RRF2M_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RRF2M_HUMAN
• UniProt AC: Q969S9
• Protein Name: Ribosome-releasing factor 2, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03059}
• Gene Name: GFM2 {ECO:0000255|HAMAP-Rule:MF_03059}
• Organism: Homo sapiens (Human).
• Sequence Length: 779
• Subcellular Localization: Mitochondrion .
• Protein Description: Mitochondrial GTPase that mediates the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis. Acts in collaboration with MRRF. GTP hydrolysis follows the ribosome disassembly and probably occurs on the ribosome large subunit. Not involved in the GTP-dependent ribosomal translocation step during translation elongation..
• Protein Sequence: MLTNLRIFAMSHQTIPSVYINNICCYKIRASLKRLKPHVPLGRNCSSLPGLIGNDIKSLHSIINPPIAKIRNIGIMAHIDAGKTTTTERILYYSGYTRSLGDVDDGDTVTDFMAQERERGITIQSAAVTFDWKGYRVNLIDTPGHVDFTLEVERCLRVLDGAVAVFDASAGVEAQTLTVWRQADKHNIPRICFLNKMDKTGASFKYAVESIREKLKAKPLLLQLPIGEAKTFKGVVDVVMKEKLLWNCNSNDGKDFERKPLLEMNDPELLKETTEARNALIEQVADLDDEFADLVLEEFSENFDLLPAEKLQTAIHRVTLAQTAVPVLCGSALKNKGIQPLLDAVTMYLPSPEERNYEFLQWYKDDLCALAFKVLHDKQRGPLVFMRIYSGTIKPQLAIHNINGNCTERISRLLLPFADQHVEIPSLTAGNIALTVGLKHTATGDTIVSSKSSALAAARRAEREGEKKHRQNNEAERLLLAGVEIPEPVFFCTIEPPSLSKQPDLEHALKCLQREDPSLKVRLDPDSGQTVLCGMGELHIEIIHDRIKREYGLETYLGPLQVAYRETILNSVRATDTLDRTLGDKRHLVTVEVEARPIETSSVMPVIEFEYAESINEGLLKVSQEAIENGIHSACLQGPLLGSPIQDVAITLHSLTIHPGTSTTMISACVSRCVQKALKKADKQVLEPLMNLEVTVARDYLSPVLADLAQRRGNIQEIQTRQDNKVVIGFVPLAEIMGYSTVLRTLTSGSATFALELSTYQAMNPQDQNTLLNRRSGLT

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
11	Phosphorylation	NLRIFAMSHQTIPSV CEEEEEECCCCCCEE	14.71	-
14	Phosphorylation	IFAMSHQTIPSVYIN EEEECCCCCCEEEEC	29.45	-
31	Phosphorylation	CCYKIRASLKRLKPH HHHHHHHHHHHHCCC	25.28	-
84	Phosphorylation	AHIDAGKTTTTERIL EEEECCCCCCCCEEE	28.58	25404012
85	Phosphorylation	HIDAGKTTTTERILY EEECCCCCCCCEEEE	34.90	25404012
86	Phosphorylation	IDAGKTTTTERILYY EECCCCCCCCEEEEE	31.71	25404012
87	Phosphorylation	DAGKTTTTERILYYS ECCCCCCCCEEEEEC	22.60	25404012
196	Ubiquitination	PRICFLNKMDKTGAS CEEEEEECCCCCCCC	51.10	-
199	Ubiquitination	CFLNKMDKTGASFKY EEEECCCCCCCCHHH	45.41	-
203	Phosphorylation	KMDKTGASFKYAVES CCCCCCCCHHHHHHH	24.50	24719451
205	Ubiquitination	DKTGASFKYAVESIR CCCCCCHHHHHHHHH	29.79	-
218	Ubiquitination	IREKLKAKPLLLQLP HHHHHHCCCEEEECC	34.31	-
218 (in isoform 2)	Ubiquitination	-	34.31	-
230	Ubiquitination	QLPIGEAKTFKGVVD ECCCCCCCCCCCHHH	50.63	-
231	Phosphorylation	LPIGEAKTFKGVVDV CCCCCCCCCCCHHHH	37.31	20068231
233	Acetylation	IGEAKTFKGVVDVVM CCCCCCCCCHHHHHH	56.90	23749302
233	Succinylation	IGEAKTFKGVVDVVM CCCCCCCCCHHHHHH	56.90	27452117
233	Malonylation	IGEAKTFKGVVDVVM CCCCCCCCCHHHHHH	56.90	26320211
241	Ubiquitination	GVVDVVMKEKLLWNC CHHHHHHHEECCCCC	39.84	-
241 (in isoform 2)	Ubiquitination	-	39.84	-
243	Ubiquitination	VDVVMKEKLLWNCNS HHHHHHEECCCCCCC	43.28	-
259	Ubiquitination	DGKDFERKPLLEMND CCCCCCCCCCCCCCC	32.59	-
271	Acetylation	MNDPELLKETTEARN CCCHHHHHHHHHHHH	66.69	30585809
334	Malonylation	VLCGSALKNKGIQPL HHCCHHHHCCCCHHH	57.22	26320211
334	Acetylation	VLCGSALKNKGIQPL HHCCHHHHCCCCHHH	57.22	25953088
336	Malonylation	CGSALKNKGIQPLLD CCHHHHCCCCHHHHH	56.66	26320211
336	Ubiquitination	CGSALKNKGIQPLLD CCHHHHCCCCHHHHH	56.66	-
348	Phosphorylation	LLDAVTMYLPSPEER HHHHHHHCCCCHHHH	13.19	-
373	Ubiquitination	DLCALAFKVLHDKQR HHHHHHHHHHHHCCC	37.98	-
378	2-Hydroxyisobutyrylation	AFKVLHDKQRGPLVF HHHHHHHCCCCCEEE	31.02	-
390	Phosphorylation	LVFMRIYSGTIKPQL EEEEEEECCCCCCEE	27.39	26503514
394	Malonylation	RIYSGTIKPQLAIHN EEECCCCCCEEEEEE	26.92	30639696
394	Ubiquitination	RIYSGTIKPQLAIHN EEECCCCCCEEEEEE	26.92	-
404 (in isoform 2)	Ubiquitination	-	27.13	21906983
426	Phosphorylation	DQHVEIPSLTAGNIA CCCCCCCCCCCCCEE	43.97	-
451	Ubiquitination	GDTIVSSKSSALAAA CCEEECCHHHHHHHH	40.71	2190698
451	Malonylation	GDTIVSSKSSALAAA CCEEECCHHHHHHHH	40.71	26320211
483 (in isoform 1)	Ubiquitination	-	5.12	21906983
510	Ubiquitination	PDLEHALKCLQREDP CCHHHHHHHHHCCCC	33.41	-
520	Ubiquitination	QREDPSLKVRLDPDS HCCCCCCEEEECCCC	29.64	-
551	Phosphorylation	HDRIKREYGLETYLG HHHHHHHHCCCCCCC	30.92	20068231
555	Phosphorylation	KREYGLETYLGPLQV HHHHCCCCCCCCHHH	29.14	22210691
556	Phosphorylation	REYGLETYLGPLQVA HHHCCCCCCCCHHHH	10.57	20068231
564	Phosphorylation	LGPLQVAYRETILNS CCCHHHHHHHHHHHH	15.32	-
577	Phosphorylation	NSVRATDTLDRTLGD HHHHCCCCCCCCCCC	26.63	22210691
611	Phosphorylation	MPVIEFEYAESINEG EEEEEEEEHHHHCCC	22.46	-
614	Phosphorylation	IEFEYAESINEGLLK EEEEEHHHHCCCCCH	23.65	-
700	Phosphorylation	EVTVARDYLSPVLAD EEEEEHHHHHHHHHH	11.97	21406692
702	Phosphorylation	TVARDYLSPVLADLA EEEHHHHHHHHHHHH	13.51	21406692
720	Phosphorylation	GNIQEIQTRQDNKVV CCCCEEEECCCCEEE	35.64	30377224
741	Phosphorylation	AEIMGYSTVLRTLTS HHHCCHHHHHHHHCC	18.31	24719451

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of RRF2M_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RRF2M_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of RRF2M_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TRIM9_HUMAN	TRIM9	physical	25416956

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.