dbPTM

T4S20_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	T4S20_HUMAN
UniProt AC	Q53R12
Protein Name	Transmembrane 4 L6 family member 20
Gene Name	TM4SF20
Organism	Homo sapiens (Human).
Sequence Length	229
Subcellular Localization	Membrane Multi-pass membrane protein . Endoplasmic reticulum membrane Multi-pass membrane protein . Ceramide alters the direction through which transmembrane helices are translocated into the endoplasmic reticulum membrane during translation of T
Protein Description	Polytopic transmembrane protein that inhibits regulated intramembrane proteolysis (RIP) of CREB3L1, inhibiting its activation and the induction of collagen synthesis. [PubMed: 25310401]
Protein Sequence	MTCCEGWTSCNGFSLLVLLLLGVVLNAIPLIVSLVEEDQFSQNPISCFEWWFPGIIGAGLMAIPATTMSLTARKRACCNNRTGMFLSSLFSVITVIGALYCMLISIQALLKGPLMCNSPSNSNANCEFSLKNISDIHPESFNLQWFFNDSCAPPTGFNKPTSNDTMASGWRASSFHFDSEENKHRLIHFSVFLGLLLVGILEVLFGLSQIVIGFLGCLCGVSKRRSQIV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference	Orthologous Protein Cluster
129	Phosphorylation	SNANCEFSLKNISDI CCCCCEEEECCHHHC	19.01	24719451

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 T4S20_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
132	N	Glycosylation	27499293
Glycosylated at Asn-132, Asn-148 and Asn-163 in presence of ceramide which inverts the orientation of TM4SF20 in membranes exposing these residues to the endoplasmic reticulum lumen.
148	N	Glycosylation	27499293
Glycosylated at Asn-132, Asn-148 and Asn-163 in presence of ceramide which inverts the orientation of TM4SF20 in membranes exposing these residues to the endoplasmic reticulum lumen.
163	N	Glycosylation	27499293
Glycosylated at Asn-132, Asn-148 and Asn-163 in presence of ceramide which inverts the orientation of TM4SF20 in membranes exposing these residues to the endoplasmic reticulum lumen.

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 T4S20_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
VKORL_HUMAN	VKORC1L1	physical	26186194
MBOA7_HUMAN	MBOAT7	physical	26186194
HSDL1_HUMAN	HSDL1	physical	26186194
TM186_HUMAN	TMEM186	physical	26186194
CAB39_HUMAN	CAB39	physical	26186194
TMM43_HUMAN	TMEM43	physical	26186194
HG2A_HUMAN	CD74	physical	26186194
RHOA_HUMAN	RHOA	physical	26186194
F210B_HUMAN	FAM210B	physical	26186194
HG2A_HUMAN	CD74	physical	28514442
F210B_HUMAN	FAM210B	physical	28514442
HSDL1_HUMAN	HSDL1	physical	28514442
TM186_HUMAN	TMEM186	physical	28514442
MBOA7_HUMAN	MBOAT7	physical	28514442
CJ035_HUMAN	C10orf35	physical	28514442
EBP_HUMAN	EBP	physical	28514442

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of T4S20_HUMAN

Related Literatures of Post-Translational Modification