dbPTM

ENR1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ENR1_HUMAN
UniProt AC	Q14264
Protein Name	Endogenous retrovirus group 3 member 1 Env polyprotein
Gene Name	ERV3-1
Organism	Homo sapiens (Human).
Sequence Length	604
Subcellular Localization	Virion.
Protein Description	Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. Endogenous envelope proteins may have kept, lost or modified their original function during evolution. This endogenous envelope protein has lost its fusogenic properties. It can inhibit cell growth through decrease expression of cyclin B1 and increased expression of p21 in vitro.; SU mediates receptor recognition.; TM anchors the envelope heterodimer to the viral membrane through one transmembrane domain. The other hydrophobic domain, called fusion peptide, mediates fusion of the viral membrane with the target cell membrane (By similarity)..
Protein Sequence	MLGMNMLLITLFLLLPLSMLKGEPWEGCLHCTHTTWSGNIMTKTLLYHTYYECAGTCLGTCTHNQTTYSVCDPGRGQPYVCYDPKSSPGTWFEIHVGSKEGDLLNQTKVFPSGKDVVSLYFDVCQIVSMGSLFPVIFSSMEYYSSCHKNRYAHPACSTDSPVTTCWDCTTWSTNQQSLGPIMLTKIPLEPDCKTSTCNSVNLTILEPDQPIWTTGLKAPLGARVSGEEIGPGAYVYLYIIKKTRTRSTQQFRVFESFYEHVNQKLPEPPPLASNLFAQLAENIASSLHVASCYVCGGMNMGDQWPWEARELMPQDNFTLTASSLEPAPSSQSIWFLKTSIIGKFCIARWGKAFTDPVGELTCLGQQYYNETLGKTLWRGKSNNSESPHPSPFSRFPSLNHSWYQLEAPNTWQAPSGLYWICGPQAYRQLPAKWSGACVLGTIRPSFFLMPLKQGEALGYPIYDETKRKSKRGITIGDWKDNEWPPERIIQYYGPATWAEDGMWGYRTPVYMLNRIIRLQAVLEIITNETAGALNLLAQQATKMRNVIYQNRLALDYLLAQEEGVCGKFNLTNCCLELDDEGKVIKEITAKIQKLAHIPVQTWKG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Phosphorylation	GMNMLLITLFLLLPL CHHHHHHHHHHHHHH	16.07	24043423
18	Phosphorylation	LFLLLPLSMLKGEPW HHHHHHHHHHCCCCC	21.82	24043423
64	N-linked_Glycosylation	CLGTCTHNQTTYSVC EEEECCCCCEEEEEE	23.81	UniProtKB CARBOHYD
105	N-linked_Glycosylation	SKEGDLLNQTKVFPS CCCCCCCCEEEEECC	55.56	UniProtKB CARBOHYD
201	N-linked_Glycosylation	TSTCNSVNLTILEPD CCCCCCEEEEEECCC	31.15	UniProtKB CARBOHYD
316	N-linked_Glycosylation	RELMPQDNFTLTASS HHHCCCCCEEEEECC	26.93	UniProtKB CARBOHYD
338	Phosphorylation	QSIWFLKTSIIGKFC CCEEEEEHHHHHHHH	27.57	26270265
339	Phosphorylation	SIWFLKTSIIGKFCI CEEEEEHHHHHHHHH	15.60	26270265
369	N-linked_Glycosylation	CLGQQYYNETLGKTL ECCHHHHHCCCCCCC	30.73	UniProtKB CARBOHYD
382	N-linked_Glycosylation	TLWRGKSNNSESPHP CCCCCCCCCCCCCCC	60.58	UniProtKB CARBOHYD
399	N-linked_Glycosylation	FSRFPSLNHSWYQLE CCCCCCCCCEEEECC	31.33	UniProtKB CARBOHYD
441	Phosphorylation	SGACVLGTIRPSFFL CCCEEECCCCCCEEE	15.06	17287340
527	N-linked_Glycosylation	AVLEIITNETAGALN HHHHHHHCCCHHHHH	33.92	UniProtKB CARBOHYD
569	N-linked_Glycosylation	EGVCGKFNLTNCCLE CCCCCCCCCCCCEEE	49.82	UniProtKB CARBOHYD

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 ENR1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ENR1_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 ENR1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of ENR1_HUMAN !!

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 ENR1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-441, AND MASSSPECTROMETRY.	17287340 [Abstract]