RBG1L_HUMAN - dbPTM
RBG1L_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RBG1L_HUMAN
UniProt AC Q5R372
Protein Name Rab GTPase-activating protein 1-like
Gene Name RABGAP1L {ECO:0000312|EMBL:CAI18937.1}
Organism Homo sapiens (Human).
Sequence Length 815
Subcellular Localization Cytoplasmic vesicle . Early endosome . Golgi apparatus . Colocalizes on endosomes partially with EEA1 (PubMed:16923123). Colocalizes and cotransports on motile vesicles with ANK2 (By similarity).
Protein Description GTP-hydrolysis activating protein (GAP) for small GTPase RAB22A, converting active RAB22A-GTP to the inactive form RAB22A-GDP. [PubMed: 16923123 Plays a role in endocytosis and intracellular protein transport. Recruited by ANK2 to phosphatidylinositol 3-phosphate (PI3P)-positive early endosomes, where it inactivates RAB22A, and promotes polarized trafficking to the leading edge of the migrating cells. Part of the ANK2/RABGAP1L complex which is required for the polarized recycling of fibronectin receptor ITGA5 ITGB1 to the plasma membrane that enables continuous directional cell migration (By similarity]
Protein Sequence MEVRASLQKVSGSSDSVATMNSEEFVLVPQYADDNSTKHEEKPQLKIVSNGDEQLEKAMEEILRDSEKRPSSLLVDCQSSSEISDHSFGDIPASQTNKPSLQLILDPSNTEISTPRPSSPGGLPEEDSVLFNKLTYLGCMKVSSPRNEVEALRAMATMKSSSQYPFPVTLYVPNVPEGSVRIIDQSSNVEIASFPIYKVLFCARGHDGTTESNCFAFTESSHGSEEFQIHVFSCEIKEAVSRILYSFCTAFKRSSRQVSDVKDSVIPTPDSDVFTFSVSLEVKEDDGKGNFSPVPKDRDKFYFKLKQGIEKKVVITVQQLSNKELAIERCFGMLLSPGRNVKNSDMHLLDMESMGKSYDGRAYVITGMWNPNAPVFLALNEETPKDKQVYMTVAVDMVVTEVVEPVRFLLETVVRVYPANERFWYFSRKTFTETFFMRLKQSEGKGHTNAGDAIYEVVSLQRESDKEEPVTPTSGGGPMSPQDDEAEEESDNELSSGTGDVSKDCPEKILYSWGELLGKWHSNLGARPKGLSTLVKSGVPEALRAEVWQLLAGCHDNQAMLDRYRILITKDSAQESVITRDIHRTFPAHDYFKDTGGDGQESLYKICKAYSVYDEDIGYCQGQSFLAAVLLLHMPEEQAFCVLVKIMYDYGLRDLYRNNFEDLHCKFYQLERLMQEQLPDLHSHFSDLNLEAHMYASQWFLTLFTAKFPLCMVFHIIDLLLCEGLNIIFHVALALLKTSKEDLLQADFEGALKFFRVQLPKRYRAEENARRLMEQACNIKVPTKKLKKYEKEYQTMRESQLQQEDPMDRYKFVYL
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
11PhosphorylationRASLQKVSGSSDSVA
HHHHEECCCCCCCEE		39.7428857561
13PhosphorylationSLQKVSGSSDSVATM
HHEECCCCCCCEEEC		24.3828857561
14PhosphorylationLQKVSGSSDSVATMN
HEECCCCCCCEEECC		37.1128857561
16PhosphorylationKVSGSSDSVATMNSE
ECCCCCCCEEECCCC		18.6628857561
19PhosphorylationGSSDSVATMNSEEFV
CCCCCEEECCCCCEE		18.0926471730
22PhosphorylationDSVATMNSEEFVLVP
CCEEECCCCCEEEEE		27.9027251275
49PhosphorylationKPQLKIVSNGDEQLE
CCCCEEECCHHHHHH		38.2730108239
66PhosphorylationMEEILRDSEKRPSSL
HHHHHHCCCCCCCCE		38.2926074081
71PhosphorylationRDSEKRPSSLLVDCQ
HCCCCCCCCEEEECC		37.3427050516
72PhosphorylationDSEKRPSSLLVDCQS
CCCCCCCCEEEECCC		28.5330576142
79PhosphorylationSLLVDCQSSSEISDH
CEEEECCCCCCCCCC		42.0126074081
80PhosphorylationLLVDCQSSSEISDHS
EEEECCCCCCCCCCC		13.2026074081
81PhosphorylationLVDCQSSSEISDHSF
EEECCCCCCCCCCCC		44.1726074081
84PhosphorylationCQSSSEISDHSFGDI
CCCCCCCCCCCCCCC		25.8128270605
87PhosphorylationSSEISDHSFGDIPAS
CCCCCCCCCCCCCHH		35.6028270605
108PhosphorylationLQLILDPSNTEISTP
EEEEECCCCCCCCCC		56.9328270605
110PhosphorylationLILDPSNTEISTPRP
EEECCCCCCCCCCCC		38.7526657352
113PhosphorylationDPSNTEISTPRPSSP
CCCCCCCCCCCCCCC		26.5725159151
114PhosphorylationPSNTEISTPRPSSPG
CCCCCCCCCCCCCCC		29.0425159151
114O-linked_GlycosylationPSNTEISTPRPSSPG
CCCCCCCCCCCCCCC		29.04OGP
118PhosphorylationEISTPRPSSPGGLPE
CCCCCCCCCCCCCCH		50.9022167270
119PhosphorylationISTPRPSSPGGLPEE
CCCCCCCCCCCCCHH		30.1929255136
128PhosphorylationGGLPEEDSVLFNKLT
CCCCHHHHHHHHHHH		24.8126074081
135PhosphorylationSVLFNKLTYLGCMKV
HHHHHHHHHCCCEEC		20.5026074081
136PhosphorylationVLFNKLTYLGCMKVS
HHHHHHHHCCCEECC		16.1326074081
157PhosphorylationEALRAMATMKSSSQY
HHHHHHHHHHCCCCC		16.4320068231
160PhosphorylationRAMATMKSSSQYPFP
HHHHHHHCCCCCCCC		25.1320068231
161PhosphorylationAMATMKSSSQYPFPV
HHHHHHCCCCCCCCE		18.8820068231
179PhosphorylationVPNVPEGSVRIIDQS
CCCCCCCCEEEEECC		13.4220068231
216 (in isoform 7)Phosphorylation-16.8022468782
221 (in isoform 7)Phosphorylation-26.1524043423
224 (in isoform 7)Phosphorylation-28.6422468782
225 (in isoform 7)Phosphorylation-68.3824043423
228 (in isoform 8)Phosphorylation-28.3222468782
233 (in isoform 8)Phosphorylation-15.1124043423
235 (in isoform 6)Phosphorylation-56.7622468782
236 (in isoform 5)Phosphorylation-5.9922468782
236 (in isoform 8)Phosphorylation-5.9922468782
237 (in isoform 8)Phosphorylation-19.8224043423
240 (in isoform 6)Phosphorylation-4.0824043423
241 (in isoform 5)Phosphorylation-22.2024043423
243 (in isoform 6)Phosphorylation-3.0922468782
244 (in isoform 5)Phosphorylation-2.5922468782
244 (in isoform 6)Phosphorylation-2.5924043423
245 (in isoform 5)Phosphorylation-9.4224043423
252AcetylationYSFCTAFKRSSRQVS
HHHHHHHHHCCCCHH		49.2425953088
252MalonylationYSFCTAFKRSSRQVS
HHHHHHHHHCCCCHH		49.2426320211
275 (in isoform 7)Phosphorylation-18.1725159151
287 (in isoform 8)Phosphorylation-52.6825159151
292PhosphorylationDDGKGNFSPVPKDRD
CCCCCCCCCCCCCCC		29.0530108239
294 (in isoform 6)Phosphorylation-9.9825159151
295 (in isoform 5)Phosphorylation-35.8925159151
336PhosphorylationRCFGMLLSPGRNVKN
HHHHHHHCCCCCCCC		22.7324719451
338 (in isoform 7)Phosphorylation-30.3429396449
340 (in isoform 7)Phosphorylation-55.8429396449
342 (in isoform 7)Phosphorylation-55.0429396449
350 (in isoform 8)Phosphorylation-45.2029396449
351 (in isoform 7)Phosphorylation-4.0729396449
352 (in isoform 8)Phosphorylation-36.9229396449
353PhosphorylationMHLLDMESMGKSYDG
CEEECHHHCCCCCCC		26.6325954137
354 (in isoform 8)Phosphorylation-5.0929396449
357 (in isoform 6)Phosphorylation-23.7929396449
358PhosphorylationMESMGKSYDGRAYVI
HHHCCCCCCCCEEEE		26.38-
358 (in isoform 5)Phosphorylation-26.3829396449
359 (in isoform 6)Phosphorylation-47.3929396449
360 (in isoform 5)Phosphorylation-14.1129396449
361 (in isoform 6)Phosphorylation-21.6129396449
362 (in isoform 5)Phosphorylation-14.4229396449
363PhosphorylationKSYDGRAYVITGMWN
CCCCCCEEEEEEECC		7.3324719451
363 (in isoform 8)Phosphorylation-7.3329396449
370 (in isoform 6)Phosphorylation-15.8529396449
371 (in isoform 5)Phosphorylation-23.8929396449
383PhosphorylationFLALNEETPKDKQVY
EEEECCCCCCCCCEE		29.4724719451
425PhosphorylationPANERFWYFSRKTFT
ECCCCEEEEEECCCC		6.7525839225
427PhosphorylationNERFWYFSRKTFTET
CCCEEEEEECCCCHH		19.7125348954
432PhosphorylationYFSRKTFTETFFMRL
EEEECCCCHHHHHHH		39.0722210691
434PhosphorylationSRKTFTETFFMRLKQ
EECCCCHHHHHHHHH		21.0822210691
448PhosphorylationQSEGKGHTNAGDAIY
HCCCCCCCCHHHHHH		35.1224719451
455PhosphorylationTNAGDAIYEVVSLQR
CCHHHHHHHHHEEEC		12.3721945579
459PhosphorylationDAIYEVVSLQRESDK
HHHHHHHEEECCCCC		24.7821945579
464PhosphorylationVVSLQRESDKEEPVT
HHEEECCCCCCCCCC		57.0523927012
471PhosphorylationSDKEEPVTPTSGGGP
CCCCCCCCCCCCCCC		31.4023927012
473PhosphorylationKEEPVTPTSGGGPMS
CCCCCCCCCCCCCCC		30.5523927012
474PhosphorylationEEPVTPTSGGGPMSP
CCCCCCCCCCCCCCC		36.3223927012
480PhosphorylationTSGGGPMSPQDDEAE
CCCCCCCCCCCHHHH		23.6523927012
490PhosphorylationDDEAEEESDNELSSG
CHHHHHHCCCCCCCC		49.3630278072
495PhosphorylationEESDNELSSGTGDVS
HHCCCCCCCCCCCCC		22.1223927012
496PhosphorylationESDNELSSGTGDVSK
HCCCCCCCCCCCCCC		53.6623927012
498PhosphorylationDNELSSGTGDVSKDC
CCCCCCCCCCCCCCC		31.9623927012
502PhosphorylationSSGTGDVSKDCPEKI
CCCCCCCCCCCCHHH		27.7623927012
511PhosphorylationDCPEKILYSWGELLG
CCCHHHHHHHHHHHH		13.07-
536UbiquitinationKGLSTLVKSGVPEAL
CCHHHHHHCCCCHHH		44.60-
570UbiquitinationRYRILITKDSAQESV
HEEEEEECCCCCCCE		42.57-
572PhosphorylationRILITKDSAQESVIT
EEEEECCCCCCCEEE		33.1522210691
576PhosphorylationTKDSAQESVITRDIH
ECCCCCCCEEEHHHH		13.5122210691
593UbiquitinationFPAHDYFKDTGGDGQ
CCHHHHHCCCCCCCH		48.42-
604PhosphorylationGDGQESLYKICKAYS
CCCHHHHHHHHHHHC		13.95-
605UbiquitinationDGQESLYKICKAYSV
CCHHHHHHHHHHHCC		47.09-
695PhosphorylationLNLEAHMYASQWFLT
CCHHHHHHHHHHHHH		8.0125690035
702PhosphorylationYASQWFLTLFTAKFP
HHHHHHHHHHHCCCH		15.4525690035
705PhosphorylationQWFLTLFTAKFPLCM
HHHHHHHHCCCHHHH		31.8624260401
807SulfoxidationQLQQEDPMDRYKFVY
HHHCCCCCCCCCEEE		7.6721406390
810PhosphorylationQEDPMDRYKFVYL--
CCCCCCCCCEEEC--		12.43-
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 RBG1L_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RBG1L_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 RBG1L_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAB13_HUMANRAB13physical
16923123
RAB34_HUMANRAB34physical
16923123
RAB36_HUMANRAB36physical
16923123
ARFG1_HUMANARFGAP1physical
25814554
UQCC2_HUMANUQCC2physical
25814554
CI043_HUMANC9orf43physical
25814554
TSN2_HUMANTSPAN2physical
25814554
WDFY3_HUMANWDFY3physical
25814554
ACAP1_HUMANACAP1physical
25814554
DREB_HUMANDBN1physical
25814554
EVI1_HUMANMECOMphysical
25814554
RB_HUMANRB1physical
25814554
PXDC1_HUMANPXDC1physical
28514442
TROP_HUMANTROphysical
28514442
BACH_HUMANACOT7physical
28514442
MLF1_HUMANMLF1physical
28514442
PKN3_HUMANPKN3physical
27173435
NCK5L_HUMANNCKAP5Lphysical
27173435
TFPT_HUMANTFPTphysical
27173435
CCHCR_HUMANCCHCR1physical
27173435
YETS4_HUMANYEATS4physical
27173435
TUFT1_HUMANTUFT1physical
27173435
GOGA5_HUMANGOLGA5physical
27173435
CLOCK_HUMANCLOCKphysical
27173435
PSMD9_HUMANPSMD9physical
27173435
VPS53_HUMANVPS53physical
27173435
DZIP3_HUMANDZIP3physical
27173435
GRAP1_HUMANGRIPAP1physical
27173435
RCOR1_HUMANRCOR1physical
27173435
VPS50_HUMANCCDC132physical
27173435
CCD93_HUMANCCDC93physical
27173435
MS18B_HUMANOIP5physical
27173435
PF21A_HUMANPHF21Aphysical
27173435
CAVN1_HUMANPTRFphysical
27173435
PHLB3_HUMANPHLDB3physical
27173435
HAUS6_HUMANHAUS6physical
27173435
RPR1A_HUMANRPRD1Aphysical
27173435
BMAL1_HUMANARNTLphysical
27173435
RABX5_HUMANRABGEF1physical
27173435
NUF2_HUMANNUF2physical
27173435
THA11_HUMANTHAP11physical
27173435
VPS51_HUMANVPS51physical
27173435
EIPR1_HUMANTSSC1physical
27173435
RABE1_HUMANRABEP1physical
27173435
KDM1A_HUMANKDM1Aphysical
27173435
STRN_HUMANSTRNphysical
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 RBG1L_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 THR-471; SER-480 ANDSER-490, AND MASS SPECTROMETRY.

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