dbPTM

HA1B_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HA1B_MOUSE
UniProt AC	P01901
Protein Name	H-2 class I histocompatibility antigen, K-B alpha chain
Gene Name	H2-K1
Organism	Mus musculus (Mouse).
Sequence Length	369
Subcellular Localization	Membrane Single-pass type I membrane protein.
Protein Description	Involved in the presentation of foreign antigens to the immune system..
Protein Sequence	MVPCTLLLLLAAALAPTQTRAGPHSLRYFVTAVSRPGLGEPRYMEVGYVDDTEFVRFDSDAENPRYEPRARWMEQEGPEYWERETQKAKGNEQSFRVDLRTLLGYYNQSKGGSHTIQVISGCEVGSDGRLLRGYQQYAYDGCDYIALNEDLKTWTAADMAALITKHKWEQAGEAERLRAYLEGTCVEWLRRYLKNGNATLLRTDSPKAHVTHHSRPEDKVTLRCWALGFYPADITLTWQLNGEELIQDMELVETRPAGDGTFQKWASVVVPLGKEQYYTCHVYHQGLPEPLTLRWEPPPSTVSNMATVAVLVVLGAAIVTGAVVAFVMKMRRRNTGGKGGDYALAPGSQTSDLSLPDCKVMVHDPHSLA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
59	Phosphorylation	TEFVRFDSDAENPRY CEEEECCCCCCCCCC	35.69	26525534
107	N-linked_Glycosylation	RTLLGYYNQSKGGSH HHHHHHCCCCCCCCC	31.03	7306483
122	S-palmitoylation	TIQVISGCEVGSDGR EEEEEECCEECCCCC	2.82	26165157
167	Acetylation	AALITKHKWEQAGEA HHHHHHHHHHHHCHH	54.72	23201123
180	Phosphorylation	EAERLRAYLEGTCVE HHHHHHHHHHCHHHH	10.00	28059163
185	Glutathionylation	RAYLEGTCVEWLRRY HHHHHCHHHHHHHHH	3.72	24333276
194	Ubiquitination	EWLRRYLKNGNATLL HHHHHHHHCCCEEEE	54.60	22790023
197	N-linked_Glycosylation	RRYLKNGNATLLRTD HHHHHCCCEEEEECC	38.86	7306483
199	Phosphorylation	YLKNGNATLLRTDSP HHHCCCEEEEECCCC	30.26	19144319
338	Ubiquitination	RRRNTGGKGGDYALA HHCCCCCCCCCEECC	62.15	22790023
342	Phosphorylation	TGGKGGDYALAPGSQ CCCCCCCEECCCCCC	13.54	25159016
348	Phosphorylation	DYALAPGSQTSDLSL CEECCCCCCCCCCCC	29.26	25521595
350	Phosphorylation	ALAPGSQTSDLSLPD ECCCCCCCCCCCCCC	26.38	24723360
351	Phosphorylation	LAPGSQTSDLSLPDC CCCCCCCCCCCCCCC	28.99	27149854
354	Phosphorylation	GSQTSDLSLPDCKVM CCCCCCCCCCCCEEE	42.73	25521595
359	Ubiquitination	DLSLPDCKVMVHDPH CCCCCCCEEEECCCC	40.52	22790023
367	Phosphorylation	VMVHDPHSLA----- EEECCCCCCC-----	31.23	22942356

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 HA1B_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 HA1B_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of HA1B_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of HA1B_MOUSE

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."; Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.; Nat. Biotechnol. 27:378-386(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-107, AND MASSSPECTROMETRY.	19349973 [Abstract]
"Amino acid sequence of the carboxyl-terminal hydrophilic region ofthe H-2Kb MHC alloantigen. Completion of the entire primary structureof the H-2Kb molecule."; Uehara H., Coligan J.E., Nathenson S.G.; Biochemistry 20:5940-5945(1981). Cited for: PROTEIN SEQUENCE OF 22-367, AND GLYCOSYLATION AT ASN-107 AND ASN-197.	7306483 [Abstract]