dbPTM

HA11_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HA11_MOUSE
UniProt AC	P01899
Protein Name	H-2 class I histocompatibility antigen, D-B alpha chain
Gene Name	H2-D1
Organism	Mus musculus (Mouse).
Sequence Length	362
Subcellular Localization	Membrane Single-pass type I membrane protein.
Protein Description	Involved in the presentation of foreign antigens to the immune system..
Protein Sequence	MGAMAPRTLLLLLAAALAPTQTRAGPHSMRYFETAVSRPGLEEPRYISVGYVDNKEFVRFDSDAENPRYEPRAPWMEQEGPEYWERETQKAKGQEQWFRVSLRNLLGYYNQSAGGSHTLQQMSGCDLGSDWRLLRGYLQFAYEGRDYIALNEDLKTWTAADMAAQITRRKWEQSGAAEHYKAYLEGECVEWLHRYLKNGNATLLRTDSPKAHVTHHPRSKGEVTLRCWALGFYPADITLTWQLNGEELTQDMELVETRPAGDGTFQKWASVVVPLGKEQNYTCRVYHEGLPEPLTLRWEPPPSTDSYMVIVAVLGVLGAMAIIGAVVAFVMKRRRNTGGKGGDYALAPGSQSSEMSLRDCKA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
55	Ubiquitination	SVGYVDNKEFVRFDS EEEEECCCEEEECCC	48.33	PubMed
62	Phosphorylation	KEFVRFDSDAENPRY CEEEECCCCCCCCCC	35.69	27841257
92	Ubiquitination	ERETQKAKGQEQWFR HHHHHHCCCCCHHHH	69.07	PubMed
110	N-linked_Glycosylation	RNLLGYYNQSAGGSH HHHHHCCCCCCCCCC	22.35	7118212
155	Ubiquitination	IALNEDLKTWTAADM EEECCCHHHHHHHHH	55.10	PubMed
170	Ubiquitination	AAQITRRKWEQSGAA HHHHHHHHHHHCCHH	52.36	PubMed
188	Glutathionylation	KAYLEGECVEWLHRY HHHHHCHHHHHHHHH	5.03	24333276
197	Ubiquitination	EWLHRYLKNGNATLL HHHHHHHHCCCEEEE	54.60	PubMed
200	N-linked_Glycosylation	HRYLKNGNATLLRTD HHHHHCCCEEEEECC	38.86	-
210	Ubiquitination	LLRTDSPKAHVTHHP EEECCCCCCCCCCCC	55.89	PubMed
220	Ubiquitination	VTHHPRSKGEVTLRC CCCCCCCCCCEEEEE	61.44	PubMed
267	Ubiquitination	AGDGTFQKWASVVVP CCCCCHHCEEEEEEE	40.30	PubMed
277	Ubiquitination	SVVVPLGKEQNYTCR EEEEECCCCCCEEEE	64.90	PubMed
280	N-linked_Glycosylation	VPLGKEQNYTCRVYH EECCCCCCEEEEEEE	34.86	3980466
332	Ubiquitination	AVVAFVMKRRRNTGG HHHHHHHHHCCCCCC	37.13	17502423PubMed
340	Ubiquitination	RRRNTGGKGGDYALA HCCCCCCCCCCCCCC	62.15	17502423PubMed
350	Phosphorylation	DYALAPGSQSSEMSL CCCCCCCCCCCCCCH	26.32	24719451
353	Phosphorylation	LAPGSQSSEMSLRDC CCCCCCCCCCCHHHC	29.67	-
356	Phosphorylation	GSQSSEMSLRDCKA- CCCCCCCCHHHCCC-	19.05	24719451

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
-	K	Ubiquitination	E3 ubiquitin ligase	K3	O41933	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of HA11_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 HA11_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of HA11_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of HA11_MOUSE

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Primary structure of the H-2Db alloantigen. II. Additional amino acidsequence information, localization of a third site of glycosylationand evidence for K and D region specific sequences."; Maloy W.L., Coligan J.E.; Immunogenetics 16:11-22(1982). Cited for: PROTEIN SEQUENCE OF 253-308 AND 332-358.	7118212 [Abstract]