dbPTM

VISTA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	VISTA_HUMAN
UniProt AC	Q9H7M9
Protein Name	V-type immunoglobulin domain-containing suppressor of T-cell activation {ECO:0000303\|PubMed:24691993}
Gene Name	VSIR {ECO:0000312\|HGNC:HGNC:30085}
Organism	Homo sapiens (Human).
Sequence Length	311
Subcellular Localization	Cell membrane Single-pass type I membrane protein .
Protein Description	Immunoregulatory receptor which inhibits the T-cell response. [PubMed: 24691993 May promote differentiation of embryonic stem cells, by inhibiting BMP4 signaling (By similarity May stimulate MMP14-mediated MMP2 activation]
Protein Sequence	MGVPTALEAGSWRWGSLLFALFLAASLGPVAAFKVATPYSLYVCPEGQNVTLTCRLLGPVDKGHDVTFYKTWYRSSRGEVQTCSERRPIRNLTFQDLHLHHGGHQAANTSHDLAQRHGLESASDHHGNFSITMRNLTLLDSGLYCCLVVEIRHHHSEHRVHGAMELQVQTGKDAPSNCVVYPSSSQDSENITAAALATGACIVGILCLPLILLLVYKQRQAASNRRAQELVRMDSNIQGIENPGFEASPPAQGIPEAKVRHPLSYVAQRQPSESGRHLLSEPSTPLSPPGPGDVFFPSLDPVPDSPNFEVI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	Reference
5	Phosphorylation	---MGVPTALEAGSW ---CCCCCHHHCCCC	20068231
11	Phosphorylation	PTALEAGSWRWGSLL CCHHHCCCCHHHHHH	20068231
37	O-linked_Glycosylation	VAAFKVATPYSLYVC HHHHEECCCCEEEEC	29351928
49	N-linked_Glycosylation	YVCPEGQNVTLTCRL EECCCCCEEEEEEEE	UniProtKB CARBOHYD
62	2-Hydroxyisobutyrylation	RLLGPVDKGHDVTFY EEECCCCCCCCCEEE	-
62	Ubiquitination	RLLGPVDKGHDVTFY EEECCCCCCCCCEEE	29967540
67	Phosphorylation	VDKGHDVTFYKTWYR CCCCCCCEEEEEEEE	22210691
71	Phosphorylation	HDVTFYKTWYRSSRG CCCEEEEEEEECCCC	22210691
75	Phosphorylation	FYKTWYRSSRGEVQT EEEEEEECCCCCCEE	22210691
76	Phosphorylation	YKTWYRSSRGEVQTC EEEEEECCCCCCEEC	22210691
91	N-linked_Glycosylation	SERRPIRNLTFQDLH CCCCCCCCCCHHEEE	UniProtKB CARBOHYD
128	N-linked_Glycosylation	SASDHHGNFSITMRN CCCCCCCCEEEEECC	UniProtKB CARBOHYD
235	Phosphorylation	QELVRMDSNIQGIEN HHHHHCCCCCCCCCC	28355574
248	Phosphorylation	ENPGFEASPPAQGIP CCCCCCCCCCCCCCC	25159151
258	Ubiquitination	AQGIPEAKVRHPLSY CCCCCHHHCCCCCHH	21906983
264	Phosphorylation	AKVRHPLSYVAQRQP HHCCCCCHHHHCCCC	21945579
265	Phosphorylation	KVRHPLSYVAQRQPS HCCCCCHHHHCCCCC	21945579
272	Phosphorylation	YVAQRQPSESGRHLL HHHCCCCCCCCCCCC	21945579
274	Phosphorylation	AQRQPSESGRHLLSE HCCCCCCCCCCCCCC	21945579
280	Phosphorylation	ESGRHLLSEPSTPLS CCCCCCCCCCCCCCC	20068231
283	Phosphorylation	RHLLSEPSTPLSPPG CCCCCCCCCCCCCCC	20068231
284	Phosphorylation	HLLSEPSTPLSPPGP CCCCCCCCCCCCCCC	20068231
287	Phosphorylation	SEPSTPLSPPGPGDV CCCCCCCCCCCCCCC	25137130
298	Phosphorylation	PGDVFFPSLDPVPDS CCCCCCCCCCCCCCC	20068231
305	Phosphorylation	SLDPVPDSPNFEVI- CCCCCCCCCCCCCC-	25137130

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 VISTA_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

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

Drug and Disease Associations

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

Regulatory Network of VISTA_HUMAN

Related Literatures of Post-Translational Modification