RBNS5_HUMAN - dbPTM
RBNS5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RBNS5_HUMAN
UniProt AC Q9H1K0
Protein Name Rabenosyn-5 {ECO:0000303|PubMed:11062261}
Gene Name RBSN {ECO:0000312|HGNC:HGNC:20759}
Organism Homo sapiens (Human).
Sequence Length 784
Subcellular Localization Cell membrane
Lipid-anchor
Cytoplasmic side. Early endosome membrane
Lipid-anchor. Enriched in endosomes that are in close proximity to clathrin-enriched regions at the cell surface.
Protein Description Rab4/Rab5 effector protein acting in early endocytic membrane fusion and membrane trafficking of recycling endosomes. Required for endosome fusion either homotypically or with clathrin coated vesicles. Plays a role in the lysosomal trafficking of CTSD/cathepsin D from the Golgi to lysosomes. Also promotes the recycling of transferrin directly from early endosomes to the plasma membrane. Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate (PtdInsP3). [PubMed: 11062261]
Protein Sequence MASLDDPGEVREGFLCPLCLKDLQSFYQLHSHYEEEHSGEDRDVKGQIKSLVQKAKKAKDRLLKREGDDRAESGTQGYESFSYGGVDPYMWEPQELGAVRSHLSDFKKHRAARIDHYVVEVNKLIIRLEKLTAFDRTNTESAKIRAIEKSVVPWVNDQDVPFCPDCGNKFSIRNRRHHCRLCGSIMCKKCMELISLPLANKLTSASKESLSTHTSPSQSPNSVHGSRRGSISSMSSVSSVLDEKDDDRIRCCTHCKDTLLKREQQIDEKEHTPDIVKLYEKLRLCMEKVDQKAPEYIRMAASLNAGETTYSLEHASDLRVEVQKVYELIDALSKKILTLGLNQDPPPHPSNLRLQRMIRYSATLFVQEKLLGLMSLPTKEQFEELKKKRKEEMERKRAVERQAALESQRRLEERQSGLASRAANGEVASLRRGPAPLRKAEGWLPLSGGQGQSEDSDPLLQQIHNITSFIRQAKAAGRMDEVRTLQENLRQLQDEYDQQQTEKAIELSRRQAEEEDLQREQLQMLRERELEREREQFRVASLHTRTRSLDFREIGPFQLEPSREPRTHLAYALDLGSSPVPSSTAPKTPSLSSTQPTRVWSGPPAVGQERLPQSSMPQQHEGPSLNPFDEEDLSSPMEEATTGPPAAGVSLDPSARILKEYNPFEEEDEEEEAVAGNPFIQPDSPAPNPFSEEDEHPQQRLSSPLVPGNPFEEPTCINPFEMDSDSGPEAEEPIEEELLLQQIDNIKAYIFDAKQCGRLDEVEVLTENLRELKHTLAKQKGGTD
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
2Acetylation------MASLDDPGE
------CCCCCCCCC		20.8522814378
3Phosphorylation-----MASLDDPGEV
-----CCCCCCCCCC		30.9123186163
117PhosphorylationRAARIDHYVVEVNKL
HHHHCCEEEEHHHHH		11.4827642862
169AcetylationFCPDCGNKFSIRNRR
CCCCCCCCEEECCCH		26.2726051181
204PhosphorylationPLANKLTSASKESLS
HHHHHCCCCCHHHHC		40.7730624053
209PhosphorylationLTSASKESLSTHTSP
CCCCCHHHHCCCCCC		31.2129255136
211PhosphorylationSASKESLSTHTSPSQ
CCCHHHHCCCCCCCC		27.6729255136
212PhosphorylationASKESLSTHTSPSQS
CCHHHHCCCCCCCCC		34.1729255136
214PhosphorylationKESLSTHTSPSQSPN
HHHHCCCCCCCCCCC		42.2829255136
215PhosphorylationESLSTHTSPSQSPNS
HHHCCCCCCCCCCCC		18.2329255136
217PhosphorylationLSTHTSPSQSPNSVH
HCCCCCCCCCCCCCC		42.9529255136
219PhosphorylationTHTSPSQSPNSVHGS
CCCCCCCCCCCCCCC		30.3229255136
222PhosphorylationSPSQSPNSVHGSRRG
CCCCCCCCCCCCCCC		20.9029255136
226PhosphorylationSPNSVHGSRRGSISS
CCCCCCCCCCCCHHC		12.1529255136
230PhosphorylationVHGSRRGSISSMSSV
CCCCCCCCHHCCHHH		19.9330278072
232PhosphorylationGSRRGSISSMSSVSS
CCCCCCHHCCHHHHH		22.9925159151
233PhosphorylationSRRGSISSMSSVSSV
CCCCCHHCCHHHHHH		22.4830278072
235PhosphorylationRGSISSMSSVSSVLD
CCCHHCCHHHHHHCC		29.5425159151
236PhosphorylationGSISSMSSVSSVLDE
CCHHCCHHHHHHCCC		19.8525159151
238PhosphorylationISSMSSVSSVLDEKD
HHCCHHHHHHCCCCC		19.3728450419
239PhosphorylationSSMSSVSSVLDEKDD
HCCHHHHHHCCCCCC		25.2528450419
277UbiquitinationEHTPDIVKLYEKLRL
CCCHHHHHHHHHHHH		45.76-
288AcetylationKLRLCMEKVDQKAPE
HHHHHHHHHHHHCHH		24.9925953088
375PhosphorylationEKLLGLMSLPTKEQF
HHHHCHHCCCCHHHH		35.92-
378PhosphorylationLGLMSLPTKEQFEEL
HCHHCCCCHHHHHHH		53.13-
416PhosphorylationRRLEERQSGLASRAA
HHHHHHHHHHHHHHH		41.8328555341
429PhosphorylationAANGEVASLRRGPAP
HHCCCHHHCCCCCCC		27.8223917254
439UbiquitinationRGPAPLRKAEGWLPL
CCCCCCCCCCCCEEC		59.48-
496PhosphorylationLRQLQDEYDQQQTEK
HHHHHHHHHHHHHHH		27.6021659604
501PhosphorylationDEYDQQQTEKAIELS
HHHHHHHHHHHHHHH		34.8121659604
541PhosphorylationREQFRVASLHTRTRS
HHHHHHHHHHHHCCC		20.1626657352
544PhosphorylationFRVASLHTRTRSLDF
HHHHHHHHHCCCCCH		38.7427251275
546PhosphorylationVASLHTRTRSLDFRE
HHHHHHHCCCCCHHH		26.2630266825
548PhosphorylationSLHTRTRSLDFREIG
HHHHHCCCCCHHHCC		31.5123401153
567PhosphorylationEPSREPRTHLAYALD
CCCCCCCCEEEEEHH		31.7727080861
571PhosphorylationEPRTHLAYALDLGSS
CCCCEEEEEHHCCCC		17.6627080861
577PhosphorylationAYALDLGSSPVPSST
EEEHHCCCCCCCCCC		38.4722199227
578PhosphorylationYALDLGSSPVPSSTA
EEHHCCCCCCCCCCC		28.2822199227
583O-linked_GlycosylationGSSPVPSSTAPKTPS
CCCCCCCCCCCCCCC		23.6330059200
588PhosphorylationPSSTAPKTPSLSSTQ
CCCCCCCCCCCCCCC		19.6322199227
590PhosphorylationSTAPKTPSLSSTQPT
CCCCCCCCCCCCCCC		46.2222199227
601PhosphorylationTQPTRVWSGPPAVGQ
CCCCEEECCCCCCCC		38.2725159151
634PhosphorylationPFDEEDLSSPMEEAT
CCCHHHCCCCCHHHC		44.7228348404
635PhosphorylationFDEEDLSSPMEEATT
CCHHHCCCCCHHHCC		35.2528348404
641PhosphorylationSSPMEEATTGPPAAG
CCCCHHHCCCCCCCC		35.2528348404
642PhosphorylationSPMEEATTGPPAAGV
CCCHHHCCCCCCCCC		55.5328348404
684PhosphorylationNPFIQPDSPAPNPFS
CCCCCCCCCCCCCCC		29.6426657352
691PhosphorylationSPAPNPFSEEDEHPQ
CCCCCCCCCCCCCCC		41.1422210691
715PhosphorylationGNPFEEPTCINPFEM
CCCCCCCCCCCCCCC		29.3327251275
724PhosphorylationINPFEMDSDSGPEAE
CCCCCCCCCCCCCCC		32.1627251275
726PhosphorylationPFEMDSDSGPEAEEP
CCCCCCCCCCCCCCC		61.2627251275
773UbiquitinationTENLRELKHTLAKQK
HHHHHHHHHHHHHHC		29.77-
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
215SPhosphorylationKinaseMAPK14Q16539
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RBNS5_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 RBNS5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAB5A_HUMANRAB5Aphysical
11062261
VPS45_HUMANVPS45physical
19931244
FAK1_HUMANPTK2physical
19931244
HSP7C_HUMANHSPA8physical
19931244
VPS45_RATVps45physical
19931244
RAB5A_HUMANRAB5Aphysical
16034420
RAB4A_HUMANRAB4Aphysical
16034420
RB22A_HUMANRAB22Aphysical
16034420
RAB14_HUMANRAB14physical
16034420
RAB24_HUMANRAB24physical
16034420
VPS45_HUMANVPS45physical
28514442
EHD3_HUMANEHD3physical
28514442
EHD4_HUMANEHD4physical
28514442
AVIL_HUMANAVILphysical
28514442
PCDA4_HUMANPCDHA4physical
28514442
IFFO1_HUMANIFFO1physical
28514442
EHD1_HUMANEHD1physical
28514442
LMX1B_HUMANLMX1Bphysical
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 RBNS5_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-214; SER-215 ANDSER-217, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-601, AND MASSSPECTROMETRY.

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