dbPTM

HA2B_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HA2B_MOUSE
UniProt AC	P14434
Protein Name	H-2 class II histocompatibility antigen, A-B alpha chain
Gene Name	H2-Aa
Organism	Mus musculus (Mouse).
Sequence Length	256
Subcellular Localization	Membrane Single-pass type I membrane protein .
Protein Description
Protein Sequence	MPRSRALILGVLALTTMLSLCGGEDDIEADHVGTYGISVYQSPGDIGQYTFEFDGDELFYVDLDKKETVWMLPEFGQLASFDPQGGLQNIAVVKHNLGVLTKRSNSTPATNEAPQATVFPKSPVLLGQPNTLICFVDNIFPPVINITWLRNSKSVADGVYETSFFVNRDYSFHKLSYLTFIPSDDDIYDCKVEHWGLEEPVLKHWEPEIPAPMSELTETVVCALGLSVGLVGIVVGTIFIIQGLRSGGTSRHPGPL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference	Orthologous Protein Cluster
145	N-linked_Glycosylation	NIFPPVINITWLRNS CCCCCCEEEEECCCC	26.35	12589760

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 HA2B_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of HA2B_MOUSE !!

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 HA2B_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of HA2B_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of HA2B_MOUSE

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Crystal structure of MHC class II I-Ab in complex with a human CLIPpeptide: prediction of an I-Ab peptide-binding motif."; Zhu Y., Rudensky A.Y., Corper A.L., Teyton L., Wilson I.A.; J. Mol. Biol. 326:1157-1174(2003). Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 24-205 IN COMPLEX WITH HUMANCLIP PEPTIDE, GLYCOSYLATION AT ASN-145, AND DISULFIDE BONDS.	12589760 [Abstract]