ASAP1_HUMAN - dbPTM
ASAP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ASAP1_HUMAN
UniProt AC Q9ULH1
Protein Name Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1
Gene Name ASAP1
Organism Homo sapiens (Human).
Sequence Length 1129
Subcellular Localization Cytoplasm. Membrane. Predominantly cytoplasmic. Partially membrane-associated..
Protein Description Possesses 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. May function as a signal transduction protein involved in the differentiation of fibroblasts into adipocytes and possibly other cell types (By similarity). Plays a role in ciliogenesis..
Protein Sequence MRSSASRLSSFSSRDSLWNRMPDQISVSEFIAETTEDYNSPTTSSFTTRLHNCRNTVTLLEEALDQDRTALQKVKKSVKAIYNSGQDHVQNEENYAQVLDKFGSNFLSRDNPDLGTAFVKFSTLTKELSTLLKNLLQGLSHNVIFTLDSLLKGDLKGVKGDLKKPFDKAWKDYETKFTKIEKEKREHAKQHGMIRTEITGAEIAEEMEKERRLFQLQMCEYLIKVNEIKTKKGVDLLQNLIKYYHAQCNFFQDGLKTADKLKQYIEKLAADLYNIKQTQDEEKKQLTALRDLIKSSLQLDQKEDSQSRQGGYSMHQLQGNKEYGSEKKGYLLKKSDGIRKVWQRRKCSVKNGILTISHATSNRQPAKLNLLTCQVKPNAEDKKSFDLISHNRTYHFQAEDEQDYVAWISVLTNSKEEALTMAFRGEQSAGENSLEDLTKAIIEDVQRLPGNDICCDCGSSEPTWLSTNLGILTCIECSGIHREMGVHISRIQSLELDKLGTSELLLAKNVGNNSFNDIMEANLPSPSPKPTPSSDMTVRKEYITAKYVDHRFSRKTCSTSSAKLNELLEAIKSRDLLALIQVYAEGVELMEPLLEPGQELGETALHLAVRTADQTSLHLVDFLVQNCGNLDKQTALGNTVLHYCSMYSKPECLKLLLRSKPTVDIVNQAGETALDIAKRLKATQCEDLLSQAKSGKFNPHVHVEYEWNLRQEEIDESDDDLDDKPSPIKKERSPRPQSFCHSSSISPQDKLALPGFSTPRDKQRLSYGAFTNQIFVSTSTDSPTSPTTEAPPLPPRNAGKGPTGPPSTLPLSTQTSSGSSTLSKKRPPPPPPGHKRTLSDPPSPLPHGPPNKGAVPWGNDGGPSSSSKTTNKFEGLSQQSSTSSAKTALGPRVLPKLPQKVALRKTDHLSLDKATIPPEIFQKSSQLAELPQKPPPGDLPPKPTELAPKPQIGDLPPKPGELPPKPQLGDLPPKPQLSDLPPKPQMKDLPPKPQLGDLLAKSQTGDVSPKAQQPSEVTLKSHPLDLSPNVQSRDAIQKQASEDSNDLTPTLPETPVPLPRKINTGKNKVRRVKTIYDCQADNDDELTFIEGEVIIVTGEEDQEWWIGHIEGQPERKGVFPVSFVHILSD
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
3Phosphorylation-----MRSSASRLSS
-----CCCHHHHHHH
41.9626270265
4Phosphorylation----MRSSASRLSSF
----CCCHHHHHHHC
36.1726270265
6Phosphorylation--MRSSASRLSSFSS
--CCCHHHHHHHCCC
35.3826270265
9PhosphorylationRSSASRLSSFSSRDS
CCHHHHHHHCCCCHH
28.3823403867
10PhosphorylationSSASRLSSFSSRDSL
CHHHHHHHCCCCHHH
33.4723403867
12PhosphorylationASRLSSFSSRDSLWN
HHHHHHCCCCHHHHH
26.8123403867
13PhosphorylationSRLSSFSSRDSLWNR
HHHHHCCCCHHHHHH
37.7923403867
34PhosphorylationVSEFIAETTEDYNSP
HHHHHHHCCCCCCCC
26.85-
79MalonylationQKVKKSVKAIYNSGQ
HHHHHHHHHHHHCCC
35.8426320211
101UbiquitinationNYAQVLDKFGSNFLS
HHHHHHHHHHHHHHC
47.68-
129PhosphorylationSTLTKELSTLLKNLL
HHHHHHHHHHHHHHH
20.3523403867
130PhosphorylationTLTKELSTLLKNLLQ
HHHHHHHHHHHHHHH
49.0523403867
149PhosphorylationNVIFTLDSLLKGDLK
HHEEEHHHHHCCCCC
38.4224719451
182AcetylationTKFTKIEKEKREHAK
HHHHHHHHHHHHHHH
72.51-
184AcetylationFTKIEKEKREHAKQH
HHHHHHHHHHHHHHH
74.32130655
209UbiquitinationEIAEEMEKERRLFQL
HHHHHHHHHHHHHHH
56.03-
232UbiquitinationVNEIKTKKGVDLLQN
HHHCCCHHHHHHHHH
70.20-
256UbiquitinationNFFQDGLKTADKLKQ
CCHHHHHHHHHHHHH
47.39-
276UbiquitinationAADLYNIKQTQDEEK
HHHHHCCCCCCCHHH
43.59-
284UbiquitinationQTQDEEKKQLTALRD
CCCCHHHHHHHHHHH
54.54-
287PhosphorylationDEEKKQLTALRDLIK
CHHHHHHHHHHHHHH
22.5824719451
305PhosphorylationQLDQKEDSQSRQGGY
CCCCCCHHHCCCCCC
31.0228857561
307PhosphorylationDQKEDSQSRQGGYSM
CCCCHHHCCCCCCCH
30.4428857561
310 (in isoform 2)Phosphorylation-35.5829978859
312PhosphorylationSQSRQGGYSMHQLQG
HHCCCCCCCHHHHCC
15.0525159151
315 (in isoform 2)Phosphorylation-21.1829978859
316 (in isoform 2)Phosphorylation-27.1729978859
330PhosphorylationYGSEKKGYLLKKSDG
HCCCCCCEEEECCCC
20.1029341593
372PhosphorylationPAKLNLLTCQVKPNA
CEEEEEEEEECCCCC
12.21-
409PhosphorylationQDYVAWISVLTNSKE
CCEEEEEEEECCCHH
10.6022210691
412PhosphorylationVAWISVLTNSKEEAL
EEEEEEECCCHHHHH
34.9822210691
428PhosphorylationMAFRGEQSAGENSLE
HHHCCCCCCCCCCHH
33.6620068231
433PhosphorylationEQSAGENSLEDLTKA
CCCCCCCCHHHHHHH
28.9127251275
493PhosphorylationVHISRIQSLELDKLG
CCHHHEEEEEHHHCC
22.8030266825
501PhosphorylationLELDKLGTSELLLAK
EEHHHCCCCHHHHHH
29.4817322306
502PhosphorylationELDKLGTSELLLAKN
EHHHCCCCHHHHHHC
25.1717322306
514PhosphorylationAKNVGNNSFNDIMEA
HHCCCCCCHHHHHHC
29.4424076635
525PhosphorylationIMEANLPSPSPKPTP
HHHCCCCCCCCCCCC
40.9725850435
527PhosphorylationEANLPSPSPKPTPSS
HCCCCCCCCCCCCCC
50.3125850435
555AcetylationVDHRFSRKTCSTSSA
CCHHHCCCCCCCCHH
53.3230588015
556PhosphorylationDHRFSRKTCSTSSAK
CHHHCCCCCCCCHHH
15.5823312004
558PhosphorylationRFSRKTCSTSSAKLN
HHCCCCCCCCHHHHH
36.2323312004
559PhosphorylationFSRKTCSTSSAKLNE
HCCCCCCCCHHHHHH
28.9323312004
560PhosphorylationSRKTCSTSSAKLNEL
CCCCCCCCHHHHHHH
16.4123312004
561PhosphorylationRKTCSTSSAKLNELL
CCCCCCCHHHHHHHH
29.5223312004
563AcetylationTCSTSSAKLNELLEA
CCCCCHHHHHHHHHH
54.5230588021
648PhosphorylationLHYCSMYSKPECLKL
HHHHHHCCCHHHHHH
32.8524719451
662PhosphorylationLLLRSKPTVDIVNQA
HHHHCCCCCEEECCC
34.2524247654
672PhosphorylationIVNQAGETALDIAKR
EECCCCHHHHHHHHH
31.4424247654
705PhosphorylationNPHVHVEYEWNLRQE
CCCCEEEEEEECCHH
25.7528270605
717PhosphorylationRQEEIDESDDDLDDK
CHHHCCCCCCCCCCC
42.4623927012
726PhosphorylationDDLDDKPSPIKKERS
CCCCCCCCCCCCCCC
45.0223927012
733PhosphorylationSPIKKERSPRPQSFC
CCCCCCCCCCCCCCC
26.7623927012
738PhosphorylationERSPRPQSFCHSSSI
CCCCCCCCCCCCCCC
32.3025159151
742PhosphorylationRPQSFCHSSSISPQD
CCCCCCCCCCCCHHH
27.2823927012
743PhosphorylationPQSFCHSSSISPQDK
CCCCCCCCCCCHHHC
14.1823401153
744PhosphorylationQSFCHSSSISPQDKL
CCCCCCCCCCHHHCC
30.0525159151
746PhosphorylationFCHSSSISPQDKLAL
CCCCCCCCHHHCCCC
20.6125159151
757PhosphorylationKLALPGFSTPRDKQR
CCCCCCCCCCCHHHH
43.3429255136
758PhosphorylationLALPGFSTPRDKQRL
CCCCCCCCCCHHHHC
21.7829255136
767PhosphorylationRDKQRLSYGAFTNQI
CHHHHCCCCCEECEE
19.64-
777PhosphorylationFTNQIFVSTSTDSPT
EECEEEEEECCCCCC
13.0926074081
778PhosphorylationTNQIFVSTSTDSPTS
ECEEEEEECCCCCCC
30.2826657352
779PhosphorylationNQIFVSTSTDSPTSP
CEEEEEECCCCCCCC
23.7826074081
780PhosphorylationQIFVSTSTDSPTSPT
EEEEEECCCCCCCCC
40.3526074081
782PhosphorylationFVSTSTDSPTSPTTE
EEEECCCCCCCCCCC
30.1126074081
784PhosphorylationSTSTDSPTSPTTEAP
EECCCCCCCCCCCCC
51.8226074081
785PhosphorylationTSTDSPTSPTTEAPP
ECCCCCCCCCCCCCC
24.5126074081
787PhosphorylationTDSPTSPTTEAPPLP
CCCCCCCCCCCCCCC
36.7226074081
788PhosphorylationDSPTSPTTEAPPLPP
CCCCCCCCCCCCCCC
33.2726074081
800UbiquitinationLPPRNAGKGPTGPPS
CCCCCCCCCCCCCCC
60.34-
803PhosphorylationRNAGKGPTGPPSTLP
CCCCCCCCCCCCCCC
71.6226074081
807PhosphorylationKGPTGPPSTLPLSTQ
CCCCCCCCCCCCCEE
45.7929978859
808PhosphorylationGPTGPPSTLPLSTQT
CCCCCCCCCCCCEEC
37.8629978859
812PhosphorylationPPSTLPLSTQTSSGS
CCCCCCCCEECCCCC
19.2726657352
813PhosphorylationPSTLPLSTQTSSGSS
CCCCCCCEECCCCCC
43.4828450419
815PhosphorylationTLPLSTQTSSGSSTL
CCCCCEECCCCCCCC
25.5828450419
816PhosphorylationLPLSTQTSSGSSTLS
CCCCEECCCCCCCCC
23.9226657352
817PhosphorylationPLSTQTSSGSSTLSK
CCCEECCCCCCCCCC
46.1928450419
819PhosphorylationSTQTSSGSSTLSKKR
CEECCCCCCCCCCCC
23.3028450419
820PhosphorylationTQTSSGSSTLSKKRP
EECCCCCCCCCCCCC
36.5728450419
821PhosphorylationQTSSGSSTLSKKRPP
ECCCCCCCCCCCCCC
36.4328450419
823PhosphorylationSSGSSTLSKKRPPPP
CCCCCCCCCCCCCCC
35.9028450419
824UbiquitinationSGSSTLSKKRPPPPP
CCCCCCCCCCCCCCC
56.78-
837PhosphorylationPPPGHKRTLSDPPSP
CCCCCCCCCCCCCCC
35.1022167270
839PhosphorylationPGHKRTLSDPPSPLP
CCCCCCCCCCCCCCC
47.6722167270
843PhosphorylationRTLSDPPSPLPHGPP
CCCCCCCCCCCCCCC
44.4425159151
864PhosphorylationWGNDGGPSSSSKTTN
CCCCCCCCCCCCCCC
46.2422199227
865PhosphorylationGNDGGPSSSSKTTNK
CCCCCCCCCCCCCCC
41.5921815630
866PhosphorylationNDGGPSSSSKTTNKF
CCCCCCCCCCCCCCC
39.9422199227
867PhosphorylationDGGPSSSSKTTNKFE
CCCCCCCCCCCCCCC
35.6522199227
877PhosphorylationTNKFEGLSQQSSTSS
CCCCCCCCCCCCCCC
36.7129507054
880PhosphorylationFEGLSQQSSTSSAKT
CCCCCCCCCCCCCHH
28.1328857561
881PhosphorylationEGLSQQSSTSSAKTA
CCCCCCCCCCCCHHH
28.1528985074
883PhosphorylationLSQQSSTSSAKTALG
CCCCCCCCCCHHHCC
30.1928985074
887PhosphorylationSSTSSAKTALGPRVL
CCCCCCHHHCCCCCC
27.1728985074
905AcetylationPQKVALRKTDHLSLD
CHHHHCCCCCCCCCC
60.19-
906PhosphorylationQKVALRKTDHLSLDK
HHHHCCCCCCCCCCC
23.4030266825
910PhosphorylationLRKTDHLSLDKATIP
CCCCCCCCCCCCCCC
30.9730266825
915PhosphorylationHLSLDKATIPPEIFQ
CCCCCCCCCCHHHHH
39.4918077418
924PhosphorylationPPEIFQKSSQLAELP
CHHHHHCHHHHHCCC
16.7218077418
925PhosphorylationPEIFQKSSQLAELPQ
HHHHHCHHHHHCCCC
35.9318077418
978PhosphorylationLPPKPQLSDLPPKPQ
CCCCCCHHCCCCCCC
31.6726074081
1002PhosphorylationLGDLLAKSQTGDVSP
HHHHHHHHCCCCCCC
27.6329396449
1004PhosphorylationDLLAKSQTGDVSPKA
HHHHHHCCCCCCCCC
42.3030242111
1008PhosphorylationKSQTGDVSPKAQQPS
HHCCCCCCCCCCCCC
25.9825159151
1015PhosphorylationSPKAQQPSEVTLKSH
CCCCCCCCCEEECCC
40.1226074081
1018PhosphorylationAQQPSEVTLKSHPLD
CCCCCCEEECCCCCC
25.1524043423
1021PhosphorylationPSEVTLKSHPLDLSP
CCCEEECCCCCCCCC
33.1923403867
1027PhosphorylationKSHPLDLSPNVQSRD
CCCCCCCCCCCCCHH
17.6925159151
1032PhosphorylationDLSPNVQSRDAIQKQ
CCCCCCCCHHHHHHH
28.0422617229
1041PhosphorylationDAIQKQASEDSNDLT
HHHHHHHHCCCCCCC
39.1723401153
1044PhosphorylationQKQASEDSNDLTPTL
HHHHHCCCCCCCCCC
28.3530266825
1048PhosphorylationSEDSNDLTPTLPETP
HCCCCCCCCCCCCCC
19.6630278072
1050PhosphorylationDSNDLTPTLPETPVP
CCCCCCCCCCCCCCC
50.1128450419
1054PhosphorylationLTPTLPETPVPLPRK
CCCCCCCCCCCCCCC
27.8725159151
1097PhosphorylationEGEVIIVTGEEDQEW
EEEEEEEECCCCCEE
28.59-
1122PhosphorylationRKGVFPVSFVHILSD
CCCEECEEEEEECCC
23.0723403867
1128PhosphorylationVSFVHILSD------
EEEEEECCC------
40.4425159151

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 ASAP1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ASAP1_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 ASAP1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
REPS2_MOUSEReps2physical
12149250
ARF6_HUMANARF6physical
18094045
SH3K1_HUMANSH3KBP1physical
17255943
CBL_HUMANCBLphysical
17255943
CBLB_HUMANCBLBphysical
17255943
SRC8_HUMANCTTNphysical
17893324
SRC8_HUMANCTTNphysical
15719014
PAXI_HUMANPXNphysical
16636290
GRB2_HUMANGRB2physical
21988832
RFIP3_HUMANRAB11FIP3physical
18685082
ARF1_HUMANARF1physical
16332543

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 ASAP1_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-843, 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-839; SER-843 ANDSER-1027, AND MASS 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-1027, AND MASSSPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-839; SER-843 ANDSER-1008, AND MASS SPECTROMETRY.

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