MYO5B_HUMAN - dbPTM
MYO5B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MYO5B_HUMAN
UniProt AC Q9ULV0
Protein Name Unconventional myosin-Vb
Gene Name MYO5B
Organism Homo sapiens (Human).
Sequence Length 1848
Subcellular Localization Cytoplasm .
Protein Description May be involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation. Required in a complex with RAB11A and RAB11FIP2 for the transport of NPC1L1 to the plasma membrane. Together with RAB11A participates in CFTR trafficking to the plasma membrane and TF (transferrin) recycling in nonpolarized cells. Together with RAB11A and RAB8A participates in epithelial cell polarization. Together with RAB25 regulates transcytosis..
Protein Sequence MSVGELYSQCTRVWIPDPDEVWRSAELTKDYKEGDKSLQLRLEDETILEYPIDVQRNQLPFLRNPDILVGENDLTALSYLHEPAVLHNLKVRFLESNHIYTYCGIVLVAINPYEQLPIYGQDVIYTYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIVSGESGAGKTVSAKYAMRYFATVGGSASETNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKYIQIGFDKRYHIIGANMRTYLLEKSRVVFQADDERNYHIFYQLCAAAGLPEFKELALTSAEDFFYTSQGGDTSIEGVDDAEDFEKTRQAFTLLGVKESHQMSIFKIIASILHLGSVAIQAERDGDSCSISPQDVYLSNFCRLLGVEHSQMEHWLCHRKLVTTSETYVKTMSLQQVINARNALAKHIYAQLFGWIVEHINKALHTSLKQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNSHVFKLEQEEYMKEQIPWTLIDFYDNQPCIDLIEAKLGILDLLDEECKVPKGTDQNWAQKLYDRHSSSQHFQKPRMSNTAFIIVHFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFHDDKDPVPATTPGKGSSSKISVRSARPPMKVSNKEHKKTVGHQFRTSLHLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWAYHDFFNRYRVLVKKRELANTDKKAICRSVLENLIKDPDKFQFGRTKIFFRAGQVAYLEKLRADKFRTATIMIQKTVRGWLQKVKYHRLKGATLTLQRYCRGHLARRLAEHLRRIRAAVVLQKHYRMQRARQAYQRVRRAAVVIQAFTRAMFVRRTYRQVLMEHKATTIQKHVRGWMARRHFQRLRDAAIVIQCAFRMLKARRELKALRIEARSAEHLKRLNVGMENKVVQLQRKIDEQNKEFKTLSEQLSVTTSTYTMEVERLKKELVHYQQSPGEDTSLRLQEEVESLRTELQRAHSERKILEDAHSREKDELRKRVADLEQENALLKDEKEQLNNQILCQSKDEFAQNSVKENLMKKELEEERSRYQNLVKEYSQLEQRYDNLRDEMTIIKQTPGHRRNPSNQSSLESDSNYPSISTSEIGDTEDALQQVEEIGLEKAAMDMTVFLKLQKRVRELEQERKKLQVQLEKREQQDSKKVQAEPPQTDIDLDPNADLAYNSLKRQELESENKKLKNDLNELRKAVADQATQNNSSHGSPDSYSLLLNQLKLAHEELEVRKEEVLILRTQIVSADQRRLAGRNAEPNINARSSWPNSEKHVDQEDAIEAYHGVCQTNSKTEDWGYLNEDGELGLAYQGLKQVARLLEAQLQAQSLEHEEEVEHLKAQLEALKEEMDKQQQTFCQTLLLSPEAQVEFGVQQEISRLTNENLDLKELVEKLEKNERKLKKQLKIYMKKAQDLEAAQALAQSERKRHELNRQVTVQRKEKDFQGMLEYHKEDEALLIRNLVTDLKPQMLSGTVPCLPAYILYMCIRHADYTNDDLKVHSLLTSTINGIKKVLKKHNDDFEMTSFWLSNTCRLLHCLKQYSGDEGFMTQNTAKQNEHCLKNFDLTEYRQVLSDLSIQIYQQLIKIAEGVLQPMIVSAMLENESIQGLSGVKPTGYRKRSSSMADGDNSYCLEAIIRQMNAFHTVMCDQGLDPEIILQVFKQLFYMINAVTLNNLLLRKDVCSWSTGMQLRYNISQLEEWLRGRNLHQSGAVQTMEPLIQAAQLLQLKKKTQEDAEAICSLCTSLSTQQIVKILNLYTPLNEFEERVTVAFIRTIQAQLQERNDPQQLLLDAKHMFPVLFPFNPSSLTMDSIHIPACLNLEFLNEV
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
1 (in isoform 3)Acetylation-34.1222814378
2Phosphorylation------MSVGELYSQ
------CCHHHHHHH
50.5727251275
169UbiquitinationSGESGAGKTVSAKYA
ECCCCCCCCHHHHHH
45.26-
170PhosphorylationGESGAGKTVSAKYAM
CCCCCCCCHHHHHHH
20.8320068231
172PhosphorylationSGAGKTVSAKYAMRY
CCCCCCHHHHHHHHH
25.0320068231
175PhosphorylationGKTVSAKYAMRYFAT
CCCHHHHHHHHHHHC
12.8330177828
179PhosphorylationSAKYAMRYFATVGGS
HHHHHHHHHHCCCCC
5.6330177828
182PhosphorylationYAMRYFATVGGSASE
HHHHHHHCCCCCCCC
15.1330177828
186PhosphorylationYFATVGGSASETNIE
HHHCCCCCCCCCCHH
23.7730177828
188PhosphorylationATVGGSASETNIEEK
HCCCCCCCCCCHHHH
46.8030177828
190PhosphorylationVGGSASETNIEEKVL
CCCCCCCCCHHHHHH
38.7130177828
199PhosphorylationIEEKVLASSPIMEAI
HHHHHHHCCHHHHHH
32.2721406692
200PhosphorylationEEKVLASSPIMEAIG
HHHHHHCCHHHHHHC
16.9121406692
211PhosphorylationEAIGNAKTTRNDNSS
HHHCCCCCCCCCCCC
28.6920068231
212PhosphorylationAIGNAKTTRNDNSSR
HHCCCCCCCCCCCCC
27.1120068231
217PhosphorylationKTTRNDNSSRFGKYI
CCCCCCCCCCCEEEE
26.2529514088
218PhosphorylationTTRNDNSSRFGKYIQ
CCCCCCCCCCEEEEE
37.5729514088
222AcetylationDNSSRFGKYIQIGFD
CCCCCCEEEEEEECC
36.1522424773
241PhosphorylationIIGANMRTYLLEKSR
EECCCHHHHHHHHCE
14.0429083192
242PhosphorylationIGANMRTYLLEKSRV
ECCCHHHHHHHHCEE
10.0229083192
246UbiquitinationMRTYLLEKSRVVFQA
HHHHHHHHCEEEEEC
43.46-
247PhosphorylationRTYLLEKSRVVFQAD
HHHHHHHCEEEEECC
22.4129083192
313PhosphorylationEKTRQAFTLLGVKES
HHHHHHHHHHCCCHH
24.8824719451
324PhosphorylationVKESHQMSIFKIIAS
CCHHHHHHHHHHHHH
20.5024719451
383PhosphorylationLCHRKLVTTSETYVK
HHCCCCCCCCHHHHH
34.73-
478PhosphorylationFKLEQEEYMKEQIPW
HHHHHHHHHHHHCCC
16.8530177828
544PhosphorylationHFQKPRMSNTAFIIV
CCCCCCCCCCEEEEE
32.1021406692
546PhosphorylationQKPRMSNTAFIIVHF
CCCCCCCCEEEEEEE
18.6821406692
559PhosphorylationHFADKVEYLSDGFLE
EEHHHHHHCCCCHHH
17.9422817900
561PhosphorylationADKVEYLSDGFLEKN
HHHHHHCCCCHHHHC
34.4820068231
602PhosphorylationDKDPVPATTPGKGSS
CCCCCCCCCCCCCCC
27.7027050516
603PhosphorylationKDPVPATTPGKGSSS
CCCCCCCCCCCCCCC
31.9529496963
608PhosphorylationATTPGKGSSSKISVR
CCCCCCCCCCCEEEC
34.6221712546
609PhosphorylationTTPGKGSSSKISVRS
CCCCCCCCCCEEECC
44.3021712546
610PhosphorylationTPGKGSSSKISVRSA
CCCCCCCCCEEECCC
35.3921712546
613PhosphorylationKGSSSKISVRSARPP
CCCCCCEEECCCCCC
18.4024719451
650PhosphorylationLMETLNATTPHYVRC
HHHHHCCCCCCEEEE
39.52-
694PhosphorylationIRISAAGYPSRWAYH
EEHHCCCCCCCHHHH
8.0317053785
727PhosphorylationDKKAICRSVLENLIK
CHHHHHHHHHHHHCC
27.0027251275
744PhosphorylationDKFQFGRTKIFFRAG
CCCCCCCEEEEEECC
28.95-
755PhosphorylationFRAGQVAYLEKLRAD
EECCHHHHHHHHCCC
19.28-
865PhosphorylationVLMEHKATTIQKHVR
HHHHHHCHHHHHHHH
29.2726270265
866PhosphorylationLMEHKATTIQKHVRG
HHHHHCHHHHHHHHH
26.6926270265
912PhosphorylationALRIEARSAEHLKRL
HHHHHHHCHHHHHHC
45.09-
943PhosphorylationEQNKEFKTLSEQLSV
HCHHHHHHHHHHHHC
40.62-
945PhosphorylationNKEFKTLSEQLSVTT
HHHHHHHHHHHHCEE
28.64-
949PhosphorylationKTLSEQLSVTTSTYT
HHHHHHHHCEECEEH
19.6727251275
956PhosphorylationSVTTSTYTMEVERLK
HCEECEEHHHHHHHH
13.62-
969PhosphorylationLKKELVHYQQSPGED
HHHHHCCCCCCCCCC
10.7720068231
972PhosphorylationELVHYQQSPGEDTSL
HHCCCCCCCCCCCHH
21.2420068231
977PhosphorylationQQSPGEDTSLRLQEE
CCCCCCCCHHHHHHH
25.9220068231
978PhosphorylationQSPGEDTSLRLQEEV
CCCCCCCHHHHHHHH
24.6620068231
987PhosphorylationRLQEEVESLRTELQR
HHHHHHHHHHHHHHH
28.4729978859
990PhosphorylationEEVESLRTELQRAHS
HHHHHHHHHHHHHHH
46.4729978859
1072UbiquitinationSRYQNLVKEYSQLEQ
HHHHHHHHHHHHHHH
54.85-
1102PhosphorylationPGHRRNPSNQSSLES
CCCCCCCCCCCCCCC
51.5626657352
1105PhosphorylationRRNPSNQSSLESDSN
CCCCCCCCCCCCCCC
40.9326657352
1106PhosphorylationRNPSNQSSLESDSNY
CCCCCCCCCCCCCCC
26.7926657352
1109PhosphorylationSNQSSLESDSNYPSI
CCCCCCCCCCCCCCC
52.1923090842
1111PhosphorylationQSSLESDSNYPSIST
CCCCCCCCCCCCCCH
47.7626657352
1113PhosphorylationSLESDSNYPSISTSE
CCCCCCCCCCCCHHH
11.4323090842
1115PhosphorylationESDSNYPSISTSEIG
CCCCCCCCCCHHHCC
20.8626657352
1117PhosphorylationDSNYPSISTSEIGDT
CCCCCCCCHHHCCCH
30.1626657352
1118PhosphorylationSNYPSISTSEIGDTE
CCCCCCCHHHCCCHH
28.8023090842
1119PhosphorylationNYPSISTSEIGDTED
CCCCCCHHHCCCHHH
22.0423090842
1124PhosphorylationSTSEIGDTEDALQQV
CHHHCCCHHHHHHHH
30.4723090842
1197PhosphorylationDPNADLAYNSLKRQE
CCCCHHHHHHHHHHH
16.7521406692
1199PhosphorylationNADLAYNSLKRQELE
CCHHHHHHHHHHHHH
23.6924719451
1207PhosphorylationLKRQELESENKKLKN
HHHHHHHHHHHHHHH
60.1216097034
1228PhosphorylationKAVADQATQNNSSHG
HHHHHHHHHCCCCCC
26.6228348404
1232PhosphorylationDQATQNNSSHGSPDS
HHHHHCCCCCCCHHH
31.1228348404
1233PhosphorylationQATQNNSSHGSPDSY
HHHHCCCCCCCHHHH
33.7128348404
1236PhosphorylationQNNSSHGSPDSYSLL
HCCCCCCCHHHHHHH
21.8028348404
1289PhosphorylationEPNINARSSWPNSEK
CCCCCCCCCCCCCCC
34.0528102081
1290PhosphorylationPNINARSSWPNSEKH
CCCCCCCCCCCCCCC
40.7926657352
1294PhosphorylationARSSWPNSEKHVDQE
CCCCCCCCCCCCCHH
43.9023312004
1307PhosphorylationQEDAIEAYHGVCQTN
HHHHHHHHHCHHCCC
6.0627642862
1333PhosphorylationDGELGLAYQGLKQVA
CCCHHHHHHHHHHHH
14.25-
1351PhosphorylationEAQLQAQSLEHEEEV
HHHHHHHCCCCHHHH
38.4528348404
1403PhosphorylationQQEISRLTNENLDLK
HHHHHHHHCCCCCHH
39.1022985185
1410UbiquitinationTNENLDLKELVEKLE
HCCCCCHHHHHHHHH
48.98-
1415AcetylationDLKELVEKLEKNERK
CHHHHHHHHHHHHHH
55.24178226381
1446PhosphorylationAAQALAQSERKRHEL
HHHHHHHHHHHHHHH
33.4925159151
1447PhosphorylationAQALAQSERKRHELN
HHHHHHHHHHHHHHH
50.5718669648
1458PhosphorylationHELNRQVTVQRKEKD
HHHHHCCEEHHHHHC
11.55-
1464AcetylationVTVQRKEKDFQGMLE
CEEHHHHHCCCHHHH
67.8712650055
1528PhosphorylationVHSLLTSTINGIKKV
HHHHHHHHHHHHHHH
17.15-
1546PhosphorylationHNDDFEMTSFWLSNT
CCCCCHHHHHHHHHH
17.36-
1547PhosphorylationNDDFEMTSFWLSNTC
CCCCHHHHHHHHHHH
17.08-
1551PhosphorylationEMTSFWLSNTCRLLH
HHHHHHHHHHHHHHH
22.23-
1642PhosphorylationPTGYRKRSSSMADGD
CCCCCCCCCCCCCCC
29.7830278072
1643PhosphorylationTGYRKRSSSMADGDN
CCCCCCCCCCCCCCC
28.3230278072
1644PhosphorylationGYRKRSSSMADGDNS
CCCCCCCCCCCCCCH
21.1630278072
1651PhosphorylationSMADGDNSYCLEAII
CCCCCCCHHHHHHHH
23.2020736484
1714PhosphorylationSTGMQLRYNISQLEE
HHCCHHHCCHHHHHH
25.9925690035
1717PhosphorylationMQLRYNISQLEEWLR
CHHHCCHHHHHHHHH
25.6925690035

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 MYO5B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MYO5B_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 MYO5B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RFIP2_HUMANRAB11FIP2physical
12393859
RB11A_HUMANRAB11Aphysical
17507647
RB11B_HUMANRAB11Bphysical
17507647
RAB25_HUMANRAB25physical
17507647
RAB8A_HUMANRAB8Aphysical
17507647
RPAC1_HUMANPOLR1Cphysical
21988832
ITF2_HUMANTCF4physical
25416956
AMOL2_HUMANAMOTL2physical
25416956
TRI54_HUMANTRIM54physical
25416956
RFIP2_HUMANRAB11FIP2physical
16473632
EXOC6_HUMANEXOC6physical
26553929
SYTL4_HUMANSYTL4physical
26553929
RAB3B_HUMANRAB3Bphysical
26553929
STX3_HUMANSTX3physical
26553929
RAB8A_HUMANRAB8Aphysical
26553929
RB11A_HUMANRAB11Aphysical
26553929

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
251850Diarrhea 2, with microvillus atrophy (DIAR2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MYO5B_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-1446, AND MASSSPECTROMETRY.
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-694, AND MASSSPECTROMETRY.

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