ACAP1_HUMAN - dbPTM
ACAP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACAP1_HUMAN
UniProt AC Q15027
Protein Name Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1
Gene Name ACAP1
Organism Homo sapiens (Human).
Sequence Length 740
Subcellular Localization Recycling endosome membrane
Peripheral membrane protein
Cytoplasmic side .
Protein Description GTPase-activating protein (GAP) for ADP ribosylation factor 6 (ARF6) required for clathrin-dependent export of proteins from recycling endosomes to trans-Golgi network and cell surface. Required for regulated export of ITGB1 from recycling endosomes to the cell surface and ITGB1-dependent cell migration..
Protein Sequence MTVKLDFEECLKDSPRFRASIELVEAEVSELETRLEKLLKLGTGLLESGRHYLAASRAFVVGICDLARLGPPEPMMAECLEKFTVSLNHKLDSHAELLDATQHTLQQQIQTLVKEGLRGFREARRDFWRGAESLEAALTHNAEVPRRRAQEAEEAGAALRTARAGYRGRALDYALQINVIEDKRKFDIMEFVLRLVEAQATHFQQGHEELSRLSQYRKELGAQLHQLVLNSAREKRDMEQRHVLLKQKELGGEEPEPSLREGPGGLVMEGHLFKRASNAFKTWSRRWFTIQSNQLVYQKKYKDPVTVVVDDLRLCTVKLCPDSERRFCFEVVSTSKSCLLQADSERLLQLWVSAVQSSIASAFSQARLDDSPRGPGQGSGHLAIGSAATLGSGGMARGREPGGVGHVVAQVQSVDGNAQCCDCREPAPEWASINLGVTLCIQCSGIHRSLGVHFSKVRSLTLDSWEPELVKLMCELGNVIINQIYEARVEAMAVKKPGPSCSRQEKEAWIHAKYVEKKFLTKLPEIRGRRGGRGRPRGQPPVPPKPSIRPRPGSLRSKPEPPSEDLGSLHPGALLFRASGHPPSLPTMADALAHGADVNWVNGGQDNATPLIQATAANSLLACEFLLQNGANVNQADSAGRGPLHHATILGHTGLACLFLKRGADLGARDSEGRDPLTIAMETANADIVTLLRLAKMREAEAAQGQAGDETYLDIFRDFSLMASDDPEKLSRRSHDLHTL
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
4Acetylation----MTVKLDFEECL
----CCEEECHHHHH		32.927974721
4Ubiquitination----MTVKLDFEECL
----CCEEECHHHHH		32.9229967540
12UbiquitinationLDFEECLKDSPRFRA
ECHHHHHCCCHHHHH		68.7529967540
14PhosphorylationFEECLKDSPRFRASI
HHHHHCCCHHHHHHH		19.1830108239
29PhosphorylationELVEAEVSELETRLE
HHHHHHHHHHHHHHH		28.1530301811
33PhosphorylationAEVSELETRLEKLLK
HHHHHHHHHHHHHHH		53.8530301811
37UbiquitinationELETRLEKLLKLGTG
HHHHHHHHHHHHCCC		64.81-
40AcetylationTRLEKLLKLGTGLLE
HHHHHHHHHCCCHHH		56.1325953088
40UbiquitinationTRLEKLLKLGTGLLE
HHHHHHHHHCCCHHH		56.1329967540
43PhosphorylationEKLLKLGTGLLESGR
HHHHHHCCCHHHCCH		34.78-
82UbiquitinationMMAECLEKFTVSLNH
HHHHHHHHHHHHCCC		33.13-
90UbiquitinationFTVSLNHKLDSHAEL
HHHHCCCCCHHHHHH		53.5729967540
114UbiquitinationQQIQTLVKEGLRGFR
HHHHHHHHHHHHHHH		49.53-
133PhosphorylationDFWRGAESLEAALTH
HHHHCHHHHHHHHHC		30.8628122231
183UbiquitinationQINVIEDKRKFDIME
HEEEECCHHHCCHHH		44.70-
185UbiquitinationNVIEDKRKFDIMEFV
EEECCHHHCCHHHHH		53.80-
218UbiquitinationSRLSQYRKELGAQLH
HHHHHHHHHHHHHHH		52.9729967540
246UbiquitinationEQRHVLLKQKELGGE
HHHHHHHHHHHHCCC		55.9829967540
248UbiquitinationRHVLLKQKELGGEEP
HHHHHHHHHHCCCCC		54.0122505724
274UbiquitinationVMEGHLFKRASNAFK
EEECCHHHHHHCHHH		54.1119608861
274AcetylationVMEGHLFKRASNAFK
EEECCHHHHHHCHHH		54.1123749302
277PhosphorylationGHLFKRASNAFKTWS
CCHHHHHHCHHHHCC		32.4924719451
281UbiquitinationKRASNAFKTWSRRWF
HHHHCHHHHCCCCEE		46.83-
281AcetylationKRASNAFKTWSRRWF
HHHHCHHHHCCCCEE		46.8325953088
297PhosphorylationIQSNQLVYQKKYKDP
EECCEEEEEECCCCC		24.1725147952
300UbiquitinationNQLVYQKKYKDPVTV
CEEEEEECCCCCEEE		41.8429967540
302UbiquitinationLVYQKKYKDPVTVVV
EEEEECCCCCEEEEE		65.5229967540
306PhosphorylationKKYKDPVTVVVDDLR
ECCCCCEEEEECCCE		16.99-
318AcetylationDLRLCTVKLCPDSER
CCEECEEEECCCCCC		26.6425953088
318UbiquitinationDLRLCTVKLCPDSER
CCEECEEEECCCCCC		26.6429967540
333PhosphorylationRFCFEVVSTSKSCLL
CEEEEEEECCCCHHH		31.94-
353PhosphorylationRLLQLWVSAVQSSIA
HHHHHHHHHHHHHHH		15.9026074081
357PhosphorylationLWVSAVQSSIASAFS
HHHHHHHHHHHHHHH		19.6726074081
358PhosphorylationWVSAVQSSIASAFSQ
HHHHHHHHHHHHHHH		12.7026074081
361PhosphorylationAVQSSIASAFSQARL
HHHHHHHHHHHHCCC		28.3326074081
364PhosphorylationSSIASAFSQARLDDS
HHHHHHHHHCCCCCC		23.7326074081
371PhosphorylationSQARLDDSPRGPGQG
HHCCCCCCCCCCCCC		19.0323401153
379PhosphorylationPRGPGQGSGHLAIGS
CCCCCCCCCCEEECC		18.3628464451
386PhosphorylationSGHLAIGSAATLGSG
CCCEEECCCCEECCC		14.4930108239
389PhosphorylationLAIGSAATLGSGGMA
EEECCCCEECCCCCC		31.2230576142
392PhosphorylationGSAATLGSGGMARGR
CCCCEECCCCCCCCC		34.9730108239
456UbiquitinationSLGVHFSKVRSLTLD
HHCCCHHHEEEEECC		40.50-
456AcetylationSLGVHFSKVRSLTLD
HHCCCHHHEEEEECC		40.5025953088
459PhosphorylationVHFSKVRSLTLDSWE
CCHHHEEEEECCCCC		28.7927067055
485NitrationNVIINQIYEARVEAM
CHHHHHHHHHHHHHH		8.1816777052
485NitrationNVIINQIYEARVEAM
CHHHHHHHHHHHHHH		8.1816777052
485Nitrated tyrosineNVIINQIYEARVEAM
CHHHHHHHHHHHHHH		8.18-
495AcetylationRVEAMAVKKPGPSCS
HHHHHEECCCCCCCC		43.6525953088
495UbiquitinationRVEAMAVKKPGPSCS
HHHHHEECCCCCCCC		43.6524816145
496UbiquitinationVEAMAVKKPGPSCSR
HHHHEECCCCCCCCH		48.9229967540
506UbiquitinationPSCSRQEKEAWIHAK
CCCCHHHHHHHHHHH		44.3829967540
513UbiquitinationKEAWIHAKYVEKKFL
HHHHHHHHHHHHHHH		35.3529967540
522AcetylationVEKKFLTKLPEIRGR
HHHHHHHCCCHHCCC		65.2825953088
522UbiquitinationVEKKFLTKLPEIRGR
HHHHHHHCCCHHCCC		65.28-
545UbiquitinationGQPPVPPKPSIRPRP
CCCCCCCCCCCCCCC		45.3829967540
547PhosphorylationPPVPPKPSIRPRPGS
CCCCCCCCCCCCCCC		37.0430576142
554PhosphorylationSIRPRPGSLRSKPEP
CCCCCCCCCCCCCCC		24.2425284369
558UbiquitinationRPGSLRSKPEPPSED
CCCCCCCCCCCCCCC		47.14-
653PhosphorylationHATILGHTGLACLFL
HHHHHCCCHHHHHHH		31.9025332170
661AcetylationGLACLFLKRGADLGA
HHHHHHHHCCCCCCC		41.2625953088
711PhosphorylationQGQAGDETYLDIFRD
CCCCCCHHHHHHHHH		33.8428796482
712PhosphorylationGQAGDETYLDIFRDF
CCCCCHHHHHHHHHH		10.5928796482
720PhosphorylationLDIFRDFSLMASDDP
HHHHHHHHCCCCCCH		22.8630377224
724PhosphorylationRDFSLMASDDPEKLS
HHHHCCCCCCHHHHH		28.6930377224
729UbiquitinationMASDDPEKLSRRSHD
CCCCCHHHHHHHCCC		58.0929967540
731PhosphorylationSDDPEKLSRRSHDLH
CCCHHHHHHHCCCCC		36.3926074081
734PhosphorylationPEKLSRRSHDLHTL-
HHHHHHHCCCCCCC-		21.9030108239
739PhosphorylationRRSHDLHTL------
HHCCCCCCC------		41.2723401153
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
554SPhosphorylationKinaseAKT1P31749
PSP
554SPhosphorylationKinaseAKT-FAMILY-GPS
554SPhosphorylationKinasePKB_GROUP-PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
554SPhosphorylation

16256741
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 ACAP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IFFO1_HUMANIFFO1physical
16189514
AKT1_HUMANAKT1physical
16256741
RFIP3_HUMANRAB11FIP3physical
18685082
ARF6_HUMANARF6physical
16527809
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 ACAP1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-274, AND MASS SPECTROMETRY.
Nitration
ReferencePubMed
"Nitroproteins from a human pituitary adenoma tissue discovered with anitrotyrosine affinity column and tandem mass spectrometry.";
Zhan X., Desiderio D.M.;
Anal. Biochem. 354:279-289(2006).
Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-485, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Phosphorylation of ACAP1 by Akt regulates the stimulation-dependentrecycling of integrin beta1 to control cell migration.";
Li J., Ballif B.A., Powelka A.M., Dai J., Gygi S.P., Hsu V.W.;
Dev. Cell 9:663-673(2005).
Cited for: FUNCTION, PHOSPHORYLATION AT SER-554, AND MUTAGENESIS OF SER-554 ANDSER-724.

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