dbPTM

T184B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	T184B_HUMAN
UniProt AC	Q9Y519
Protein Name	Transmembrane protein 184B
Gene Name	TMEM184B
Organism	Homo sapiens (Human).
Sequence Length	407
Subcellular Localization	Membrane Multi-pass membrane protein .
Protein Description	May activate the MAP kinase signaling pathway..
Protein Sequence	MTVRGDVLAPDPASPTTAAASPSVSVIPEGSPTAMEQPVFLMTTAAQAISGFFVWTALLITCHQIYMHLRCYSCPNEQRYIVRILFIVPIYAFDSWLSLLFFTNDQYYVYFGTVRDCYEALVIYNFLSLCYEYLGGESSIMSEIRGKPIESSCMYGTCCLWGKTYSIGFLRFCKQATLQFCVVKPLMAVSTVVLQAFGKYRDGDFDVTSGYLYVTIIYNISVSLALYALFLFYFATRELLSPYSPVLKFFMVKSVIFLSFWQGMLLAILEKCGAIPKIHSARVSVGEGTVAAGYQDFIICVEMFFAALALRHAFTYKVYADKRLDAQGRCAPMKSISSSLKETMNPHDIVQDAIHNFSPAYQQYTQQSTLEPGPTWRGGAHGLSRSHSLSGARDNEKTLLLSSDDEF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
23	Phosphorylation	TTAAASPSVSVIPEG CCCCCCCCEEECCCC	25.24	-
241	Phosphorylation	FATRELLSPYSPVLK HHHHHHHCCCCHHHH	34.12	-
244	Phosphorylation	RELLSPYSPVLKFFM HHHHCCCCHHHHHHH	16.36	-
334	Ubiquitination	QGRCAPMKSISSSLK CCCCCCHHHHHHHHH	43.51	-
335	Phosphorylation	GRCAPMKSISSSLKE CCCCCHHHHHHHHHH	22.81	28060719
337	Phosphorylation	CAPMKSISSSLKETM CCCHHHHHHHHHHHC	22.44	30242111
338	Phosphorylation	APMKSISSSLKETMN CCHHHHHHHHHHHCC	37.71	30242111
339	Phosphorylation	PMKSISSSLKETMNP CHHHHHHHHHHHCCH	36.35	30576142
341	Ubiquitination	KSISSSLKETMNPHD HHHHHHHHHHCCHHH	53.76	-
358	Phosphorylation	QDAIHNFSPAYQQYT HHHHHHCCHHHHHHH	17.59	26356563
361	Phosphorylation	IHNFSPAYQQYTQQS HHHCCHHHHHHHHCC	10.26	27642862
364	Phosphorylation	FSPAYQQYTQQSTLE CCHHHHHHHHCCCCC	7.32	26356563
365	Phosphorylation	SPAYQQYTQQSTLEP CHHHHHHHHCCCCCC	18.78	26356563
377	Methylation	LEPGPTWRGGAHGLS CCCCCCCCCCCCCCC	35.82	115918621
384	Phosphorylation	RGGAHGLSRSHSLSG CCCCCCCCCCCCCCC	36.01	26699800
386	Phosphorylation	GAHGLSRSHSLSGAR CCCCCCCCCCCCCCC	17.66	27461979
388	Phosphorylation	HGLSRSHSLSGARDN CCCCCCCCCCCCCCC	26.02	28355574
390	Phosphorylation	LSRSHSLSGARDNEK CCCCCCCCCCCCCCC	33.16	30108239
397	Ubiquitination	SGARDNEKTLLLSSD CCCCCCCCEEEECCC	51.21	-
398	Phosphorylation	GARDNEKTLLLSSDD CCCCCCCEEEECCCC	19.23	26055452
402	Phosphorylation	NEKTLLLSSDDEF-- CCCEEEECCCCCC--	31.52	30266825
403	Phosphorylation	EKTLLLSSDDEF--- CCEEEECCCCCC---	49.39	25159151

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 T184B_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of T184B_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 T184B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SNIP1_HUMAN	SNIP1	physical	28514442
RENI_HUMAN	REN	physical	28514442
CLASR_HUMAN	CLASRP	physical	28514442
CCDC9_HUMAN	CCDC9	physical	28514442
ACINU_HUMAN	ACIN1	physical	28514442
SHIP2_HUMAN	INPPL1	physical	28514442
NCBP3_HUMAN	C17orf85	physical	28514442
YTHD1_HUMAN	YTHDF1	physical	28514442
BBS4_HUMAN	BBS4	physical	27173435

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 T184B_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-403, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403, AND MASSSPECTROMETRY.	19413330 [Abstract]
"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-398; SER-402 ANDSER-403, AND MASS SPECTROMETRY.	18669648 [Abstract]
"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 SER-402 AND SER-403, ANDMASS SPECTROMETRY.	18691976 [Abstract]
"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-402 AND SER-403, ANDMASS SPECTROMETRY.	17081983 [Abstract]