dbPTM

PD1L1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PD1L1_HUMAN
UniProt AC	Q9NZQ7
Protein Name	Programmed cell death 1 ligand 1 {ECO:0000303\|PubMed:28813417}
Gene Name	CD274 {ECO:0000312\|HGNC:HGNC:17635}
Organism	Homo sapiens (Human).
Sequence Length	290
Subcellular Localization	Cell membrane Single-pass type I membrane protein . Early endosome membrane Single-pass type I membrane protein . Recycling endosome membrane Single-pass type I membrane protein . Associates with CMTM6 at recycling endosomes, where it is protec
Protein Description	Plays a critical role in induction and maintenance of immune tolerance to self. As a ligand for the inhibitory receptor PDCD1/CD279, modulates the activation threshold of T-cells and limits T-cell effector response. [PubMed: 11015443 The PDCD1/CD279-mediated inhibitory pathway is exploited by tumors to attenuate anti-tumor immunity and facilitate tumor survival]
Protein Sequence	MRIFAVFIFMTYWHLLNAFTVTVPKDLYVVEYGSNMTIECKFPVEKQLDLAALIVYWEMEDKNIIQFVHGEEDLKVQHSSYRQRARLLKDQLSLGNAALQITDVKLQDAGVYRCMISYGGADYKRITVKVNAPYNKINQRILVVDPVTSEHELTCQAEGYPKAEVIWTSSDHQVLSGKTTTTNSKREEKLFNVTSTLRINTTTNEIFYCTFRRLDPEENHTAELVIPELPLAHPPNERTHLVILGAILLCLGVALTFIFRLRKGRMMDVKKCGIQDTNSKKQSDTHLEET

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
35	N-linked_Glycosylation	YVVEYGSNMTIECKF EEEEECCCEEEEEEC	27.53	UniProtKB CARBOHYD
112	Phosphorylation	KLQDAGVYRCMISYG CHHHCCEEEEEEEEC	9.36	22817900
118	Phosphorylation	VYRCMISYGGADYKR EEEEEEEECCCCEEE	14.51	22817900
123	Phosphorylation	ISYGGADYKRITVKV EEECCCCEEEEEEEE	11.13	22817900
134	Phosphorylation	TVKVNAPYNKINQRI EEEECCCCCCCCCEE	27.03	22817900
180	Phosphorylation	QVLSGKTTTTNSKRE CEECCCEECCCCHHH	34.80	-
184	Phosphorylation	GKTTTTNSKREEKLF CCEECCCCHHHHHHE	30.88	-
192	N-linked_Glycosylation	KREEKLFNVTSTLRI HHHHHHEECCEEEEE	46.74	19159218
195	Phosphorylation	EKLFNVTSTLRINTT HHHEECCEEEEEECC	22.59	-
200	N-linked_Glycosylation	VTSTLRINTTTNEIF CCEEEEEECCCCCEE	25.57	UniProtKB CARBOHYD
219	N-linked_Glycosylation	RRLDPEENHTAELVI ECCCCCCCCEEEEEE	35.83	UniProtKB CARBOHYD
270	Acetylation	KGRMMDVKKCGIQDT CCCCEEEECCCCCCC	37.77	11794147
272	S-palmitoylation	RMMDVKKCGIQDTNS CCEEEECCCCCCCCC	4.87	30514902
277	Phosphorylation	KKCGIQDTNSKKQSD ECCCCCCCCCCCCCC	25.64	30108239
279	Phosphorylation	CGIQDTNSKKQSDTH CCCCCCCCCCCCCCC	43.24	30108239
283	Phosphorylation	DTNSKKQSDTHLEET CCCCCCCCCCCCCCC	54.05	20164059
285	Phosphorylation	NSKKQSDTHLEET-- CCCCCCCCCCCCC--	33.34	30108239
290	Phosphorylation	SDTHLEET------- CCCCCCCC-------	34.24	30108239

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
112	Y	Phosphorylation	Kinase	JAK1	P23458	PSP
180	T	Phosphorylation	Kinase	GSK3B	P49841	PSP
184	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
195	S	Phosphorylation	Kinase	AMPKA1	Q13131	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PD1L1_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 PD1L1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PTN11_HUMAN	PTPN11	physical	11224527
PDCD1_HUMAN	PDCD1	physical	21982860
CD80_HUMAN	CD80	physical	21982860
S39AB_HUMAN	SLC39A11	physical	26186194
THADA_HUMAN	THADA	physical	26186194
XPO7_HUMAN	XPO7	physical	26186194
UTP20_HUMAN	UTP20	physical	26186194
GCN1_HUMAN	GCN1L1	physical	26186194
XPO6_HUMAN	XPO6	physical	26186194
IPO7_HUMAN	IPO7	physical	26186194
ATR_HUMAN	ATR	physical	26186194
TM160_HUMAN	TMEM160	physical	26186194
TNPO2_HUMAN	TNPO2	physical	26186194
TNPO1_HUMAN	TNPO1	physical	26186194
SAAL1_HUMAN	SAAL1	physical	26186194
TTI1_HUMAN	TTI1	physical	26186194
HEAT1_HUMAN	HEATR1	physical	26186194
COG2_HUMAN	COG2	physical	26186194
EXOC1_HUMAN	EXOC1	physical	26186194
HIP1R_HUMAN	HIP1R	physical	26186194
XPO4_HUMAN	XPO4	physical	26186194
UBP22_HUMAN	USP22	physical	26186194
EXOC7_HUMAN	EXOC7	physical	26186194
INT2_HUMAN	INTS2	physical	26186194
NUP85_HUMAN	NUP85	physical	26186194
CIP2A_HUMAN	KIAA1524	physical	26186194
RINT1_HUMAN	RINT1	physical	26186194
CK5P3_HUMAN	CDK5RAP3	physical	26186194
COG1_HUMAN	COG1	physical	26186194
MTOR_HUMAN	MTOR	physical	26186194
COG3_HUMAN	COG3	physical	26186194
TNPO3_HUMAN	TNPO3	physical	26186194
ATM_HUMAN	ATM	physical	26186194
COG7_HUMAN	COG7	physical	26186194
KIF14_HUMAN	KIF14	physical	26186194
STAG1_HUMAN	STAG1	physical	26186194
COG4_HUMAN	COG4	physical	26186194
VAC14_HUMAN	VAC14	physical	26186194
NF1_HUMAN	NF1	physical	26186194
PDS5B_HUMAN	PDS5B	physical	26186194
CTR3_HUMAN	SLC7A3	physical	26186194
COG5_HUMAN	COG5	physical	26186194
F1142_HUMAN	FAM114A2	physical	26186194
MINP1_HUMAN	MINPP1	physical	26186194
DOLK_HUMAN	DOLK	physical	26186194
GSK3B_HUMAN	GSK3B	physical	27572267
ATR_HUMAN	ATR	physical	28514442
CK5P3_HUMAN	CDK5RAP3	physical	28514442
XPO4_HUMAN	XPO4	physical	28514442
XPO7_HUMAN	XPO7	physical	28514442
UTP20_HUMAN	UTP20	physical	28514442
DOLK_HUMAN	DOLK	physical	28514442
S39AB_HUMAN	SLC39A11	physical	28514442
COG1_HUMAN	COG1	physical	28514442
MTOR_HUMAN	MTOR	physical	28514442
THADA_HUMAN	THADA	physical	28514442
COG5_HUMAN	COG5	physical	28514442
COG3_HUMAN	COG3	physical	28514442
TNPO2_HUMAN	TNPO2	physical	28514442
XPO6_HUMAN	XPO6	physical	28514442
HIP1R_HUMAN	HIP1R	physical	28514442
COG7_HUMAN	COG7	physical	28514442
UBP22_HUMAN	USP22	physical	28514442
TNPO3_HUMAN	TNPO3	physical	28514442
ATM_HUMAN	ATM	physical	28514442
COG2_HUMAN	COG2	physical	28514442
TTI1_HUMAN	TTI1	physical	28514442
CIP2A_HUMAN	KIAA1524	physical	28514442
GCN1_HUMAN	GCN1L1	physical	28514442
STAG1_HUMAN	STAG1	physical	28514442
IPO7_HUMAN	IPO7	physical	28514442
COG8_HUMAN	COG8	physical	28514442
INT2_HUMAN	INTS2	physical	28514442

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 PD1L1_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"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-192, AND MASSSPECTROMETRY.	19159218 [Abstract]