DP13A_HUMAN - dbPTM
DP13A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DP13A_HUMAN
UniProt AC Q9UKG1
Protein Name DCC-interacting protein 13-alpha
Gene Name APPL1
Organism Homo sapiens (Human).
Sequence Length 709
Subcellular Localization Early endosome membrane
Peripheral membrane protein . Nucleus . Early endosomal membrane-bound and nuclear. Translocated into the nucleus upon release from endosomal membranes following internalization of EGF.
Protein Description Adapter protein that interacts with proteins involved in different cellular signaling pathways. Required for the regulation of cell proliferation in response to extracellular signals from an early endosomal compartment. Links Rab5 to nuclear signal transduction. Involved in the regulation of the insulin receptor signaling pathway..
Protein Sequence MPGIDKLPIEETLEDSPQTRSLLGVFEEDATAISNYMNQLYQAMHRIYDAQNELSAATHLTSKLLKEYEKQRFPLGGDDEVMSSTLQQFSKVIDELSSCHAVLSTQLADAMMFPITQFKERDLKEILTLKEVFQIASNDHDAAINRYSRLSKKRENDKVKYEVTEDVYTSRKKQHQTMMHYFCALNTLQYKKKIALLEPLLGYMQAQISFFKMGSENLNEQLEEFLANIGTSVQNVRREMDSDIETMQQTIEDLEVASDPLYVPDPDPTKFPVNRNLTRKAGYLNARNKTGLVSSTWDRQFYFTQGGNLMSQARGDVAGGLAMDIDNCSVMAVDCEDRRYCFQITSFDGKKSSILQAESKKDHEEWICTINNISKQIYLSENPEETAARVNQSALEAVTPSPSFQQRHESLRPAAGQSRPPTARTSSSGSLGSESTNLAALSLDSLVAPDTPIQFDIISPVCEDQPGQAKAFGQGGRRTNPFGESGGSTKSETEDSILHQLFIVRFLGSMEVKSDDHPDVVYETMRQILAARAIHNIFRMTESHLLVTCDCLKLIDPQTQVTRLTFPLPCVVLYATHQENKRLFGFVLRTSSGRSESNLSSVCYIFESNNEGEKICDSVGLAKQIALHAELDRRASEKQKEIERVKEKQQKELNKQKQIEKDLEEQSRLIAASSRPNQASSEGQFVVLSSSQSEESDLGEGGKKRESEA
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
6Ubiquitination--MPGIDKLPIEETL
--CCCCCCCCCHHHH
55.0024816145
16PhosphorylationIEETLEDSPQTRSLL
CHHHHCCCCCHHHHH
14.9921815630
31PhosphorylationGVFEEDATAISNYMN
HCCHHHHHHHHHHHH
36.5227732954
34PhosphorylationEEDATAISNYMNQLY
HHHHHHHHHHHHHHH
21.3127732954
36PhosphorylationDATAISNYMNQLYQA
HHHHHHHHHHHHHHH
7.2227732954
41PhosphorylationSNYMNQLYQAMHRIY
HHHHHHHHHHHHHHH
5.6227732954
46UbiquitinationQLYQAMHRIYDAQNE
HHHHHHHHHHHHHHH
18.9721963094
49UbiquitinationQAMHRIYDAQNELSA
HHHHHHHHHHHHHHH
39.0321890473
53UbiquitinationRIYDAQNELSAATHL
HHHHHHHHHHHHHHH
31.8322817900
63AcetylationAATHLTSKLLKEYEK
HHHHHHHHHHHHHHH
53.2425953088
63UbiquitinationAATHLTSKLLKEYEK
HHHHHHHHHHHHHHH
53.2421963094
66UbiquitinationHLTSKLLKEYEKQRF
HHHHHHHHHHHHHCC
69.5527667366
70UbiquitinationKLLKEYEKQRFPLGG
HHHHHHHHHCCCCCC
45.9622817900
85PhosphorylationDDEVMSSTLQQFSKV
CHHHHHHHHHHHHHH
22.6822468782
97PhosphorylationSKVIDELSSCHAVLS
HHHHHHHHHCCHHHH
28.9522817900
98PhosphorylationKVIDELSSCHAVLST
HHHHHHHHCCHHHHH
23.6522817900
124UbiquitinationQFKERDLKEILTLKE
HCCCCCHHHHHCHHH
47.1729967540
130UbiquitinationLKEILTLKEVFQIAS
HHHHHCHHHHHHHHC
46.7429967540
160UbiquitinationKRENDKVKYEVTEDV
CCCCCCCCEEEEHHH
41.2429967540
161PhosphorylationRENDKVKYEVTEDVY
CCCCCCCEEEEHHHH
20.7227642862
258PhosphorylationIEDLEVASDPLYVPD
HHHHHHHCCCCCCCC
44.96-
263UbiquitinationVASDPLYVPDPDPTK
HHCCCCCCCCCCCCC
5.9727667366
272UbiquitinationDPDPTKFPVNRNLTR
CCCCCCCCCCCCHHH
24.8322053931
280UbiquitinationVNRNLTRKAGYLNAR
CCCCHHHHHCCCCCC
40.7127667366
289UbiquitinationGYLNARNKTGLVSST
CCCCCCCCCCCCCCC
38.1221890473
290PhosphorylationYLNARNKTGLVSSTW
CCCCCCCCCCCCCCC
39.0225394399
294PhosphorylationRNKTGLVSSTWDRQF
CCCCCCCCCCCCCEE
27.3925394399
295PhosphorylationNKTGLVSSTWDRQFY
CCCCCCCCCCCCEEE
26.4926846344
296PhosphorylationKTGLVSSTWDRQFYF
CCCCCCCCCCCEEEE
24.7126846344
311PhosphorylationTQGGNLMSQARGDVA
ECCCCHHHHHCCCCC
24.6925394399
333UbiquitinationDNCSVMAVDCEDRRY
CCCEEEEEECCCCEE
4.7022505724
343UbiquitinationEDRRYCFQITSFDGK
CCCEEEEEEEECCCC
34.1927667366
350AcetylationQITSFDGKKSSILQA
EEEECCCCCCCCEEC
51.8622361671
350UbiquitinationQITSFDGKKSSILQA
EEEECCCCCCCCEEC
51.8622505724
351UbiquitinationITSFDGKKSSILQAE
EEECCCCCCCCEECC
55.7729967540
352PhosphorylationTSFDGKKSSILQAES
EECCCCCCCCEECCC
26.54-
360UbiquitinationSILQAESKKDHEEWI
CCEECCCCCCCHHHE
54.4427667366
361UbiquitinationILQAESKKDHEEWIC
CEECCCCCCCHHHEE
73.8629967540
374PhosphorylationICTINNISKQIYLSE
EEEECCCCCEEEECC
22.1922817900
375UbiquitinationCTINNISKQIYLSEN
EEECCCCCEEEECCC
36.6029967540
378PhosphorylationNNISKQIYLSENPEE
CCCCCEEEECCCHHH
11.1529978859
386PhosphorylationLSENPEETAARVNQS
ECCCHHHHHHHHHHH
24.7728555341
393PhosphorylationTAARVNQSALEAVTP
HHHHHHHHHHHHHCC
29.6229255136
399PhosphorylationQSALEAVTPSPSFQQ
HHHHHHHCCCHHHHH
25.7029255136
401PhosphorylationALEAVTPSPSFQQRH
HHHHHCCCHHHHHHH
24.6619664994
403PhosphorylationEAVTPSPSFQQRHES
HHHCCCHHHHHHHHH
39.7729255136
410PhosphorylationSFQQRHESLRPAAGQ
HHHHHHHHHCCCCCC
24.4526657352
418PhosphorylationLRPAAGQSRPPTART
HCCCCCCCCCCCCCC
45.9225002506
422PhosphorylationAGQSRPPTARTSSSG
CCCCCCCCCCCCCCC
31.3026074081
425PhosphorylationSRPPTARTSSSGSLG
CCCCCCCCCCCCCCC
30.4227080861
426PhosphorylationRPPTARTSSSGSLGS
CCCCCCCCCCCCCCC
19.5627080861
427PhosphorylationPPTARTSSSGSLGSE
CCCCCCCCCCCCCCC
37.8024400094
428PhosphorylationPTARTSSSGSLGSES
CCCCCCCCCCCCCCH
31.9726074081
430PhosphorylationARTSSSGSLGSESTN
CCCCCCCCCCCCHHC
31.3529496963
433PhosphorylationSSSGSLGSESTNLAA
CCCCCCCCCHHCEEE
33.4029496963
435PhosphorylationSGSLGSESTNLAALS
CCCCCCCHHCEEEEC
25.0527080861
436PhosphorylationGSLGSESTNLAALSL
CCCCCCHHCEEEECC
30.1428464451
442PhosphorylationSTNLAALSLDSLVAP
HHCEEEECCCCCCCC
25.9627080861
445PhosphorylationLAALSLDSLVAPDTP
EEEECCCCCCCCCCC
30.0027080861
451PhosphorylationDSLVAPDTPIQFDII
CCCCCCCCCEEEEEE
22.6427080861
459PhosphorylationPIQFDIISPVCEDQP
CEEEEEEECCCCCCC
16.1822817900
473UbiquitinationPGQAKAFGQGGRRTN
CCCCCCCCCCCCCCC
30.0422817900
479PhosphorylationFGQGGRRTNPFGESG
CCCCCCCCCCCCCCC
45.9723312004
485PhosphorylationRTNPFGESGGSTKSE
CCCCCCCCCCCCCCC
49.1628348404
488PhosphorylationPFGESGGSTKSETED
CCCCCCCCCCCCCHH
35.8728348404
489PhosphorylationFGESGGSTKSETEDS
CCCCCCCCCCCCHHH
41.6924719451
490UbiquitinationGESGGSTKSETEDSI
CCCCCCCCCCCHHHH
48.2521906983
491PhosphorylationESGGSTKSETEDSIL
CCCCCCCCCCHHHHH
50.2522817900
493PhosphorylationGGSTKSETEDSILHQ
CCCCCCCCHHHHHHH
52.7828857561
496UbiquitinationTKSETEDSILHQLFI
CCCCCHHHHHHHHHH
22.3322817900
496PhosphorylationTKSETEDSILHQLFI
CCCCCHHHHHHHHHH
22.3323312004
509PhosphorylationFIVRFLGSMEVKSDD
HHHHHHCCCEECCCC
17.5729759185
513UbiquitinationFLGSMEVKSDDHPDV
HHCCCEECCCCCCHH
34.5621906983
514PhosphorylationLGSMEVKSDDHPDVV
HCCCEECCCCCCHHH
54.14-
522PhosphorylationDDHPDVVYETMRQIL
CCCCHHHHHHHHHHH
12.9125147952
524PhosphorylationHPDVVYETMRQILAA
CCHHHHHHHHHHHHH
10.44-
590PhosphorylationLFGFVLRTSSGRSES
EEEEEEECCCCCCCC
24.0827251275
591PhosphorylationFGFVLRTSSGRSESN
EEEEEECCCCCCCCC
25.1027251275
592PhosphorylationGFVLRTSSGRSESNL
EEEEECCCCCCCCCC
37.3027251275
595PhosphorylationLRTSSGRSESNLSSV
EECCCCCCCCCCCCE
49.2327251275
597PhosphorylationTSSGRSESNLSSVCY
CCCCCCCCCCCCEEE
44.3027251275
604PhosphorylationSNLSSVCYIFESNNE
CCCCCEEEEEECCCC
13.3922817900
621UbiquitinationKICDSVGLAKQIALH
EEHHHHCHHHHHHHH
5.1524816145
623UbiquitinationCDSVGLAKQIALHAE
HHHHCHHHHHHHHHH
47.4829967540
636PhosphorylationAELDRRASEKQKEIE
HHHHHHHHHHHHHHH
43.4427251275
638UbiquitinationLDRRASEKQKEIERV
HHHHHHHHHHHHHHH
65.2624816145
644UbiquitinationEKQKEIERVKEKQQK
HHHHHHHHHHHHHHH
50.9322053931
655UbiquitinationKQQKELNKQKQIEKD
HHHHHHHHHHHHHHH
72.0624816145
661UbiquitinationNKQKQIEKDLEEQSR
HHHHHHHHHHHHHHH
70.0621890473
673PhosphorylationQSRLIAASSRPNQAS
HHHHHHHHCCCCCCC
20.1829978859
674PhosphorylationSRLIAASSRPNQASS
HHHHHHHCCCCCCCC
47.2123312004
680PhosphorylationSSRPNQASSEGQFVV
HCCCCCCCCCCCEEE
21.1123312004
681PhosphorylationSRPNQASSEGQFVVL
CCCCCCCCCCCEEEE
49.0829978859
689PhosphorylationEGQFVVLSSSQSEES
CCCEEEEECCCCCCC
19.1426657352
690PhosphorylationGQFVVLSSSQSEESD
CCEEEEECCCCCCCC
28.3828464451
691PhosphorylationQFVVLSSSQSEESDL
CEEEEECCCCCCCCC
34.0617525332
693PhosphorylationVVLSSSQSEESDLGE
EEEECCCCCCCCCCC
45.3325849741
696PhosphorylationSSSQSEESDLGEGGK
ECCCCCCCCCCCCCC
33.8030576142
703UbiquitinationSDLGEGGKKRESEA-
CCCCCCCCCCCCCC-
60.5632015554

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
410SPhosphorylationKinasePRKACAP17612
GPS
410SPhosphorylationKinasePKA-Uniprot
430SPhosphorylationKinasePRKCAP17252
GPS
430SPhosphorylationKinasePKCAP20444
PSP
-KUbiquitinationE3 ubiquitin ligaseNEDD4P46934
PMID:21320486

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
410SPhosphorylation

17765681

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 DP13A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DP13B_HUMANAPPL2physical
16189514
AKT2_HUMANAKT2physical
10490823
DCC_HUMANDCCphysical
12011067
MTA2_HUMANMTA2physical
19686092
HDAC1_HUMANHDAC1physical
19686092
HDAC2_HUMANHDAC2physical
19686092
RBBP4_HUMANRBBP4physical
19686092
RBBP7_HUMANRBBP7physical
19686092
RUVB2_HUMANRUVBL2physical
19433865
MTA2_HUMANMTA2physical
15016378
RBBP7_HUMANRBBP7physical
15016378
FSHR_HUMANFSHRphysical
15070827
PAQR1_HUMANADIPOR1physical
16622416
RAB5A_HUMANRAB5Aphysical
16622416
DP13B_HUMANAPPL2physical
17030088
AKT2_HUMANAKT2physical
17030088
DP13A_HUMANAPPL1physical
17581628
P85A_HUMANPIK3R1physical
12621049
AKT1_HUMANAKT1physical
12621049
ANDR_HUMANARphysical
12621049
HDAC3_HUMANHDAC3physical
23752268
PAQR1_HUMANADIPOR1physical
23762377
TRAF6_HUMANTRAF6physical
23909487
DPYL5_HUMANDPYSL5physical
21988832
KXDL1_HUMANKXD1physical
21988832
CKLF4_HUMANCMTM4physical
21988832
K1468_HUMANKIAA1468physical
22863883
TTC4_HUMANTTC4physical
22863883
DP13A_HUMANAPPL1physical
25416956
DP13B_HUMANAPPL2physical
25416956
UBE2O_HUMANUBE2Ophysical
25416956
REBL1_HUMANRHEBL1physical
25416956
BATF3_HUMANBATF3physical
25814554
BRWD1_HUMANBRWD1physical
25814554
RTCB_HUMANRTCBphysical
25814554
DOK3_HUMANDOK3physical
25814554
DOK7_HUMANDOK7physical
25814554
IN80E_HUMANINO80Ephysical
25814554
KLF15_HUMANKLF15physical
25814554
MAGC3_HUMANMAGEC3physical
25814554
ZN829_HUMANZNF829physical
25814554
CBL_HUMANCBLphysical
25814554
CBLB_HUMANCBLBphysical
25814554
DOK2_HUMANDOK2physical
25814554
ID1_HUMANID1physical
25814554
P85A_HUMANPIK3R1physical
25814554
SH22A_HUMANSH2D2Aphysical
25814554
SOCS6_HUMANSOCS6physical
25814554
SCAPE_HUMANSCAPERphysical
25814554
AKT1_HUMANAKT1physical
25814554
P85B_HUMANPIK3R2physical
25814554
P53_HUMANTP53physical
25814554
HDAC1_HUMANHDAC1physical
25241761
TRAF2_HUMANTRAF2physical
25241761
PK3CA_HUMANPIK3CAphysical
25241761
AKT1_HUMANAKT1physical
25241761
TGFR1_HUMANTGFBR1physical
26583432
KPCZ_HUMANPRKCZphysical
26583432
TBB3_HUMANTUBB3physical
26583432
ZN830_HUMANZNF830physical
28514442

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 DP13A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401, 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 THR-399 AND SER-401, ANDMASS SPECTROMETRY.
"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-691, AND MASSSPECTROMETRY.
"A role of the Lowe syndrome protein OCRL in early steps of theendocytic pathway.";
Erdmann K.S., Mao Y., McCrea H.J., Zoncu R., Lee S., Paradise S.,Modregger J., Biemesderfer D., Toomre D., De Camilli P.;
Dev. Cell 13:377-390(2007).
Cited for: INTERACTION WITH OCRL, F&H MOTIF, AND PHOSPHORYLATION AT SER-410.

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