KLRG2_HUMAN - dbPTM
KLRG2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KLRG2_HUMAN
UniProt AC A4D1S0
Protein Name Killer cell lectin-like receptor subfamily G member 2
Gene Name KLRG2
Organism Homo sapiens (Human).
Sequence Length 409
Subcellular Localization Membrane
Single-pass membrane protein .
Protein Description
Protein Sequence MEESWEAAPGGQAGAELPMEPVGSLVPTLEQPQVPAKVRQPEGPESSPSPAGAVEKAAGAGLEPSSKKKPPSPRPGSPRVPPLSLGYGVCPEPPSPGPALVKLPRNGEAPGAEPAPSAWAPMELQVDVRVKPVGAAGGSSTPSPRPSTRFLKVPVPESPAFSRHADPAHQLLLRAPSQGGTWGRRSPLAAARTESGCDAEGRASPAEGSAGSPGSPTCCRCKELGLEKEDAALLPRAGLDGDEKLPRAVTLTGLPMYVKSLYWALAFMAVLLAVSGVVIVVLASRAGARCQQCPPGWVLSEEHCYYFSAEAQAWEASQAFCSAYHATLPLLSHTQDFLGRYPVSRHSWVGAWRGPQGWHWIDEAPLPPQLLPEDGEDNLDINCGALEEGTLVAANCSTPRPWVCAKGTQ
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
1Acetylation-------MEESWEAA
-------CCCCCCCC		13.39-
46PhosphorylationRQPEGPESSPSPAGA
CCCCCCCCCCCCHHH		51.1628102081
47PhosphorylationQPEGPESSPSPAGAV
CCCCCCCCCCCHHHH		27.9521712546
49PhosphorylationEGPESSPSPAGAVEK
CCCCCCCCCHHHHHH		29.3621712546
72PhosphorylationSSKKKPPSPRPGSPR
CCCCCCCCCCCCCCC		41.9123312004
77PhosphorylationPPSPRPGSPRVPPLS
CCCCCCCCCCCCCCC		16.5323312004
84PhosphorylationSPRVPPLSLGYGVCP
CCCCCCCCCCCEECC		26.0626356563
87PhosphorylationVPPLSLGYGVCPEPP
CCCCCCCCEECCCCC		16.2126356563
95PhosphorylationGVCPEPPSPGPALVK
EECCCCCCCCCCEEE		53.8825849741
139PhosphorylationPVGAAGGSSTPSPRP
ECCCCCCCCCCCCCC		30.0721955146
140PhosphorylationVGAAGGSSTPSPRPS
CCCCCCCCCCCCCCC		47.8422496350
141PhosphorylationGAAGGSSTPSPRPST
CCCCCCCCCCCCCCC		29.5021955146
143PhosphorylationAGGSSTPSPRPSTRF
CCCCCCCCCCCCCCC		33.3621955146
147PhosphorylationSTPSPRPSTRFLKVP
CCCCCCCCCCCEEEE		33.2321955146
148PhosphorylationTPSPRPSTRFLKVPV
CCCCCCCCCCEEEEC		28.2921955146
158PhosphorylationLKVPVPESPAFSRHA
EEEECCCCCCHHCCC		18.5619664994
162PhosphorylationVPESPAFSRHADPAH
CCCCCCHHCCCCHHH		25.8427251275
174MethylationPAHQLLLRAPSQGGT
HHHHHHHHCCCCCCC		44.41115481347
177PhosphorylationQLLLRAPSQGGTWGR
HHHHHCCCCCCCCCC		40.2428857561
181PhosphorylationRAPSQGGTWGRRSPL
HCCCCCCCCCCCCHH		31.4125849741
186PhosphorylationGGTWGRRSPLAAART
CCCCCCCCHHHHHHC		23.9324719451
193PhosphorylationSPLAAARTESGCDAE
CHHHHHHCCCCCCCC		29.7628857561
195PhosphorylationLAAARTESGCDAEGR
HHHHHCCCCCCCCCC		44.0728857561
204PhosphorylationCDAEGRASPAEGSAG
CCCCCCCCCCCCCCC		24.2319664994
209PhosphorylationRASPAEGSAGSPGSP
CCCCCCCCCCCCCCC		22.4423663014
212PhosphorylationPAEGSAGSPGSPTCC
CCCCCCCCCCCCCCH		26.2921712546
215PhosphorylationGSAGSPGSPTCCRCK
CCCCCCCCCCCHHCH		22.0321712546
217PhosphorylationAGSPGSPTCCRCKEL
CCCCCCCCCHHCHHH		26.4023663014
244AcetylationAGLDGDEKLPRAVTL
CCCCCCCCCCCCEEC		69.417380721
260PhosphorylationGLPMYVKSLYWALAF
CCCHHHHHHHHHHHH		19.3518491316
262PhosphorylationPMYVKSLYWALAFMA
CHHHHHHHHHHHHHH		8.8418491316
284PhosphorylationVVIVVLASRAGARCQ
CEEEEECCCCCCCCC		20.6418491316
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 KLRG2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KLRG2_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 KLRG2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FGRL1_HUMANFGFRL1physical
28514442
EPHB1_HUMANEPHB1physical
28514442
ZDHC6_HUMANZDHHC6physical
28514442
LTBP1_HUMANLTBP1physical
28514442
WNT11_HUMANWNT11physical
28514442
GLRX3_HUMANGLRX3physical
28514442
FA5_HUMANF5physical
28514442
APBA2_HUMANAPBA2physical
28514442
STBD1_HUMANSTBD1physical
28514442
WNT5B_HUMANWNT5Bphysical
28514442
RL40_HUMANUBA52physical
28514442
LRC4B_HUMANLRRC4Bphysical
28514442
PRS23_HUMANPRSS23physical
28514442
TNFL9_HUMANTNFSF9physical
28514442
PP2BC_HUMANPPP3CCphysical
28514442
CANB1_HUMANPPP3R1physical
28514442
SIA7C_HUMANST6GALNAC3physical
28514442
PTPRS_HUMANPTPRSphysical
28514442
EPHB4_HUMANEPHB4physical
28514442
STK39_HUMANSTK39physical
28514442
FND3B_HUMANFNDC3Bphysical
28514442
TNKS1_HUMANTNKSphysical
28514442
TIMP3_HUMANTIMP3physical
28514442
F1712_HUMANFAM171A2physical
28514442
PP2BB_HUMANPPP3CBphysical
28514442
TM192_HUMANTMEM192physical
28514442
EMIL3_HUMANEMILIN3physical
28514442
CD47_HUMANCD47physical
28514442
EGFL7_HUMANEGFL7physical
28514442
SIA7D_HUMANST6GALNAC4physical
28514442
AURKA_HUMANAURKAphysical
28514442
EPHA4_HUMANEPHA4physical
28514442
COL12_HUMANCOLEC12physical
28514442
ZDH18_HUMANZDHHC18physical
28514442
UBXN1_HUMANUBXN1physical
28514442
P121A_HUMANPOM121physical
28514442
GXLT2_HUMANGXYLT2physical
28514442
PP2BA_HUMANPPP3CAphysical
28514442
TOR1B_HUMANTOR1Bphysical
28514442
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 KLRG2_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 MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-204; SER-209; SER-212 AND SER-215, AND MASSSPECTROMETRY.
Phosphorylation
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 MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-204; SER-209; SER-212 AND SER-215, AND MASSSPECTROMETRY.

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