RGL1_HUMAN - dbPTM
RGL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RGL1_HUMAN
UniProt AC Q9NZL6
Protein Name Ral guanine nucleotide dissociation stimulator-like 1
Gene Name RGL1
Organism Homo sapiens (Human).
Sequence Length 768
Subcellular Localization
Protein Description Probable guanine nucleotide exchange factor..
Protein Sequence MKLLWQAKMSSIQDWGEEVEEGAVYHVTLKRVQIQQAANKGARWLGVEGDQLPPGHTVSQYETCKIRTIKAGTLEKLVENLLTAFGDNDFTYISIFLSTYRGFASTKEVLELLLDRYGNLTSPNCEEDGSQSSSESKMVIRNAIASILRAWLDQCAEDFREPPHFPCLQKLLDYLTRMMPGSDPERRAQNLLEQFQKQEVETDNGLPNTISFSLEEEEELEGGESAEFTCFSEDLVAEQLTYMDAQLFKKVVPHHCLGCIWSRRDKKENKHLAPTIRATISQFNTLTKCVVSTILGGKELKTQQRAKIIEKWINIAHECRLLKNFSSLRAIVSALQSNSIYRLKKTWAAVPRDRMLMFEELSDIFSDHNNHLTSRELLMKEGTSKFANLDSSVKENQKRTQRRLQLQKDMGVMQGTVPYLGTFLTDLTMLDTALQDYIEGGLINFEKRRREFEVIAQIKLLQSACNSYCMTPDQKFIQWFQRQQLLTEEESYALSCEIEAAADASTTSPKPRKSMVKRLSLLFLGSDMITSPTPTKEQPKSTASGSSGESMDSVSVSSCESNHSEAEEGSITPMDTPDEPQKKLSESSSSCSSIHSMDTNSSGMSSLINPLSSPPSCNNNPKIHKRSVSVTSITSTVLPPVYNQQNEDTCIIRISVEDNNGNMYKSIMLTSQDKTPAVIQRAMLKHNLDSDPAEEYELVQVISEDKELVIPDSANVFYAMNSQVNFDFILRKKNSMEEQVKLRSRTSLTLPRTAKRGCWSNRHSKITL
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
11PhosphorylationLWQAKMSSIQDWGEE
HHHHHHHCCHHHHHH		22.2922468782
17 (in isoform 2)Methylation-55.40-
21 (in isoform 2)Methylation-58.59-
122PhosphorylationDRYGNLTSPNCEEDG
HHHCCCCCCCCCCCC		19.7922210691
133PhosphorylationEEDGSQSSSESKMVI
CCCCCCCCHHHHHHH		30.4122210691
326PhosphorylationCRLLKNFSSLRAIVS
HHHHHCHHHHHHHHH		37.5423312004
327PhosphorylationRLLKNFSSLRAIVSA
HHHHCHHHHHHHHHH		20.1024719451
333PhosphorylationSSLRAIVSALQSNSI
HHHHHHHHHHHCCCC		19.6920873877
337PhosphorylationAIVSALQSNSIYRLK
HHHHHHHCCCCHHCH		33.1320873877
339PhosphorylationVSALQSNSIYRLKKT
HHHHHCCCCHHCHHH		26.6628857561
341PhosphorylationALQSNSIYRLKKTWA
HHHCCCCHHCHHHHE		15.0920873877
346PhosphorylationSIYRLKKTWAAVPRD
CCHHCHHHHEECCHH		20.8124719451
362PhosphorylationMLMFEELSDIFSDHN
EEHHHHHHHHHCCCC		31.75-
381 (in isoform 2)Phosphorylation-54.4624719451
383PhosphorylationELLMKEGTSKFANLD
HHHHHHCCHHHCCCC		29.8129083192
384PhosphorylationLLMKEGTSKFANLDS
HHHHHCCHHHCCCCH		36.3129083192
495PhosphorylationEEESYALSCEIEAAA
HHHHHHHHHEEEECC		11.0927251275
505PhosphorylationIEAAADASTTSPKPR
EEECCCCCCCCCCCC		32.5328348404
506PhosphorylationEAAADASTTSPKPRK
EECCCCCCCCCCCCH		32.7728857561
507PhosphorylationAAADASTTSPKPRKS
ECCCCCCCCCCCCHH		40.3028857561
508PhosphorylationAADASTTSPKPRKSM
CCCCCCCCCCCCHHH		30.8928857561
520PhosphorylationKSMVKRLSLLFLGSD
HHHHHHHHHHHHCCC		27.3623403867
526PhosphorylationLSLLFLGSDMITSPT
HHHHHHCCCCCCCCC		26.5923403867
543 (in isoform 2)Phosphorylation-20.9827251275
555 (in isoform 2)Phosphorylation-21.8924719451
627PhosphorylationNPKIHKRSVSVTSIT
CCCCCCCCCEEEEEE		24.4428348404
629PhosphorylationKIHKRSVSVTSITST
CCCCCCCEEEEEEEE		22.4126657352
631PhosphorylationHKRSVSVTSITSTVL
CCCCCEEEEEEEEEC		13.6029116813
632PhosphorylationKRSVSVTSITSTVLP
CCCCEEEEEEEEECC		23.0129802988
634PhosphorylationSVSVTSITSTVLPPV
CCEEEEEEEEECCCC		20.3629116813
635PhosphorylationVSVTSITSTVLPPVY
CEEEEEEEEECCCCC		18.1730177828
636PhosphorylationSVTSITSTVLPPVYN
EEEEEEEEECCCCCC		19.8829116813
664 (in isoform 2)Phosphorylation-12.9424719451
666 (in isoform 2)Phosphorylation-8.8527251275
669 (in isoform 2)Phosphorylation-3.8727251275
670PhosphorylationMYKSIMLTSQDKTPA
EEEEEEEECCCCCHH		13.6318187866
671 (in isoform 2)Phosphorylation-32.2127251275
746PhosphorylationQVKLRSRTSLTLPRT
HHHHHCCCCCCCCCC		29.3623403867
747PhosphorylationVKLRSRTSLTLPRTA
HHHHCCCCCCCCCCC		20.4623403867
749PhosphorylationLRSRTSLTLPRTAKR
HHCCCCCCCCCCCCC		34.1923403867
764PhosphorylationGCWSNRHSKITL---
CCCCCCCCCCCC---		23.6324501219
767PhosphorylationSNRHSKITL------
CCCCCCCCC------		30.1024719451
784 (in isoform 2)Phosphorylation-24719451
802 (in isoform 2)Phosphorylation-24719451
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 RGL1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RGL1_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 RGL1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
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 RGL1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-670, AND MASSSPECTROMETRY.

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