GAPD1_MOUSE - dbPTM
GAPD1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GAPD1_MOUSE
UniProt AC Q6PAR5
Protein Name GTPase-activating protein and VPS9 domain-containing protein 1
Gene Name Gapvd1
Organism Mus musculus (Mouse).
Sequence Length 1458
Subcellular Localization Membrane
Peripheral membrane protein . Endosome. Recruited to the plasma membrane by TRIP10/CIP4 in response to insulin.
Protein Description Acts both as a GTPase-activating protein (GAP) and a guanine nucleotide exchange factor (GEF), and participates in various processes such as endocytosis, insulin receptor internalization or LC2A4/GLUT4 trafficking. Acts as a GEF for the Ras-related protein RAB31 by exchanging bound GDP for free GTP, leading to regulate LC2A4/GLUT4 trafficking. In the absence of insulin, it maintains RAB31 in an active state and promotes a futile cycle between LC2A4/GLUT4 storage vesicles and early endosomes, retaining LC2A4/GLUT4 inside the cells. Upon insulin stimulation, it is translocated to the plasma membrane, releasing LC2A4/GLUT4 from intracellular storage vesicles. Also involved in EGFR trafficking and degradation, possibly by promoting EGFR ubiquitination and subsequent degradation by the proteasome. Has GEF activity for Rab5 and GAP activity for Ras..
Protein Sequence MVKLDIHTLAHHLKQERLYVSSEKQLIQRLNADVLKTAEKLYRTAWIAKQQRINLDRLIITSAEASPAECCQHAKILEDTQFVDGYKQLGFQETAYGEFLSRLRENPRLIASSLVAGEKLNQENTQSVIYTVFTSLYGNCIMQEDESYLLQVLRYLIEFELKESDNPRRLLRRGTCAFSILFKLFSEGLFSAKLFLTATLHEPIMQLLVEDEDHLETDPNKLIERFSPAQQEKLFGEKGSDRFRQKVQEMVDSNEAKLVALVNKFIGYLKQNTYCFPHSLRWIVSQMYKTLSCVDRLEVGEVRAMCTDLLLACFICPAVVNPEQYGIISDAPINEVARFNLMQVGRLLQQLAMTGTEEGDPRTKNSLGKFDKGCVAAFLDVVIGGRAVETPPMSSVNLLEGLSRTVVYISYSQLITLVNFMKSVMSGDQLKEDRMALDNLLANLPQAKPGKSSSLDMTPYSTPQMSPATTPANKKNRLPIATRSRSRSNMLMDLHMDHEGSSQETIQEVQPEEVLVISLGTGPQLTPGMMSENEVLNMQLSDGGQGDVPVDENKLHGKPDKTLRFSLCSDNLEGISEGPSNRSNSVSSLDLEGESVSELGAGPSGSNGVEALQLLEHEQATTQDNLDDKLRKFEIRDMMGLTDDRDISETVSETWSTDVLGSDFDPNVDEDRLQEIAGAAAENVLGSLLCLPGSGSVLLDPCTGSTISETTSEAWSVEVLPSDSEAPDLKQEERLQELESCSGLGSTSDDTDVREVSSRPSTPGLSVVSGISATSEDIPNKIEDLRSECSSDFGGKDSVTSPDMDDIAHGAHQLTSPPSQSESLLAMFDPLSSHEGASAVVRPKVHYARPSHPPPDPPILEGAVGGNEARLPNFGSHVLTAAEMEAFKQRHSYPERLVRSRSSDIVSSVRRPMSDPSWNRRPGNEELPPAAATGATSLVAAPHSSSSSPSKDSSRGETEERKDSDDERSDRSRPWWRKRFVSAMPKAPIPFRKKEKQEKDKDDLGPDRFSTLTDEPSPRLSAQAQVAEDILDKYRNAIKRTSPSEGAMANDESAEVMGDGESAHDSPREEALQNISADDLPDSASQAAHPQDSAFSYRDVKKKLRLALCSADSVAFPVLTHSTRNGLPDHTDPEDNEIVCFLKVQIAEAINLQDKSLMAQLQETMRCVCRFDNRTCRKLLASIAEDYRKRAPYIAYLTRCRQGLQTTQAHLERLLQRVLRDKEVANRYFTTVCVRLLLESKEKKIREFIQDFQKLTAADDKTAQVEDFLQFLYGVMAQDVIWQNASEEQLQDAQLAIERSVMNRIFKLAFYPNQDGDILRDQVLHEHIQRLSKVVTANHRALQIPEVYLREAPWPSAQSEIRTISAYKTPRDKVQCILRMCSTIMNLLSLANEDSVPGADDFVPVLVFVLIKANPPCLLSTVQYISSFYASCLSGEESYWWMQFTAAVEFIKTIDDRK
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
24UbiquitinationRLYVSSEKQLIQRLN
HHCCCCHHHHHHHHC
52.9622790023
24 (in isoform 4)Ubiquitination-52.9622790023
36UbiquitinationRLNADVLKTAEKLYR
HHCHHHHHHHHHHHH
45.6027667366
49UbiquitinationYRTAWIAKQQRINLD
HHHHHHHHHHCCCCC
37.5222790023
49 (in isoform 4)Ubiquitination-37.5222790023
71S-nitrosocysteineEASPAECCQHAKILE
CCCHHHHHHHHHHCC
2.21-
71S-nitrosylationEASPAECCQHAKILE
CCCHHHHHHHHHHCC
2.2120925432
227PhosphorylationNKLIERFSPAQQEKL
HHHHHHCCHHHHHHH
26.08-
233UbiquitinationFSPAQQEKLFGEKGS
CCHHHHHHHHCCCCC
44.7927667366
270AcetylationNKFIGYLKQNTYCFP
HHHHHHHHHCCCCCH
32.7722826441
390PhosphorylationIGGRAVETPPMSSVN
ECCCCCCCCCCCHHH
26.5422817900
452PhosphorylationPQAKPGKSSSLDMTP
CCCCCCCCCCCCCCC
30.9526239621
453PhosphorylationQAKPGKSSSLDMTPY
CCCCCCCCCCCCCCC
38.1026239621
454PhosphorylationAKPGKSSSLDMTPYS
CCCCCCCCCCCCCCC
35.1627742792
458PhosphorylationKSSSLDMTPYSTPQM
CCCCCCCCCCCCCCC
20.8125521595
460PhosphorylationSSLDMTPYSTPQMSP
CCCCCCCCCCCCCCC
18.9328833060
461PhosphorylationSLDMTPYSTPQMSPA
CCCCCCCCCCCCCCC
34.5128833060
462PhosphorylationLDMTPYSTPQMSPAT
CCCCCCCCCCCCCCC
16.2328833060
466PhosphorylationPYSTPQMSPATTPAN
CCCCCCCCCCCCCCC
13.2127087446
466 (in isoform 4)Phosphorylation-13.2129514104
469PhosphorylationTPQMSPATTPANKKN
CCCCCCCCCCCCCCC
36.3728833060
470PhosphorylationPQMSPATTPANKKNR
CCCCCCCCCCCCCCC
23.6228833060
482PhosphorylationKNRLPIATRSRSRSN
CCCCCCCCCCCCCCC
29.8728725479
562PhosphorylationLHGKPDKTLRFSLCS
CCCCCCCCEEEEEEC
30.4625619855
566PhosphorylationPDKTLRFSLCSDNLE
CCCCEEEEEECCCCC
23.2521082442
569PhosphorylationTLRFSLCSDNLEGIS
CEEEEEECCCCCCCC
34.5225521595
576PhosphorylationSDNLEGISEGPSNRS
CCCCCCCCCCCCCCC
47.5625293948
580PhosphorylationEGISEGPSNRSNSVS
CCCCCCCCCCCCCCC
56.5925293948
740PhosphorylationERLQELESCSGLGST
HHHHHHHHCCCCCCC
26.6325521595
742PhosphorylationLQELESCSGLGSTSD
HHHHHHCCCCCCCCC
46.4627742792
746PhosphorylationESCSGLGSTSDDTDV
HHCCCCCCCCCCCCH
29.7625521595
747PhosphorylationSCSGLGSTSDDTDVR
HCCCCCCCCCCCCHH
34.0827087446
748PhosphorylationCSGLGSTSDDTDVRE
CCCCCCCCCCCCHHH
34.8827742792
751PhosphorylationLGSTSDDTDVREVSS
CCCCCCCCCHHHHHC
41.1925619855
757PhosphorylationDTDVREVSSRPSTPG
CCCHHHHHCCCCCCC
18.8425521595
758PhosphorylationTDVREVSSRPSTPGL
CCHHHHHCCCCCCCC
54.0825521595
761PhosphorylationREVSSRPSTPGLSVV
HHHHCCCCCCCCEEE
46.2325521595
762PhosphorylationEVSSRPSTPGLSVVS
HHHCCCCCCCCEEEE
24.8625521595
766PhosphorylationRPSTPGLSVVSGISA
CCCCCCCEEEECCCC
26.7927087446
769PhosphorylationTPGLSVVSGISATSE
CCCCEEEECCCCCCC
28.4020469934
772PhosphorylationLSVVSGISATSEDIP
CEEEECCCCCCCCCC
29.0825159016
774PhosphorylationVVSGISATSEDIPNK
EEECCCCCCCCCCHH
26.3425159016
775PhosphorylationVSGISATSEDIPNKI
EECCCCCCCCCCHHH
32.7525159016
787PhosphorylationNKIEDLRSECSSDFG
HHHHHHHHHHCCCCC
50.6925521595
790PhosphorylationEDLRSECSSDFGGKD
HHHHHHHCCCCCCCC
28.9625521595
791PhosphorylationDLRSECSSDFGGKDS
HHHHHHCCCCCCCCC
48.9329233185
847PhosphorylationVVRPKVHYARPSHPP
EECCCCCCCCCCCCC
13.8028285833
871PhosphorylationVGGNEARLPNFGSHV
CCCCCCCCCCCHHHH
5.3924719451
876PhosphorylationARLPNFGSHVLTAAE
CCCCCCHHHHHHHHH
13.29-
892PhosphorylationEAFKQRHSYPERLVR
HHHHHHHCCHHHHHH
44.5730635358
893PhosphorylationAFKQRHSYPERLVRS
HHHHHHCCHHHHHHC
11.7329899451
900PhosphorylationYPERLVRSRSSDIVS
CHHHHHHCCCCCHHH
29.0927087446
902PhosphorylationERLVRSRSSDIVSSV
HHHHHCCCCCHHHHC
33.3427087446
903PhosphorylationRLVRSRSSDIVSSVR
HHHHCCCCCHHHHCC
30.1925521595
907PhosphorylationSRSSDIVSSVRRPMS
CCCCCHHHHCCCCCC
24.3725619855
908PhosphorylationRSSDIVSSVRRPMSD
CCCCHHHHCCCCCCC
14.5621082442
914PhosphorylationSSVRRPMSDPSWNRR
HHCCCCCCCCCCCCC
49.4030635358
917PhosphorylationRRPMSDPSWNRRPGN
CCCCCCCCCCCCCCC
41.8129472430
933PhosphorylationELPPAAATGATSLVA
CCCHHHHCCCCEEEE
23.7125777480
936PhosphorylationPAAATGATSLVAAPH
HHHHCCCCEEEECCC
24.7625293948
937PhosphorylationAAATGATSLVAAPHS
HHHCCCCEEEECCCC
21.9525293948
943PhosphorylationTSLVAAPHSSSSSPS
CEEEECCCCCCCCCC
35.2724719451
944PhosphorylationSLVAAPHSSSSSPSK
EEEECCCCCCCCCCC
30.7525266776
945PhosphorylationLVAAPHSSSSSPSKD
EEECCCCCCCCCCCC
31.0727742792
946PhosphorylationVAAPHSSSSSPSKDS
EECCCCCCCCCCCCC
37.5427742792
947PhosphorylationAAPHSSSSSPSKDSS
ECCCCCCCCCCCCCC
48.4927742792
948PhosphorylationAPHSSSSSPSKDSSR
CCCCCCCCCCCCCCC
34.8330372032
950PhosphorylationHSSSSSPSKDSSRGE
CCCCCCCCCCCCCCC
51.5527742792
953PhosphorylationSSSPSKDSSRGETEE
CCCCCCCCCCCCCCC
26.1827742792
954PhosphorylationSSPSKDSSRGETEER
CCCCCCCCCCCCCCC
55.2127742792
958PhosphorylationKDSSRGETEERKDSD
CCCCCCCCCCCCCCC
46.0721454597
964PhosphorylationETEERKDSDDERSDR
CCCCCCCCCCCCCCC
50.4226824392
969PhosphorylationKDSDDERSDRSRPWW
CCCCCCCCCCCCHHH
35.0123140645
982PhosphorylationWWRKRFVSAMPKAPI
HHHHHHHHHCCCCCC
19.01-
1010PhosphorylationDLGPDRFSTLTDEPS
CCCCCHHHHCCCCCC
24.3318846507
1011PhosphorylationLGPDRFSTLTDEPSP
CCCCHHHHCCCCCCH
30.8518846507
1013PhosphorylationPDRFSTLTDEPSPRL
CCHHHHCCCCCCHHH
38.1025619855
1017PhosphorylationSTLTDEPSPRLSAQA
HHCCCCCCHHHHHHH
22.1726824392
1021PhosphorylationDEPSPRLSAQAQVAE
CCCCHHHHHHHHHHH
21.4418846507
1041PhosphorylationYRNAIKRTSPSEGAM
HHHHHHHCCCCCCCC
39.7328833060
1041 (in isoform 6)Phosphorylation-39.7329895711
1042PhosphorylationRNAIKRTSPSEGAMA
HHHHHHCCCCCCCCC
30.3823684622
1042 (in isoform 6)Phosphorylation-30.3829895711
1044PhosphorylationAIKRTSPSEGAMAND
HHHHCCCCCCCCCCC
48.7223684622
1044 (in isoform 6)Phosphorylation-48.7229895711
1053PhosphorylationGAMANDESAEVMGDG
CCCCCCCCCCCCCCC
32.3728833060
1053 (in isoform 6)Phosphorylation-32.3729895711
1061 (in isoform 6)Phosphorylation-49.8729895711
1062PhosphorylationEVMGDGESAHDSPRE
CCCCCCCCCCCCHHH
36.1128833060
1066PhosphorylationDGESAHDSPREEALQ
CCCCCCCCHHHHHHH
18.9128833060
1076PhosphorylationEEALQNISADDLPDS
HHHHHCCCHHHCCCC
32.9425293948
1083PhosphorylationSADDLPDSASQAAHP
CHHHCCCCHHHCCCC
28.0723737553
1085PhosphorylationDDLPDSASQAAHPQD
HHCCCCHHHCCCCCC
25.0525521595
1093PhosphorylationQAAHPQDSAFSYRDV
HCCCCCCCCCCHHHH
26.4323737553
1096PhosphorylationHPQDSAFSYRDVKKK
CCCCCCCCHHHHHHH
20.9823737553
1097PhosphorylationPQDSAFSYRDVKKKL
CCCCCCCHHHHHHHH
12.3623737553
1241AcetylationVRLLLESKEKKIREF
HHHHHHCHHHHHHHH
65.2623864654
1243AcetylationLLLESKEKKIREFIQ
HHHHCHHHHHHHHHH
58.1823864654
1307UbiquitinationSVMNRIFKLAFYPNQ
HHHHHHHHHHCCCCC
36.2122790023
1307 (in isoform 4)Ubiquitination-36.2122790023
1313 (in isoform 4)Ubiquitination-40.99-

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
902SPhosphorylationKinaseAMPKA1Q13131
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GAPD1_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 GAPD1_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of GAPD1_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GAPD1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-902, 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-903 AND 1085, AND MASSSPECTROMETRY.

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