GRSF1_HUMAN - dbPTM
GRSF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GRSF1_HUMAN
UniProt AC Q12849
Protein Name G-rich sequence factor 1
Gene Name GRSF1
Organism Homo sapiens (Human).
Sequence Length 480
Subcellular Localization Cytoplasm. Mitochondrion matrix, mitochondrion nucleoid . Localizes to mitochondrial RNA granules found in close proximity to the mitochondrial nucleoids.
Protein Description Regulator of post-transcriptional mitochondrial gene expression, required for assembly of the mitochondrial ribosome and for recruitment of mRNA and lncRNA. Binds RNAs containing the 14 base G-rich element. Preferentially binds RNAs transcribed from three contiguous genes on the light strand of mtDNA, the ND6 mRNA, and the long non-coding RNAs for MT-CYB and MT-ND5, each of which contains multiple consensus binding sequences..
Protein Sequence MAGTRWVLGALLRGCGCNCSSCRRTGAACLPFYSAAGSIPSGVSGRRRLLLLLGAAAAAASQTRGLQTGPVPPGRLAGPPAVATSAAAAAAASYSALRASLLPQSLAAAAAVPTRSYSQESKTTYLEDLPPPPEYELAPSKLEEEVDDVFLIRAQGLPWSCTMEDVLNFFSDCRIRNGENGIHFLLNRDGKRRGDALIEMESEQDVQKALEKHRMYMGQRYVEVYEINNEDVDALMKSLQVKSSPVVNDGVVRLRGLPYSCNEKDIVDFFAGLNIVDITFVMDYRGRRKTGEAYVQFEEPEMANQALLKHREEIGNRYIEIFPSRRNEVRTHVGSYKGKKIASFPTAKYITEPEMVFEEHEVNEDIQPMTAFESEKEIELPKEVPEKLPEAADFGTTSSLHFVHMRGLPFQANAQDIINFFAPLKPVRITMEYSSSGKATGEADVHFETHEDAVAAMLKDRSHVHHRYIELFLNSCPKGK
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
25PhosphorylationNCSSCRRTGAACLPF
CCHHCCCCCCCCEEE		16.30-
33PhosphorylationGAACLPFYSAAGSIP
CCCCEEEHHHCCCCC		8.75-
34PhosphorylationAACLPFYSAAGSIPS
CCCEEEHHHCCCCCC		16.42-
80UbiquitinationPGRLAGPPAVATSAA
CCCCCCCCHHHHHHH		38.1521890473
82 (in isoform 5)Phosphorylation-8.02-
100O-linked_GlycosylationSYSALRASLLPQSLA
HHHHHHHHHCCHHHH		24.8155821241
105O-linked_GlycosylationRASLLPQSLAAAAAV
HHHHCCHHHHHHHCC		20.3155821245
114O-linked_GlycosylationAAAAAVPTRSYSQES
HHHHCCCCCCCCCCC		26.1655821251
114PhosphorylationAAAAAVPTRSYSQES
HHHHCCCCCCCCCCC		26.1628102081
116PhosphorylationAAAVPTRSYSQESKT
HHCCCCCCCCCCCCC		31.4526437602
118PhosphorylationAVPTRSYSQESKTTY
CCCCCCCCCCCCCCC		28.8128985074
121PhosphorylationTRSYSQESKTTYLED
CCCCCCCCCCCCHHC		27.8928102081
135PhosphorylationDLPPPPEYELAPSKL
CCCCCCCCCCCCHHH		23.2428674151
191AcetylationFLLNRDGKRRGDALI
EEECCCCCCCCCEEE		43.1269083
200SulfoxidationRGDALIEMESEQDVQ
CCCEEEECCCHHHHH		5.6421406390
202PhosphorylationDALIEMESEQDVQKA
CEEEECCCHHHHHHH		38.97-
208UbiquitinationESEQDVQKALEKHRM
CCHHHHHHHHHHHCH		55.58-
208AcetylationESEQDVQKALEKHRM
CCHHHHHHHHHHHCH		55.5869087
212AcetylationDVQKALEKHRMYMGQ
HHHHHHHHHCHHHCC		37.0469091
238PhosphorylationDVDALMKSLQVKSSP
HHHHHHHHCCCCCCC		15.2928464451
242 (in isoform 1)Ubiquitination-32.0521906983
242UbiquitinationLMKSLQVKSSPVVND
HHHHCCCCCCCCCCC		32.0521890473
243PhosphorylationMKSLQVKSSPVVNDG
HHHCCCCCCCCCCCC		40.8030266825
244PhosphorylationKSLQVKSSPVVNDGV
HHCCCCCCCCCCCCE		18.9230266825
294PhosphorylationRRKTGEAYVQFEEPE
CCCCCCEEEEECCHH		7.18-
309AcetylationMANQALLKHREEIGN
HHHHHHHHHHHHHHH		41.2727452117
309UbiquitinationMANQALLKHREEIGN
HHHHHHHHHHHHHHH		41.27-
318PhosphorylationREEIGNRYIEIFPSR
HHHHHHHEEEECCCC		13.6028152594
324PhosphorylationRYIEIFPSRRNEVRT
HEEEECCCCCCCCCC		32.8726074081
331PhosphorylationSRRNEVRTHVGSYKG
CCCCCCCCCCCCCCC		26.5329396449
335PhosphorylationEVRTHVGSYKGKKIA
CCCCCCCCCCCCEEE		23.6828102081
336PhosphorylationVRTHVGSYKGKKIAS
CCCCCCCCCCCEEEC		20.1729396449
3372-HydroxyisobutyrylationRTHVGSYKGKKIASF
CCCCCCCCCCEEECC		66.98-
340UbiquitinationVGSYKGKKIASFPTA
CCCCCCCEEECCCCC		52.77-
343PhosphorylationYKGKKIASFPTAKYI
CCCCEEECCCCCEEC		34.9226074081
346PhosphorylationKKIASFPTAKYITEP
CEEECCCCCEECCCH		33.5026074081
349PhosphorylationASFPTAKYITEPEMV
ECCCCCEECCCHHHC		15.6026074081
351PhosphorylationFPTAKYITEPEMVFE
CCCCEECCCHHHCEE		42.2626074081
376SumoylationMTAFESEKEIELPKE
CCCCCCCCCCCCCCC		73.58-
425UbiquitinationINFFAPLKPVRITME
HHHHCCCCCEEEEEE		40.17-
434PhosphorylationVRITMEYSSSGKATG
EEEEEEECCCCCCCC		12.53-
435PhosphorylationRITMEYSSSGKATGE
EEEEEECCCCCCCCE		42.06-
436PhosphorylationITMEYSSSGKATGEA
EEEEECCCCCCCCEE		38.07-
468PhosphorylationRSHVHHRYIELFLNS
CCCHHHHHHHHHHHC		8.3928152594
478UbiquitinationLFLNSCPKGK-----
HHHHCCCCCC-----		81.37-
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 GRSF1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GRSF1_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 GRSF1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HCD2_HUMANHSD17B10physical
23473034
MRRP1_HUMANTRMT10Cphysical
23473034
RT26_HUMANMRPS26physical
23473034
RM11_HUMANMRPL11physical
23473034
TFAM_HUMANTFAMphysical
23473034
NDKM_HUMANNME4physical
23473034
RT25_HUMANMRPS25physical
23473034
GRP75_HUMANHSPA9physical
23473034
RL28_HUMANRPL28physical
23473034
RL14_HUMANRPL14physical
23473034
RT34_HUMANMRPS34physical
23473034
RT22_HUMANMRPS22physical
23473034
RM47_HUMANMRPL47physical
23473034
MRM3_HUMANRNMTL1physical
23473034
RM48_HUMANMRPL48physical
23473034
RT07_HUMANMRPS7physical
23473034
ATPB_HUMANATP5Bphysical
23473034
ATPO_HUMANATP5Ophysical
23473034
ECHA_HUMANHADHAphysical
23473034
C1QBP_HUMANC1QBPphysical
23473034
SYHM_HUMANHARS2physical
23473034
RT15_HUMANMRPS15physical
23473034
RT02_HUMANMRPS2physical
23473034
DHX30_HUMANDHX30physical
23473034
PTCD3_HUMANPTCD3physical
23473034
RM24_HUMANMRPL24physical
23473034
RT27_HUMANMRPS27physical
23473034
PAPD1_HUMANMTPAPphysical
23473034
RM02_HUMANMRPL2physical
23473034
RM21_HUMANMRPL21physical
23473034
RT29_HUMANDAP3physical
23473034
RM04_HUMANMRPL4physical
23473034
PNPT1_HUMANPNPT1physical
23473034
RM28_HUMANMRPL28physical
23473034
MDHM_HUMANMDH2physical
23473034
RT28_HUMANMRPS28physical
23473034
RT31_HUMANMRPS31physical
23473034
ACOT9_HUMANACOT9physical
23473034
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 GRSF1_HUMAN

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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-244, AND MASSSPECTROMETRY.

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