PSD4_HUMAN - dbPTM
PSD4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PSD4_HUMAN
UniProt AC Q8NDX1
Protein Name PH and SEC7 domain-containing protein 4
Gene Name PSD4
Organism Homo sapiens (Human).
Sequence Length 1056
Subcellular Localization Cell membrane . Cell projection, ruffle membrane . In interphase associated with the plasma membrane, in particular with membrane ruffling regions (PubMed:23603394). Accumulates in dynamic actin-rich membrane ruffles and microvilli-like structures (P
Protein Description Guanine nucleotide exchange factor for ARF6 and ARL14/ARF7. Through ARL14 activation, controls the movement of MHC class II-containing vesicles along the actin cytoskeleton in dendritic cells. Involved in membrane recycling. Interacts with several phosphatidylinositol phosphate species, including phosphatidylinositol 3,4-bisphosphate, phosphatidylinositol 3,5-bisphosphate and phosphatidylinositol 4,5-bisphosphate..
Protein Sequence MMGDYRLPDHPQPMEILNLYLGDSLEPHPGECPRETCSHEDPPEPFEEQTWATDPPEPTRQNVPPWGSGVELTHLGSWVHQDGLEPCQEQTRATDPPESTRQDAPPWGSGVELTHLGSPSAQREHRQNTASPGSPVNSHLPGSPKQNRSTSTQVVFWAGILQAQMCVLDLEEELEKTEGLKAGLKCCLPTPPVDLPGDTGLHSSPPENEDSGEDSSEPEGEGQAWLREGTPDSSPQWGAEEESMFFSNPLFLASPCSENSASGECFSWGASDSHAGVRTGPESPATLEPPLPEDTVLWELESEPDLGDGAAISGHCTPPFPVPIYKPHSICWASVAAAEGAPAAPPGHGESEGDRLGPAPSAAPCVDEALTWESGCVGSDLGPAAHPVQPWASLSPEGWQRGGPFWPQVTLNSQDRDEREGGHPQESLPCTLAPCPWRSPASSPEPSSPESESRGPGPRPSPASSQEGSPQLQHHSSGILPKWTLDASQSSLLETDGEQPSSLKKKEAGEAPKPGEEVKSEGTARPAETGDVQPDIHLTSAEHENLRTPMNSSWLPGSPMPQAQSPEEGQRPPAGDKLANGVRNNKVAWNLASRLYRLEGFRKSEVAAYLQKNNDFSRAVAEEYLSFFQFGGQSLDRALRSFLQALVLSGETQERERILYQFSRRFHHCNPGIFPSVDSVHTLTCAIMLLNTDLHGQNIGKSMSCQEFITNLNGLRDGGNFPKELLKALYWSIRSEKLEWAVDEEDTARPEKAQPSLPAGKMSKPFLQLAQDPTVPTYKQGILARKMHQDADGKKTPWGKRGWKMFHTLLRGMVLYFLKQGEDHCLEGESLVGQMVDEPVGVHHSLATPATHYTKKPHVFQLRTADWRLYLFQAPTAKEMSSWIARINLAAATHSAPPFPAAVGSQRRFVRPILPVGPAQSSLEEQHRSHENCLDAAADDLLDLQRNLPERRGRGRELEEHRLRKEYLEYEKTRYETYVQLLVARLHCPSDALDLWEEQLGREAGGTREPKLSLKKSHSSPSLHQDEAPTTAKVKRNISERRTYRKIIPKRNRNQL
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
20PhosphorylationPMEILNLYLGDSLEP
CHHHHHHHCCCCCCC
13.9427642862
24PhosphorylationLNLYLGDSLEPHPGE
HHHHCCCCCCCCCCC
32.6028348404
50PhosphorylationPEPFEEQTWATDPPE
CCCCCCCCCCCCCCC
21.98-
68PhosphorylationQNVPPWGSGVELTHL
CCCCCCCCCEEEEEC
35.4826074081
73PhosphorylationWGSGVELTHLGSWVH
CCCCEEEEECCCCHH
11.1026074081
77PhosphorylationVELTHLGSWVHQDGL
EEEEECCCCHHCCCC
32.0826657352
94PhosphorylationCQEQTRATDPPESTR
HHHHHCCCCCCCCCC
45.8326074081
99PhosphorylationRATDPPESTRQDAPP
CCCCCCCCCCCCCCC
34.3629978859
100PhosphorylationATDPPESTRQDAPPW
CCCCCCCCCCCCCCC
30.5929978859
109PhosphorylationQDAPPWGSGVELTHL
CCCCCCCCCCEEEEC
35.4823401153
114PhosphorylationWGSGVELTHLGSPSA
CCCCCEEEECCCHHH
11.1022115753
118PhosphorylationVELTHLGSPSAQREH
CEEEECCCHHHHHHH
23.2623401153
120PhosphorylationLTHLGSPSAQREHRQ
EEECCCHHHHHHHHH
38.4422115753
129PhosphorylationQREHRQNTASPGSPV
HHHHHHCCCCCCCCC
21.8522115753
131PhosphorylationEHRQNTASPGSPVNS
HHHHCCCCCCCCCHH
27.9623401153
134PhosphorylationQNTASPGSPVNSHLP
HCCCCCCCCCHHCCC
29.1123401153
138PhosphorylationSPGSPVNSHLPGSPK
CCCCCCHHCCCCCCC
27.0020164059
143PhosphorylationVNSHLPGSPKQNRST
CHHCCCCCCCCCCCC
27.3023401153
181UbiquitinationLEKTEGLKAGLKCCL
HHHCCCCCCCCCEEC
51.7929967540
230PhosphorylationQAWLREGTPDSSPQW
CCHHCCCCCCCCCCC
21.1226074081
233PhosphorylationLREGTPDSSPQWGAE
HCCCCCCCCCCCCCC
45.1626074081
234PhosphorylationREGTPDSSPQWGAEE
CCCCCCCCCCCCCCC
28.6126074081
254PhosphorylationSNPLFLASPCSENSA
CCCEEECCCCCCCCC
28.6926074081
257PhosphorylationLFLASPCSENSASGE
EEECCCCCCCCCCCC
43.1026074081
260PhosphorylationASPCSENSASGECFS
CCCCCCCCCCCCCCC
21.5426074081
271PhosphorylationECFSWGASDSHAGVR
CCCCCCCCCCCCCCC
35.3926074081
273PhosphorylationFSWGASDSHAGVRTG
CCCCCCCCCCCCCCC
16.8526074081
279PhosphorylationDSHAGVRTGPESPAT
CCCCCCCCCCCCCCC
55.4726074081
283PhosphorylationGVRTGPESPATLEPP
CCCCCCCCCCCCCCC
23.9826074081
286PhosphorylationTGPESPATLEPPLPE
CCCCCCCCCCCCCCC
34.7326074081
295PhosphorylationEPPLPEDTVLWELES
CCCCCCCCEEEEEEC
18.8126074081
317PhosphorylationAAISGHCTPPFPVPI
CEECCCCCCCCCCCC
28.4620058876
371PhosphorylationPCVDEALTWESGCVG
CCCCHHCCCCCCCCC
33.9528348404
374PhosphorylationDEALTWESGCVGSDL
CHHCCCCCCCCCCCC
29.1128348404
379PhosphorylationWESGCVGSDLGPAAH
CCCCCCCCCCCCCCC
14.8428348404
393PhosphorylationHPVQPWASLSPEGWQ
CCCCCCHHCCCCHHH
26.0526074081
395PhosphorylationVQPWASLSPEGWQRG
CCCCHHCCCCHHHCC
20.5726074081
410PhosphorylationGPFWPQVTLNSQDRD
CCCCCEEEECCCCCC
18.2523186163
413PhosphorylationWPQVTLNSQDRDERE
CCEEEECCCCCCCCC
36.2523917254
431PhosphorylationPQESLPCTLAPCPWR
CCCCCCCCEECCCCC
24.8228348404
439PhosphorylationLAPCPWRSPASSPEP
EECCCCCCCCCCCCC
22.4328348404
442PhosphorylationCPWRSPASSPEPSSP
CCCCCCCCCCCCCCC
50.2230108239
443PhosphorylationPWRSPASSPEPSSPE
CCCCCCCCCCCCCCC
35.0730108239
447PhosphorylationPASSPEPSSPESESR
CCCCCCCCCCCHHCC
57.7928192239
448PhosphorylationASSPEPSSPESESRG
CCCCCCCCCCHHCCC
43.3226657352
451PhosphorylationPEPSSPESESRGPGP
CCCCCCCHHCCCCCC
44.2330108239
453PhosphorylationPSSPESESRGPGPRP
CCCCCHHCCCCCCCC
52.3930108239
461PhosphorylationRGPGPRPSPASSQEG
CCCCCCCCCCCCCCC
34.0829978859
464PhosphorylationGPRPSPASSQEGSPQ
CCCCCCCCCCCCCCC
35.6228450419
465PhosphorylationPRPSPASSQEGSPQL
CCCCCCCCCCCCCCC
34.0628450419
469PhosphorylationPASSQEGSPQLQHHS
CCCCCCCCCCCCCCC
14.5528464451
476PhosphorylationSPQLQHHSSGILPKW
CCCCCCCCCCCCCEE
28.3028450419
477PhosphorylationPQLQHHSSGILPKWT
CCCCCCCCCCCCEEE
26.0428450419
484PhosphorylationSGILPKWTLDASQSS
CCCCCEEEECHHHHH
22.3829970186
488PhosphorylationPKWTLDASQSSLLET
CEEEECHHHHHHCCC
30.2022115753
490PhosphorylationWTLDASQSSLLETDG
EEECHHHHHHCCCCC
22.0630576142
491PhosphorylationTLDASQSSLLETDGE
EECHHHHHHCCCCCC
29.3622115753
495PhosphorylationSQSSLLETDGEQPSS
HHHHHCCCCCCCCCC
49.6430576142
501PhosphorylationETDGEQPSSLKKKEA
CCCCCCCCCCCHHHC
48.2529978859
502PhosphorylationTDGEQPSSLKKKEAG
CCCCCCCCCCHHHCC
51.3929978859
548PhosphorylationAEHENLRTPMNSSWL
HHCCCCCCCCCCCCC
30.01-
552PhosphorylationNLRTPMNSSWLPGSP
CCCCCCCCCCCCCCC
19.3519845377
553PhosphorylationLRTPMNSSWLPGSPM
CCCCCCCCCCCCCCC
27.8519845377
558PhosphorylationNSSWLPGSPMPQAQS
CCCCCCCCCCCCCCC
18.9819845377
565PhosphorylationSPMPQAQSPEEGQRP
CCCCCCCCCCCCCCC
36.9824850871
586UbiquitinationANGVRNNKVAWNLAS
HHCHHCCHHHHHHHH
36.56-
603UbiquitinationYRLEGFRKSEVAAYL
HHHHCCCHHHHHHHH
49.0229967540
604PhosphorylationRLEGFRKSEVAAYLQ
HHHCCCHHHHHHHHH
32.8030108239
609PhosphorylationRKSEVAAYLQKNNDF
CHHHHHHHHHHCCHH
10.4230108239
663PhosphorylationERILYQFSRRFHHCN
HHHHHHHHHHHHCCC
13.6624719451
723UbiquitinationRDGGNFPKELLKALY
CCCCCCCHHHHHHHH
57.7829967540
752UbiquitinationEDTARPEKAQPSLPA
CCCCCHHHCCCCCCC
55.8129967540
761AcetylationQPSLPAGKMSKPFLQ
CCCCCCCCCCHHHHH
41.9525953088
761UbiquitinationQPSLPAGKMSKPFLQ
CCCCCCCCCCHHHHH
41.9529967540
763PhosphorylationSLPAGKMSKPFLQLA
CCCCCCCCHHHHHHH
40.4328857561
764UbiquitinationLPAGKMSKPFLQLAQ
CCCCCCCHHHHHHHC
35.9729967540
779UbiquitinationDPTVPTYKQGILARK
CCCCCHHHHCHHHHH
44.5229967540
786UbiquitinationKQGILARKMHQDADG
HHCHHHHHCCCCCCC
34.8229967540
808PhosphorylationRGWKMFHTLLRGMVL
HHHHHHHHHHHHHHH
19.07-
816PhosphorylationLLRGMVLYFLKQGED
HHHHHHHHHHHCCCC
8.75-
870PhosphorylationRTADWRLYLFQAPTA
ECCCEEEEEEECCCH
9.2627461979
876PhosphorylationLYLFQAPTAKEMSSW
EEEEECCCHHHHHHH
54.0727461979
881PhosphorylationAPTAKEMSSWIARIN
CCCHHHHHHHHHHHH
24.5027461979
882PhosphorylationPTAKEMSSWIARINL
CCHHHHHHHHHHHHH
22.6127461979
905PhosphorylationPFPAAVGSQRRFVRP
CCCCCCCCCCCCEEE
17.5728857561
921PhosphorylationLPVGPAQSSLEEQHR
CCCCCCCCCHHHHHH
38.7127080861
922PhosphorylationPVGPAQSSLEEQHRS
CCCCCCCCHHHHHHC
27.9327080861
975PhosphorylationLEYEKTRYETYVQLL
HHHHHHHHHHHHHHH
20.18-
1013PhosphorylationGTREPKLSLKKSHSS
CCCCCCCCCCCCCCC
44.2430576142
1016UbiquitinationEPKLSLKKSHSSPSL
CCCCCCCCCCCCCCC
59.7129967540
1017PhosphorylationPKLSLKKSHSSPSLH
CCCCCCCCCCCCCCC
27.3223401153
1019PhosphorylationLSLKKSHSSPSLHQD
CCCCCCCCCCCCCCC
51.5423927012
1020PhosphorylationSLKKSHSSPSLHQDE
CCCCCCCCCCCCCCC
17.0623401153
1022PhosphorylationKKSHSSPSLHQDEAP
CCCCCCCCCCCCCCC
40.1923401153
1030PhosphorylationLHQDEAPTTAKVKRN
CCCCCCCCCHHHHCH
46.5723927012
1031PhosphorylationHQDEAPTTAKVKRNI
CCCCCCCCHHHHCHH
24.3424702127
1039PhosphorylationAKVKRNISERRTYRK
HHHHCHHHHHHCHHH
28.7126074081
1043PhosphorylationRNISERRTYRKIIPK
CHHHHHHCHHHHCCC
33.62-
1046UbiquitinationSERRTYRKIIPKRNR
HHHHCHHHHCCCCCC
34.28-

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 PSD4_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PSD4_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 PSD4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
USP9X_HUMANUSP9Xphysical
20339350

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 PSD4_HUMAN

loading...

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-491 AND SER-1019, ANDMASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129; SER-131 ANDSER-143, AND MASS SPECTROMETRY.

TOP