ARAP2_HUMAN - dbPTM
ARAP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARAP2_HUMAN
UniProt AC Q8WZ64
Protein Name Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 2
Gene Name ARAP2
Organism Homo sapiens (Human).
Sequence Length 1704
Subcellular Localization Cytoplasm.
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 (By similarity)..
Protein Sequence MSSVSEVNVDIKDFLMSINLEQYLLHFHESGFTTVKDCAAINDSLLQKIGISPTGHRRRILKQLQIILSKMQDIPIYANVHKTKKNDDPSKDYHVPSSDQNICIELSNSGSVQTSSPPQLETVRKNLEDSDASVERSQYPQSDDKLSPPKRDFPTAEEPHLNLGSLNDSLFGSDNIKIESLITKKTVDHTVEEQQTEKVKLITENLSKLPNADSECLSFVGCSTSGTNSGNGTNGLLEGSPPSPFFKFQGEMIVNDLYVPSSPILAPVRSRSKLVSRPSRSFLLRHRPVPEIPGSTKGVSGSYFRERRNVATSTEKSVAWQNSNEENSSSIFPYGETFLFQRLENSKKRSIKNEFLTQGEALKGEAATATNSFIIKSSIYDNRKEKISEDKVEDIWIPREDKNNFLIDTASESEYSTVEECFQSLRRKNSKASKSRTQKALILDSVNRHSYPLSSTSGNADSSAVSSQAISPYACFYGASAKKVKSGWLDKLSPQGKRMFQKRWVKFDGLSISYYNNEKEMYSKGIIPLSAISTVRVQGDNKFEVVTTQRTFVFRVEKEEERNDWISILLNALKSQSLTSQSQAVVTPEKCGYLELRGYKAKIFTVLSGNSVWLCKNEQDFKSGLGITIIPMNVANVKQVDRTVKQSFEIITPYRSFSFTAETEKEKQDWIEAVQQSIAETLSDYEVAEKIWFNESNRSCADCKAPDPDWASINLCVVICKKCAGQHRSLGPKDSKVRSLKMDASIWSNELIELFIVIGNKRANDFWAGNLQKDEELHMDSPVEKRKNFITQKYKEGKFRKTLLASLTKEELNKALCAAVVKPDVLETMALLFSGADVMCATGDPVHSTPYLLAKKAGQSLQMEFLYHNKFSDFPQHDIHSEGVLSQESSQSTFLCDFLYQAPSAASKLSSEKKLLEETNKKWCVLEGGFLSYYENDKSTTPNGTININEVICLAIHKEDFYLNTGPIFIFEIYLPSERVFLFGAETSQAQRKWTEAIAKHFVPLFAENLTEADYDLIGQLFYKDCHALDQWRKGWFAMDKSSLHFCLQMQEVQGDRMHLRRLQELTISTMVQNGEKLDVLLLVEKGRTLYIHGHTKLDFTVWHTAIEKAAGTDGNALQDQQLSKNDVPIIVNSCIAFVTQYGLGCKYIYQKNGDPLHISELLESFKKDARSFKLRAGKHQLEDVTAVLKSFLSDIDDALLTKELYPYWISALDTQDDKERIKKYGAFIRSLPGVNRATLAAIIEHLYRVQKCSEINHMNAHNLALVFSSCLFQTKGQTSEEVNVIEDLINNYVEIFEVKEDQVKQMDIENSFITKWKDTQVSQAGDLLIEVYVERKEPDCSIIIRISPVMEAEELTNDILAIKNIIPTKGDIWATFEVIENEELERPLHYKENVLEQVLRWSSLAEPGSAYLVVKRFLTADTIKHCSDRSTLGSIKEGILKIKEEPSKILSGNKFQDRYFVLRDGFLFLYKDVKSSKHDKMFSLSSMKFYRGVKKKMKPPTSWGLTAYSEKHHWHLCCDSSRTQTEWMTSIFIAQHEYDIWPPAGKERKRSITKNPKIGGLPLIPIQHEGNATLARKNIESARAELERLRLSEKCDKESVDSSLKERASMVAHCLEHKDDKLRNRPRKHRSFNCLEDTEPEAPLGQPKGHKGLKTLRKTEDRNSKATLDSDHKLPSRVIEELNVVLQRSRTLPKELQDEQILK
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
52PhosphorylationLLQKIGISPTGHRRR
HHHHHCCCCCHHHHH
15.9328674419
54PhosphorylationQKIGISPTGHRRRIL
HHHCCCCCHHHHHHH
38.5423403867
69PhosphorylationKQLQIILSKMQDIPI
HHHHHHHHHCCCCCE
18.70-
77PhosphorylationKMQDIPIYANVHKTK
HCCCCCEEEEEECCC
6.1821945579
142PhosphorylationERSQYPQSDDKLSPP
CHHHCCCCCCCCCCC
43.1830108239
147PhosphorylationPQSDDKLSPPKRDFP
CCCCCCCCCCCCCCC
44.9224719451
258PhosphorylationEMIVNDLYVPSSPIL
EEEECEEECCCCCCC
17.1229978859
261PhosphorylationVNDLYVPSSPILAPV
ECEEECCCCCCCCCC
38.4124719451
262PhosphorylationNDLYVPSSPILAPVR
CEEECCCCCCCCCCC
15.1927050516
279PhosphorylationSKLVSRPSRSFLLRH
CCCCCCCCCHHHHCC
39.1729978859
281PhosphorylationLVSRPSRSFLLRHRP
CCCCCCCHHHHCCCC
25.2824719451
295PhosphorylationPVPEIPGSTKGVSGS
CCCCCCCCCCCCCCH
22.9128555341
296PhosphorylationVPEIPGSTKGVSGSY
CCCCCCCCCCCCCHH
37.42-
302PhosphorylationSTKGVSGSYFRERRN
CCCCCCCHHHHHHCC
17.37-
303PhosphorylationTKGVSGSYFRERRNV
CCCCCCHHHHHHCCC
15.3525884760
350PhosphorylationLENSKKRSIKNEFLT
HHHHCCCCHHHHHHC
46.9623312004
357PhosphorylationSIKNEFLTQGEALKG
CHHHHHHCCCCHHCC
39.59-
368PhosphorylationALKGEAATATNSFII
HHCCCCCCCCCEEEE
40.8524719451
377PhosphorylationTNSFIIKSSIYDNRK
CCEEEEECCCCCCCC
16.1528152594
378PhosphorylationNSFIIKSSIYDNRKE
CEEEEECCCCCCCCH
21.8428152594
380PhosphorylationFIIKSSIYDNRKEKI
EEEECCCCCCCCHHC
14.7628796482
388PhosphorylationDNRKEKISEDKVEDI
CCCCHHCCCCCCCCC
51.3030177828
391AcetylationKEKISEDKVEDIWIP
CHHCCCCCCCCCEEE
43.3926210075
391UbiquitinationKEKISEDKVEDIWIP
CHHCCCCCCCCCEEE
43.39-
411PhosphorylationNFLIDTASESEYSTV
CCEEECCCHHHCCHH
43.6928348404
413PhosphorylationLIDTASESEYSTVEE
EEECCCHHHCCHHHH
39.0628348404
416PhosphorylationTASESEYSTVEECFQ
CCCHHHCCHHHHHHH
23.1728348404
417PhosphorylationASESEYSTVEECFQS
CCHHHCCHHHHHHHH
30.9128348404
424PhosphorylationTVEECFQSLRRKNSK
HHHHHHHHHHHHCCC
12.0024719451
439MethylationASKSRTQKALILDSV
CCCCHHHHHHHHCCC
44.54-
451PhosphorylationDSVNRHSYPLSSTSG
CCCCCCCCCCCCCCC
11.3216497976
457PhosphorylationSYPLSSTSGNADSSA
CCCCCCCCCCCCCCC
31.8126356563
462PhosphorylationSTSGNADSSAVSSQA
CCCCCCCCCCCCCCC
20.1326356563
463PhosphorylationTSGNADSSAVSSQAI
CCCCCCCCCCCCCCC
32.9826356563
466PhosphorylationNADSSAVSSQAISPY
CCCCCCCCCCCCCCC
19.2226356563
467PhosphorylationADSSAVSSQAISPYA
CCCCCCCCCCCCCCH
19.6226356563
471PhosphorylationAVSSQAISPYACFYG
CCCCCCCCCCHHHHC
18.1828442448
473PhosphorylationSSQAISPYACFYGAS
CCCCCCCCHHHHCCC
14.8216497976
477PhosphorylationISPYACFYGASAKKV
CCCCHHHHCCCCCCC
16.2128152594
480PhosphorylationYACFYGASAKKVKSG
CHHHHCCCCCCCCCC
35.9426356563
493PhosphorylationSGWLDKLSPQGKRMF
CCHHHHCCHHHHHHH
22.4025159151
523PhosphorylationNNEKEMYSKGIIPLS
CCCCCEECCCEEEHH
24.0924719451
567PhosphorylationEERNDWISILLNALK
HHCCHHHHHHHHHHH
11.7024706070
577PhosphorylationLNALKSQSLTSQSQA
HHHHHHCCCCCCCCC
40.4822817900
580PhosphorylationLKSQSLTSQSQAVVT
HHHCCCCCCCCCEEC
32.8822817900
582PhosphorylationSQSLTSQSQAVVTPE
HCCCCCCCCCEECHH
21.6322817900
587PhosphorylationSQSQAVVTPEKCGYL
CCCCCEECHHHCCEE
21.0925159151
593PhosphorylationVTPEKCGYLELRGYK
ECHHHCCEEEECCCE
13.38-
600AcetylationYLELRGYKAKIFTVL
EEEECCCEEEEEEEE
46.137683195
616AcetylationGNSVWLCKNEQDFKS
CCEEEEECCHHCCCC
62.447683407
654PhosphorylationSFEIITPYRSFSFTA
HEEEECCCCCEEEEC
15.39-
729PhosphorylationKCAGQHRSLGPKDSK
HHCCCCCCCCCCCHH
35.24-
781PhosphorylationDEELHMDSPVEKRKN
CHHHCCCCCHHHHHC
24.2227251275
867PhosphorylationSLQMEFLYHNKFSDF
CCCHHHHHCCCCCCC
14.52-
910PhosphorylationPSAASKLSSEKKLLE
HHHHHHCCHHHHHHH
39.9429083192
911PhosphorylationSAASKLSSEKKLLEE
HHHHHCCHHHHHHHH
64.9629083192
919PhosphorylationEKKLLEETNKKWCVL
HHHHHHHHCCCEEEE
42.8529083192
922MethylationLLEETNKKWCVLEGG
HHHHHCCCEEEEECC
48.14-
932PhosphorylationVLEGGFLSYYENDKS
EEECCEEEEEECCCC
24.3327050516
977PhosphorylationIFEIYLPSERVFLFG
EEEEECCCCEEEEEC
35.1324719451
1113PhosphorylationAIEKAAGTDGNALQD
HHHHHHCCCCCHHHH
35.6930576142
1134PhosphorylationDVPIIVNSCIAFVTQ
CCCEEHHHHHHHHHH
8.9430576142
1140PhosphorylationNSCIAFVTQYGLGCK
HHHHHHHHHHCCCCE
15.0430576142
1186PhosphorylationKHQLEDVTAVLKSFL
CHHHHHHHHHHHHHH
24.30-
1219UbiquitinationALDTQDDKERIKKYG
CCCCCCHHHHHHHHH
58.12-
1269PhosphorylationHNLALVFSSCLFQTK
HHHHHHHHHHHHCCC
16.8028961369
1275PhosphorylationFSSCLFQTKGQTSEE
HHHHHHCCCCCCHHH
29.7928961369
1320PhosphorylationFITKWKDTQVSQAGD
HHHCCCCCCHHHCCC
27.43-
1437UbiquitinationRSTLGSIKEGILKIK
CHHCCHHHHCCHHCC
52.14-
1574PhosphorylationIQHEGNATLARKNIE
EEECCCHHHHHHHHH
25.5828122231
1600PhosphorylationSEKCDKESVDSSLKE
HHHCCHHHHCHHHHH
36.6422817900
1632PhosphorylationNRPRKHRSFNCLEDT
CCCCCCCCCCCCCCC
22.1126657352
1692PhosphorylationVVLQRSRTLPKELQD
HHHHHHCCCCHHHCC
48.9724719451

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 ARAP2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARAP2_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 ARAP2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ARAP2_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 ARAP2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-1600, AND MASSSPECTROMETRY.

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