REEP4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: REEP4_HUMAN
• UniProt AC: Q9H6H4
• Protein Name: Receptor expression-enhancing protein 4
• Gene Name: REEP4
• Organism: Homo sapiens (Human).
• Sequence Length: 257
• Subcellular Localization: Endoplasmic reticulum membrane ; Multi-pass membrane protein .
• Protein Description: Microtubule-binding protein required to ensure proper cell division and nuclear envelope reassembly by sequestering the endoplasmic reticulum away from chromosomes during mitosis. Probably acts by clearing the endoplasmic reticulum membrane from metaphase chromosomes..
• Protein Sequence: MVSWMICRLVVLVFGMLCPAYASYKAVKTKNIREYVRWMMYWIVFALFMAAEIVTDIFISWFPFYYEIKMAFVLWLLSPYTKGASLLYRKFVHPSLSRHEKEIDAYIVQAKERSYETVLSFGKRGLNIAASAAVQAATKSQGALAGRLRSFSMQDLRSISDAPAPAYHDPLYLEDQVSHRRPPIGYRAGGLQDSDTEDECWSDTEAVPRAPARPREKPLIRSQSLRVVKRKPPVREGTSRSLKVRTRKKTVPSDVDS

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
29	Phosphorylation	ASYKAVKTKNIREYV HHHHHHHCCCHHHHH	23.79	-
90	Ubiquitination	GASLLYRKFVHPSLS HHHHHHHHHHCHHHH	37.88	21890473
90 (in isoform 2)	Ubiquitination	-	37.88	21890473
90 (in isoform 1)	Ubiquitination	-	37.88	21890473
101 (in isoform 2)	Ubiquitination	-	54.57	21890473
101 (in isoform 1)	Ubiquitination	-	54.57	21890473
101	Ubiquitination	PSLSRHEKEIDAYIV HHHHHCHHHHCEEEE	54.57	21906983
106	Phosphorylation	HEKEIDAYIVQAKER CHHHHCEEEEECCCC	9.62	-
111 (in isoform 1)	Ubiquitination	-	36.25	21890473
111	Ubiquitination	DAYIVQAKERSYETV CEEEEECCCCCHHHH	36.25	21890473
111 (in isoform 2)	Ubiquitination	-	36.25	21890473
114	Phosphorylation	IVQAKERSYETVLSF EEECCCCCHHHHHHH	28.54	25627689
115	Phosphorylation	VQAKERSYETVLSFG EECCCCCHHHHHHHH	23.11	25627689
117	Phosphorylation	AKERSYETVLSFGKR CCCCCHHHHHHHHHH	20.65	25627689
120	Phosphorylation	RSYETVLSFGKRGLN CCHHHHHHHHHHHHH	27.84	28555341
123	2-Hydroxyisobutyrylation	ETVLSFGKRGLNIAA HHHHHHHHHHHHHHH	41.08	-
123 (in isoform 2)	Ubiquitination	-	41.08	21890473
123	Ubiquitination	ETVLSFGKRGLNIAA HHHHHHHHHHHHHHH	41.08	21890473
123 (in isoform 1)	Ubiquitination	-	41.08	21890473
131	Phosphorylation	RGLNIAASAAVQAAT HHHHHHHHHHHHHHH	14.03	29083192
139	Ubiquitination	AAVQAATKSQGALAG HHHHHHHHCCCHHHH	35.73	-
140	Phosphorylation	AVQAATKSQGALAGR HHHHHHHCCCHHHHH	29.50	-
140	O-linked_Glycosylation	AVQAATKSQGALAGR HHHHHHHCCCHHHHH	29.50	30620550
147	Methylation	SQGALAGRLRSFSMQ CCCHHHHHHHCCCHH	22.71	115491015
149	Methylation	GALAGRLRSFSMQDL CHHHHHHHCCCHHHH	34.00	115491007
150	Phosphorylation	ALAGRLRSFSMQDLR HHHHHHHCCCHHHHH	26.68	30266825
152	Phosphorylation	AGRLRSFSMQDLRSI HHHHHCCCHHHHHHC	19.44	29255136
158	Phosphorylation	FSMQDLRSISDAPAP CCHHHHHHCCCCCCC	33.47	28796482
160	Phosphorylation	MQDLRSISDAPAPAY HHHHHHCCCCCCCCC	29.03	28796482
167	Phosphorylation	SDAPAPAYHDPLYLE CCCCCCCCCCCCCCC	13.00	28796482
172	Phosphorylation	PAYHDPLYLEDQVSH CCCCCCCCCCCCCCC	17.27	28796482
178	Phosphorylation	LYLEDQVSHRRPPIG CCCCCCCCCCCCCCC	12.97	28796482
186	Phosphorylation	HRRPPIGYRAGGLQD CCCCCCCCCCCCCCC	9.67	-
194	Phosphorylation	RAGGLQDSDTEDECW CCCCCCCCCCCCCCC	33.21	22167270
196	Phosphorylation	GGLQDSDTEDECWSD CCCCCCCCCCCCCCC	49.65	22167270
202	Phosphorylation	DTEDECWSDTEAVPR CCCCCCCCCCCCCCC	46.44	22167270
204	Phosphorylation	EDECWSDTEAVPRAP CCCCCCCCCCCCCCC	21.96	23927012
222	Phosphorylation	REKPLIRSQSLRVVK CCCCCCCCCCEEEEE	19.68	25056879
224	Phosphorylation	KPLIRSQSLRVVKRK CCCCCCCCEEEEECC	21.27	28355574
238	Phosphorylation	KPPVREGTSRSLKVR CCCCCCCCCCCEEEE	19.06	28102081
239	Phosphorylation	PPVREGTSRSLKVRT CCCCCCCCCCEEEEC	30.63	26074081
241	Phosphorylation	VREGTSRSLKVRTRK CCCCCCCCEEEECCC	32.10	26074081
246	Phosphorylation	SRSLKVRTRKKTVPS CCCEEEECCCCCCCC	50.24	-
250	Phosphorylation	KVRTRKKTVPSDVDS EEECCCCCCCCCCCC	40.46	28176443
253	Phosphorylation	TRKKTVPSDVDS--- CCCCCCCCCCCC---	46.02	28176443
257	Phosphorylation	TVPSDVDS------- CCCCCCCC-------	41.80	28176443

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

Oops, there are no upstream regulatory protein records of REEP4_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of REEP4_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 REEP4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TAXB1_HUMAN	TAX1BP1	physical	26186194
TAXB1_HUMAN	TAX1BP1	physical	28514442

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

"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-152, AND MASSSPECTROMETRY.
PubMed: 19413330

"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 SER-152; SER-194; THR-196;SER-202; THR-250 AND SER-253, AND MASS SPECTROMETRY.
PubMed: 18669648

"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-152; SER-194; THR-196AND SER-202, AND MASS SPECTROMETRY.
PubMed: 17081983