dbPTM

THY1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	THY1_HUMAN
UniProt AC	P04216
Protein Name	Thy-1 membrane glycoprotein
Gene Name	THY1
Organism	Homo sapiens (Human).
Sequence Length	161
Subcellular Localization	Cell membrane Lipid-anchor, GPI-anchor.
Protein Description	May play a role in cell-cell or cell-ligand interactions during synaptogenesis and other events in the brain..
Protein Sequence	MNLAISIALLLTVLQVSRGQKVTSLTACLVDQSLRLDCRHENTSSSPIQYEFSLTRETKKHVLFGTVGVPEHTYRSRTNFTSKYNMKVLYLSAFTSKDEGTYTCALHHSGHSPPISSQNVTVLRDKLVKCEGISLLAQNTSWLLLLLLSLSLLQATDFMSL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MNLAISIALLLTV --CCHHHHHHHHHHH	9.01	24043423
12	Phosphorylation	ISIALLLTVLQVSRG HHHHHHHHHHHHCCC	21.09	24043423
17	Phosphorylation	LLTVLQVSRGQKVTS HHHHHHHCCCCCEEE	20.10	24043423
20	Pyrrolidone_carboxylic_acid	VLQVSRGQKVTSLTA HHHHCCCCCEEEHHE	35.62	-
20	Pyrrolidone_carboxylic_acid	VLQVSRGQKVTSLTA HHHHCCCCCEEEHHE	35.62	-
23	Phosphorylation	VSRGQKVTSLTACLV HCCCCCEEEHHEEEC	25.67	21406692
24	Phosphorylation	SRGQKVTSLTACLVD CCCCCEEEHHEEECC	27.06	21406692
26	Phosphorylation	GQKVTSLTACLVDQS CCCEEEHHEEECCCH	18.32	21406692
28	S-palmitoylation	KVTSLTACLVDQSLR CEEEHHEEECCCHHC	2.99	29575903
33	Phosphorylation	TACLVDQSLRLDCRH HEEECCCHHCCEECC	15.82	21406692
42	N-linked_Glycosylation	RLDCRHENTSSSPIQ CCEECCCCCCCCCCE	38.85	19349973
42	N-linked_Glycosylation	RLDCRHENTSSSPIQ CCEECCCCCCCCCCE	38.85	19349973
74	Phosphorylation	VGVPEHTYRSRTNFT CCCCCCCCCCCCCCC	14.43	25307156
76	Phosphorylation	VPEHTYRSRTNFTSK CCCCCCCCCCCCCCC	32.80	30243723
78	Phosphorylation	EHTYRSRTNFTSKYN CCCCCCCCCCCCCCC	35.61	28348404
79	N-linked_Glycosylation	HTYRSRTNFTSKYNM CCCCCCCCCCCCCCE	36.77	UniProtKB CARBOHYD
81	Phosphorylation	YRSRTNFTSKYNMKV CCCCCCCCCCCCEEE	26.78	28348404
82	Phosphorylation	RSRTNFTSKYNMKVL CCCCCCCCCCCEEEE	29.07	28348404
84	Phosphorylation	RTNFTSKYNMKVLYL CCCCCCCCCEEEEEE	21.91	30243723
90	Phosphorylation	KYNMKVLYLSAFTSK CCCEEEEEEEEEECC	11.12	24927040
92	Phosphorylation	NMKVLYLSAFTSKDE CEEEEEEEEEECCCC	14.05	24076635
95	Phosphorylation	VLYLSAFTSKDEGTY EEEEEEEECCCCCEE	34.29	29083192
96	Phosphorylation	LYLSAFTSKDEGTYT EEEEEEECCCCCEEE	31.49	20886841
119	N-linked_Glycosylation	SPPISSQNVTVLRDK CCCCCCCCEEEEEHH	33.12	19349973
119	N-linked_Glycosylation	SPPISSQNVTVLRDK CCCCCCCCEEEEEHH	33.12	19159218
130	GPI-anchor	LRDKLVKCEGISLLA EEHHEEECCHHHHHH	4.52	-
134	Phosphorylation	LVKCEGISLLAQNTS EEECCHHHHHHHCHH	28.34	24043423
139	N-linked_Glycosylation	GISLLAQNTSWLLLL HHHHHHHCHHHHHHH	30.39	UniProtKB CARBOHYD
140	Phosphorylation	ISLLAQNTSWLLLLL HHHHHHCHHHHHHHH	14.81	24043423
141	Phosphorylation	SLLAQNTSWLLLLLL HHHHHCHHHHHHHHH	24.23	24043423
149	Phosphorylation	WLLLLLLSLSLLQAT HHHHHHHHHHHHHHH	18.84	24043423
151	Phosphorylation	LLLLLSLSLLQATDF HHHHHHHHHHHHHHH	24.53	24043423
156	Phosphorylation	SLSLLQATDFMSL-- HHHHHHHHHHHCC--	19.46	24043423
160	Phosphorylation	LQATDFMSL------ HHHHHHHCC------	30.81	24043423

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 THY1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of THY1_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 THY1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
THY1_HUMAN	THY1	physical	1347022
LCK_HUMAN	LCK	physical	1351058
FYN_HUMAN	FYN	physical	1351058
GAG_HV1H2	gag	physical	10708443
ENV_HV1H2	env	physical	10708443
UBC9_HUMAN	UBE2I	physical	22939629
TIM44_HUMAN	TIMM44	physical	22939629
VDAC3_HUMAN	VDAC3	physical	22939629
TIAR_HUMAN	TIAL1	physical	22939629
UBL4A_HUMAN	UBL4A	physical	22939629
ZFR_HUMAN	ZFR	physical	22939629
UBE4B_HUMAN	UBE4B	physical	22939629
VATE1_HUMAN	ATP6V1E1	physical	22939629
MPLKI_HUMAN	MPLKIP	physical	22939629
UBAP2_HUMAN	UBAP2	physical	22939629

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 THY1_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."; Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.; Nat. Biotechnol. 27:378-386(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-42 AND ASN-119, AND MASSSPECTROMETRY.	19349973 [Abstract]
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-119, AND MASSSPECTROMETRY.	19159218 [Abstract]