ACAP2_HUMAN - dbPTM
ACAP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACAP2_HUMAN
UniProt AC Q15057
Protein Name Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2
Gene Name ACAP2
Organism Homo sapiens (Human).
Sequence Length 778
Subcellular Localization Endosome membrane
Peripheral membrane protein.
Protein Description GTPase-activating protein (GAP) for ADP ribosylation factor 6 (ARF6)..
Protein Sequence MKMTVDFEECLKDSPRFRAALEEVEGDVAELELKLDKLVKLCIAMIDTGKAFCVANKQFMNGIRDLAQYSSNDAVVETSLTKFSDSLQEMINFHTILFDQTQRSIKAQLQNFVKEDLRKFKDAKKQFEKVSEEKENALVKNAQVQRNKQHEVEEATNILTATRKCFRHIALDYVLQINVLQSKRRSEILKSMLSFMYAHLAFFHQGYDLFSELGPYMKDLGAQLDRLVVDAAKEKREMEQKHSTIQQKDFSSDDSKLEYNVDAANGIVMEGYLFKRASNAFKTWNRRWFSIQNNQLVYQKKFKDNPTVVVEDLRLCTVKHCEDIERRFCFEVVSPTKSCMLQADSEKLRQAWIKAVQTSIATAYREKGDESEKLDKKSSPSTGSLDSGNESKEKLLKGESALQRVQCIPGNASCCDCGLADPRWASINLGITLCIECSGIHRSLGVHFSKVRSLTLDTWEPELLKLMCELGNDVINRVYEANVEKMGIKKPQPGQRQEKEAYIRAKYVERKFVDKYSISLSPPEQQKKFVSKSSEEKRLSISKFGPGDQVRASAQSSVRSNDSGIQQSSDDGRESLPSTVSANSLYEPEGERQDSSMFLDSKHLNPGLQLYRASYEKNLPKMAEALAHGADVNWANSEENKATPLIQAVLGGSLVTCEFLLQNGANVNQRDVQGRGPLHHATVLGHTGQVCLFLKRGANQHATDEEGKDPLSIAVEAANADIVTLLRLARMNEEMRESEGLYGQPGDETYQDIFRDFSQMASNNPEKLNRFQQDSQKF
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
57UbiquitinationKAFCVANKQFMNGIR
CEEHHHCHHHHHHHH		34.86-
69PhosphorylationGIRDLAQYSSNDAVV
HHHHHHHHCCCCHHH		14.4129759185
70PhosphorylationIRDLAQYSSNDAVVE
HHHHHHHCCCCHHHH		15.5829759185
71PhosphorylationRDLAQYSSNDAVVET
HHHHHHCCCCHHHHH		33.5229759185
106MalonylationDQTQRSIKAQLQNFV
CHHHHHHHHHHHHHH		31.1826320211
106UbiquitinationDQTQRSIKAQLQNFV
CHHHHHHHHHHHHHH		31.18-
114UbiquitinationAQLQNFVKEDLRKFK
HHHHHHHHHHHHHHH		41.1829967540
134UbiquitinationFEKVSEEKENALVKN
HHHHCHHHHHHHHHH		52.82-
140UbiquitinationEKENALVKNAQVQRN
HHHHHHHHHHHHHHH		47.6329967540
148UbiquitinationNAQVQRNKQHEVEEA
HHHHHHHHHHHHHHH		56.0429967540
189UbiquitinationSKRRSEILKSMLSFM
HHHHHHHHHHHHHHH		2.7024816145
197PhosphorylationKSMLSFMYAHLAFFH
HHHHHHHHHHHHHHH		6.72-
233UbiquitinationRLVVDAAKEKREMEQ
HHHHHHHHHHHHHHH		66.5424816145
243PhosphorylationREMEQKHSTIQQKDF
HHHHHHHCCCCCCCC		33.9526699800
244PhosphorylationEMEQKHSTIQQKDFS
HHHHHHCCCCCCCCC		23.6425849741
248UbiquitinationKHSTIQQKDFSSDDS
HHCCCCCCCCCCCCC		44.3529967540
259PhosphorylationSDDSKLEYNVDAANG
CCCCCCEEEEECCCC		30.81-
261UbiquitinationDSKLEYNVDAANGIV
CCCCEEEEECCCCEE		5.3324816145
272PhosphorylationNGIVMEGYLFKRASN
CCEEEEEEHHHHHHC		8.82-
278PhosphorylationGYLFKRASNAFKTWN
EEHHHHHHCHHHHCC		32.4924719451
282UbiquitinationKRASNAFKTWNRRWF
HHHHCHHHHCCCCEE		50.6624816145
282MalonylationKRASNAFKTWNRRWF
HHHHCHHHHCCCCEE		50.6626320211
290PhosphorylationTWNRRWFSIQNNQLV
HCCCCEEEEECCEEE		19.1224076635
298PhosphorylationIQNNQLVYQKKFKDN
EECCEEEEEECCCCC		24.1728152594
319UbiquitinationDLRLCTVKHCEDIER
CEEECEEECHHHHHH		25.1224816145
319AcetylationDLRLCTVKHCEDIER
CEEECEEECHHHHHH		25.1225953088
326UbiquitinationKHCEDIERRFCFEVV
ECHHHHHHHHEEEEE		36.9924816145
334PhosphorylationRFCFEVVSPTKSCML
HHEEEEECCCCCHHH		31.8427050516
336PhosphorylationCFEVVSPTKSCMLQA
EEEEECCCCCHHHHC		28.2526091039
337AcetylationFEVVSPTKSCMLQAD
EEEECCCCCHHHHCC		45.0725953088
338PhosphorylationEVVSPTKSCMLQADS
EEECCCCCHHHHCCH		13.7729978859
345PhosphorylationSCMLQADSEKLRQAW
CHHHHCCHHHHHHHH		39.3829978859
347UbiquitinationMLQADSEKLRQAWIK
HHHCCHHHHHHHHHH		53.5824816145
354UbiquitinationKLRQAWIKAVQTSIA
HHHHHHHHHHHHHHH		31.6324816145
358PhosphorylationAWIKAVQTSIATAYR
HHHHHHHHHHHHHHH		18.5921406692
359PhosphorylationWIKAVQTSIATAYRE
HHHHHHHHHHHHHHH		7.9821406692
362PhosphorylationAVQTSIATAYREKGD
HHHHHHHHHHHHHCC		23.6621406692
364PhosphorylationQTSIATAYREKGDES
HHHHHHHHHHHCCHH		18.2321406692
367AcetylationIATAYREKGDESEKL
HHHHHHHHCCHHHHC		63.767378605
377UbiquitinationESEKLDKKSSPSTGS
HHHHCCCCCCCCCCC		56.69-
378PhosphorylationSEKLDKKSSPSTGSL
HHHCCCCCCCCCCCC		53.9023401153
379PhosphorylationEKLDKKSSPSTGSLD
HHCCCCCCCCCCCCC		31.5823927012
381PhosphorylationLDKKSSPSTGSLDSG
CCCCCCCCCCCCCCC		47.5523401153
382PhosphorylationDKKSSPSTGSLDSGN
CCCCCCCCCCCCCCC		33.8929255136
384PhosphorylationKSSPSTGSLDSGNES
CCCCCCCCCCCCCHH		29.1429255136
387PhosphorylationPSTGSLDSGNESKEK
CCCCCCCCCCHHHHH		49.1429255136
391PhosphorylationSLDSGNESKEKLLKG
CCCCCCHHHHHHHHC		50.5529255136
450UbiquitinationSLGVHFSKVRSLTLD
HHCCCHHHEEEEECC		40.50-
453PhosphorylationVHFSKVRSLTLDTWE
CCHHHEEEEECCCCC		28.7928450419
453UbiquitinationVHFSKVRSLTLDTWE
CCHHHEEEEECCCCC		28.7924816145
455PhosphorylationFSKVRSLTLDTWEPE
HHHEEEEECCCCCHH		24.6728450419
462UbiquitinationTLDTWEPELLKLMCE
ECCCCCHHHHHHHHH		56.0424816145
479PhosphorylationNDVINRVYEANVEKM
HHHHHHHHHHHHHHC		13.1930622161
490UbiquitinationVEKMGIKKPQPGQRQ
HHHCCCCCCCCCCCH		47.1424816145
497UbiquitinationKPQPGQRQEKEAYIR
CCCCCCCHHHHHHHH		59.2224816145
499UbiquitinationQPGQRQEKEAYIRAK
CCCCCHHHHHHHHHH		39.0324816145
506UbiquitinationKEAYIRAKYVERKFV
HHHHHHHHHHHHHHH		39.7224816145
515AcetylationVERKFVDKYSISLSP
HHHHHHCCCCCCCCC		35.2818603707
516PhosphorylationERKFVDKYSISLSPP
HHHHHCCCCCCCCCH		13.5323403867
517PhosphorylationRKFVDKYSISLSPPE
HHHHCCCCCCCCCHH		16.0825022875
518UbiquitinationKFVDKYSISLSPPEQ
HHHCCCCCCCCCHHH		4.3324816145
519PhosphorylationFVDKYSISLSPPEQQ
HHCCCCCCCCCHHHH		19.4930278072
521PhosphorylationDKYSISLSPPEQQKK
CCCCCCCCCHHHHHH		31.4519664994
525UbiquitinationISLSPPEQQKKFVSK
CCCCCHHHHHHHCCC		67.1924816145
527UbiquitinationLSPPEQQKKFVSKSS
CCCHHHHHHHCCCCC		48.1224816145
527AcetylationLSPPEQQKKFVSKSS
CCCHHHHHHHCCCCC		48.1218603715
531PhosphorylationEQQKKFVSKSSEEKR
HHHHHHCCCCCHHHC		29.9228270605
532AcetylationQQKKFVSKSSEEKRL
HHHHHCCCCCHHHCC		53.3418603723
533PhosphorylationQKKFVSKSSEEKRLS
HHHHCCCCCHHHCCC		35.1628270605
534UbiquitinationKKFVSKSSEEKRLSI
HHHCCCCCHHHCCCH		54.2124816145
534PhosphorylationKKFVSKSSEEKRLSI
HHHCCCCCHHHCCCH		54.2128270605
540PhosphorylationSSEEKRLSISKFGPG
CCHHHCCCHHHCCCH		28.9330278072
542PhosphorylationEEKRLSISKFGPGDQ
HHHCCCHHHCCCHHH		20.6828464451
553PhosphorylationPGDQVRASAQSSVRS
CHHHHHHHHHHHCCC		19.1028555341
556PhosphorylationQVRASAQSSVRSNDS
HHHHHHHHHCCCCCC		30.4329449344
557PhosphorylationVRASAQSSVRSNDSG
HHHHHHHHCCCCCCC		14.9629449344
563PhosphorylationSSVRSNDSGIQQSSD
HHCCCCCCCCCCCCC		41.8821815630
568PhosphorylationNDSGIQQSSDDGRES
CCCCCCCCCCCCCCC		21.2523186163
569PhosphorylationDSGIQQSSDDGRESL
CCCCCCCCCCCCCCC		35.0723186163
575PhosphorylationSSDDGRESLPSTVSA
CCCCCCCCCCCCCCC		44.1923312004
578PhosphorylationDGRESLPSTVSANSL
CCCCCCCCCCCCCCC		46.8923312004
579PhosphorylationGRESLPSTVSANSLY
CCCCCCCCCCCCCCC		19.2826657352
581PhosphorylationESLPSTVSANSLYEP
CCCCCCCCCCCCCCC		23.0930576142
584PhosphorylationPSTVSANSLYEPEGE
CCCCCCCCCCCCCCC		31.8526657352
586PhosphorylationTVSANSLYEPEGERQ
CCCCCCCCCCCCCCC		29.2928796482
595PhosphorylationPEGERQDSSMFLDSK
CCCCCCCCCCCCCCC		18.50-
596PhosphorylationEGERQDSSMFLDSKH
CCCCCCCCCCCCCCC		23.1121815630
602UbiquitinationSSMFLDSKHLNPGLQ
CCCCCCCCCCCCCHH		52.3429967540
617AcetylationLYRASYEKNLPKMAE
HHHHHHHHCHHHHHH		56.407825209
695AcetylationGQVCLFLKRGANQHA
HHEEEEEECCCCCCC		41.2625953088
708UbiquitinationHATDEEGKDPLSIAV
CCCCCCCCCHHHHHH		60.4929967540
738PhosphorylationMNEEMRESEGLYGQP
CCHHHHHHCCCCCCC		26.9728796482
742PhosphorylationMRESEGLYGQPGDET
HHHHCCCCCCCCCHH		25.2720007894
749PhosphorylationYGQPGDETYQDIFRD
CCCCCCHHHHHHHHH		31.0928796482
750PhosphorylationGQPGDETYQDIFRDF
CCCCCHHHHHHHHHH		11.3521082442
760SulfoxidationIFRDFSQMASNNPEK
HHHHHHHHHHCCHHH		4.2321406390
767UbiquitinationMASNNPEKLNRFQQD
HHHCCHHHHHHHHHH		52.9329967540
775PhosphorylationLNRFQQDSQKF----
HHHHHHHHHCC----		30.8217525332
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 ACAP2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACAP2_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 ACAP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RFIP3_HUMANRAB11FIP3physical
18685082
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 ACAP2_HUMAN

loading...

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-521, AND MASSSPECTROMETRY.
"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-379 AND SER-384, ANDMASS SPECTROMETRY.
"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 SER-521, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-775, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-742 AND TYR-750, ANDMASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory