DPB1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DPB1_HUMAN
• UniProt AC: P04440
• Protein Name: HLA class II histocompatibility antigen, DP beta 1 chain
• Gene Name: HLA-DPB1
• Organism: Homo sapiens (Human).
• Sequence Length: 258
• Subcellular Localization: Cell membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus, trans-Golgi network membrane; Single-pass type I membrane protein. Endosome membrane; Single-pass type I membrane pro
• Protein Description: Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route, where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules, and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments, exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides, autophagosomes constitutively fuse with MHC class II loading compartments. In addition to APCs, other cells of the gastrointestinal tract, such as epithelial cells, express MHC class II molecules and CD74 and act as APCs, which is an unusual trait of the GI tract. To produce a MHC class II molecule that presents an antigen, three MHC class II molecules (heterodimers of an alpha and a beta chain) associate with a CD74 trimer in the ER to form a heterononamer. Soon after the entry of this complex into the endosomal/lysosomal system where antigen processing occurs, CD74 undergoes a sequential degradation by various proteases, including CTSS and CTSL, leaving a small fragment termed CLIP (class-II-associated invariant chain peptide). The removal of CLIP is facilitated by HLA-DM via direct binding to the alpha-beta-CLIP complex so that CLIP is released. HLA-DM stabilizes MHC class II molecules until primary high affinity antigenic peptides are bound. The MHC II molecule bound to a peptide is then transported to the cell membrane surface. In B-cells, the interaction between HLA-DM and MHC class II molecules is regulated by HLA-DO. Primary dendritic cells (DCs) also to express HLA-DO. Lysosomal microenvironment has been implicated in the regulation of antigen loading into MHC II molecules, increased acidification produces increased proteolysis and efficient peptide loading..
• Protein Sequence: MMVLQVSAAPRTVALTALLMVLLTSVVQGRATPENYLFQGRQECYAFNGTQRFLERYIYNREEFARFDSDVGEFRAVTELGRPAAEYWNSQKDILEEKRAVPDRMCRHNYELGGPMTLQRRVQPRVNVSPSKKGPLQHHNLLVCHVTDFYPGSIQVRWFLNGQEETAGVVSTNLIRNGDWTFQILVMLEMTPQQGDVYTCQVEHTSLDSPVTVEWKAQSDSARSKTLTGAGGFVLGLIICGVGIFMHRRSKKVQRGSA

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Phosphorylation	-MMVLQVSAAPRTVA -CCEEECCCCHHHHH	13.02	24043423
12	Phosphorylation	QVSAAPRTVALTALL ECCCCHHHHHHHHHH	14.74	24043423
16	Phosphorylation	APRTVALTALLMVLL CHHHHHHHHHHHHHH	12.91	24043423
24	Phosphorylation	ALLMVLLTSVVQGRA HHHHHHHHHHHCCCC	18.47	24043423
25	Phosphorylation	LLMVLLTSVVQGRAT HHHHHHHHHHCCCCC	21.91	24043423
32	Phosphorylation	SVVQGRATPENYLFQ HHHCCCCCCCCCEEE	29.76	24043423
36	Phosphorylation	GRATPENYLFQGRQE CCCCCCCCEEECCCE	13.77	24043423
48	N-linked_Glycosylation	RQECYAFNGTQRFLE CCEEECCCCHHHHHH	44.42	UniProtKB CARBOHYD
57	Phosphorylation	TQRFLERYIYNREEF HHHHHHHHCCCHHHH	9.81	-
59	Phosphorylation	RFLERYIYNREEFAR HHHHHHCCCHHHHHC	10.15	-
69	Phosphorylation	EEFARFDSDVGEFRA HHHHCCCCCCCHHHH	31.33	-
219	Phosphorylation	TVEWKAQSDSARSKT EEEEEECCCCCCCCE	38.09	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of DPB1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of DPB1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of DPB1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RTN4_HUMAN	RTN4	physical	21900206
ROBO2_HUMAN	ROBO2	physical	21900206
TRIP6_HUMAN	TRIP6	physical	25416956
LZTS2_HUMAN	LZTS2	physical	25416956
ARMC8_HUMAN	ARMC8	physical	26186194
MKLN1_HUMAN	MKLN1	physical	26186194
RANB9_HUMAN	RANBP9	physical	26186194
RBP10_HUMAN	RANBP10	physical	26186194
RMD5A_HUMAN	RMND5A	physical	26186194
GID4_HUMAN	GID4	physical	26186194
GID8_HUMAN	GID8	physical	26186194
NFS1_HUMAN	NFS1	physical	26186194
YPEL5_HUMAN	YPEL5	physical	26186194
LYRM4_HUMAN	LYRM4	physical	26186194
LYRM4_HUMAN	LYRM4	physical	28514442
NFS1_HUMAN	NFS1	physical	28514442
ARMC8_HUMAN	ARMC8	physical	28514442
ERP29_HUMAN	ERP29	physical	28514442
MKLN1_HUMAN	MKLN1	physical	28514442
IDE_HUMAN	IDE	physical	28514442

Drug and Disease Associations

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