GARL3_HUMAN - dbPTM
GARL3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GARL3_HUMAN
UniProt AC Q5VVW2
Protein Name GTPase-activating Rap/Ran-GAP domain-like protein 3
Gene Name GARNL3
Organism Homo sapiens (Human).
Sequence Length 1013
Subcellular Localization
Protein Description
Protein Sequence MVVDFCRRFVARSLCIILMKHFCSSSVSEDLGCRRGDFSRKHYGSVELLISSDADGAIQRAGRFRVENGSSDENATALPGTWRRTDVHLENPEYHTRWYFKYFLGQVHQNYIGNDAEKSPFFLSVTLSDQNNQRVPQYRAILWRKTGTQKICLPYSPTKTLSVKSILSAMNLDKFEKGPREIFHPEIQKDLLVLEEQEGSVNFKFGVLFAKDGQLTDDEMFSNEIGSEPFQKFLNLLGDTITLKGWTGYRGGLDTKNDTTGIHSVYTVYQGHEIMFHVSTMLPYSKENKQQVERKRHIGNDIVTIVFQEGEESSPAFKPSMIRSHFTHIFALVRYNQQNDNYRLKIFSEESVPLFGPPLPTPPVFTDHQEFRDFLLVKLINGEKATLETPTFAQKRRRTLDMLIRSLHQDLMPDLHKNMLNRRSFSDVLPESPKSARKKEEARQAEFVRIGQALKLKSIVRGDAPSSLAASGICKKEPWEPQCFCSNFPHEAVCADPWGQALLVSTDAGVLLVDDDLPSVPVFDRTLPVKQMHVLETLDLLVLRADKGKDARLFVFRLSALQKGLEGKQAGKSRSDCRENKLEKTKGCHLYAINTHHSRELRIVVAIRNKLLLITRKHNKPSGVTSTSLLSPLSESPVEEFQYIREICLSDSPMVMTLVDGPAEESDNLICVAYRHQFDVVNESTGEAFRLHHVEANRVNFVAAIDVYEDGEAGLLLCYNYSCIYKKVCPFNGGSFLVQPSASDFQFCWNQAPYAIVCAFPYLLAFTTDSMEIRLVVNGNLVHTAVVPQLQLVASRSDIYFTATAAVNEVSSGGSSKGASARNSPQTPPGRDTPVFPSSLGEGEIQSKNLYKIPLRNLVGRSIERPLKSPLVSKVITPPTPISVGLAAIPVTHSLSLSRMEIKEIASRTRRELLGLSDEGGPKSEGAPKAKSKPRKRLEESQGGPKPGAVRSSSSDRIPSGSLESASTSEANPEGHSASSDQDPVADREGSPVSGSSPFQLTAFSDEDIIDLK
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
13PhosphorylationCRRFVARSLCIILMK
HHHHHHHHHHHHHHH
20.1825690035
25PhosphorylationLMKHFCSSSVSEDLG
HHHHHHCCCCHHHCC
35.62-
26PhosphorylationMKHFCSSSVSEDLGC
HHHHHCCCCHHHCCC
17.23-
45PhosphorylationFSRKHYGSVELLISS
CCCCCCCEEEEEEEC
12.7828348404
51PhosphorylationGSVELLISSDADGAI
CEEEEEEECCCCCHH
23.33-
52PhosphorylationSVELLISSDADGAIQ
EEEEEEECCCCCHHH
29.80-
124PhosphorylationEKSPFFLSVTLSDQN
CCCCEEEEEEECCCC
14.1124719451
126PhosphorylationSPFFLSVTLSDQNNQ
CCEEEEEEECCCCCC
19.7124719451
128PhosphorylationFFLSVTLSDQNNQRV
EEEEEEECCCCCCCC
27.9924719451
155PhosphorylationTQKICLPYSPTKTLS
CCEEECCCCCCCCCC
17.84-
156PhosphorylationQKICLPYSPTKTLSV
CEEECCCCCCCCCCH
24.93-
158PhosphorylationICLPYSPTKTLSVKS
EECCCCCCCCCCHHH
30.62-
165PhosphorylationTKTLSVKSILSAMNL
CCCCCHHHHHHHCCH
26.9722210691
168PhosphorylationLSVKSILSAMNLDKF
CCHHHHHHHCCHHHH
24.6524719451
240PhosphorylationFLNLLGDTITLKGWT
HHHHHCCEEEEECCC
17.6724114839
242PhosphorylationNLLGDTITLKGWTGY
HHHCCEEEEECCCCC
25.2224114839
259PhosphorylationGLDTKNDTTGIHSVY
CCCCCCCCCCCCEEE
35.9928348404
260PhosphorylationLDTKNDTTGIHSVYT
CCCCCCCCCCCEEEE
36.6828348404
267PhosphorylationTGIHSVYTVYQGHEI
CCCCEEEEEECCCEE
15.5828348404
269PhosphorylationIHSVYTVYQGHEIMF
CCEEEEEECCCEEEE
10.8528348404
284PhosphorylationHVSTMLPYSKENKQQ
EEHHCCCCCHHHHHH
28.5424719451
285PhosphorylationVSTMLPYSKENKQQV
EHHCCCCCHHHHHHH
31.3924719451
389PhosphorylationGEKATLETPTFAQKR
CCCCCCCCCCHHHHH
30.6423917254
395AcetylationETPTFAQKRRRTLDM
CCCCHHHHHHHHHHH
44.4326822725
399PhosphorylationFAQKRRRTLDMLIRS
HHHHHHHHHHHHHHH
25.87-
424PhosphorylationKNMLNRRSFSDVLPE
HHHHHCCCHHHHCCC
26.3529978859
426PhosphorylationMLNRRSFSDVLPESP
HHHCCCHHHHCCCCC
28.2329978859
432PhosphorylationFSDVLPESPKSARKK
HHHHCCCCCCHHHHH
35.3721815630
591PhosphorylationKTKGCHLYAINTHHS
HCCCCEEEEEECCCC
5.0329052541
595PhosphorylationCHLYAINTHHSRELR
CEEEEEECCCCCHHH
18.1729052541
617AcetylationKLLLITRKHNKPSGV
EEEEEECCCCCCCCC
42.77164389
817UbiquitinationVSSGGSSKGASARNS
CCCCCCCCCCCCCCC
61.26-
820PhosphorylationGGSSKGASARNSPQT
CCCCCCCCCCCCCCC
36.11-
824PhosphorylationKGASARNSPQTPPGR
CCCCCCCCCCCCCCC
16.9027251275
827PhosphorylationSARNSPQTPPGRDTP
CCCCCCCCCCCCCCC
34.5321082442
869PhosphorylationSIERPLKSPLVSKVI
CCCCCCCCCCCCCCC
31.0227251275
892PhosphorylationGLAAIPVTHSLSLSR
EEEECCCCCCCCCCH
10.6128348404
894PhosphorylationAAIPVTHSLSLSRME
EECCCCCCCCCCHHH
15.4128348404
896PhosphorylationIPVTHSLSLSRMEIK
CCCCCCCCCCHHHHH
27.5824719451
898PhosphorylationVTHSLSLSRMEIKEI
CCCCCCCCHHHHHHH
26.6327251275
965PhosphorylationIPSGSLESASTSEAN
CCCCCCCCCCCCCCC
32.5827732954
967PhosphorylationSGSLESASTSEANPE
CCCCCCCCCCCCCCC
41.5727732954
968PhosphorylationGSLESASTSEANPEG
CCCCCCCCCCCCCCC
30.2427732954
969PhosphorylationSLESASTSEANPEGH
CCCCCCCCCCCCCCC
32.0127732954
977PhosphorylationEANPEGHSASSDQDP
CCCCCCCCCCCCCCC
40.4827732954
979PhosphorylationNPEGHSASSDQDPVA
CCCCCCCCCCCCCCC
37.1527732954
980PhosphorylationPEGHSASSDQDPVAD
CCCCCCCCCCCCCCC
38.7227732954
991PhosphorylationPVADREGSPVSGSSP
CCCCCCCCCCCCCCC
19.8527732954
994PhosphorylationDREGSPVSGSSPFQL
CCCCCCCCCCCCCEE
36.0227732954
996PhosphorylationEGSPVSGSSPFQLTA
CCCCCCCCCCCEEEE
27.6027732954
997PhosphorylationGSPVSGSSPFQLTAF
CCCCCCCCCCEEEEC
33.0027732954
1002PhosphorylationGSSPFQLTAFSDEDI
CCCCCEEEECCCCCC
18.1827732954
1005PhosphorylationPFQLTAFSDEDIIDL
CCEEEECCCCCCCCC
37.31-

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 GARL3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GARL3_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 GARL3_HUMAN !!

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

Oops, there are no PPI records of GARL3_HUMAN !!

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 GARL3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-827, AND MASSSPECTROMETRY.

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