GUF1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: GUF1_HUMAN
• UniProt AC: Q8N442
• Protein Name: Translation factor GUF1, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03137}
• Gene Name: GUF1 {ECO:0000255|HAMAP-Rule:MF_03137}
• Organism: Homo sapiens (Human).
• Sequence Length: 669
• Subcellular Localization: Mitochondrion inner membrane ; Peripheral membrane protein ; Matrix side .
• Protein Description: Promotes mitochondrial protein synthesis. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Binds to mitochondrial ribosomes in a GTP-dependent manner..
• Protein Sequence: MWTLVGRGWGCARALAPRATGAALLVAPGPRSAPTLGAAPESWATDRLYSSAEFKEKLDMSRFPVENIRNFSIVAHVDHGKSTLADRLLELTGTIDKTKNNKQVLDKLQVERERGITVKAQTASLFYNCEGKQYLLNLIDTPGHVDFSYEVSRSLSACQGVLLVVDANEGIQAQTVANFFLAFEAQLSVIPVINKIDLKNADPERVENQIEKVFDIPSDECIKISAKLGTNVESVLQAIIERIPPPKVHRKNPLRALVFDSTFDQYRGVIANVALFDGVVSKGDKIVSAHTQKTYEVNEVGVLNPNEQPTHKLYAGQVGYLIAGMKDVTEAQIGDTLCLHKQPVEPLPGFKSAKPMVFAGMYPLDQSEYNNLKSAIEKLTLNDSSVTVHRDSSLALGAGWRLGFLGLLHMEVFNQRLEQEYNASVILTTPTVPYKAVLSSSKLIKEHREKEITIINPAQFPDKSKVTEYLEPVVLGTIITPDEYTGKIMMLCEARRAVQKNMIFIDQNRVMLKYLFPLNEIVVDFYDSLKSLSSGYASFDYEDAGYQTAELVKMDILLNGNTVEELVTVVHKDKAHSIGKAICERLKDSLPRQLFEIAIQAAIGSKIIARETVKAYRKNVLAKCYGGDITRKMKLLKRQAEGKKKLRKIGNVEVPKDAFIKVLKTQSSK

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
20	Phosphorylation	RALAPRATGAALLVA HHHCCCCCCCEEEEE	28.74	22210691
42	Phosphorylation	TLGAAPESWATDRLY CCCCCCCHHHHHHCC	22.43	-
87	Methylation	GKSTLADRLLELTGT CCCHHHHHHHHHHCC	35.25	-
98	Phosphorylation	LTGTIDKTKNNKQVL HHCCCCCCCCCHHHH	34.94	30622161
99	Ubiquitination	TGTIDKTKNNKQVLD HCCCCCCCCCHHHHH	65.35	-
102	Ubiquitination	IDKTKNNKQVLDKLQ CCCCCCCHHHHHHHH	51.70	17203973
351	Acetylation	VEPLPGFKSAKPMVF CCCCCCCCCCCCEEE	56.25	19413330
453	Phosphorylation	EHREKEITIINPAQF HHHCCCCEEECHHHC	19.52	-
464	Phosphorylation	PAQFPDKSKVTEYLE HHHCCCHHHCCCCCC	39.47	-
477	Phosphorylation	LEPVVLGTIITPDEY CCEEEEEEEECCCCC	12.68	22817900
484	Phosphorylation	TIITPDEYTGKIMML EEECCCCCCCHHHHH	28.33	19690332

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

Oops, there are no upstream regulatory protein records of GUF1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of GUF1_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 GUF1_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of GUF1_HUMAN !!

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.

Related Literatures of Post-Translational Modification

Ubiquitylation

"The proteomic reactor facilitates the analysis of affinity-purifiedproteins by mass spectrometry: application for identifyingubiquitinated proteins in human cells.";
Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M.,Haines D.S., Figeys D.;
J. Proteome Res. 6:298-305(2007).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-102, AND MASSSPECTROMETRY.
PubMed: 17203973