTVSHSGFLYK
EEEEECCCCCCCEEE
17.8921945579
747PhosphorylationVLPTVSHSGFLYKTA
EEECCCCCCCEEEEC
24.5921945579
751PhosphorylationVSHSGFLYKTASAGK
CCCCCCEEEECCHHH
12.2021945579
752MalonylationSHSGFLYKTASAGKL
CCCCCEEEECCHHHH
39.5026320211
752UbiquitinationSHSGFLYKTASAGKL
CCCCCEEEECCHHHH
39.5029967540
755UbiquitinationGFLYKTASAGKLLQD
CCEEEECCHHHHHHH
42.6729967540
773UbiquitinationREEFSRRWCVLGDGV
HHHHHHHEECCCCCH
3.8829967540
782PhosphorylationVLGDGVLSYFENERA
CCCCCHHHHHCCCCC
25.93-
783PhosphorylationLGDGVLSYFENERAV
CCCCHHHHHCCCCCC
15.68-
787UbiquitinationVLSYFENERAVTPNG
HHHHHCCCCCCCCCC
34.5229967540
791PhosphorylationFENERAVTPNGEIRA
HCCCCCCCCCCCEEC
15.2824719451
828PhosphorylationYTEGERLYLFGLESA
EECCCEEEEEECCCH
13.25-
871UbiquitinationRLGRLPYKAGLSLQR
HHCCCCCCCCCCCCH
33.7621890473
871 (in isoform 3)Ubiquitination-33.7621890473
871 (in isoform 6)Ubiquitination-33.7621890473
875PhosphorylationLPYKAGLSLQRAQEG
CCCCCCCCCCHHHHC
22.8724719451
956SulfoxidationIQKAAASMGDTLSEQ
HHHHHHHCCCCCCHH
4.8930846556
975PhosphorylationSDIPVIVYRCVDYIT
CCCCEEEEEHHHHHH
6.2825147952
992PhosphorylationGLTSEGIYRKCGQTS
CCCCHHHHHHHCCCH
18.1823917254
1000UbiquitinationRKCGQTSKTQRLLES
HHHCCCHHHHHHHHH
52.6529967540
1007PhosphorylationKTQRLLESLRQDARS
HHHHHHHHHHHHHHH
28.9028674151
1018UbiquitinationDARSVHLKEGEQHVD
HHHHCCCCCCCHHHH
49.1229967540
1032AcetylationDDVSSALKRFLRDLP
HHHHHHHHHHHHHCC
40.6025953088
1032MalonylationDDVSSALKRFLRDLP
HHHHHHHHHHHHHCC
40.6026320211
1032UbiquitinationDDVSSALKRFLRDLP
HHHHHHHHHHHHHCC
40.6029967540
1044PhosphorylationDLPDGLFTRAQRLTW
HCCCCCCHHHHHCEE
30.0921406692
1050PhosphorylationFTRAQRLTWLEASEI
CHHHHHCEEHHHHCC
30.1430377224
1055PhosphorylationRLTWLEASEIEDEEE
HCEEHHHHCCCCHHH
29.7230377224
1090UbiquitinationKALISHLYCVQCFSD
HHHHHHHHHHHHCCC
5.7829967540
1219PhosphorylationVGIREKDYWTCFEVN
CCCCCCCEEEEEEEC
17.43-
1268PhosphorylationAMEAMLLYLASRVGD
HHHHHHHHHHHHHCC
9.0319690332
1271PhosphorylationAMLLYLASRVGDTKH
HHHHHHHHHHCCCCC
25.5524719451
1324PhosphorylationVRSQRPWSGAPETSH
HHHCCCCCCCCCCCC
27.9724719451
1335UbiquitinationETSHRPEKEWPIKSL
CCCCCCCCCCCCCCE
68.6929967540
1419PhosphorylationVPEVRLGSVSLIPLR
CCCEECCCEEEEECC
17.0825106551
1421PhosphorylationEVRLGSVSLIPLRGS
CEECCCEEEEECCCC
23.4420873877
1426MethylationSVSLIPLRGSENEMR
CEEEEECCCCHHHHH
41.03-
1428PhosphorylationSLIPLRGSENEMRRS
EEEECCCCHHHHHHH
30.7126657352
1435PhosphorylationSENEMRRSVAAFTAD
CHHHHHHHHHHHHCC
13.0211804590
1435 (in isoform 6)Phosphorylation-13.0218669648
1440PhosphorylationRRSVAAFTADPLSLL
HHHHHHHHCCHHHHH
25.9828634120
1445PhosphorylationAFTADPLSLLRNV--
HHHCCHHHHHHCC--
30.6427251275

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
231YPhosphorylationKinasePTK6Q13882
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARAP1_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 ARAP1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
XRCC6_HUMANXRCC6physical
16169070
SH3K1_HUMANSH3KBP1physical
21275903
SHIP1_HUMANINPP5Dphysical
21275903
KCD12_HUMANKCTD12physical
21275903
PSD3_HUMANPSD3physical
21275903
TP53B_HUMANTP53BP1physical
21275903
TES_HUMANTESphysical
21275903
WAPL_HUMANWAPALphysical
21275903
A4_HUMANAPPphysical
21832049

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 ARAP1_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-342; TYR-343; SER-738;TYR-1268 AND SER-1435, 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 TYR-431 AND SER-1435, ANDMASS 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-428, AND MASSSPECTROMETRY.
"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-229; TYR-231; THR-354AND TYR-737, AND MASS SPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-737, AND MASSSPECTROMETRY.

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