ASAP1_MOUSE - dbPTM
ASAP1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ASAP1_MOUSE
UniProt AC Q9QWY8
Protein Name Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1
Gene Name Asap1
Organism Mus musculus (Mouse).
Sequence Length 1147
Subcellular Localization Cytoplasm. Membrane. Predominantly cytoplasmic. Partially membrane-associated.
Protein Description May function as a signal transduction protein involved in the differentiation of fibroblasts into adipocytes and possibly other cell types. Plays a role in ciliogenesis (By similarity). Posseses phosphatidylinositol 4,5-bisphosphate-dependent GTPase-activating protein activity for ARF1 (ADP ribosylation factor 1) and ARF5 and a lesser activity towards ARF6. May coordinate membrane trafficking with cell growth or actin cytoskeleton remodeling by binding to both SRC and PIP2..
Protein Sequence MRSSASRLSSFSSRDSLWNRMPDQISVSEFIAETTEDYNSPTTSSFTTRLHNCRNTVTLLEEALDQDRTALQKVKKSVKAIYNSGQDHVQNEENYAQVLDKFGSNFLSRDNPDLGTAFVKFSTLTKELSTLLKNLLQGLSHNVIFTLDSLLKGDLKGVKGDLKKPFDKAWKDYETKFTKIEKEKREHAKQHGMIRTEITGAEIAEEMEKERRLFQLQMCEYLIKVNEIKTKKGVDLLQNLIKYYHAQCNFFQDGLKTADKLKQYIEKLAADLYNIKQTQDEEKKQLTALRDLIKSSLQLDPKEVGGLYVASRANSSRRDSQSRQGGYSMHQLQGNKEYGSEKKGFLLKKSDGIRKVWQRRKCAVKNGILTISHATSNRQPAKLNLLTCQVKPNAEDKKSFDLISHNRTYHFQAEDEQDYIAWISVLTNSKEEALTMAFRGEQSTGENSLEDLTKAIIEDVQRLPGNDICCDCGSSEPTWLSTNLGILTCIECSGIHREMGVHISRIQSLELDKLGTSELLLAKNVGNNSFNDIMEANLPSPSPKPTPSSDMTVRKEYITAKYVDHRFSRKTCASSSAKLNELLEAIKSRDLLALIQVYAEGVELMEPLLEPGQELGETALHLAVRTADQTSLHLVDFLVQNCGNLDKQTSVGNTVLHYCSMYGKPECLKLLLRSKPTVDIVNQNGETALDIAKRLKATQCEDLLSQAKSGKFNPHVHVEYEWNLRQDEMDESDDDLDDKPSPIKKERSPRPQSFCHSSSISPQDKLALPGFSTPRDKQRLSYGAFTNQIFASTSTDLPTSPTSEAPPLPPRNAGKGPTGPPSTLPLGTQTSSGSSTLSKKRPPPPPPGHKRTLSDPPSPLPHGPPNKGAIPWGNDVGPLSSSKTANKFEGLSQQASTSSAKTALGPRVLPKLPQKVALRKTETSHHLSLDRTNIPPETFQKSSQLTELPQKPPLGELPPKPVELAPKPQVGELPPKPGELPPKPQLGDLPPKPQLSDLPPKPQMKDLPPKPQLGDLLAKSQAGDVSAKVQPPSEVTQRSHTGDLSPNVQSRDAIQKQASEDSNDLTPTLPETPVPLPRKINTGKNKVRRVKTIYDCQADNDDELTFIEGEVIIVTGEEDQEWWIGHIEGQPERKGVFPVSFVHILSD
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
4Phosphorylation----MRSSASRLSSF
----CCCHHHHHHHC		36.17-
6Phosphorylation--MRSSASRLSSFSS
--CCCHHHHHHHCCC		35.3829514104
9PhosphorylationRSSASRLSSFSSRDS
CCHHHHHHHCCCCHH		28.3823984901
10PhosphorylationSSASRLSSFSSRDSL
CHHHHHHHCCCCHHH		33.4721743459
12PhosphorylationASRLSSFSSRDSLWN
HHHHHHCCCCHHHHH		26.8121743459
13PhosphorylationSRLSSFSSRDSLWNR
HHHHHCCCCHHHHHH		37.7919060867
16PhosphorylationSSFSSRDSLWNRMPD
HHCCCCHHHHHHCCC		33.8923984901
175PhosphorylationKAWKDYETKFTKIEK
HHHHHHHHHHHHHHH		25.8118779572
232UbiquitinationVNEIKTKKGVDLLQN
HHHCCCHHHHHHHHH		70.2022790023
232UbiquitinationVNEIKTKKGVDLLQN
HHHCCCHHHHHHHHH		70.2022790023
308PhosphorylationPKEVGGLYVASRANS
HHHHCCEEEEECCCC		9.3916413287
312 (in isoform 4)Phosphorylation-28.2229514104
313 (in isoform 4)Phosphorylation-20.1229514104
327PhosphorylationSQSRQGGYSMHQLQG
CCCCCCCCCHHHHCC		15.0525338131
435PhosphorylationNSKEEALTMAFRGEQ
CCHHHHHHHHHCCCC		17.3225159016
443PhosphorylationMAFRGEQSTGENSLE
HHHCCCCCCCCCCHH		33.7928066266
444PhosphorylationAFRGEQSTGENSLED
HHCCCCCCCCCCHHH		48.4828066266
448PhosphorylationEQSTGENSLEDLTKA
CCCCCCCCHHHHHHH		28.9128066266
453PhosphorylationENSLEDLTKAIIEDV
CCCHHHHHHHHHHHH		30.6530635358
508PhosphorylationVHISRIQSLELDKLG
CCHHHEEEEEHHHCC		22.8018779572
516PhosphorylationLELDKLGTSELLLAK
EEHHHCCCCHHHHHH		29.48-
517PhosphorylationELDKLGTSELLLAKN
EHHHCCCCHHHHHHC		25.17-
540PhosphorylationIMEANLPSPSPKPTP
HHHCCCCCCCCCCCC		40.9725521595
542PhosphorylationEANLPSPSPKPTPSS
HCCCCCCCCCCCCCC		50.3120415495
546PhosphorylationPSPSPKPTPSSDMTV
CCCCCCCCCCCCCEE		41.7620415495
548PhosphorylationPSPKPTPSSDMTVRK
CCCCCCCCCCCEECH		41.2620415495
549PhosphorylationSPKPTPSSDMTVRKE
CCCCCCCCCCEECHH		32.3820415495
552PhosphorylationPTPSSDMTVRKEYIT
CCCCCCCEECHHHHH		23.3429899451
664AcetylationHYCSMYGKPECLKLL
HHHHHHCCHHHHHHH		21.8422826441
698PhosphorylationIAKRLKATQCEDLLS
HHHHHHHHHHHHHHH		31.97-
705PhosphorylationTQCEDLLSQAKSGKF
HHHHHHHHHHHCCCC		35.08-
729OxidationWNLRQDEMDESDDDL
EECCHHHCCCCCCCC		10.4917242355
732PhosphorylationRQDEMDESDDDLDDK
CHHHCCCCCCCCCCC		41.9225521595
741PhosphorylationDDLDDKPSPIKKERS
CCCCCCCCCCCCCCC		45.0225521595
748PhosphorylationSPIKKERSPRPQSFC
CCCCCCCCCCCCCCC		26.7625619855
753PhosphorylationERSPRPQSFCHSSSI
CCCCCCCCCCCCCCC		32.3026824392
757PhosphorylationRPQSFCHSSSISPQD
CCCCCCCCCCCCHHH		27.2825619855
758PhosphorylationPQSFCHSSSISPQDK
CCCCCCCCCCCHHHC		14.1825619855
759PhosphorylationQSFCHSSSISPQDKL
CCCCCCCCCCHHHCC		30.0525619855
761PhosphorylationFCHSSSISPQDKLAL
CCCCCCCCHHHCCCC		20.6125619855
772PhosphorylationKLALPGFSTPRDKQR
CCCCCCCCCCHHHHC		43.3429514104
773PhosphorylationLALPGFSTPRDKQRL
CCCCCCCCCHHHHCC		21.7829514104
781PhosphorylationPRDKQRLSYGAFTNQ
CHHHHCCCHHHHCCC		24.5728285833
782PhosphorylationRDKQRLSYGAFTNQI
HHHHCCCHHHHCCCE		19.6416413287
792PhosphorylationFTNQIFASTSTDLPT
HCCCEEEECCCCCCC		16.4930635358
793PhosphorylationTNQIFASTSTDLPTS
CCCEEEECCCCCCCC		32.0130635358
794PhosphorylationNQIFASTSTDLPTSP
CCEEEECCCCCCCCC		19.8930635358
795PhosphorylationQIFASTSTDLPTSPT
CEEEECCCCCCCCCC		41.4630635358
799PhosphorylationSTSTDLPTSPTSEAP
ECCCCCCCCCCCCCC		55.4230635358
800PhosphorylationTSTDLPTSPTSEAPP
CCCCCCCCCCCCCCC		25.0027087446
802PhosphorylationTDLPTSPTSEAPPLP
CCCCCCCCCCCCCCC		38.6830635358
803PhosphorylationDLPTSPTSEAPPLPP
CCCCCCCCCCCCCCC		34.8430635358
818PhosphorylationRNAGKGPTGPPSTLP
CCCCCCCCCCCCCCC		71.6221189417
823O-linked_GlycosylationGPTGPPSTLPLGTQT
CCCCCCCCCCCCCCC		37.8622517741
831PhosphorylationLPLGTQTSSGSSTLS
CCCCCCCCCCCCCCC		23.9225619855
835PhosphorylationTQTSSGSSTLSKKRP
CCCCCCCCCCCCCCC		36.5725619855
836PhosphorylationQTSSGSSTLSKKRPP
CCCCCCCCCCCCCCC		36.4325619855
838PhosphorylationSSGSSTLSKKRPPPP
CCCCCCCCCCCCCCC		35.9025619855
852PhosphorylationPPPGHKRTLSDPPSP
CCCCCCCCCCCCCCC		35.1027087446
854PhosphorylationPGHKRTLSDPPSPLP
CCCCCCCCCCCCCCC		47.6727087446
858PhosphorylationRTLSDPPSPLPHGPP
CCCCCCCCCCCCCCC		44.4427087446
881PhosphorylationNDVGPLSSSKTANKF
CCCCCCCCCHHCHHC		39.9425338131
884PhosphorylationGPLSSSKTANKFEGL
CCCCCCHHCHHCCCC		37.0929899451
887AcetylationSSSKTANKFEGLSQQ
CCCHHCHHCCCCCCC		42.1823806337
892PhosphorylationANKFEGLSQQASTSS
CHHCCCCCCCCCCCC		30.9729899451
896PhosphorylationEGLSQQASTSSAKTA
CCCCCCCCCCCCHHH		25.2029514104
923PhosphorylationVALRKTETSHHLSLD
EEECCCCCCCCCCCC		38.2926824392
924PhosphorylationALRKTETSHHLSLDR
EECCCCCCCCCCCCC		11.5929472430
928PhosphorylationTETSHHLSLDRTNIP
CCCCCCCCCCCCCCC		24.7029899451
1026PhosphorylationKSQAGDVSAKVQPPS
HHCCCCCCCEECCCC		27.41-
1033PhosphorylationSAKVQPPSEVTQRSH
CCEECCCCHHHCCCC		51.9222871156
1036PhosphorylationVQPPSEVTQRSHTGD
ECCCCHHHCCCCCCC		17.7622871156
1039PhosphorylationPSEVTQRSHTGDLSP
CCHHHCCCCCCCCCC		18.6425619855
1041PhosphorylationEVTQRSHTGDLSPNV
HHHCCCCCCCCCCCH		33.3725168779
1045PhosphorylationRSHTGDLSPNVQSRD
CCCCCCCCCCHHCHH		21.1125521595
1050PhosphorylationDLSPNVQSRDAIQKQ
CCCCCHHCHHHHHHH		28.0425619855
1059PhosphorylationDAIQKQASEDSNDLT
HHHHHHHHCCCCCCC		39.1725521595
1062PhosphorylationQKQASEDSNDLTPTL
HHHHHCCCCCCCCCC		28.3525521595
1066PhosphorylationSEDSNDLTPTLPETP
HCCCCCCCCCCCCCC		19.6626824392
1068PhosphorylationDSNDLTPTLPETPVP
CCCCCCCCCCCCCCC		50.1125619855
1072PhosphorylationLTPTLPETPVPLPRK
CCCCCCCCCCCCCCC		27.8725619855
1086AcetylationKINTGKNKVRRVKTI
CCCCCCCCEEEEEEE		40.37-
1140PhosphorylationRKGVFPVSFVHILSD
CCCEECEEEEEECCC		23.0721743459
1146PhosphorylationVSFVHILSD------
EEEEEECCC------		40.4424925903
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
308YPhosphorylationKinasePYK2Q14289
PSP
308YPhosphorylationKinasePTK2BQ9QVP9
GPS
308YPhosphorylationKinaseSRCP05480
PSP
782YPhosphorylationKinasePTK2BQ14289
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ASAP1_MOUSE !!
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 ASAP1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
REPS2_MOUSEReps2physical
12149250
APC7_HUMANANAPC7physical
18685082
ASAP2_HUMANASAP2physical
18685082
CN166_HUMANC14orf166physical
18685082
DYN1_HUMANDNM1physical
18685082
GOGB1_HUMANGOLGB1physical
18685082
MACF1_HUMANMACF1physical
18685082
MYOME_HUMANPDE4DIPphysical
18685082
RFIP3_HUMANRAB11FIP3physical
18685082
RAI14_HUMANRAI14physical
18685082
BRE1A_HUMANRNF20physical
18685082
SET_HUMANSETphysical
18685082
3BP1_HUMANSH3BP1physical
18685082
MED4_HUMANMED4physical
18685082
ARHG2_MOUSEArhgef2physical
18685082
DTBP1_MOUSEDtnbp1physical
18685082
SESD1_MOUSESestd1physical
18685082
UACA_MOUSEUacaphysical
18685082
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ASAP1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-732, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-858, AND MASSSPECTROMETRY.
"The tyrosine kinase Pyk2 regulates Arf1 activity by phosphorylationand inhibition of the Arf-GTPase-activating protein ASAP1.";
Kruljac-Letunic A., Moelleken J., Kallin A., Wieland F., Blaukat A.;
J. Biol. Chem. 278:29560-29570(2003).
Cited for: PHOSPHORYLATION AT TYR-308, AND INTERACTION WITH PTK2B/PYK2.

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