RGS14_HUMAN - dbPTM
RGS14_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RGS14_HUMAN
UniProt AC O43566
Protein Name Regulator of G-protein signaling 14
Gene Name RGS14
Organism Homo sapiens (Human).
Sequence Length 566
Subcellular Localization Nucleus. Nucleus, PML body. Cytoplasm . Membrane. Cell membrane. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle . Cytoplasm, cytoskeleton, spindle pole. Cell projection, dendrite. Cell projection, dend
Protein Description Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. Besides, modulates signal transduction via G protein alpha subunits by functioning as a GDP-dissociation inhibitor (GDI). Has GDI activity on G(i) alpha subunits GNAI1 and GNAI3, but not on GNAI2 and G(o) alpha subunit GNAO1. Has GAP activity on GNAI0, GNAI2 and GNAI3. May act as a scaffold integrating G protein and Ras/Raf MAPkinase signaling pathways. Inhibits platelet-derived growth factor (PDGF)-stimulated ERK1/ERK2 phosphorylation; a process depending on its interaction with HRAS and that is reversed by G(i) alpha subunit GNAI1. Acts as a positive modulator of microtubule polymerisation and spindle organization through a G(i)-alpha-dependent mechanism. Plays a role in cell division. Required for the nerve growth factor (NGF)-mediated neurite outgrowth. Involved in stress resistance. May be involved in visual memory processing capacity and hippocampal-based learning and memory..
Protein Sequence MPGKPKHLGVPNGRMVLAVSDGELSSTTGPQGQGEGRGSSLSIHSLPSGPSSPFPTEEQPVASWALSFERLLQDPLGLAYFTEFLKKEFSAENVTFWKACERFQQIPASDTQQLAQEARNIYQEFLSSQALSPVNIDRQAWLGEEVLAEPRPDMFRAQQLQIFNLMKFDSYARFVKSPLYRECLLAEAEGRPLREPGSSRLGSPDATRKKPKLKPGKSLPLGVEELGQLPPVEGPGGRPLRKSFRRELGGTANAALRRESQGSLNSSASLDLGFLAFVSSKSESHRKSLGSTEGESESRPGKYCCVYLPDGTASLALARPGLTIRDMLAGICEKRGLSLPDIKVYLVGNEQALVLDQDCTVLADQEVRLENRITFELELTALERVVRISAKPTKRLQEALQPILEKHGLSPLEVVLHRPGEKQPLDLGKLVSSVAAQRLVLDTLPGVKISKARDKSPCRSQGCPPRTQDKATHPPPASPSSLVKVPSSATGKRQTCDIEGLVELLNRVQSSGAHDQRGLLRKEDLVLPEFLQLPAQGPSSEETPPQTKSAAQPIGGSLNSTTDSAL
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
20PhosphorylationGRMVLAVSDGELSST
CCEEEEEECCCCCCC		34.0023401153
25PhosphorylationAVSDGELSSTTGPQG
EEECCCCCCCCCCCC		22.7229978859
26PhosphorylationVSDGELSSTTGPQGQ
EECCCCCCCCCCCCC		42.4829978859
27PhosphorylationSDGELSSTTGPQGQG
ECCCCCCCCCCCCCC		32.1829978859
28PhosphorylationDGELSSTTGPQGQGE
CCCCCCCCCCCCCCC		49.1429978859
37MethylationPQGQGEGRGSSLSIH
CCCCCCCCCCCEEEE		37.20115383627
39PhosphorylationGQGEGRGSSLSIHSL
CCCCCCCCCEEEEEC		27.0928450419
40PhosphorylationQGEGRGSSLSIHSLP
CCCCCCCCEEEEECC		29.0328450419
42PhosphorylationEGRGSSLSIHSLPSG
CCCCCCEEEEECCCC		21.8728464451
45PhosphorylationGSSLSIHSLPSGPSS
CCCEEEEECCCCCCC		40.0628464451
48PhosphorylationLSIHSLPSGPSSPFP
EEEEECCCCCCCCCC		69.5028450419
51PhosphorylationHSLPSGPSSPFPTEE
EECCCCCCCCCCCCC		54.9228450419
52PhosphorylationSLPSGPSSPFPTEEQ
ECCCCCCCCCCCCCC		33.4228464451
56PhosphorylationGPSSPFPTEEQPVAS
CCCCCCCCCCCCCHH		53.1628450419
63PhosphorylationTEEQPVASWALSFER
CCCCCCHHHHHCHHH		17.0827080861
67PhosphorylationPVASWALSFERLLQD
CCHHHHHCHHHHHCC		19.8128450419
86UbiquitinationAYFTEFLKKEFSAEN
HHHHHHHHHHCCCHH		56.42-
90PhosphorylationEFLKKEFSAENVTFW
HHHHHHCCCHHCCHH		35.4526074081
95PhosphorylationEFSAENVTFWKACER
HCCCHHCCHHHHHHH		35.0526074081
98UbiquitinationAENVTFWKACERFQQ
CHHCCHHHHHHHHHC		38.68-
122PhosphorylationAQEARNIYQEFLSSQ
HHHHHHHHHHHHHCC		12.9228796482
127PhosphorylationNIYQEFLSSQALSPV
HHHHHHHHCCCCCCC		26.2329978859
128PhosphorylationIYQEFLSSQALSPVN
HHHHHHHCCCCCCCC		22.9429978859
132PhosphorylationFLSSQALSPVNIDRQ
HHHCCCCCCCCCCCH		29.8024076635
176UbiquitinationDSYARFVKSPLYREC
HHHHHHHCCHHHHHH		43.5829967540
177PhosphorylationSYARFVKSPLYRECL
HHHHHHCCHHHHHHH		18.1623312004
198PhosphorylationRPLREPGSSRLGSPD
CCCCCCCCCCCCCCC		24.0123401153
199PhosphorylationPLREPGSSRLGSPDA
CCCCCCCCCCCCCCC		37.1230108239
203PhosphorylationPGSSRLGSPDATRKK
CCCCCCCCCCCCCCC		24.9723401153
207PhosphorylationRLGSPDATRKKPKLK
CCCCCCCCCCCCCCC		50.8626552605
218PhosphorylationPKLKPGKSLPLGVEE
CCCCCCCCCCCCHHH		40.9320058876
243PhosphorylationGGRPLRKSFRRELGG
CCCCCHHHHHHHHCC		19.9726074081
251PhosphorylationFRRELGGTANAALRR
HHHHHCCHHHHHHHH		18.23-
260PhosphorylationNAALRRESQGSLNSS
HHHHHHHCCCCCCCC		37.7212534294
263PhosphorylationLRRESQGSLNSSASL
HHHHCCCCCCCCCCC		19.4227251275
266PhosphorylationESQGSLNSSASLDLG
HCCCCCCCCCCCCHH		32.3527080861
267PhosphorylationSQGSLNSSASLDLGF
CCCCCCCCCCCCHHH		22.3227080861
269PhosphorylationGSLNSSASLDLGFLA
CCCCCCCCCCHHHHE		25.1027080861
282PhosphorylationLAFVSSKSESHRKSL
HEHHCCCCHHHHHHC		46.4023312004
284PhosphorylationFVSSKSESHRKSLGS
HHCCCCHHHHHHCCC		35.3723312004
287UbiquitinationSKSESHRKSLGSTEG
CCCHHHHHHCCCCCC		44.61-
288PhosphorylationKSESHRKSLGSTEGE
CCHHHHHHCCCCCCC		37.6123401153
291PhosphorylationSHRKSLGSTEGESES
HHHHHCCCCCCCCCC		28.6923401153
292PhosphorylationHRKSLGSTEGESESR
HHHHCCCCCCCCCCC		46.3323927012
296PhosphorylationLGSTEGESESRPGKY
CCCCCCCCCCCCCCE		52.2923927012
298PhosphorylationSTEGESESRPGKYCC
CCCCCCCCCCCCEEE		53.7223927012
302UbiquitinationESESRPGKYCCVYLP
CCCCCCCCEEEEECC		37.4929967540
338PhosphorylationICEKRGLSLPDIKVY
HHHHCCCCCCCCEEE		40.4522985185
410PhosphorylationILEKHGLSPLEVVLH
HHHHCCCCCEEEEEE		31.8423898821
422UbiquitinationVLHRPGEKQPLDLGK
EEECCCCCCCCCHHH		64.2329967540
429UbiquitinationKQPLDLGKLVSSVAA
CCCCCHHHHHHHHHH		53.6829967540
448UbiquitinationLDTLPGVKISKARDK
HHCCCCCEECCCCCC		47.3729967540
456PhosphorylationISKARDKSPCRSQGC
ECCCCCCCCCHHCCC		33.2626074081
460PhosphorylationRDKSPCRSQGCPPRT
CCCCCCHHCCCCCCC		37.3326074081
472PhosphorylationPRTQDKATHPPPASP
CCCCCCCCCCCCCCH		40.4326552605
478PhosphorylationATHPPPASPSSLVKV
CCCCCCCCHHHHEEC		30.9628787133
480PhosphorylationHPPPASPSSLVKVPS
CCCCCCHHHHEECCC		33.5328787133
481PhosphorylationPPPASPSSLVKVPSS
CCCCCHHHHEECCCC		40.3328122231
484UbiquitinationASPSSLVKVPSSATG
CCHHHHEECCCCCCC		54.4429967540
487PhosphorylationSSLVKVPSSATGKRQ
HHHEECCCCCCCCCC		35.2826074081
488PhosphorylationSLVKVPSSATGKRQT
HHEECCCCCCCCCCC		24.6326074081
490PhosphorylationVKVPSSATGKRQTCD
EECCCCCCCCCCCCC		45.2226074081
492UbiquitinationVPSSATGKRQTCDIE
CCCCCCCCCCCCCHH		36.6629967540
495PhosphorylationSATGKRQTCDIEGLV
CCCCCCCCCCHHHHH		19.0426074081
496PhosphorylationATGKRQTCDIEGLVE
CCCCCCCCCHHHHHH		3.6212534294
510PhosphorylationELLNRVQSSGAHDQR
HHHHHHHHCCCCCCC		28.07-
522UbiquitinationDQRGLLRKEDLVLPE
CCCCCCCHHHCCCHH		56.3929967540
539PhosphorylationQLPAQGPSSEETPPQ
CCCCCCCCCCCCCCC		58.1528122231
540PhosphorylationLPAQGPSSEETPPQT
CCCCCCCCCCCCCCC		42.4528122231
543PhosphorylationQGPSSEETPPQTKSA
CCCCCCCCCCCCCCC		35.9028122231
547PhosphorylationSEETPPQTKSAAQPI
CCCCCCCCCCCCCCC		32.5128122231
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
260SPhosphorylationKinasePKA-FAMILY-GPS
260SPhosphorylationKinasePKA_GROUP-PhosphoELM
495TPhosphorylationKinasePKA-FAMILY-GPS
496TPhosphorylationKinasePKA_GROUP-PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RGS14_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 RGS14_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAP2A_HUMANRAP2Aphysical
10926822
RAP1A_HUMANRAP1Aphysical
10926822
GNAI1_HUMANGNAI1physical
11976690
GNAI1_HUMANGNAI1physical
11387333
GNAI2_HUMANGNAI2physical
11387333
GNAI3_HUMANGNAI3physical
11387333
GNA11_HUMANGNA11physical
17603074
A4_HUMANAPPphysical
21832049
WASP_HUMANWASphysical
21988832
XPO1_HUMANXPO1physical
21988832
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 RGS14_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-42; SER-45 ANDSER-260, AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory