TMUB1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TMUB1_HUMAN
• UniProt AC: Q9BVT8
• Protein Name: Transmembrane and ubiquitin-like domain-containing protein 1
• Gene Name: TMUB1
• Organism: Homo sapiens (Human).
• Sequence Length: 246
• Subcellular Localization: Membrane ; Multi-pass membrane protein . Cell junction, synapse, postsynaptic cell membrane . Recycling endosome . Cytoplasm . Nucleus . Nucleus, nucleolus .; iHOPS: Cytoplasm . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Nucleus,
• Protein Description: Involved in sterol-regulated ubiquitination and degradation of HMG-CoA reductase HMGCR. [PubMed: 21343306 Involved in positive regulation of AMPA-selective glutamate receptor GRIA2 recycling to the cell surface (By similarity Acts as negative regulator of hepatocyte growth during regeneration (By similarity; iHOPS: May contribute to the regulation of translation during cell-cycle progression. May contribute to the regulation of cell proliferation (By similarity May be involved in centrosome assembly. Modulates stabilization and nucleolar localization of tumor suppressor CDKN2A and enhances association between CDKN2A and NPM1 (By similarity]
• Protein Sequence: MTLIEGVGDEVTVLFSVLACLLVLALAWVSTHTAEGGDPLPQPSGTPTPSQPSAAMAATDSMRGEAPGAETPSLRHRGQAAQPEPSTGFTATPPAPDSPQEPLVLRLKFLNDSEQVARAWPHDTIGSLKRTQFPGREQQVRLIYQGQLLGDDTQTLGSLHLPPNCVLHCHVSTRVGPPNPPCPPGSEPGPSGLEIGSLLLPLLLLLLLLLWYCQIQYRPFFPLTATLGLAGFTLLLSLLAFAMYRP

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
71	Phosphorylation	GEAPGAETPSLRHRG CCCCCCCCCCCCCCC	20.04	29255136
73	Phosphorylation	APGAETPSLRHRGQA CCCCCCCCCCCCCCC	45.51	29255136
77	Methylation	ETPSLRHRGQAAQPE CCCCCCCCCCCCCCC	32.27	115918669
86	Phosphorylation	QAAQPEPSTGFTATP CCCCCCCCCCCCCCC	39.23	27174698
87	Phosphorylation	AAQPEPSTGFTATPP CCCCCCCCCCCCCCC	47.21	27174698
90	O-linked_Glycosylation	PEPSTGFTATPPAPD CCCCCCCCCCCCCCC	30.85	OGP
90	Phosphorylation	PEPSTGFTATPPAPD CCCCCCCCCCCCCCC	30.85	25850435
92	Phosphorylation	PSTGFTATPPAPDSP CCCCCCCCCCCCCCC	27.09	25159151
92	O-linked_Glycosylation	PSTGFTATPPAPDSP CCCCCCCCCCCCCCC	27.09	OGP
98	Phosphorylation	ATPPAPDSPQEPLVL CCCCCCCCCCCCEEE	27.68	25159151
98	O-linked_Glycosylation	ATPPAPDSPQEPLVL CCCCCCCCCCCCEEE	27.68	OGP
108	Acetylation	EPLVLRLKFLNDSEQ CCEEEEEEECCCHHH	41.18	25953088
108	Ubiquitination	EPLVLRLKFLNDSEQ CCEEEEEEECCCHHH	41.18	21906983
113	Phosphorylation	RLKFLNDSEQVARAW EEEECCCHHHHHHHC	28.93	21815630
124	Phosphorylation	ARAWPHDTIGSLKRT HHHCCCCHHHCCCCC	24.97	23403867
127	Phosphorylation	WPHDTIGSLKRTQFP CCCCHHHCCCCCCCC	27.20	25159151
129	Ubiquitination	HDTIGSLKRTQFPGR CCHHHCCCCCCCCCC	55.91	21906983
155	O-linked_Glycosylation	LLGDDTQTLGSLHLP ECCCCCCCCCCCCCC	34.87	OGP
186	Phosphorylation	NPPCPPGSEPGPSGL CCCCCCCCCCCCCCH	46.52	25332170
197	Phosphorylation	PSGLEIGSLLLPLLL CCCHHHHHHHHHHHH	22.85	25332170

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

Oops, there are no upstream regulatory protein records of TMUB1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TMUB1_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 TMUB1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
AMFR_HUMAN	AMFR	physical	21343306
ERLN2_HUMAN	ERLIN2	physical	21343306
SYVN1_HUMAN	SYVN1	physical	21343306
RN139_HUMAN	RNF139	physical	21343306
A4_HUMAN	APP	physical	21832049
NPM_HUMAN	NPM1	physical	24240191
RAGP1_HUMAN	RANGAP1	physical	24240191
TBG1_HUMAN	TUBG1	physical	24240191

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

Phosphorylation

"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-71; THR-92 AND SER-98,AND MASS SPECTROMETRY.
PubMed: 18669648

"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-92 AND SER-98, AND MASSSPECTROMETRY.
PubMed: 18691976