dbPTM

COPT1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	COPT1_HUMAN
UniProt AC	O15431
Protein Name	High affinity copper uptake protein 1
Gene Name	SLC31A1
Organism	Homo sapiens (Human).
Sequence Length	190
Subcellular Localization	Cell membrane Multi-pass membrane protein. Localizes to the apical membrane in intestinal epithelial cells..
Protein Description	High-affinity, saturable copper transporter involved in dietary copper uptake..
Protein Sequence	MDHSHHMGMSYMDSNSTMQPSHHHPTTSASHSHGGGDSSMMMMPMTFYFGFKNVELLFSGLVINTAGEMAGAFVAVFLLAMFYEGLKIARESLLRKSQVSIRYNSMPVPGPNGTILMETHKTVGQQMLSFPHLLQTVLHIIQVVISYFLMLIFMTYNGYLCIAVAAGAGTGYFLFSWKKAVVVDITEHCH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MDHSHHMGMSY ----CCCCCCCCCCC	15.72	-
10	Phosphorylation	HSHHMGMSYMDSNST CCCCCCCCCCCCCCC	16.15	-
11	Phosphorylation	SHHMGMSYMDSNSTM CCCCCCCCCCCCCCC	8.96	-
15	N-linked_Glycosylation	GMSYMDSNSTMQPSH CCCCCCCCCCCCCCC	36.92	12466020
15	N-linked_Glycosylation	GMSYMDSNSTMQPSH CCCCCCCCCCCCCCC	36.92	12466020
27	O-linked_Glycosylation	PSHHHPTTSASHSHG CCCCCCCCCCCCCCC	27.09	17525160
92	Phosphorylation	GLKIARESLLRKSQV HHHHHHHHHHHHHCE	27.44	23532336
96	2-Hydroxyisobutyrylation	ARESLLRKSQVSIRY HHHHHHHHHCEEEEE	45.25	-
96	Ubiquitination	ARESLLRKSQVSIRY HHHHHHHHHCEEEEE	45.25	-
103	Phosphorylation	KSQVSIRYNSMPVPG HHCEEEEECCCCCCC	15.21	23186163
105	Phosphorylation	QVSIRYNSMPVPGPN CEEEEECCCCCCCCC	18.61	28857561
114	Phosphorylation	PVPGPNGTILMETHK CCCCCCCEEEEECCC	19.99	25159151
119	Phosphorylation	NGTILMETHKTVGQQ CCEEEEECCCCHHHH	18.08	23186163

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 COPT1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
27	T	Glycosylation		17525160
O-Glycosylation at Thr-27 protects from proteolytic cleavage in the N-terminal extracellular domain.

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 COPT1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
COPT1_HUMAN	SLC31A1	physical	12466020
CCS_HUMAN	CCS	physical	24297923

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
DB00188	Bortezomib
DB00958	Carboplatin
DB00515	Cisplatin
DB00526	Oxaliplatin

Regulatory Network of COPT1_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"O-linked glycosylation at threonine 27 protects the coppertransporter hCTR1 from proteolytic cleavage in mammalian cells."; Maryon E.B., Molloy S.A., Kaplan J.H.; J. Biol. Chem. 282:20376-20387(2007). Cited for: GLYCOSYLATION AT ASN-15 AND THR-27.	17525160 [Abstract]
O-linked Glycosylation
Reference	PubMed
"O-linked glycosylation at threonine 27 protects the coppertransporter hCTR1 from proteolytic cleavage in mammalian cells."; Maryon E.B., Molloy S.A., Kaplan J.H.; J. Biol. Chem. 282:20376-20387(2007). Cited for: GLYCOSYLATION AT ASN-15 AND THR-27.	17525160 [Abstract]