LARP6_HUMAN - dbPTM
LARP6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LARP6_HUMAN
UniProt AC Q9BRS8
Protein Name La-related protein 6
Gene Name LARP6
Organism Homo sapiens (Human).
Sequence Length 491
Subcellular Localization Cytoplasm . Nucleus . Shuttles between the nucleus and the cytoplasm.
Protein Description Regulates the coordinated translation of type I collagen alpha-1 and alpha-2 mRNAs, CO1A1 and CO1A2. Stabilizes mRNAs through high-affinity binding of a stem-loop structure in their 5' UTR. This regulation requires VIM and MYH10 filaments, and the helicase DHX9..
Protein Sequence MAQSGGEARPGPKTAVQIRVAIQEAEDVDELEDEEEGAETRGAGDPARYLSPGWGSASEEEPSRGHSGTTASGGENEREDLEQEWKPPDEELIKKLVDQIEFYFSDENLEKDAFLLKHVRRNKLGYVSVKLLTSFKKVKHLTRDWRTTAHALKYSVVLELNEDHRKVRRTTPVPLFPNENLPSKMLLVYDLYLSPKLWALATPQKNGRVQEKVMEHLLKLFGTFGVISSVRILKPGRELPPDIRRISSRYSQVGTQECAIVEFEEVEAAIKAHEFMITESQGKENMKAVLIGMKPPKKKPAKDKNHDEEPTASIHLNKSLNKRVEELQYMGDESSANSSSDPESNPTSPMAGRRHAATNKLSPSGHQNLFLSPNASPCTSPWSSPLAQRKGVSRKSPLAEEGRLNCSTSPEIFRKCMDYSSDSSVTPSGSPWVRRRRQAEMGTQEKSPGTSPLLSRKMQTADGLPVGVLRLPRGPDNTRGFHGHERSRACV
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
2Acetylation------MAQSGGEAR
------CCCCCCCCC		16.5519413330
41MethylationEEEGAETRGAGDPAR
HHCHHHCCCCCCHHH		25.19115481847
49PhosphorylationGAGDPARYLSPGWGS
CCCCHHHHCCCCCCC		17.4030266825
51PhosphorylationGDPARYLSPGWGSAS
CCHHHHCCCCCCCCC		16.6630266825
56PhosphorylationYLSPGWGSASEEEPS
HCCCCCCCCCCCCCC		23.3230266825
58PhosphorylationSPGWGSASEEEPSRG
CCCCCCCCCCCCCCC		47.4330266825
63PhosphorylationSASEEEPSRGHSGTT
CCCCCCCCCCCCCCC		54.9230266825
67PhosphorylationEEPSRGHSGTTASGG
CCCCCCCCCCCCCCC		40.4330206219
69PhosphorylationPSRGHSGTTASGGEN
CCCCCCCCCCCCCCC		23.3930206219
70PhosphorylationSRGHSGTTASGGENE
CCCCCCCCCCCCCCH		23.5030624053
72PhosphorylationGHSGTTASGGENERE
CCCCCCCCCCCCHHH		45.2828985074
117MalonylationEKDAFLLKHVRRNKL
HHHHHHHHHHHHCCC		42.0526320211
128PhosphorylationRNKLGYVSVKLLTSF
HCCCCEEEHHHHHCH		12.68-
133PhosphorylationYVSVKLLTSFKKVKH
EEEHHHHHCHHHHHH		42.4223312004
134PhosphorylationVSVKLLTSFKKVKHL
EEHHHHHCHHHHHHH		34.7323312004
147PhosphorylationHLTRDWRTTAHALKY
HHCCCHHHHHHHHHH		24.8730206219
148PhosphorylationLTRDWRTTAHALKYS
HCCCHHHHHHHHHHE		14.1030206219
154PhosphorylationTTAHALKYSVVLELN
HHHHHHHHEEEEEEC		13.9330206219
155PhosphorylationTAHALKYSVVLELNE
HHHHHHHEEEEEECC		12.2630206219
183PhosphorylationFPNENLPSKMLLVYD
CCCCCCCCCEEEEEE		33.5924719451
194PhosphorylationLVYDLYLSPKLWALA
EEEEEHHCHHHHHHH		13.3624719451
202PhosphorylationPKLWALATPQKNGRV
HHHHHHHCCCCCCHH		27.4022199227
225PhosphorylationLKLFGTFGVISSVRI
HHHHHHHHHHEEEEE		18.7132142685
228PhosphorylationFGTFGVISSVRILKP
HHHHHHHEEEEECCC		22.0024719451
247PhosphorylationPPDIRRISSRYSQVG
CCCHHHHHHHHHCCC		13.6227282143
267PhosphorylationIVEFEEVEAAIKAHE
EEEHHHHHHHHHHHE		35.3532645325
338PhosphorylationGDESSANSSSDPESN
CCCCCCCCCCCCCCC		30.8228348404
339PhosphorylationDESSANSSSDPESNP
CCCCCCCCCCCCCCC		38.2728348404
340PhosphorylationESSANSSSDPESNPT
CCCCCCCCCCCCCCC		57.9428348404
344PhosphorylationNSSSDPESNPTSPMA
CCCCCCCCCCCCCCC		54.2028348404
347PhosphorylationSDPESNPTSPMAGRR
CCCCCCCCCCCCCHH		50.1130624053
348PhosphorylationDPESNPTSPMAGRRH
CCCCCCCCCCCCHHC		17.5930624053
362PhosphorylationHAATNKLSPSGHQNL
CCCCCCCCCCCCCCC		20.7329514088
364PhosphorylationATNKLSPSGHQNLFL
CCCCCCCCCCCCCEE		45.6029514088
372PhosphorylationGHQNLFLSPNASPCT
CCCCCEECCCCCCCC		14.5827422710
376PhosphorylationLFLSPNASPCTSPWS
CEECCCCCCCCCCCC		27.4427422710
379PhosphorylationSPNASPCTSPWSSPL
CCCCCCCCCCCCCHH		41.0029514088
380PhosphorylationPNASPCTSPWSSPLA
CCCCCCCCCCCCHHH		30.9627422710
383PhosphorylationSPCTSPWSSPLAQRK
CCCCCCCCCHHHHHC		26.0129514088
384PhosphorylationPCTSPWSSPLAQRKG
CCCCCCCCHHHHHCC		21.7727422710
393PhosphorylationLAQRKGVSRKSPLAE
HHHHCCCCCCCCCHH		42.5326699800
396PhosphorylationRKGVSRKSPLAEEGR
HCCCCCCCCCHHHCC		24.8422199227
407PhosphorylationEEGRLNCSTSPEIFR
HHCCCCCCCCHHHHH		30.7430266825
408PhosphorylationEGRLNCSTSPEIFRK
HCCCCCCCCHHHHHH		50.9630266825
409PhosphorylationGRLNCSTSPEIFRKC
CCCCCCCCHHHHHHH		12.3019664994
419PhosphorylationIFRKCMDYSSDSSVT
HHHHHHCCCCCCCCC		5.3428985074
420PhosphorylationFRKCMDYSSDSSVTP
HHHHHCCCCCCCCCC		24.3325954137
421PhosphorylationRKCMDYSSDSSVTPS
HHHHCCCCCCCCCCC		34.9728348404
423PhosphorylationCMDYSSDSSVTPSGS
HHCCCCCCCCCCCCC		28.7630576142
424PhosphorylationMDYSSDSSVTPSGSP
HCCCCCCCCCCCCCH		34.6925954137
426PhosphorylationYSSDSSVTPSGSPWV
CCCCCCCCCCCCHHH		17.4324129246
428PhosphorylationSDSSVTPSGSPWVRR
CCCCCCCCCCHHHHH		42.4024129246
430PhosphorylationSSVTPSGSPWVRRRR
CCCCCCCCHHHHHHH		21.6728985074
443PhosphorylationRRQAEMGTQEKSPGT
HHHHHCCCCCCCCCC		32.0423927012
447PhosphorylationEMGTQEKSPGTSPLL
HCCCCCCCCCCCHHH		28.0126503892
450PhosphorylationTQEKSPGTSPLLSRK
CCCCCCCCCHHHHHH		30.4730266825
451PhosphorylationQEKSPGTSPLLSRKM
CCCCCCCCHHHHHHC		21.3326503892
455PhosphorylationPGTSPLLSRKMQTAD
CCCCHHHHHHCCCCC		37.2222167270
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
348SPhosphorylationKinaseMTORP42345
PSP
409SPhosphorylationKinaseMTORP42345
PSP
451SPhosphorylationKinaseAKT1P31749
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LARP6_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 LARP6_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 LARP6_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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-447 AND SER-451, AND MASS SPECTROMETRY.
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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-447 AND SER-451, AND MASS SPECTROMETRY.
"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 SER-56; SER-58; SER-447 ANDSER-451, AND MASS SPECTROMETRY.

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