RAB14_HUMAN - dbPTM
RAB14_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RAB14_HUMAN
UniProt AC P61106
Protein Name Ras-related protein Rab-14
Gene Name RAB14
Organism Homo sapiens (Human).
Sequence Length 215
Subcellular Localization Recycling endosome . Early endosome membrane
Lipid-anchor
Cytoplasmic side . Golgi apparatus membrane
Lipid-anchor
Cytoplasmic side . Golgi apparatus, trans-Golgi network membrane
Lipid-anchor
Cytoplasmic side . Cytoplasmic vesicle, phagosome
Protein Description Involved in membrane trafficking between the Golgi complex and endosomes during early embryonic development. Regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. May act by modulating the kinesin KIF16B-cargo association to endosomes (By similarity). Regulates, together with its guanine nucleotide exchange factor DENND6A, the specific endocytic transport of ADAM10, N-cadherin/CDH2 shedding and cell-cell adhesion..
Protein Sequence MATAPYNYSYIFKYIIIGDMGVGKSCLLHQFTEKKFMADCPHTIGVEFGTRIIEVSGQKIKLQIWDTAGQERFRAVTRSYYRGAAGALMVYDITRRSTYNHLSSWLTDARNLTNPNTVIILIGNKADLEAQRDVTYEEAKQFAEENGLLFLEASAKTGENVEDAFLEAAKKIYQNIQDGSLDLNAAESGVQHKPSAPQGGRLTSEPQPQREGCGC
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------MATAPYNYS
------CCCCCCCHH		16.6922223895
3Phosphorylation-----MATAPYNYSY
-----CCCCCCCHHH		27.2024173317
8PhosphorylationMATAPYNYSYIFKYI
CCCCCCCHHHEEEEE		9.3025884760
14PhosphorylationNYSYIFKYIIIGDMG
CHHHEEEEEEECCCC		6.1320068231
20SulfoxidationKYIIIGDMGVGKSCL
EEEEECCCCCCHHHH		3.8521406390
26S-nitrosocysteineDMGVGKSCLLHQFTE
CCCCCHHHHHHHHCC		5.51-
26S-nitrosylationDMGVGKSCLLHQFTE
CCCCCHHHHHHHHCC		5.5119483679
34UbiquitinationLLHQFTEKKFMADCP
HHHHHCCCCHHCCCC		48.53-
35MalonylationLHQFTEKKFMADCPH
HHHHCCCCHHCCCCC		33.8526320211
35AcetylationLHQFTEKKFMADCPH
HHHHCCCCHHCCCCC		33.8525953088
35UbiquitinationLHQFTEKKFMADCPH
HHHHCCCCHHCCCCC		33.85-
43PhosphorylationFMADCPHTIGVEFGT
HHCCCCCCCEEEECC		12.4520068231
56PhosphorylationGTRIIEVSGQKIKLQ
CCEEEEECCCEEEEE		23.7920068231
59UbiquitinationIIEVSGQKIKLQIWD
EEEECCCEEEEEEEC		45.38-
59AcetylationIIEVSGQKIKLQIWD
EEEECCCEEEEEEEC		45.3825953088
61UbiquitinationEVSGQKIKLQIWDTA
EECCCEEEEEEECCC		41.18-
67PhosphorylationIKLQIWDTAGQERFR
EEEEEECCCCHHHHH		20.0728857561
80PhosphorylationFRAVTRSYYRGAAGA
HHHHHHHHHHCCCCE		8.22-
81PhosphorylationRAVTRSYYRGAAGAL
HHHHHHHHHCCCCEE		12.10-
91PhosphorylationAAGALMVYDITRRST
CCCEEEEEECCCCHH		6.40-
94PhosphorylationALMVYDITRRSTYNH
EEEEEECCCCHHHHH		19.6820071362
97PhosphorylationVYDITRRSTYNHLSS
EEECCCCHHHHHHHH		31.7722167270
98PhosphorylationYDITRRSTYNHLSSW
EECCCCHHHHHHHHH		26.9122167270
99PhosphorylationDITRRSTYNHLSSWL
ECCCCHHHHHHHHHH		11.2223403867
103PhosphorylationRSTYNHLSSWLTDAR
CHHHHHHHHHHHHCC		16.3623403867
104PhosphorylationSTYNHLSSWLTDARN
HHHHHHHHHHHHCCC		32.2523403867
107PhosphorylationNHLSSWLTDARNLTN
HHHHHHHHHCCCCCC		22.73-
125UbiquitinationVIILIGNKADLEAQR
EEEEECCHHHHHHHH		37.7621906983
135PhosphorylationLEAQRDVTYEEAKQF
HHHHHCCCHHHHHHH		29.5128102081
136PhosphorylationEAQRDVTYEEAKQFA
HHHHCCCHHHHHHHH		16.1828102081
140UbiquitinationDVTYEEAKQFAEENG
CCCHHHHHHHHHHHC		49.5921906983
156UbiquitinationLFLEASAKTGENVED
EEEEECCCCCCCHHH		55.35-
170AcetylationDAFLEAAKKIYQNIQ
HHHHHHHHHHHHHHC		46.9125953088
170UbiquitinationDAFLEAAKKIYQNIQ
HHHHHHHHHHHHHHC		46.9121906983
171UbiquitinationAFLEAAKKIYQNIQD
HHHHHHHHHHHHHCC		41.7521906983
173PhosphorylationLEAAKKIYQNIQDGS
HHHHHHHHHHHCCCC		12.3728152594
180PhosphorylationYQNIQDGSLDLNAAE
HHHHCCCCCCCCHHH		27.3123401153
188PhosphorylationLDLNAAESGVQHKPS
CCCCHHHHCCCCCCC		39.2723663014
193AcetylationAESGVQHKPSAPQGG
HHHCCCCCCCCCCCC		24.4726051181
193MalonylationAESGVQHKPSAPQGG
HHHCCCCCCCCCCCC		24.4726320211
193UbiquitinationAESGVQHKPSAPQGG
HHHCCCCCCCCCCCC		24.47-
195PhosphorylationSGVQHKPSAPQGGRL
HCCCCCCCCCCCCCC		58.3421955146
203PhosphorylationAPQGGRLTSEPQPQR
CCCCCCCCCCCCCCC		29.6825072903
204PhosphorylationPQGGRLTSEPQPQRE
CCCCCCCCCCCCCCC		52.4528857561
213GeranylgeranylationPQPQREGCGC-----
CCCCCCCCCC-----		4.27-
215GeranylgeranylationPQREGCGC-------
CCCCCCCC-------		6.15-
215MethylationPQREGCGC-------
CCCCCCCC-------		6.15-
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 RAB14_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RAB14_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 RAB14_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RUFY1_HUMANRUFY1physical
20534812
A4_HUMANAPPphysical
21832049
UCRI_HUMANUQCRFS1physical
22939629
TACC3_HUMANTACC3physical
22939629
OPTN_HUMANOPTNphysical
19702578
RFIP5_HUMANRAB11FIP5physical
19702578
RFIP1_HUMANRAB11FIP1physical
19702578
VATC1_HUMANATP6V1C1physical
26344197
ANXA2_HUMANANXA2physical
18332131
CCHL_HUMANHCCSphysical
27173435
GLCM_HUMANGBAphysical
27173435
COMT_HUMANCOMTphysical
27173435
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 RAB14_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.

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