ASAP2_HUMAN - dbPTM
ASAP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ASAP2_HUMAN
UniProt AC O43150
Protein Name Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
Gene Name ASAP2
Organism Homo sapiens (Human).
Sequence Length 1006
Subcellular Localization Cytoplasm. Golgi apparatus, Golgi stack membrane
Peripheral membrane protein. Cell membrane
Peripheral membrane protein. Colocalizes with F-actin and ARF6 in phagocytic cups.
Protein Description Activates the small GTPases ARF1, ARF5 and ARF6. Regulates the formation of post-Golgi vesicles and modulates constitutive secretion. Modulates phagocytosis mediated by Fc gamma receptor and ARF6. Modulates PXN recruitment to focal contacts and cell migration..
Protein Sequence MPDQISVSEFVAETHEDYKAPTASSFTTRTAQCRNTVAAIEEALDVDRMVLYKMKKSVKAINSSGLAHVENEEQYTQALEKFGGNCVCRDDPDLGSAFLKFSVFTKELTALFKNLIQNMNNIISFPLDSLLKGDLKGVKGDLKKPFDKAWKDYETKITKIEKEKKEHAKLHGMIRTEISGAEIAEEMEKERRFFQLQMCEYLLKVNEIKIKKGVDLLQNLIKYFHAQCNFFQDGLKAVESLKPSIETLSTDLHTIKQAQDEERRQLIQLRDILKSALQVEQKEDSQIRQSTAYSLHQPQGNKEHGTERNGSLYKKSDGIRKVWQKRKCSVKNGFLTISHGTANRPPAKLNLLTCQVKTNPEEKKCFDLISHDRTYHFQAEDEQECQIWMSVLQNSKEEALNNAFKGDDNTGENNIVQELTKEIISEVQRMTGNDVCCDCGAPDPTWLSTNLGILTCIECSGIHRELGVHYSRMQSLTLDVLGTSELLLAKNIGNAGFNEIMECCLPAEDSVKPNPGSDMNARKDYITAKYIERRYARKKHADNAAKLHSLCEAVKTRDIFGLLQAYADGVDLTEKIPLANGHEPDETALHLAVRSVDRTSLHIVDFLVQNSGNLDKQTGKGSTALHYCCLTDNAECLKLLLRGKASIEIANESGETPLDIAKRLKHEHCEELLTQALSGRFNSHVHVEYEWRLLHEDLDESDDDMDEKLQPSPNRREDRPISFYQLGSNQLQSNAVSLARDAANLAKEKQRAFMPSILQNETYGALLSGSPPPAQPAAPSTTSAPPLPPRNVGKVQTASSANTLWKTNSVSVDGGSRQRSSSDPPAVHPPLPPLRVTSTNPLTPTPPPPVAKTPSVMEALSQPSKPAPPGISQIRPPPLPPQPPSRLPQKKPAPGADKSTPLTNKGQPRGPVDLSATEALGPLSNAMVLQPPAPMPRKSQATKLKPKRVKALYNCVADNPDELTFSEGDVIIVDGEEDQEWWIGHIDGDPGRKGAFPVSFVHFIAD
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
59MalonylationYKMKKSVKAINSSGL
HHHHHHHHHHHCCCC
51.1126320211
75PhosphorylationHVENEEQYTQALEKF
CCCCHHHHHHHHHHH
12.2327642862
75 (in isoform 2)Nitration-12.23-
81UbiquitinationQYTQALEKFGGNCVC
HHHHHHHHHCCCEEE
50.5929967540
129PhosphorylationIISFPLDSLLKGDLK
HHHCCHHHHCCCCCC
43.1924719451
201PhosphorylationFQLQMCEYLLKVNEI
HHHHHHHHHHHHCCC
16.65-
212UbiquitinationVNEIKIKKGVDLLQN
HCCCCHHHHHHHHHH
68.58-
242UbiquitinationLKAVESLKPSIETLS
HHHHHHHCCHHHHHC
46.1029967540
242AcetylationLKAVESLKPSIETLS
HHHHHHHCCHHHHHC
46.1023954790
244PhosphorylationAVESLKPSIETLSTD
HHHHHCCHHHHHCCC
31.3121406692
247PhosphorylationSLKPSIETLSTDLHT
HHCCHHHHHCCCHHH
25.0821406692
249PhosphorylationKPSIETLSTDLHTIK
CCHHHHHCCCHHHHH
27.5621406692
250PhosphorylationPSIETLSTDLHTIKQ
CHHHHHCCCHHHHHH
45.7721406692
254PhosphorylationTLSTDLHTIKQAQDE
HHCCCHHHHHHCCHH
36.8521406692
274UbiquitinationIQLRDILKSALQVEQ
HHHHHHHHHHHCHHH
33.7329967540
282UbiquitinationSALQVEQKEDSQIRQ
HHHCHHHHHCHHHHH
50.4029967540
285PhosphorylationQVEQKEDSQIRQSTA
CHHHHHCHHHHHHHC
28.7128857561
290PhosphorylationEDSQIRQSTAYSLHQ
HCHHHHHHHCHHCCC
12.7328555341
293PhosphorylationQIRQSTAYSLHQPQG
HHHHHHCHHCCCCCC
16.3225159151
294PhosphorylationIRQSTAYSLHQPQGN
HHHHHCHHCCCCCCC
19.5325394399
311PhosphorylationHGTERNGSLYKKSDG
CCCCCCCCEEECCCC
31.8824719451
313PhosphorylationTERNGSLYKKSDGIR
CCCCCCEEECCCCHH
20.3329978859
321AcetylationKKSDGIRKVWQKRKC
ECCCCHHHHHHHCCC
46.006570287
325AcetylationGIRKVWQKRKCSVKN
CHHHHHHHCCCEEEC
37.816570225
329PhosphorylationVWQKRKCSVKNGFLT
HHHHCCCEEECCEEE
38.8822817900
336PhosphorylationSVKNGFLTISHGTAN
EEECCEEEEECCCCC
20.4122817900
338PhosphorylationKNGFLTISHGTANRP
ECCEEEEECCCCCCC
15.6122817900
405UbiquitinationEALNNAFKGDDNTGE
HHHHHHCCCCCCCCC
60.0529967540
546UbiquitinationKHADNAAKLHSLCEA
HHHCHHHHHHHHHHH
44.3029967540
549PhosphorylationDNAAKLHSLCEAVKT
CHHHHHHHHHHHHHH
45.1928857561
555UbiquitinationHSLCEAVKTRDIFGL
HHHHHHHHHHHHHHH
44.9129967540
556PhosphorylationSLCEAVKTRDIFGLL
HHHHHHHHHHHHHHH
27.29-
662UbiquitinationETPLDIAKRLKHEHC
CCHHHHHHHHCHHHH
59.6129967540
689PhosphorylationNSHVHVEYEWRLLHE
CCCCEEEEEEEHHHC
21.5027642862
701PhosphorylationLHEDLDESDDDMDEK
HHCCCCCCCCCHHHH
46.1129255136
712PhosphorylationMDEKLQPSPNRREDR
HHHHCCCCCCCCCCC
23.1123403867
722PhosphorylationRREDRPISFYQLGSN
CCCCCCCCEEECCCC
22.1526657352
724PhosphorylationEDRPISFYQLGSNQL
CCCCCCEEECCCCHH
8.9525106551
728PhosphorylationISFYQLGSNQLQSNA
CCEEECCCCHHHHHH
29.9629978859
737PhosphorylationQLQSNAVSLARDAAN
HHHHHHHHHHHHHHH
17.5624719451
756PhosphorylationKQRAFMPSILQNETY
HHHHHCCHHHCCCCH
24.9226356563
762PhosphorylationPSILQNETYGALLSG
CHHHCCCCHHHHHCC
34.5026356563
763PhosphorylationSILQNETYGALLSGS
HHHCCCCHHHHHCCC
8.3327259358
768PhosphorylationETYGALLSGSPPPAQ
CCHHHHHCCCCCCCC
37.7726356563
770PhosphorylationYGALLSGSPPPAQPA
HHHHHCCCCCCCCCC
30.7526356563
780PhosphorylationPAQPAAPSTTSAPPL
CCCCCCCCCCCCCCC
39.3226356563
781PhosphorylationAQPAAPSTTSAPPLP
CCCCCCCCCCCCCCC
24.5826356563
782PhosphorylationQPAAPSTTSAPPLPP
CCCCCCCCCCCCCCC
27.5126356563
783PhosphorylationPAAPSTTSAPPLPPR
CCCCCCCCCCCCCCC
38.5826356563
797PhosphorylationRNVGKVQTASSANTL
CCCCCEEECCCCCCE
31.3423312004
798 (in isoform 2)Phosphorylation-5.6126657352
799PhosphorylationVGKVQTASSANTLWK
CCCEEECCCCCCEEE
33.1128857561
800 (in isoform 2)Phosphorylation-24.0722199227
800PhosphorylationGKVQTASSANTLWKT
CCEEECCCCCCEEEC
24.0728857561
803PhosphorylationQTASSANTLWKTNSV
EECCCCCCEEECCEE
33.4428857561
807PhosphorylationSANTLWKTNSVSVDG
CCCCEEECCEEECCC
22.5728102081
809PhosphorylationNTLWKTNSVSVDGGS
CCEEECCEEECCCCC
22.4728857561
811PhosphorylationLWKTNSVSVDGGSRQ
EEECCEEECCCCCCC
17.8227535140
816PhosphorylationSVSVDGGSRQRSSSD
EEECCCCCCCCCCCC
30.6728102081
820PhosphorylationDGGSRQRSSSDPPAV
CCCCCCCCCCCCCCC
26.3430278072
821PhosphorylationGGSRQRSSSDPPAVH
CCCCCCCCCCCCCCC
40.7330278072
822PhosphorylationGSRQRSSSDPPAVHP
CCCCCCCCCCCCCCC
56.2230278072
837PhosphorylationPLPPLRVTSTNPLTP
CCCCCCEEECCCCCC
24.3328060719
838PhosphorylationLPPLRVTSTNPLTPT
CCCCCEEECCCCCCC
24.2728060719
839PhosphorylationPPLRVTSTNPLTPTP
CCCCEEECCCCCCCC
31.3324719451
843PhosphorylationVTSTNPLTPTPPPPV
EEECCCCCCCCCCCC
26.7728060719
845PhosphorylationSTNPLTPTPPPPVAK
ECCCCCCCCCCCCCC
43.1028985074
899PhosphorylationPAPGADKSTPLTNKG
CCCCCCCCCCCCCCC
35.4921406692
900PhosphorylationAPGADKSTPLTNKGQ
CCCCCCCCCCCCCCC
28.2321406692
903PhosphorylationADKSTPLTNKGQPRG
CCCCCCCCCCCCCCC
35.7721406692

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 ASAP2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ASAP2_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 ASAP2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PAXI_HUMANPXNphysical
10749932
FAK2_HUMANPTK2Bphysical
10022920
SRC_HUMANSRCphysical
10022920
SH3K1_HUMANSH3KBP1physical
25416956
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 ASAP2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-701 AND SER-822, ANDMASS SPECTROMETRY.
"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-701, AND MASSSPECTROMETRY.
"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-701, AND MASSSPECTROMETRY.

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